ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
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stringlengths 108
11.1k
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O67074 | MKSSPKSLKMRDNLLDGTFVVIDLEATGFDVEKSEVIDLAAVRVEGGIITEKFSTLVYPGYFIPERIKKLTGITNAMLVGQPTIEEVLPEFLEFVGDNIVVGHFVEQDIKFINKYTKQYRGKKFRNPSLCTLKLARKVFPGLKKYSLKEIAENFGFETNGVHRALKDATLTAEIFIKILEELWFKYGIGDYYSLKRLEKGKF | Cofactor: Binds 2 divalent metal cations. Magnesium or manganese.
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 23045
Sequence Length: 202
EC: 2.7.7.7
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P57337 | MNRKRTIILDTETTGINQTSLPHINHRIIEIGAVEIIDRCFTGNNFHVYIQPGRSIESGALKVHGITNKFLLDKPIFKDIADSFLNYIKNSILVIHNASFDVGFINQELEILNKKIKINTFCSIIDTLKIARELFPGKKNTLDALCTRYKINKSHRNLHSAIVDSYLLGKLYLLMTGGQDSLFSDNTINYKENFKKLKKNIQLKNNTLRILHPTLKENDLHEKYLQYMKDKSTCLWN | Cofactor: Binds 2 divalent metal cations. Magnesium or manganese.
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 27365
Sequence Length: 237
EC: 2.7.7.7
|
Q89AN3 | MKKYDRKIVLDIETTGMNPAGCFYKNHKIIEIGAVEMINNVFTGNNFHSYIQPNRLIDKQSFKIHGITDNFLLDKPKFHEISVKFLEYITNSDLIIHNAKFDVGFINYELNMINSDKRKISDYCNVVDTLPLARQLFPGKKNSLDALCNRYKINVSHRDFHSALIDAKLLAKVYTFMTSFQQSISIFDKNSNLNSIQKNAKLDSRVPFRSTLLLATKDELQQHMKYLKYVKQETGNCVWLEDKYN | Cofactor: Binds 2 divalent metal cations. Magnesium or manganese.
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 28519
Sequence Length: 245
EC: 2.7.7.7
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P03007 | MSTAITRQIVLDTETTGMNQIGAHYEGHKIIEIGAVEVVNRRLTGNNFHVYLKPDRLVDPEAFGVHGIADEFLLDKPTFAEVADEFMDYIRGAELVIHNAAFDIGFMDYEFSLLKRDIPKTNTFCKVTDSLAVARKMFPGKRNSLDALCARYEIDNSKRTLHGALLDAQILAEVYLAMTGGQTSMAFAMEGETQQQQGEATIQRIVRQASKLRVVFATDEEIAAHEARLDLVQKKGGSCLWRA | Cofactor: Binds 2 divalent metal cations. Magnesium or manganese.
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease . Contacts both the beta sliding clamp (dnaN) and the polymerase subunit (dnaE), stabilizing their interaction .
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 27099
Sequence Length: 243
EC: 2.7.7.7
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O68045 | MGLARLSLRLRIFLFFAALAMGNLAALVAGLVFGFHKLARPEALSGFVIGGTVAGLVILGLIGVVWALFDANLARPIERLAGSIRARTQTAVDSALDESAGRYLGDLAPAAAAIAQHLNETRSALTEAVQRETTRLAREKDRLETLLSDVPVGVLLCTADHALVFYNGQAVDLLGGAHAPGLDRRVFDYLHPAPIRHAHARLLATADPDAASDLLCATVADGRTLAARMRLISEGEDHQVRRLAGYVLTLRDVSADLRAHAGREALMDELFDRIRRPAAALQSLMGVLIAEDGPADPQARAQLREAARAEAGHLAQAIHSLHDRHEAMRADWWPLAMIRASDFGAAVQARVAAEGAGDLLPVTAALLLRLEGFEMVALIAHLVRRLGPGRAEKRLEVLEDGAGALIALEWRGAAVAIADLELWLSEPLDVGQAEVTGRRVLSVHATDLWPERLHEGRHRLCLPLREARRIGPDPHPVPRPVPRQVVYDFDLLGRGGESALAETPLDKLTFVVFDTETTGLFPTGGDEIVQIAAVRIVNGRRVAGEVFDTLVNPGRPIPAASTAVHGITEAMVATAPAIAEVGRRFHKFAEGAVLVAHNAPFDLEFLRRKELLIGKNFDNPVLDTVLLSAVVFGAAEGHSLDALTHRLGITIPEEARHTALGDTVATAEAFLRLLPALKARGLTTFGAVLTEVRKHGRLMRDMNA | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 75683
Sequence Length: 704
EC: 2.7.7.7
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Q9ZCJ9 | MSSLREIILDTETTGLDPQQGHRIVEIGAIEMVNKVLTGKHFHFYINPERDMPFEAYKIHGISGEFLKDKPLFKTIANDFLKFIADSTLIIHNAPFDIKFLNHELSLLKRTEIKFLELTNTIDTLVMARNMFPGARYSLDALCKRFKVDNSGRQLHGALKDAALLAEVYVALTGGRQSTFKMINKPDEINNLAVKCVDVQQIKRGIVVKPTKEELQKHKEFIDKILIQA | Cofactor: Binds 2 divalent metal cations. Magnesium or manganese.
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 26078
Sequence Length: 229
EC: 2.7.7.7
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O83649 | MIYDWVFAVHEHVAFTAFDTETTGLKAEEDRIIEIGAVTFDRKGIIARFSTLIFPDRAIPPDVSKINHITDDMLVNKPRFCEIVSDFSRFIKGTVLVAHNANFDVEFLNAELSLCKKQPLSHKVVDTYAMAQAVFPGLGRHQYRLQNLALQFGLTVHAAHRAEDDARVCMELFTTMIAHHAKQNGHCVNHAQSPTIKKLIQEIQASSTDCSQELF | Cofactor: Binds 2 divalent metal cations. Magnesium or manganese.
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 24239
Sequence Length: 215
EC: 2.7.7.7
|
P09122 | MSYQALYRVFRPQRFEDVVGQEHITKTLQNALLQKKFSHAYLFSGPRGTGKTSAAKIFAKAVNCEHAPVDEPCNECAACKGITNGSISDVIEIDAASNNGVDEIRDIRDKVKFAPSAVTYKVYIIDEVHMLSIGAFNALLKTLEEPPEHCIFILATTEPHKIPLTIISRCQRFDFKRITSQAIVGRMNKIVDAEQLQVEEGSLEIIASAADGGMRDALSLLDQAISFSGDILKVEDALLITGAVSQLYIGKLAKSLHDKNVSDALETLNELLQQGKDPAKLIEDMIFYFRDMLLYKTAPGLEGVLEKVKVDETFRELSEQIPAQALYEMIDILNKSHQEMKWTNHPRIFFEVAVVKICQTSHQSAADLPEVDMLMKKIQQLEQEVERLKTTGIKAAAESPKKEAPRVPKGGKSNYKAPVGRIHEILKEATRPDLDLLRNSWGKLLAHLKQQNKVSHAALLNDSEPVAAGSAAFVLKFKYEIHCKMVAEDNNGVRTNLEQILESMLGKRMDLIGVPEAQWGKIREEFLEDHQQENEGSNEPAEEDPLIAEAKKLVGADLIEIKD | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 62763
Sequence Length: 563
EC: 2.7.7.7
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P57553 | MNYQILARKWRPQYFRDIIGQKHIVTAISNGLSLGRIHHAWLLSGTRGIGKTTIARLLAKSLNCQNGITSDPCRQCIICKEIEKGLCLDVIEIDGASRTKVEEMREILDSIYYSPIKSRFKVYLIDEVHMLSRHSFNALLKTLEEPPEHVKFVLATTDVDRIPKTIISRCLYFKLQIISEEKIFKFLKYILIKESIDTDEYSLKKIAYHAHGSIRDALNLLEHAINLGNGHVNIKNVTDMLGLLPEKYSFLLTDAVLKKDSKKTMLLLNKISSIGVEWEEILIEMLRFLYHISTSQSFPLVWEKIFTEKYKNQIQKIAQNNKKTNIQLCYQILLNGRKELKFAPSQKIGVEMSLLRVISAI | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 41607
Sequence Length: 361
EC: 2.7.7.7
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Q8K983 | MNYQILARKWRPQSFKKIIGQKYIVKAISNGFSLGKIHHAWLLSGTRGVGKTTIARLIAKSLNCEIGITSLPCRKCTICQEIEKGICLDFIEIDAASRTKVEEIREILDNIYYTPSKSRFKVYLIDEVHMLSRHSFNALLKTLEEPPQHIKFILATTDVEKIPKTIRSRCLHFKLNILSEEDIFNFLKHILKKGGNNFDEEALKIISDYANGSMRDALNLLEHAMHLSKNNINLKNTTEMLGIPNKKHAFLLTKFLLEQDSKKMMCLLNKISKIGLEWQNILIEMMRFLHHIAMLKSYPKIWNQIFIKNNENEIKKIAENNSKYNIQLCYKILLKGRKELFFSPNHKMGVEMILLQAITEIKR | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 42186
Sequence Length: 363
EC: 2.7.7.7
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Q8EQ56 | MQPSKVNKHRIIFHIDMNCFYASVEMAHNPSLKGKPLAIAGNPEERKGIIVTSSYEARGKGVKTTMPIWQAKKLCPDLILMRPNFDRYRAASREIFKMLAEITPYVQPVSIDEGYMDITDTIYAKDPLVTANQLQQRILSGLDIPCSIGIAPNKFLAKMASDMKKPLGITVLRKREVEKLLWPMSVEEMYGIGEKTAQKLNSIEIKTIGDLAKKNVYELKQLLGVNGERLQNRANGIDNRLVDPEAVHDFKSIGSSQTLPHDSTDVTELMQLIHELVDNVERRVKRKEAAGKTVQITIRYHDRKTITRSKKLYNYIDNHREILFVAKELFEQHWNEAPVRLLGVSLQDMETKRNIGEQLDLFTYEAIEKKEKLKVTVDKLTKKYGSNIITSQKNKNESQENQQPRTSFQKDFLDDYKKP | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 48075
Sequence Length: 419
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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B1ZN03 | MILPTIVHLDADAFFVSCELALKPELRGTKCAVGGRERGIISSASYEARACGVYTPMPTTRALKVCPDLIMLPHTGGLYSRVSRQMFELCETLTPLVQRNSIDEGYLDLGPCGFKTSAEIEQAVHGLQHKIEQQLQITASFGLAVNKLVAQIASKLRKPKGFVVVPSGTEAEFLAPLPIGKLPGVGPKTEERLVGRHGIKLVRDLLARGEAELEAIFGDGWREMRDGALGIDDRPVETEHEDAKSYSQQETFDEDIASFAEIERVVKRMIDELLPKIREDGKRVRTMTVKVRYPDFSQESHGRSLSAGTDLEAPFYPLVTPLLRQAWTKKRPLRLVSVRFSGVEDTPVQLEMFAQNEEKRRRLAAVLDHLNRRGGDAVVQHGHQLAKRPPPR | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 43631
Sequence Length: 392
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q6MA55 | MTLRKIIHIDMDAFYASVEMRDDPSLVLKPIAVGGDPDKRGVIATANYLARKFGVRSAMPSWKAKQLCPDLIILFPDFDKYKRESKAIHEIFHLFTDLIEPLSLDEAFLDVTDVDALRGSATWIAQEIRQLIWKERGLTASAGVAPNKFLAKVASDWHKPNGQFVLTPKEVDAFMVHLPVEKIFGIGHVMAKKLHSLGLMNCGDLQTLDITTLQKLFGSRAWNLYELCRGIDHRFVISDRIRKSLSVESTFLEDLNNLELCYQEIPNLIERLMIRYEKISNQYYKKKPFIKIKFADFTTTTVENTFFKAFDLETYQTLIRIGWERKKAPVRLLGLGMSLSLEEEIQLTLF | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 40194
Sequence Length: 350
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q6KZW2 | MIMLIDFDYFFAQVEEINDPSLKGKPVVVSVYSGRNERSGAVATSNYEARALGIKSGMPLYRALEIGKNRAVFLPIRKDFYQKYSDKIMDIISEYSEKMEIASIDEAYIDIDGNDCKIGIANEIKNRILNETGIKVSIGIGINKVIAKMAAEMAKPNGIKCISADETGEFLNNIKINDIPGIGKVLSKNLNEIGIEYLRDIKNFDVNKIKSILGESKTNYLYELYENKYFSPVEPRVKKNFGRYLTLPENTRDIDKIVPYLKKSIDAAYEKAPGIPQEISVVAIMEDLDIVSRSYTGNAIKRDDSINIALNLLNKIISEDNRNIRRIGVRLSKISKNNTLDDFF | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 38809
Sequence Length: 344
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q3KH18 | MTQRKIIHVDCDCFYAAIEMRDDPSLAGKPLAVGGSADRRGVIATCNYEARAYGVRSAMSSGHALKLCPDLTIVKPRMDAYREASKEIHTIFSDYTDLIEPLSLDEAYLDVSDSAHFGGSATRIAQDIRRRVSNQLHITVSAGVAPNKFLAKIASDWRKPNGLFVITPDQVEEFVSGLPVSKLHGVGKVTADKLGKLGINDCLQLREWDKLALVREFGSFGERLWSLARGIDERLVHNDSRRQSISVENTYDVDLPDLRSCLDKLPELLETLKTRMARIDSSYRPGKPFVKVKFHDFTQTTLEQAGAGRDLGSYQLMLTQAFNRGGKPVRLLGVGVRLEDLRGGFEQMELFER | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 39375
Sequence Length: 353
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q87Y22 | MTQRKIIHIDCDCFYAAIEMRDEPELAGKPLAVGGSAERRGVIATCNYEARAYGVRSAMSSRHALKLCPDLTIVKPRMEAYKEASREIHSIFRDYTDLIEPLSLDEAFLDVSDTHHFSGSATRIAQDIRRRVSNQLHITVSAGVAPNKFLAKIASDWKKPNGLFVITPDQVEDFVASLPVTKLHGVGKVTADKLGRLGIVDCADLRSRSKLALVREFGSFGERLWSLAHGIDDRPVQNDSRRQSVSVENTYDTDLPDLAACLEKLPALLETLGTRMERMEGQYRPGKPFVKVKFHDFTQTTLEQSGAGRDLGSYEQLLTQAFARGGKPVRLLGIGVRLHDLRDAHEQLELFST | Cofactor: Binds 2 magnesium ions per subunit.
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 39320
Sequence Length: 353
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q92076 | EEGWVPGPSLISLQMRVTPKLMRLAWDGFPLHYSEKHGWGYLVPGRQDNLPAASAEPEGPVCPHRAIERLYRQHCLQRGQEQPPEEAGVEDELMVLEGSSMWQKVEELSQLELDMERPGRAEQSQMQDEDGLPELVEESSQPSFHHGNGPYNDVNIPGCWFFKLPHKDGNENNVGSPFAKDFLPRMEDGTLRAAVGRTHGTRALEINKMVSFWRNAHKRVSSQVVVWLKKGELPRAVTRHPAYSEEEDYGAILPQVVTAGTITRRAVEPTWLTASNARADRVGSELKAMVQVPPGYSLVGADVDSQELWIAAVLGEAHFAGMHGCTAFGWMTLQGKKSDGTDLHSKTAATVGISREHAKVFNYGRIYGAGQPFAERLLMQFNHRLTQQQAREKAQQMYAVTKGIRRFHLSEEGEWLVKELELAVDKAEDGTVSAQDVQKIQREAMRKSRRKKKWDVVAHRMWAGGTESEMFNKLESIALSASPQTPVLGCHISRALEPAVAKGEFLTSRVNWVVQSSAVDYLHLMLVSMKWLFEEYDINGRFCISIHDEVRYLVQEQDRYRAALALQITNLLTRCMFAYKLGLQDLPQSVAFFSAVDIDRCLRKEVTMNCATPSNPTGMEKKYGIPRGEALDIYQIIEITKGSLEKK | Function: Involved in the replication of mitochondrial DNA. Associates with mitochondrial DNA (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 72855
Sequence Length: 647
Subcellular Location: Mitochondrion
EC: 2.7.7.7
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P17396 | MHPFSRLFRNIQSLGEEEVQELLGPPEDALPLLAGEDLNHRVADALNLHLPTADLQWVHKTNAITGLYSNQAAQFNPNWIQPEFPELHLHNDLIQKLQQYFGPLTINEKRKLQLNFPARFFPKATKYFPLIKGIKNNYPNFALEHFFATANYLWTLWEAGILYLRKNQTTLTFKGKPYSWEHRQLVQHNGQQHKSHLQSRQNSSMVACSGHLLHNHLSSESVSVSTRNLSNNISDKSQKSTRTGLCSYKQIQTDRLEHLARISCGSKIFIGQQGSSPKTLYKSISSNFRNQTWAYNSSRNSGHTTWFSSASNSNKSRSREKAYSSNSTSKRYSPPLNYEKSDFSSPGVRRRITRLDNNGTPTQCLWRSFYNTKPCGSYCIHHIVSSLDDWGPCTVTGDVTIKSPRTPRRITGGVFLVDKNPNNSSESRLVVDFSQFSRGHTRVHWPKFAVPNLQTLANLLSTNLQWLSLDVSAAFYHIPISPAAVPHLLVGSPGLERFYTCLSSSTHNRNNSQLQTMHNLCTRHVYSSLLLLFKTYGRKLHLLAHPFIMGFRKLPMGVGLSPFLLAQFTSALASMVRRNFPHCVVFAYMDDLVLGARTSEHLTAIYSHICSVFLDLGIHLNVNKTKWWGNHLHFMGYVITSSGVLPQDKHVKKISRYLHSVPVNQPLDYKICERLTGILNYVAPFTLCGYAALMPLYHAIASRMAFIFSSLYKSWLLSLYEELWPVVRQRGVVCTVFADATPTGWGIATTCQLLSGTFAFPLPIATAELIAACLARCWTGARLLGTDNSVVLSGKLTSFPWLLACVAHWILRGTSFCYVPSALNPADLPSRGLLPALRPLPRLRLRPQTSRISLWAASPPVSPRRPVRVAWSSPVQTCEPWIPP | Function: Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 99708
Sequence Length: 884
Domain: Terminal protein domain (TP) is hepadnavirus-specific. Spacer domain is highly variable and separates the TP and RT domains. Polymerase/reverse-transcriptase domain (RT) and ribonuclease H domain (RH) are similar to retrovirus reverse transcriptase/RNase H.
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P11292 | SKRYSPPLNYEKSDFSSPGVRGRITRLDNNGTPPQCLWRSFYNTKPCGSYCIHHIVSSLDDWGPCTVTGDVTIKSPRTPRRITGGVFLVDKNPNNSSESRLVVDFSQFSRGHTRVHWPKFAVPNLQTLANLLSTNLQWLSLDVSAAFYHIPISPAAVPHLLVGSPGLERFTTCLSSSTHNGNDSQLQTMHALCTRHVYSSLLLLFKTYGRKLHLLAHPFIMGFRKLPMGVGLSPFLLAQFTSALASMVRRNFPHCVVFAYMDDLVLGARTSEHLTAIYSHICSVFLDLGIHLNVNKTKWWGNHLHFMGYVITSSGVLPQDKHVKKLSRYLRSVPVNQPLDYKICERLTGILNYVAPFTLCGYAALMPLYHAIASRTAFIFSSLYKSWLLSLYEELWPVVRQRGVVCTVFADATPTGWGIATTCQLLSGTFAFPLPIATAELIAACLARCWTGARLLGTDNSVVLSGKLTSFPWLLACVANWILRGTSFCYVPSALNPADLPSRGLLPVLRPLPRLRLRPQTSRISLWAASPPVSPRRPVRVAWSSPVQTCEPWIPP | Function: Multifunctional enzyme that converts the viral RNA genome into dsDNA in viral cytoplasmic capsids. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3'- to 5'-endonucleasic mode. Neo-synthesized pregenomic RNA (pgRNA) are encapsidated together with the P protein, and reverse-transcribed inside the nucleocapsid. Initiation of reverse-transcription occurs first by binding the epsilon loop on the pgRNA genome, and is initiated by protein priming, thereby the 5'-end of (-)DNA is covalently linked to P protein. Partial (+)DNA is synthesized from the (-)DNA template and generates the relaxed circular DNA (RC-DNA) genome. After budding and infection, the RC-DNA migrates in the nucleus, and is converted into a plasmid-like covalently closed circular DNA (cccDNA). The activity of P protein does not seem to be necessary for cccDNA generation, and is presumably released from (+)DNA by host nuclear DNA repair machinery (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 61872
Sequence Length: 556
Domain: Terminal protein domain (TP) is hepadnavirus-specific. Spacer domain is highly variable and separates the TP and RT domains. Polymerase/reverse-transcriptase domain (RT) and ribonuclease H domain (RH) are similar to retrovirus reverse transcriptase/RNase H (By similarity).
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P30322 | EFPKYDSITELDVYCNQNNKSDVQMYNFITKLESEYGNITVTVYKGSKTISNDKSILNECELYFVFNIGSNKRVVCLADNKTWDQSLKYWNSSKYPYPRWCDEYLTESEFVRSIGEYKFHVNNGTVKYWEKYYNFPDMVFNYSDKKHDLRIGSLDLETYGDNCFELGLGNLNVYAGGFALNDGFKKLYYLNNDTELNSGEAIIKKMFGDLFDYIAEDRKARNNYTIYAHNLGRFDSVFIIRSLCSEGYKINGQWIDNSILYLKIVDSTRKLTIKLRDSIKLVPHSLDKALSSNGCNISKGMFPHKFVNKDTLNYIGDKPDIKYYVDENKFNESKLKKYKSLPSILNLKKECLNYLDKDILGLLELMNKVSLTYFNEYKLNITKFSTLPSITLNIFGIRFYDDQNSIKMINGPLSEFIRSSYFGGNSDIFVSGEERLVKNGYHYDMNSQYPYAMLQSMPTGNPVFSTNTDLNYYRNGFVFARVTPPSKDTLVNLFIPRRSDDGSVICDRNTFYEFIPTPDLKQGLEYGYKFEVICGINFPDACGNGELFSEFVNHFYEIKSSSTDLGQKYIAKLSLNSLYGKFGQKEREYSIRLLEKDKAKEIISKNHYSYMSEVSDNYTLIKSGGRLNSKLRRLYAEQARINTINDDLLSSKFIKSRGIPSAVQISAMISSYARTSINPFKNIPGNLAIASNTDSLILRKPLEDHLIGKEIGKWKLEHKFKNGVFVKPKLYCYEDVDINELIRKASGVTASNLTYENFVELVNGKDVLTNKELFRLNWETLNIEIVNINTKISGIKE | Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 91922
Sequence Length: 797
Subcellular Location: Mitochondrion
EC: 2.7.7.7
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P10582 | MQPARRHTKKKNMNYMRYESLTREQFERFLKDVHKCYRGEPRYVIPYEGHLIAVQDFEEPYPKAGAVTMLASAFMELLINRVYPSIQGSAKFTLQYRLNIDGNPINITLSKAIKLTYADGTRIANEFILKEIINVLNKYAENYQSCDVEAISVRAYSEGSIDLNQASIPTKDESLNYLKGALIKYSDINNLEIPKMGRRSKRRYQSYIPVDKTEMKNKTLFFVADLETLLLKRRDTDVDKTHVPYAGGYMMVDMEKWVNADHITTFYAHDYSKVCQDFHDMSEKMLTEMINRIVKDVQRRGSSMVVYFHNLSQFDGIMILSFLTKSYKNCHIEPIMRNDCIYSIKLYKVSKNGDKRLVLTFMDSYLLLKVKLADLADSFCPELGGKGSFDHQNVTVDKLPSIREDSLTYLKQDILITAAVMQRAKAIIWEEYGIDILKVLTISALALKIFRRVYYKDDDDNWIYIPDDNEAQFIREGYYGGHTDVYKPYGENLYYYDVNSLYPSSMLDDMPIGKTRWVSDLGSKKSKIVLNDMFGFIRAFIICPKHIKKPLLPYKKDDGTIIFPTGRFLGVYFSEELKYAVSLGYKVYPICGYIFDRKESPFKRFVYDIYSKRLDAKAKGEKALDFIYKITMNSLYGRFGISPESTTTQIVSTEESRKLALYNDGFVQSYELSSDKCLVTCKNVRSLDLLKLSSDRPTYAAVQISAAVTGYARIRMHPFISRDDCYYTDTDSVVVERELPEEEVSPTALGKFKHEHFVEYGIFLAPKSYMLKASSVDQPIIKFKGAGKDEADEEWFINQLADPRAKKVISYVRKFSRNFRELLVQEKMCKYTMGLESKKREYVFDKNGVWVDTKPCHIGDFDVKSINPTSYWIIMNLLEENEDLRNEFSNSEIMIANWEIKADAAKKRKASKLRGKPLRGGDTPSHIEE | Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 107533
Sequence Length: 929
Subcellular Location: Mitochondrion
EC: 2.7.7.7
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P33537 | MIKFYFTTFHMKFPARLFSTSGNRANFEENSSNEVQNQIKYLKDFKKENPKFNWESTTEPKHMILSNIGEYEKNDFNLKSLLNINEFNINVELLRQLFMKLDKNFTYALGVILRNVDSNTNISVDRHFLVNFNTDPVIILQQIYDRIIFLSEKYYLVPVDKLFIKLRKLNFKVKNPVFHPIAKEKTNIHTTIPKGKSKLSRAEFVPHTMDLKFYGVETKHDKEKNIRIFDNGKVILKVKIIKDGVYHLIDVISRDNRLLYQFEDVKHGDGLKRYWINDNMYYYYYDNTLVNVETPQKVGNIEPAKRDKTQDKKILAFDIETFQVPTGNGDSTMIAYACGFYDGKKSLTYYISDFISQREMLLACIKDMLKYDKHTVYCHNFSKFDINFIIKILVQEFVVEKIISKDLDILSIKISYKFEPKKKGGKAERHTITIADSCRLLPGSLDKLAKDHNIITKKGKFPYKFVNKDNLEYVGLLPDYEYYIDPKKGEMITLFEWAAMYTNKWSMRKETIIYLEKDIKALYQLMMEMSNNTYSTFRINITRVKTASALAFLVYRTIFLPNEVEEENETNSPNNILSLFDKKEEKKLTPKYFLPKLKGRLERAVRAAYFGGRNEIFIPIINNIFSFDFNSLYPTAMMMPMPVGIPVHTFCKNLNEIFGFVRAKIITPAINIPVLPCRVKVNGVQKLIFPIGEWTGWYFSEELKLAVEYGYKIEVLESYVFEKRDDPFKEYIEHFASIKDNTKGSKKQMAKLLLNTLYGRTGMNDSAAEIKMLTTNELDNIQLTNNVIHEFEVDDDKHYVRYDKKPCPVLCAQSEKNYELLSYLDGEKDDGFIINSTSIAAATASWSRILMYKHIINSAYTDTDSIFVEKPLDSAFIGEGCGKFKAEYNGQLIKRAIFISGKLYLLDFGGKLEIKCKGITKNKDNTTHNLDINDFEALYNGESRVLFQERWGRSLELGTVTVKYQKYNLISGYDKREKLYSLGKWVNTSPLCINENFEVISKALVSDVGESWYRKRIHYNK | Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 119076
Sequence Length: 1021
Subcellular Location: Mitochondrion
EC: 2.7.7.7
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P33538 | MSKFSFFNYRINMRNSHATLGSLPCFIKFNYLSSSSHSKFYSTSTDSPMGHIVSASKSSWYNYYSHKNYDPLTRESFHDELRGFISLYKKQFKEEKFFFMAKIKFNNNDIRSISTVQIGSTDPLEVLRLLEAITSTYMHTHTGISEAVSEPFEYELFSLGDGLPKGNIIFTFKPTSNPSIKTKYEHKSNIKRNKNINLSKKNPLNKFKYNGYTIPNTMDLSQWPNIHFINDGKNAVSLNNIIKSGVDNMTLSFFITINKKYNEITVLLNNTPIFKIKDEKIMSEDDLSSFKRTITENEQDKVYVFENGEMVFFSENVKTSFIKKITRQDLINFENPKIITLDLETRSVPIHPIKEGKDGKEGKVDSIMFPILMSVYNGKFVKSFLFSQSAWETEMMNAFKSIMLRKYDGYKVYTHNFSYFDGIFIIDILSRLGEVKPFMRNGKILKLTFNFTLPNSKRKYTLYFMDSLLILPDSLDKLSNFFNNKVKKLFFPHSFLDDNTIPINYVGKCPDYKYFPKAYTEDFTIEQYQEYANKFKNNNWDLKKELIKYCEIDTIALYQVLVSFQRKIYEKFMIDCTKYPTIPSLAFAIFRKKYLVEDMIPNIKSKLHNIIKLSYFGGICELYKPFGVNIKSYDVNSLYPFAMKYFKMPSGIPKYVKGTLQNIVRFTDSICEVPFGFYNVKVKTPLNLDKPFLPTRLNTPAGTRTAFPLGQWEGWYFSEEILNAMKHGYEFEFIEGYLFEESSMFDEYIDLLYNIKKNSPKESPWYYISKLLMNSLYGRFGLNPEGEEIFITSEEEGDAIIATKEYVTITPLSSGNVLISAKLPEEAFGDMNISVPISSAIAAYSRIHMSHFLTKYSNNIYYIDTDGIKVDIDLDKDEVDSKELGKMKYEYVFEEYTSLGPKVYGGLLYDKKGKLIELVKLRGYSSKLPYNKLKEGLVKDHTLELTQKKWKRKLSESTVYLKNTHLLFL | Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 112830
Sequence Length: 969
Subcellular Location: Mitochondrion
EC: 2.7.7.7
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A2RI77 | MAEEKVLEVKNLHVNFHTYAGDVKAIRNVSFDLEKGQTLAIVGESGSGKSVTTKTLMGLNAKNAEIPEGELLFKGRNLLDLKEEEWQKIRGNEISMIFQDPMTSLDPTMRIGKQIAEPLLKHNKGMSKADAMKRALELMQQVGIPDAEVHINDYPHQWSGGMRQRAVIAIALAADPEILIADEPTTALDVTIQAQIMHMMAELQERINSSIVFITHDLGVVAGFAHKVAVMYAGEIVEYGTVEEIFYNPQHPYTWGLLDSMPTVDSSVDRLVSIPGTPPDLLNPPKGDAFAARNKFALAIDFEEEPPYFEVSPTHFAKTWLLDPRAPKVTPSDNILARWKRWEELKGDK | Function: Part of the ABC transporter DppABCDF involved in dipeptide transport . Responsible for energy coupling to the transport system (Probable).
Catalytic Activity: a dipeptide(out) + ATP + H2O = a dipeptide(in) + ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38910
Sequence Length: 349
Subcellular Location: Cell membrane
EC: 7.4.2.9
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A0A0H2ZGN6 | MSLLDIKNLSVRFGDTTAVPVVDGLDLSVDKGEVLAIVGESGSGKSVTMMALMGLIDAPGWVSADHLRFDGHDMLTLKGRQRRRIVGKDMAMVFQDPMTALNPSYTVGYQIEEVLRLHLGLRGKALRQRALELLERVEIPAAASRLDAYPHQLSGGMSQRVAIAMAIAAEPKLLIADEPTTALDVTIQAQIMELLLNLQRDQDMALILITHDLAVVAETAQRVCVMYAGEAVEIGGVPALFDRPTHPYTEALIKAIPEHCAGEARLATLPGIVPGRYDRPRGCLLSPRCPYAQEHCRQERPALEAHERGAVRCFYPLNLLNEVA | Function: Part of the ABC transporter DppABCDF involved in the uptake of various di/tripeptides . Is also involved in the uptake of phaseolotoxin, a toxic tripeptide inhibiting the enzyme ornithine carbamoyltransferase . Responsible for energy coupling to the transport system (Probable).
Catalytic Activity: a dipeptide(out) + ATP + H2O = a dipeptide(in) + ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 35399
Sequence Length: 324
Subcellular Location: Cell inner membrane
EC: 7.4.2.9
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P26906 | MKRVKKLWGMGLALGLSFALMGCTANEQAGKEGSHDKAKTSGEKVLYVNNENEPTSFDPPIGFNNVSWQPLNNIMEGLTRLGKDHEPEPAMAEKWSVSKDNKTYTFTIRENAKWTNGDPVTAGDFEYAWKRMLDPKKGASSAFLGYFIEGGEAYNSGKGKKDDVKVTAKDDRTLEVTLEAPQKYFLSVVSNPAYFPVNEKVDKDNPKWFAESDTFVGNGPFKLTEWKHDDSITMEKSDTYWDKDTVKLDKVKWAMVSDRNTDYQMFQSGELDTAYVPAELSDQLLDQDNVNIVDQAGLYFYRFNVNMEPFQNENIRKAFAMAVDQEEIVKYVTKNNEKPAHAFVSPGFTQPDGKDFREAGGDLIKPNESKAKQLLEKGMKEENYNKLPAITLTYSTKPEHKKIAEAIQQKLKNSLGVDVKLANMEWNVFLEDQKALKFQFSQSSFLPDYADPISFLEAFQTGNSMNRTGWANKEYDQLIKQAKNEADEKTRFSLMHQAEELLINEAPIIPVYFYNQVHLQNEQVKGIVRHPVGYIDLKWADKN | Function: Probably part of the ABC transporter DppBCDE involved in dipeptide transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 61819
Sequence Length: 543
Subcellular Location: Cell membrane
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P37313 | MSTQEATLQQPLLQAIDLKKHYPVKKGMFAPERLVKALDGVSFNLERGKTLAVVGESGCGKSTLGRLLTMIEMPTGGELYYQGQDLLKHDPQAQKLRRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSKEQRREKALSMMAKVGLKTEHYDRYPHMFSGGQRQRIAIARGLMLDPDVVIADEPVSALDVSVRAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKDQIFNNPRHPYTQALLSATPRLNPDDRRERIKLSGELPSPLNPPPGCAFNARCRRRFGPCTQLQPQLKDYGGQLVACFAVDQDENPQR | Function: Part of the ABC transporter DppABCDF involved in dipeptide transport . Responsible for energy coupling to the transport system (Probable).
Catalytic Activity: a dipeptide(out) + ATP + H2O = a dipeptide(in) + ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37560
Sequence Length: 334
Subcellular Location: Cell inner membrane
EC: 7.4.2.9
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A2RI78 | MTEPKKVVEIKNLDLTFNKGKKGANKAINNVSLDIYEGETFGLVGESGSGKTTIGRAILKLYDNFITGGEILFEGKDVRNLKGSELREYRSEAQMIFQDPQASLNGRMRVKDIVAEGLDANGLVKTKAERDARVLELLRLVGLNDDHLTRYPHEFSGGQRQRIGIARALAVKPKFVVADEPISALDVSIQAQVVNLMRDIQAKENLTYLFIAHDLSMVKYISDRIGVMHWGKILEVGTSEQVYNHPIHPYTKSLLSSIPSPDPISERQRTPIVYDPTAELDGQEREMREITPGHFVFSTEAEAEVYKKNATL | Function: Part of the ABC transporter DppABCDF involved in dipeptide transport . Responsible for energy coupling to the transport system (Probable).
Catalytic Activity: a dipeptide(out) + ATP + H2O = a dipeptide(in) + ADP + H(+) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34883
Sequence Length: 312
Subcellular Location: Cell membrane
EC: 7.4.2.9
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Q8NLQ9 | MSEHAAEHHRDTQNFLTSEPHTTAIEDNKKRQPPKNLADGMIKALRPKQWVKNVLVLAAPLAAGADAIFNQRTIIDVAIAFVVFCFGASAIYLVNDARDVEADREHPTKRFRPIAAGVLPVGMAYGMAVALIALSIGLSFLATDGVALACVIGVYIALQLGYCFGWKHMPVIDIALVSSGFMLRAMAGGVAAGIELSQWFLLVAAFGSLFMASGKRYAEILLHERTGAKIRKSLESYTPTYLRFVWTMAATAVVMSYALWGFDLSQHSTDAGPWYQISMVPFTIAILRYAAGVDTGDGGAPDEVALSDKVLQVLALAWVFCIVMAVYIMPMF | Cofactor: Divalent metal cations such as Mg(2+), Mn(2+) or Ca(2+).
Function: Involved in the biosynthesis of decaprenylphosphoryl arabinose (DPA) a precursor for arabinan synthesis in mycobacterial cell wall biosynthesis. Catalyzes the transfer of a 5-phosphoribosyl residue from phosphoribose diphosphate (pRpp) to decaprenyl phosphate (DP) to form decaprenylphosphoryl-5-phosphoribose (DPPR).
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + H(+) + trans,octa-cis-decaprenyl phosphate = diphosphate + trans,octa-cis-decaprenylphospho-beta-D-ribofuranose 5-phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36054
Sequence Length: 332
Pathway: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
Subcellular Location: Membrane
EC: 2.4.2.45
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A0R626 | MDATHMSEEAQPTAGPPKNLVSGLIKAVRPRQWIKNLLVLAAPLAAVGSGIEYDYADVAAKVSVAFVVFCLAASSIYLINDARDVEADRAHPTKRFRPIAAGVVPEWMAYSLAGLLAVASLVISWWLTANLAIVMAVYIAVQLAYCFGLKHQAVLDICIVSSGFLIRAIAGGVAADIPLSQWFLLVMAFGSLFMAAGKRYAELQLAERTGAKIRKSLESYTSSYLRFVWTLSATAMVVCYGLWAFSRDRANDLMTLDAQDASWYAVTMIPFTIAILRYAVDIDGGIAGEPEEIALKDRVLQILFLAWIGTIGAAIYFS | Cofactor: Divalent metal cations such as Mg(2+), Mn(2+) or Ca(2+).
Function: Involved in the biosynthesis of decaprenylphosphoryl arabinose (DPA) a precursor for arabinan synthesis in mycobacterial cell wall biosynthesis. Catalyzes the transfer of a 5-phosphoribosyl residue from phosphoribose diphosphate (pRpp) to decaprenyl phosphate (DP) to form decaprenylphosphoryl-5-phosphoribose (DPPR).
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + H(+) + trans,octa-cis-decaprenyl phosphate = diphosphate + trans,octa-cis-decaprenylphospho-beta-D-ribofuranose 5-phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34527
Sequence Length: 318
Pathway: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
Subcellular Location: Membrane
EC: 2.4.2.45
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Q95WU5 | MTLSAWIILVTLAMASVLTPEDNVRLRRLTAYVANADASIVLLTYTEYEEGTNHGNSMLWRINDPLEAEYPFDPDDISLLNAERVCPELVGVGDLQYSTHNQAFYFTAQGPDGTSQVYSYNHKLETCTQISFLPISVSNLKVSPKGNSVLFSAEIFVYPNNHASVDDPLNFAHDEFARIQARPYKAFAYEQLYTRHWDEDILPSQYRHLFAARLERSSEYDDDYVRITVDNSIDLMPRFDGDCPMRPFADASSYTFDSHGRYVAFVTQVGSTAAFYTNDSIWITDLQQFLDAKKPVRDVVLPLRCATCWNKARDQRPAFSYDGIFLYYASMDEEQSESDLLRLRKQNVSDLFEYDCDSLFCGPVTGEGVFNLTAGVFDRSIGQFIIPTDSTEDSIYILAEDHARTNLFRYNEESSTVTRLTYNGTLGSLLYLRHNKIFLATMSSYTRPTDLVMLDLTVATEFTATRDPSDTMKDDLIKISYLTDLNRQRLRHIDELQEPEEFYLPSKSFPDQYVHSWYFAPANLRDSHEYPLILYVHGGPESPWANSWSYRWNPQLIAARGYGVLATNFHGSSSFGEVFQKSVRGNWYSYPLEDIMDAWSNIYTHADKAYLSREKVCAMGASFGATFMNYMNSHVNNVTCYVTHDGVFDTMCNALETDELFFPVRELGGFLLDEQVDNQQLYEKWNPARFVENMSAPMLVIHGQKDYRIQVYHGISLFQALRLRGIKTKLVYFPTQSHWVWQPQESLFWHTQVFDWLDTYL | Function: May be involved in metabolism of dipeptides or may affect host defense mechanisms.
Sequence Mass (Da): 87648
Sequence Length: 761
Subcellular Location: Membrane
EC: 3.4.14.-
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Q8DPI7 | MKITNYEIYKLKKSGLTNQQILKVLEYGENVDQELLLGDIADISGCRNPAVFMERYFQIDDAHLSKEFQKFPSFSILDDCYPWDLSEIYDAPVLLFYKGNLDLLKFPKVAVVGSRACSKQGAKSVEKVIQGLENELVIVSGLAKGIDTAAHMAALQNGGKTIAVIGTGLDVFYPKANKRLQDYIGNDHLVLSEYGPGEQPLKFHFPARNRIIAGLCRGVIVAEAKMRSGSLITCERAMEEGRDVFAIPGSILDGLSDGCHHLIQEGAKLVTSGQDVLAEFEF | Function: Protein that helps load RecA onto ssDNA during transformation . Required for DNA transformation . Not required for DNA uptake but for a later stage of transformation . Thought to interact at the cell pole with newly imported transforming ssDNA which it binds cooperatively, protecting linear and circular ssDNA from nuclease action . Forms bridges between DNA segments . Favors the loading of RecA onto ssDNA and formation of RecA-DNA filaments, triggering RecA-catalysis of ATP-driven homologous DNA pairing .
Sequence Mass (Da): 31063
Sequence Length: 282
Domain: The regions responsible for dimerization and for DprA-RecA interaction partially overlap, it is suggested that when RecA interacts with the DprA-ssDNA NPC it rearranges or disrupts the DprA dimer, leading to nucleation of RecA on ssDNA .
Subcellular Location: Cytoplasm
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A0R607 | MSTTEFPTTTKRLMGWGRTAPTVASVLSTSDPEVIVRAVTRAAEEGGRGVIARGLGRSYGDNAQNGGGLVIDMPALNRIHSIDSGTRLVDVDAGVSLDQLMKAALPHGLWVPVLPGTRQVTVGGAIGCDIHGKNHHSAGSFGNHVRSMELLTANGEVRHLTPAGPDSDLFWATVGGNGLTGIILRATIEMTPTETAYFIADGDVTGSLDETIAFHSDGSEANYTYSSAWFDAISKPPKLGRAAISRGSLAKLDQLPSKLQKDPLKFDAPQLLTLPDIFPNGLANKFTFMPIGELWYRKSGTYRNKVQNLTQFYHPLDMFGEWNRAYGSAGFLQYQFVVPTEAVEEFKSIIVDIQRSGHYSFLNVFKLFGPGNQAPLSFPIPGWNVCVDFPIKAGLHEFVTELDRRVLEFGGRLYTAKDSRTTAETFHAMYPRIDEWIRIRRSVDPDGVFASDMARRLQLL | Function: Component of the DprE1-DprE2 complex that catalyzes the 2-step epimerization of decaprenyl-phospho-ribose (DPR) to decaprenyl-phospho-arabinose (DPA), a key precursor that serves as the arabinose donor required for the synthesis of cell-wall arabinans . DprE1 catalyzes the first step of epimerization, namely FAD-dependent oxidation of the C2' hydroxyl of DPR to yield the keto intermediate decaprenyl-phospho-2'-keto-D-arabinose (DPX) . The intermediate DPX is then transferred to DprE2 subunit of the epimerase complex, most probably through a 'substrate channel' at the interface of DprE1-DprE2 complex (By similarity). Can also use farnesyl-phosphoryl-beta-D-ribofuranose (FPR) as substrate in vitro . Appears to be essential for the growth of M.smegmatis .
Catalytic Activity: FAD + H(+) + trans,octa-cis-decaprenylphospho-beta-D-ribofuranose = FADH2 + trans,octa-cis-decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose
Sequence Mass (Da): 50377
Sequence Length: 460
Pathway: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
Subcellular Location: Periplasm
EC: 1.1.98.3
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Q8NEX9 | MAALTDLSFMYRWFKNCNLVGNLSEKYVFITGCDSGFGNLLAKQLVDRGMQVLAACFTEEGSQKLQRDTSYRLQTTLLDVTKSESIKAAAQWVRDKVGEQGLWALVNNAGVGLPSGPNEWLTKDDFVKVINVNLVGLIEVTLHMLPMVKRARGRVVNMSSSGGRVAVIGGGYCVSKFGVEAFSDSIRRELYYFGVKVCIIEPGNYRTAILGKENLESRMRKLWERLPQETRDSYGEDYFRIYTDKLKNIMQVAEPRVRDVINSMEHAIVSRSPRIRYNPGLDAKLLYIPLAKLPTPVTDFILSRYLPRPADSV | Function: Displays weak conversion of all-trans-retinal to all-trans-retinol in the presence of NADH. Has apparently no steroid dehydrogenase activity.
Sequence Mass (Da): 35263
Sequence Length: 313
Subcellular Location: Cytoplasm
EC: 1.1.1.-
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P42291 | MENFSIFNVTVNVWHADLDVGNSDLSLRALTGLLLSLLILSTLLGNTLVCLAVIKFRHLRSKVTNFFVISLAVSDLFVALLVMPWKAVTEVAGFWVFGDFCDTWVAFDIMCSTASILNLCIISLDRYWAIASPFRYERKMTQRVAFIMIGVAWTLSILISFIPVQLSWHKSHEADEELNGVNHTENCDSSLNRTYAISSSLISFYIPVVIMIGTYTRIYRIAQTQIRRISSLERAVEHAQRCSSRLSNENSLKTSFRKETKVLKTLSIIMGVFVFCWLPFFVLNCMIPFCHMNLPGQNEPEPPCVSETTFNIFVWFGWANSSLNPVIYAFNADFRKAFTTILGCNRFCSSNNVEAVNFSNELVSYHHDTTFQKDIPVTFNNSHLPNVVDQDQEVLEGTCFDKVSVLSTSHGTRSQKNLHLPAGVQFECEAEITLETITPFTSTGPLECLPQLVADEDRHYTTKLY | Function: This is one of the five types (D1 to D5) of receptors for dopamine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52641
Sequence Length: 465
Subcellular Location: Cell membrane
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P35406 | MAVLDLNLTTVIDSGFMESDRSVRVLTGCFLSVLILSTLLGNTLVCAAVTKFRHLRSKVTNFFVISLAVSDLLVAVLVMPWKAVTEVAGFWPFGAFCDIWVAFDIMCSTASILNLCVISVDRYWAISSPFRYERKMTPRVAFVMISGAWTLSVLISFIPVQLKWHKAQPIGFLEVNASRRDLPTDNCDSSLNRTYAISSSLISFYIPVAIMIVTYTQIYRIAQKQIRRISALERAAESAQIRHDSMGSGSNMDLESSFKLSFKRETKVLKTLSVIMGVFVCCWLPFFILNCMVPFCKRTSNGLPCISPTTFDVFVWFGWANSSLNPIIYAFNADFRRAFAILLGCQRLCPGSISMETPSLNKN | Function: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase. Could be involved in growth hormone release.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40652
Sequence Length: 363
Subcellular Location: Cell membrane
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P21728 | MRTLNTSAMDGTGLVVERDFSVRILTACFLSLLILSTLLGNTLVCAAVIRFRHLRSKVTNFFVISLAVSDLLVAVLVMPWKAVAEIAGFWPFGSFCNIWVAFDIMCSTASILNLCVISVDRYWAISSPFRYERKMTPKAAFILISVAWTLSVLISFIPVQLSWHKAKPTSPSDGNATSLAETIDNCDSSLSRTYAISSSVISFYIPVAIMIVTYTRIYRIAQKQIRRIAALERAAVHAKNCQTTTGNGKPVECSQPESSFKMSFKRETKVLKTLSVIMGVFVCCWLPFFILNCILPFCGSGETQPFCIDSNTFDVFVWFGWANSSLNPIIYAFNADFRKAFSTLLGCYRLCPATNNAIETVSINNNGAAMFSSHHEPRGSISKECNLVYLIPHAVGSSEDLKKEEAAGIARPLEKLSPALSVILDYDTDVSLEKIQPITQNGQHPT | Function: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49293
Sequence Length: 446
Subcellular Location: Cell membrane
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O02664 | NTLLVCAAVIRFRHLRSKVTNFFVISLAVSDLLVAVLVMPWKAVAEIAGFWPFGSFCNIWVAFDIMCSTASILNLCVISVDRYWAISSPFRYERKMTPKAAFILIGVAWTLSVLISFIPVQLSWHKAKPTSPPDGNATSLDETVDNCDSSLSRTYSISSSLVNFYNPVAIMXVTYTRIHR | Function: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20114
Sequence Length: 180
Subcellular Location: Cell membrane
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P18901 | MAPNTSTMDEAGLPAERDFSFRILTACFLSLLILSTLLGNTLVCAAVIRFRHLRSKVTNFFVISLAVSDLLVAVLVMPWKAVAEIAGFWPLGPFCNIWVAFDIMCSTASILNLCVISVDRYWAISSPFQYERKMTPKAAFILISVAWTLSVLISFIPVQLSWHKAKPTWPLDGNFTSLEDTEDDNCDTRLSRTYAISSSLISFYIPVAIMIVTYTSIYRIAQKQIRRISALERAAVHAKNCQTTAGNGNPVECAQSESSFKMSFKRETKVLKTLSVIMGVFVCCWLPFFISNCMVPFCGSEETQPFCIDSITFDVFVWFGWANSSLNPIIYAFNADFQKAFSTLLGCYRLCPTTNNAIETVSINNNGAVVFSSHHEPRGSISKDCNLVYLIPHAVGSSEDLKKEEAGGIAKPLEKLSPALSVILDYDTDVSLEKIQPVTHSGQHST | Function: Dopamine receptor whose activity is mediated by G proteins which activate adenylyl cyclase.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49428
Sequence Length: 446
Subcellular Location: Cell membrane
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P24628 | MDPQNLSMYNDDINNGTNGTAVDQKPHYNYYAMLLTLLVFVIVFGNVLVCIAVSREKALQTTTNYLIVSLAVADLLVATLVMPWAVYMEVVGEWRFSRIHCDIFVTLDVMMCTASILNLCAISIDRYTAVAMPMLYNTRYSSKRRVTVMISVVWVLSFAISCPLLFGLNNTGSKVCIIDNPAFVIYSSIVSFYVPFIVTLLVYVQIYIVLRKRRKRVNTKRNSRGVAVDAHKDKCTHPEDVKLCSVFVKSNGSFPADKKKVILVQEAGKHPEDMEMEMMSSTSPPEKTKHKSASPDHNQLAVPATSNQCKNASLTSPVESPYKAEKNGHPKDSTKPAKVFEIQSMPNGKTRTSIKTMSKKKLSQHKEKKATQMLAIVLGVFIICWLPFFIIHILNMHCNCNIPQALYSAFTWLGYVNSAVNPIIYTTFNVEFRKAFIKILHC | Function: This is one of the five types (D1 to D5) of receptors for dopamine. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. In Xenopus D2R is involved in the regulation of the melanotrope cells of the intermediate pituitary during background adaptation of the animal.
PTM: Palmitoylated. Palmitoylation is probably required for proper localization to the plasma membrane and stability of the receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49738
Sequence Length: 442
Subcellular Location: Cell membrane
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Q8IS44 | MLSPFDWRRGISSSGTGGTMAAQPLSSTAATTAAATGATAATAATAATTSATLSTAAASTSTTAAPSAGATWINHHLAVEADSSQPANGSDAQAGVEGPTMPAGYLPLYEDVETAAEDAGYALIDDISEWLLGSVGSEAAVGGPENSTNLAVTGANGTLAWLEALNSTQPAQSNSSAEDGERGRYSLRSFVEQQLAGGGAAGAGDGGDAGIALIDSGEEAALDNVADAETDYGMLGGFGDAELLQRTATVARETLGNRTAPSTTSYDGGGSGDVGVAGGLAGTAGGGVGGAGGSGGSTFMLLLENFNDYFPNYNGSTVSGTSTIAPGVAITGSRGSGLLLEQNLTGLYLDGYRLNCTNETLNLTDSCGELRVVDHNYWALILILFPILTLFGNILVILSVCRERSLQTVTNYFIVSLAIADLLVAVVVMPFAVYFLVNGAWALPDVVCDFYIAMDVICSTSSIFNLVAISIDRYIAVTQPIKYAKHKNSRRVCLTILLVWAISAAIGSPIVLGLNNTPNREPDVCAFYNADFILYSSLSSFYIPCIIMVFLYWNIFKALRSRARKQRAARKPHLSELTGGSVIENIAQTRRLAETALDSSRHASRILPDEAATNTASGSNEEEDENAISPDIDDCHVIVNDKSTEFMLATVVEETGNSVVAQITTQPQLVVADPNGNHDSGYAASNVDDVLAGVAPASASAATSAAPRSSGSPPDSPLPSGATLQRSSVSSQRRPTGDDSPKRGEPALRSVGVDNSSVAMKPLSFVRYGVQEAMTLARNDSTLSTTSKTSSRKDKKNSQASRFTIYKVHKASKKKREKSSAKKERKATKTLAIVLGVFLFCWLPFFSCNIMDAMCAKFKKDCRPGLTAYMMTTWLGYINSFVNPVIYTIFNPEFRKAFKKIMHMG | Function: Receptor for dopamine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 95057
Sequence Length: 905
Subcellular Location: Cell membrane
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C5M444 | MTSNILLLLHPTVVTDQHIVENIKLKISNTHKDFHLSQTTIDRLTQGSIEFDNNSFDEIIYINPNEEQYREIPNSLMKLIFDLLKLNGKFTGDLPTDQNLDVLMNGFLIINQNEWNKPQPEETVVTLKKKSTTTNNNSNTSTIKKSFPMFKKLNNDNASTPGLTDSSAGTSEDETATVSNKRKLVESKLVYFSDDDDDDDYDGSSDGEDLINENDLIAESNKYKIIVPKKCELPNGKKRKKACKDCTCGLKELEEEEIKSQGKLQDTVLANMAQSATIEAIKIEERMKKNKIKFTEEDLSEIDFTVAGKTGGCGSCSLGDAFRCDGCPFLGLPPFKPGEVVRID | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2.
Sequence Mass (Da): 38463
Sequence Length: 344
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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A8NWK4 | MAPTAVYTQKDSPSSSQPSSKGPALAIGSLETAQDGKYQSLITELEATRQVDKLLLDRLVDGATTLEPSKYNSVHVTLASSDYQSLQESTLRSLLTQLLTGLTPLGTLHLLNLTDGLKTLPSELTLSGFLVLSAAGENPGDSIVAQKPAHAIGASVSLKKRGSATTTSTTAFVTTTTTTSTSTTTATVTSAPSVPLLLRKRGDPAKKKALWALTTDASASPSTKIDADALLTAEDKARPVPTCAPVDRSAPRRKKACKNCSCGLAELEEEEKRNAPVVVIDSSIDGEGGAKAVDKAERERLLEAAKNAPKATSSCGSCFLGDAFRCAGCPYLGLPAFKPGEKVEIDFGMDDF | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2.
Sequence Mass (Da): 36803
Sequence Length: 352
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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P0CM12 | MPAPVPPTAFAQPSGPATQLVLGSMQRAPEYQALLTSLKSAAPPSSSVQGEMVDRILDNATTLPPPPLTIHLVLPLPLPSNLLSAIPPSTQIFIHIPADSESQLGALHSALASHSFTPVLPTPSPSTLAYTSPSAPSLPAVASEPSPAPSSSTPVTLSGARPLQLRRNGDKARKAALWAIDSPLIPDGGKSLLTPADRTRPDCVFPAENGKPVKRRRACKDCTCGLKELEQEEEAQTSAAVQEAQKAFFLEGDDDIPENLKKATEGMEGIWPADKRAEAKKTSSCGSCYLGDAFRCSSCPYLGLPPFKPGEQVQVSIGDDI | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the scaffold complex CFD1-NBP35. Electrons are transferred to DRE2 from NADPH via the FAD- and FMN-containing protein TAH18. TAH18-DRE2 are also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit RNR2.
Sequence Mass (Da): 33768
Sequence Length: 321
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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Q5CWQ7 | MTQLIITHQSDSKLEESEVFLSELNRIKKEEDKFGKFSSLSDLRAIVKKGEFRIVSIYLSSGSILGEIFTFEFLKEFYGVLDFGSVLKVNILALDSIDKVKAFERNLLFSGFIKVKKLKGDGLNSSDSDFEIVIKAEKPSWKPEEGKVLVDDIDLEGSVPDIKNYVPLGQGKESCKSKERACNNCNCGRADLEKEIGVEAARKVYQEKVETGTARSSCGNCYLGDAFRCSGCPYKGMPAFKPGEKVSLANAEGDANDHTVDMNLIHEEKVDLITTTFDDDGSGVNNVQSKGGVLKLNI | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Sequence Mass (Da): 32851
Sequence Length: 298
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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B0WQ75 | MNFVQENNQVLYIWGGTISADIEQEVNQLKSIPGVKVNVENAERVLLGGYGQSQFDIILANVSTGNSELVSHLLKLTKPKGKAVFKDDSAAGGAETVRANLLLSGFINIASAEGNVYIAEKPNYEIGSAAKLSLGGGANKAKVAAVWKLDVDDDGEAEERIDEDELLDEEDKVKPSAESLRVCGTTGKRKACKDCSCGLAEELDAESKGAAVAAAQSAKSSCGSCYLGDAFRCATCPYLGMPAFKPGEKIQLSDTQMQADV | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Sequence Mass (Da): 27574
Sequence Length: 261
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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O15692 | MNSLSLELNKEQEVLIISDVENSESIINQVKELSKTVTTSLSKEQQQIQNNFDHVIIISSKPFNSALISMYSNLLKKGGKLSIYQTNENETLVNSGMDFLIGGLVDFKATSNSTYKTIVHADKPSWDTNESSTINIPSTSSNNPWASIEGGDRINENDLVSENDKTSKPATTLDDCEVGKTKKACKNCTCGRAEEENQSKPKLTKEMIENPGVGSSCGNCSLGDAFRCGGCPYRGLPTFKVGEKIQLPDDFLVDDI | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Sequence Mass (Da): 27987
Sequence Length: 256
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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Q9V3Y2 | MENFKGLQKSLYIWTDSADLDKRVEQLKAATGGDVALENVHRLSFSSYANSSFDLIVIECAQLTDSYVKLLHMLKPSGKLHLVSYIGPAASLLQEIKLSGFINCREDSPDALTAEKPGYETGSSARLSFAKKNASAVNVWKISGDDEELIDEEELLDEEDKQKPDPAGLRVCSTTGKRKACKNCSCGLAEELETEKQSQKATENAKSSCGNCYLGDAFRCSTCPYLGMPAFKPGEKVQLADNLLKSDI | Function: Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Sequence Mass (Da): 27105
Sequence Length: 248
Domain: The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation.
Subcellular Location: Cytoplasm
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Q10SU5 | MVDWASDSDNDKFEWDTDGEAETSSAPALRNIDAPGPSTRLPQDANGKANGSGALVAEFMGMGFPKEMILKAIKEIGDTDTEQLLELLLTYQAIGGDASVGNCSASACAPQTLEVDEEEDDTNWDEYDTAGNCDRTPHSDGSGDEDFFQEMSEKDEKMKSLVNMGFPEDEAKMAIDRCGLDAPVAVLVDSIYASQEAGNGYSANLSDYEDTEFSSFGGRKKTRFVDGSKKRKRYGSGPSGNQVPFDGSHEEPMPLPNPMVGFSLPNERLRSVHRNLPDQALGPPFFYYENVALAPKGVWTTISRFLYDIQPEFVDSKYFCAAARKRGYIHNLPIENRSPVLPMPPKTISEAFPNTKRWWPSWDPRRQFNCLQTCMASAKLTERIRCALGRFSDVPTPQVQKYVLDECRKWNLVWVGKNKVAPLEPDEMEFLLGYPRNHTRGVSRTERYRALGNSFQVDTVAYHLSVLRDLFPNGMNVLSLFSGIGGAEVALHRLGIHMKTVISVEKSEVNRTILKSWWDQTQTGTLIEIADVRHLTTERIETFIRRFGGFDLVIGGSPCNNLAGSNRHHRDGLEGEHSALFYDYIRILEHVKATMSAV | Function: Involved in de novo DNA methylation. Required for CpG and non-CpG methylation. Required for normal establishment and maintenance of RNA-directed DNA methylation (RdDM) mediated by small interfering RNAs (siRNAs). Regulates proper plant development in both vegetative and reproductive stages through DNA methylation.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 66788
Sequence Length: 598
Subcellular Location: Nucleus
EC: 2.1.1.37
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P0DW07 | MRNVTRSHMVLHQIQSVLKKYEEVSAQELYESLDKGTVQREFGVRSVDLSRLSVSEEQFSELLLLFKLYSDQQQQSSIEFVATVPSEVDVRLRKTIAVIREMIHGAQNTILVTGYAVSEYVDEIMERVLEKALAGVNVDIFLDRNPQTDRYIENIRGRNLPSNFNVYVYKGSQGYSSLHAKVIMVDEEKAFVSSANLSYNGIVNNIEIGTLVGGEKILVIKNVLLELVKNNYFEKIIWYA | Function: Component of antiviral defense system DISARM (defense island system associated with restriction-modification), composed of DrmE, DrmA, DrmB, DrmC and DrmMII. DISARM is probably a multi-gene restriction module, this subunit is probably a phospholipase or nuclease. Expression of DISARM in B.subtilis (strain BEST7003) confers resistance to phages Nf, phi29, phi105, phi3T, SPO1, SPR and SPP1. Protection is over 10(7)-fold against phi3T, 10(4)-10(5)-fold against Nf, phi29, phi105 and SPR, 100-fold against SPO1 and 10-fold against SPP1. DISARM does not interfere with phage adsorption, but instead interferes with (phi3T) DNA replication early in its cycle, preventing replication, circularization and lysogeny and probably causes phage DNA degradation (DNA is degraded in SPP1-infected cells).
Sequence Mass (Da): 27389
Sequence Length: 240
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q9VQS6 | MFAVMRIDNDDCRSDFRRKMRPKCEFICKYCQRRFTKPYNLMIHERTHKSPEITYSCEVCGKYFKQRDNLRQHRCSQCVWR | Function: Putative transcription factor. May function redundantly with odd and sob in leg joint formation during the larval stages, acting downstream of Notch activation. Acts in a hierarchy during foregut and hindgut patterning and morphogenesis, antagonizing lin to relieve the repressive effect on bowl. Involved in cell rearrangement during elongation of the embryonic hindgut. Regulates expression of hindgut patterning genes to establish the small intestine region of the embryonic hindgut. Required in the foregut for spatially localized gene expression and morphogenesis of the proventriculus.
Sequence Mass (Da): 10120
Sequence Length: 81
Domain: The C2H2-type domain 1 is essential for binding to and repressing lin, while the C2H2-type domain 2 contributes to lin binding.
Subcellular Location: Nucleus
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P26295 | MSKKLRNFLVRIIVAAFASFAVMAIPPYHHNTVLAKTVSVNQTYGEYKDYYTVIGESNIDQSAFPKIYKTTERVYKGQGTSEKRVTVSDVVYNPLDGYKRSTGAYGVVTKDMIDMSKGYREKWETNPEPSGWFRFYNRADNEEISEKEYDSRRTKSYKVTNNVPVVLTTLKGKKYNSHLFVASHLFADSLGGKSIRKNAITGTQMQNVGTRKGGMQYIEKKVLSHITKNPDVYVFYSAIPEYQGAELLARSVLVSALSSDGVINETVRVFNTADGFNINYEKGGLLTESPVSEIDNIEDSTTDEIENSVDDSEEIVYNDTTTEEEEN | Function: May have a role in S.equisimilis virulence.
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.
Sequence Mass (Da): 36844
Sequence Length: 327
EC: 3.1.21.1
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Q44064 | MSRPSRVLGLPLLSLGLTLLVSTPLQAQEAQTFRAVKQDLVKLYQSHPSTFYCGCNIKFSGKKMAPDWESCGYLPRKQANRAARIEWEHVVPAWEFGHQLQCWQEGGRKNCGKSAEFNKMEGDMHNLFPAIGEVNGDRANYRFSDWNGKPNQYGKCQMLVDFKEQRVQPPKGPVRGQIARAYLYMGEQYGLRLAAQQRKLFEAWDRQYPADRWECERNRRIGKLQGNTNPFIEKQCQ | Function: Endonuclease which is capable of degrading plasmid DNA.
Sequence Mass (Da): 27377
Sequence Length: 237
Subcellular Location: Periplasm
EC: 3.1.21.-
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Q566S6 | MERALGVGIGPLAAGTVGLLILLKVIQRLRRRPNIQDKVVVITGASSGLGKECARVFHAAGARLILCGRDQRRLQEVVEELGNKTYGKTKTYTPCTVTFDLSNTSVVCSAAAEILKRHGHVDVLINIAGVSYRGNILDTHVSVQREVMETNYFGPVALTQAILPSMVDRGSGHIVVISSVQGKISIPYRSAYAASKHAMQAYYDCLRAEVDSLGLHVSVLSPGYVRTNMSINAVTGDGSKYGVMDRTTATGADPVDVAKDILKAVCQKKKDVVMAGLGPTTAIYLRTLWPALYFRVMASRARKQTGKEE | Function: Putative oxidoreductase.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 33348
Sequence Length: 309
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.-.-
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Q6IAN0 | MVSPATRKSLPKVKAMDFITSTAILPLLFGCLGVFGLFRLLQWVRGKAYLRNAVVVITGATSGLGKECAKVFYAAGAKLVLCGRNGGALEELIRELTASHATKVQTHKPYLVTFDLTDSGAIVAAAAEILQCFGYVDILVNNAGISYRGTIMDTTVDVDKRVMETNYFGPVALTKALLPSMIKRRQGHIVAISSIQGKMSIPFRSAYAASKHATQAFFDCLRAEMEQYEIEVTVISPGYIHTNLSVNAITADGSRYGVMDTTTAQGRSPVEVAQDVLAAVGKKKKDVILADLLPSLAVYLRTLAPGLFFSLMASRARKERKSKNS | Function: Putative oxidoreductase.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 35119
Sequence Length: 325
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.-.-
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Q99J47 | MISPSFRKGMLKERVMDLASQTTILPLLFGCLGIFSLFRLLQRIRSKAYLRNAVVVVTGATSGLGRECAKVFHAAGAKLVLCGRNVKALEELSRELAGSSQGQTHQPFVVTFDLADPGTIAAAAAEILQCFGYVDVLINNAGISYRGTISDTIVDVDRKVMEINYFGPVALTKALLPSMVERKQGHIVAISSIQGKISIPFRSAYSASKHATQAFFDCLRAEMEEANIKVTVISPGYIHTNLSVNAVTADGSRYGALDKNTAQGRSAAEVAQDVFDAVGKKKKDVLLTDFVPSMAVYIRTLAPGLFFRIMASRARKERKSKSS | Function: Putative oxidoreductase.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34987
Sequence Length: 323
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.-.-
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Q0IH28 | MDLTSWAIFPLLLASIGVYGLYKLLQKLRSGAYLQAAVVVITGATSGLGKECAKVFYAAGSHLVLCGRDEERLKDLVQELNNMRLKSTQLHKPHMVIFDLSDVEAVNTAAKEILHLAGRVDILINNAGISYRGTILDTKVSVDRMVMDTNYFGPVALTKALLPSMIKNRRGHVVVISSVQGKISIPFRSAYSASKHATQAFFDCLRAEMSPYDIDVTVVNPGYIKTNLSLNAVTGDGSGYGVMDKNTADGRTPEEVAQTVLRAVGERRKELLVAGLVPTLAVYLRTLAPTLFFSIMSARAKKRTKAKGFITNSNLKAKITVCI | Function: Putative oxidoreductase.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 35153
Sequence Length: 323
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.-.-
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Q8CHS7 | MGLMAVLMLPLLLLGISGLLFIYQEASRLWSKSAVQNKVVVITDAISGLGKECARVFHAGGARLVLCGKNWEGLESLYATLTSVADPSKTFTPKLVLLDLSDISCVQDVAKEVLDCYGCVDILINNASVKVKGPAHKISLELDKKIMDANYFGPITLTKVLLPNMISRRTGQIVLVNNIQAKFGIPFRTAYAASKHAVMGFFDCLRAEVEEYDVVVSTVSPTFIRSYRASPEQRNWETSICKFFCRKLAYGVHPVEVAEEVMRTVRRKKQEVFMANPVPKAAVFIRTFFPEFFFAVVACGVKEKLNVPEEG | Function: NADH-dependent oxidoreductase which catalyzes the oxidation of all-trans-retinol to all-trans-retinal . Plays a role in the regulation of cardiac and skeletal muscle metabolic functions (Probable). Maintains Ca(2+) intracellular homeostasis by repressing Ca(2+) release from the sarcoplasmic reticulum (SR) in myotubes, possibly through local alternations in NAD/NADH or retinol/retinal . Also plays a role in Ca(2+) homeostasis by controlling Ca(2+) overload in the cytosol and the SR in myotubes . Involved in glucose uptake into skeletal muscles and muscle performance by activating PI3K and mTORC2-mediated AKT1 phosphorylation signaling pathways, possibly through the action of its downstream catalytic product all-trans-retinoic acid .
Catalytic Activity: all-trans-retinol + NAD(+) = all-trans-retinal + H(+) + NADH
Sequence Mass (Da): 34468
Sequence Length: 311
Domain: The N-terminus region encompasses a short hydrophobic sequence bound to the sarcoplasmic reticulum membrane, whereas the C-terminus catalytic domain faces the myoplasm.
Subcellular Location: Sarcoplasmic reticulum membrane
EC: 1.1.1.105
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P36655 | MAQRIFTLILLLCSTSVFAGLFDAPGRSQFVPADQAFAFDFQQNQHDLNLTWQIKDGYYLYRKQIRITPEHAKIADVQLPQGVWHEDEFYGKSEIYRDRLTLPVTINQASAGATLTVTYQGCADAGFCYPPETKTVPLSEVVANNAAPQPVSVPQQEQPTAQLPFSALWALLIGIGIAFTPCVLPMYPLISGIVLGGKQRLSTARALLLTFIYVQGMALTYTALGLVVAAAGLQFQAALQHPYVLIGLAIVFTLLAMSMFGLFTLQLPSSLQTRLTLMSNRQQGGSPGGVFVMGAIAGLICSPCTTAPLSAILLYIAQSGNMWLGGGTLYLYALGMGLPLMLITVFGNRLLPKSGPWMEQVKTAFGFVILALPVFLLERVIGDVWGLRLWSALGVAFFGWAFITSLQAKRGWMRIVQIILLAAALVSVRPLQDWAFGATHTAQTQTHLNFTQIKTVDELNQALVEAKGKPVMLDLYADWCVACKEFEKYTFSDPQVQKALADTVLLQANVTANDAQDVALLKHLNVLGLPTILFFDGQGQEHPQARVTGFMDAETFSAHLRDRQP | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps.
Catalytic Activity: [protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61795
Sequence Length: 565
Subcellular Location: Cell inner membrane
EC: 1.8.1.8
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P44919 | MKKLFLFFTLIFTAFAANSGLFDKKQTFLKVDDAFAFSATLSTDKSQLQAHWDIADGYYLYQDKISAELVGKSNPLSLHTQQAAELHQDPYFGEVKVFTHSIDGIFRGAFNNADDKVEITYQGCTEGFCYPPETKVLRIGDLVVSQKQIVEKTVEKNTALLSEQDRLADGLFHSKWAIFGFFVLGLGLAFTPCVLPMLPLLSAIVIGQQQRPNMMRAFSLAFLYVQGMALTYTLLGLAVAAIGLPFQIALQHPYVMIGLSILFVALALSMFGLFTIQLPNSLQNKLNTWSQKQTSGAFGGAFAMGMIAGLVASPCTSAPLSGALLYVAQSGDLFTGAVTLYLLALGMGVPLMLITLFGNKILPKSGEWMNTVKQTFGFVMLALPVFLLSRILPEVWEPRLWAGLATVFFIWFALQMSKNGFGYAIKIISFALAMVTVQPLQNWIWQTQTTTQSAVENMPVSQVKFKQIKNTEELDRTLAENPHSIAMLDLYADWCVACKEFEKLTFSDPQVQQQFQNILLLQVSMTKNSPENKALMERFNVMGLPTILFFDQQNNEIKGSRVTGFMDADAFSNWIEKLL | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps (By similarity).
Catalytic Activity: [protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64406
Sequence Length: 579
Subcellular Location: Cell inner membrane
EC: 1.8.1.8
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Q5QVU3 | MIQRFITCLAALTLVFAVVAPAHSVQSNPFQQDNQFLSVDQAFDFDSEVNDSKVTVSWVVAPEYYLYQHRFKVVPENALAAEPELPQGESHNDEFFGESIVYRNYVEWSFTLNPEFSGDTITVQYQGCADAGLCYPPTEKQIKLSSTSETAPATAPPNTDSSLFGIGEQHLIITLLLFFALGIGLAFTPCVFPMYPILSGVVLGNRERNWKNTLWLSFIYVQGMAITYSLLGLVVASAGMQYQAYFQHPVVLIVLAVLFALFALSMFGAYTLQLPISWQSKLQSFSGQQSGGNIVGVFIIGAISGLVASPCTTAPLSGALLFIAQSGDMVSGVAILYALSLGMGVPLILFGLSGGKLLPKAGAWMNVVKQFFGWLLLAVTLFLIERLIPTSISMWLWIFYFILAAVSLAVSISQPLRITTKVITIVLLAAAATTGSYWQVNKAQLEQKSHGLFTVVSNVSDIQQQVAESDRWVMLDLYADWCVACKEFEQYTFSDEQVQAQFQEFKLIQADVTRNNAQDVEILSRYKVLGLPTILFFDPEGNERPEYRVTGYMNAEDFKKHLEKIVSE | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps.
Catalytic Activity: [protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62859
Sequence Length: 568
Subcellular Location: Cell inner membrane
EC: 1.8.1.8
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Q9JYM0 | MKKLICLFAVFLMLCGRAFALDANDLLPPEKAFVPELAVADDGVNVRFRIADGYYMYQAKIVGKTDPADLLGQPSFSKGEEKEDEFFGRQTVYHHEAQVAFPYAKAVGEPYKLVLTYQGCAEAGVCYPPVDTEFDIFGNGTYHPQTDEPASAKDRFLQPSSQNGSGALPPPKGDEGGDSRFKLSWDTLNANLLAFFLAGLGLSFTACMYPLLPIVSSIVVGDKKAGKARAFVLSVVYVQGLALTYTLVGIVAGLTGALLTVWLQQAWVVLAASALMVVLALSMFGLFNIQLPNAVQSYFQNQSSRLSGGKIVSVFIMGILSALIVGPCVAPPLAFALGYIGQTGDAVLGGLALYTLALGTGVPLIAIGTFGGHILPKAGDWMNAVKYAFGFILLAVAVYLATPHLPYYLVVALYTLLMLVPAFMLLVNGRRQKRRPKAVAFALGGILLIGGAWFGWQGANGKTTALHHFLTLNPPAEAGKSSEHGKMFADTAALKAAMDTALKEHPDKPVVLDFYADWCISCKEMAAYTLNQPEVHQAVDMERFFQIDVTANTPEHQALLKEYGLFGPPGVFVVRSDGSRSEPLLGFVKADKFIEWYEQNR | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps (By similarity).
Catalytic Activity: [protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64925
Sequence Length: 601
Subcellular Location: Cell inner membrane
EC: 1.8.1.8
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Q7MZX2 | MIKRTLMLFLLLCSPLLTPAAANALFEQPGQNPYLPVDQAFMFDFQQKGDKLTLDWQIKPGYYLYHKQLHIEPQQATLGKITLPQGTAHRDEFFGETEVYFQQLIVNVPVTKANNNSNIVVTYQGCAAAGYCYPPETRLVPLSAVIPSKTTDAISAEPVHKTPESASNDQQHLPFSPLWAILIGIGIAFTPCVLPMYPLISSIILGSQRPKSLKQIFWLALSYVQGMAVTYTLLGLIVAAAGLQFQAALQHPYVLIGLSVLFILLALSMFGLYSLQLPSAVQTRLVNWSNQQKNGSLFGVFAMGALAGLICSPCTTAPLSAILLYIAQSGNTVAGGLTLYLYALGMGLPLIAVTLFGHKLLPRSGPWMQYVKEAFGFIILALPVFLLERVIGDAWGIRLWSLLAVSFLGWGFVLTIRSQNGWVRVIQLILLILMLIATRPLQDWFWGTTVTQQSQHSLNFRQINNWQELEQIMTQNSHKTVMLDFYADWCTACKEFEKYTFSDPQVQSQLGDTLLLQANVTNNSPQQKQLLEKLSVRGLPTILFFDSQGKEIPDSRVNGFMDATRFNEHLQHLPK | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps.
Catalytic Activity: [protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64073
Sequence Length: 575
Subcellular Location: Cell inner membrane
EC: 1.8.1.8
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Q15ZS2 | MKLIASFSIFMLMSIWSFASLGQSNSFDSLFSNEPEFLKVDQAFVFDYVQNGDQLVVTWDIADDYYLYQQQFKAVSKNASLGEPIFPTGKMKEDEFFDEPQEVYYHKVSVTYPILQSQDDSAVKIRYQGCAEAGLCYPPTTQVVYLNAVNASDDLSNTDEASVESSGSVSQQFELADLLTGDQSLIWVLLIFLALGVGLAFTPCVFPMYPILSGIVIGQGKSISTSRAFVLSFVYVQGMALTYSLLGLVVASAGVQFQAALQHPIILGALIVVFALLALVMFGAWEFQLPSSWQEKLNGVSNQQKSGSYLGVLLMGAISGLVASPCTTAPLTGILLYIAQTSDLLLGFSALYALSLGMGIPLILFGITGGKLLPKAGAWMNIIKVTFGFMMLAVALMFVERLVSHMATDILWSLLGLVTFSYFYVMNQASSVTFGKGVRALVIFIGLFASAMYGYQTIFGQTSSVAGHTEQSHPRFEVVKNLDDFEQKLAAANAQGKTVMVDLYADWCVACKEFEKYTFPDTQVVDALSNTVWMQIDLTDNTATNIAFQEHFSILGLPTILFFDLQGKEISGSRVTGFMQASAFAAHAKNIL | Function: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps.
Catalytic Activity: [protein]-dithiol + NAD(+) = [protein]-disulfide + H(+) + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64665
Sequence Length: 592
Subcellular Location: Cell inner membrane
EC: 1.8.1.8
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D3RPC1 | MEQKKLAIIATKGSLDWAYPPFILASTAAALGYEVQVFFTFYGLQLLKKKPNLEVTPLGNPGMPMPMGMDKWFPVLGLALPGMQGMMTAMMKQKMKSKGVASIEELRELCQEAEVKMIACQMTVDLFDMPKAEFIDGVEYAGAAAFFEFAGESDICLYI | Function: Sulfur carrier protein probably involved in sulfur trafficking for oxidative dissimilatory sulfur metabolism. May be a component of a cytoplasmic sulfur relay system delivering sulfur to DsrC. Binds sulfur in the presence of sulfide in vitro.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17555
Sequence Length: 159
Pathway: Energy metabolism; sulfur metabolism.
Subcellular Location: Cell membrane
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O87896 | MKFALQINEGPYQHQASDSAYQFAKAALEKGHEIFRVFFYHDGVNNSTRLTTPPQDDRHIVNRWAELAEQYELDMVVCVAAAQRRGIVDEGEASRNGKDATNIHPKFRISGLGQLVEAAIQADRLVVFGD | Function: Not known. Could be involved in the oxidation of intracellular sulfur.
Sequence Mass (Da): 14588
Sequence Length: 130
Subcellular Location: Cytoplasm
EC: 2.8.1.-
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Q86MA2 | MTPRRVAKLVQFSGSYLNTEWARKFILGSLLQRYNPQSLTTVGSSAAGNSGEDASLDKELLHLQRSLSEVWSLPAQPLDAVSEGRILRLLARYATGEGVMSIEALNELSHVLSCIRGSPQRVEGPIDMEELLLAIGYAKPGDNLRRVAFAGELQYPPSALAHMRAHLRDDMERDGSDPFDILRVVTHNPAYAIDSASTSEVDDAIGVHKDPVTGEECFVVYVSDATVYCPFDSPLEQLTARLLTTTTYLPEGVFFMLPKPIVDAATLREDRPCRTFDIRFQIDEVTGELKNYSVGVGWLHKLRRITYDEVQALYDEEAQVGNQHHHTERESTQASPAKREEGKKGMVASGGTSSCRPSWMTVEDESILRRIYRAAQKRYETRQLRAGDRFIHADLPEPLIKVGAGAQVLSVEDQIIGTRDARLAVAEMMIAANEVCSRVAQENHLSIPFRGTRELSLDHVAAKSYREPHGVVSVQSLDPQYVFFAEAMQRSIRQLSGVTRAVYFHTPIYHAGLDTHNYTHSTSPLRRYADMLVHHQLKVWLWRTSHCSSGGGVLHSAQKSSPVLIEQPIAEHTMATLCSMISSKQEQSSILQESSQRYWLLKHIKQNILTKSPHHRFICLVGDTRSVKCAPEYARFVVECSHDSPSQPDGGVHRTVPWAGRWKQRHHEYLYVSDIYITELQFAHVVLHSLPDVVVGAVVECEVREVHPTQGYLSLAIVKVWSGGDERRFEPLWKKCLLPSLDS | Function: 3'-5'exoribonuclease which is involved in the post-transcriptional processing, editing and degradation of mitochondrial RNAs, including mRNAs, rRNAs and guided RNAs (gRNA) . As part of the mitochondrial 3' processome (MPsome), involved in the maturation of guided RNA (gRNA) precursors by catalyzing the processive 3'-5' degradation of uridylated gRNA precursors . Plays a role in the degradation of 12S rRNA processing intermediates and maturation by-products .
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 83357
Sequence Length: 743
Subcellular Location: Mitochondrion
EC: 3.1.13.1
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P39112 | MVVRRKVHVLLIARSFHSYTPCFRVTTRGKRQRSKSKQQAKVELDHTRELDNDQATETVVDRSVGPEKDIESINKDFLQRTKGLEPDIELKQLPQIKQEFNQRYKDRYVKPSEDWYVNSWRSLTKPKIPLYKLINSDFQLITKLKAPNPMEFQPVQLMESPLNVGDFVLLKMRPNELAMCVSLPSSTMDPRYTFVTIDGTMCFATKNRVLLRIPHKLPAGIHSLIQPESHHKHLPIGTVKNFSNQTNILPIVARQLITSRYPAQISKLAWKDLPITTKKLQLLHRSLQNYMGPWQIPFFTLVGLVQKLDLNKALDDKNGINYLTSLVNNYHTVNDIPINSPTFVSTYWAIMQQQESNLWGEIHLNTALLSPISVTIIPLKSQHLYYAQVIEKLEANSYREVNKFVKLVNERKYRDISALYPSVIQLLKDFAAGNFHNNGIIVALISKIFRKIERYKDCDITRDICQDLINEITPNSIPNPLLLNMDLALPASSKLVKWQQKLYDLTNIEELQWKKSGTDDDRYDFGDLRVFCIDSETAHEIDDGVSVKNYGRDGLYTLYIHIADPTSMFPESTNVDIEGISTDILNVALKRSFTTYLPDTVVPMLPQSICHLSDLGKQGQRTKTISFSVDVKITSKCSGKSIEIMYDSFKIRKGIVSNFPKATYEDVDRILGTPNSEASPVKKDLESLSMISKLLREQRIKNSNAVIFGEGFNKGLVMLNADSEGELTEVTFSDQEETLSTILVSEMMILANTLTGRYFAENKIGGVFRCYKQLPLGEVAQQQYDSMITSTKKGIFPKLKDIVKLSSLLNSSFYTGRPFRHEMIGAKQYLTVTSPLRRFPDLINHLQIHRHLQKKPLCFNQTQIDSLIWPIQSRADILKRASRNSSTYWTLNYLKKLTKLEPERTFDVMVTSVPQNGFTGCVFPDLSFARGTLKLHPSSMHYPMIGDIVKNCKISKIDCLEGMLELEKL | Function: Essential for mitochondrial biogenesis.
Catalytic Activity: Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 110822
Sequence Length: 969
Subcellular Location: Mitochondrion matrix
EC: 3.1.13.1
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B9LV23 | MIAIVVSRADSASEHIGEHLLDLGDWERRDDPSRPDADGGGTYYRTDGFELREFDDLHIYLDDPAAAFGGGAGDETNDAASDDTDETPEFLAFVSRHSGETGELLTAHVTGNFGPAPYGGEPDTLARAAPGAEKRVVEALAAHAPEGYDVGIECTHHGPTDTSVPSLFVELGSDEPQWTDADAARAVARAVLDLRGTDADLVTDAGETTDEIDDDPHPRHVVGFGGGHYAPRFTRIVRETEWAVGHVGADWALGELGAPDANRDVIEQAFARSKANVAVIEGEKPDLEATVEALGHRVVSETWVRAVGDRPLPLVERLESDLATIDEGLRFGEVVPASPDAIRVRGLPEDLLSRAQGVDADAARVAVETNAVAFDTEQAGTRAAGSVAFADDEVSPGYDDLVADLAGVLERGYDTVDITDGAVIARETAFDPELAAKRGVPEGPAFGRLASGESVEVDGETIAPADVSRERTNRFPIDSPTDSAAEPPTEPSE | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 52128
Sequence Length: 493
EC: 3.1.1.96
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Q18KS1 | MIGLVVSSADTASVTISDQLHELVEWESHRDAAGDEYEQYDDFEMRTIDEWHLEAENASELFSTTPQIIAFLSRHSGDTGPLLTTHFTGNFGPAEYGGEPGSFAQACPMIQQTLLEAFDRYAPSKYDVGIECTHHGPTTVGAPSLFVELGSSKAEWNDPDGAHAVAQAILELSGEDAPANVETDRTVVGFGGGHYAPRFERIIRETDWVVGHIGADWALDSMGAPAANRDIINHAVTASDADVALVADDRPELTKVISQADIRVVQERWLRETTGVSRPMVSALENALVPIASGLRLGTPATEYDPATSDEFVITDRHTDNDAVGTVHTKDSTDIDTGTNHNVDAERTESEDSHNIRDAIDRADADAVVLAFPTSLMETISGIDIETTNQVFSEHTLAFETTEGGTRPTGRMIVSDYLSVESITHALIDILKLKYDRVERTDETLRVRRQVFDPAKAATLDVPEGPAFGRLAAGESVTVAGRTIDPEAVHTTETVTFPVFSTSSSSSSSSSSSSSSSSSSS | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 56102
Sequence Length: 521
EC: 3.1.1.96
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A2BKX3 | MLALIYSARDPAGSGTARIIRELLGGDRCSLPRAVECTLLSNGVYLVGFDADSIFLDFLGEVLPANIEGYVVLSRHSGGKPSLTVHHTGNPGPEAPYGGKPWSLAPAWPRTAAGLLRTYRRVAEEMGLTGEFQVTLEATHHGPTELEKPIVFIEIGSSEREWVRRDTQNAMAETVIRFMERDLVSVECSKVAIGIGDTHYPIKHTRNVLERGYCYSHIFSKHVLDNLTLELLEQALEKTRDKVDTVVLAKVPSRVKQLARSFAEKYGLQLEK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 30141
Sequence Length: 272
EC: 3.1.1.96
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A8ABM7 | MKVTVVYYPGDPAAKGAAEALEREYGIKALELPEDPPFFDFNSLAGDAFIVLSRHSSEKRVKAFTVHHTGNFGEAKLGGEPKRLGVAYPSLACSLLRAMNAFRREGYDVTYEATHHGPTSDKPLVFAEIGSVKEDWEDPANHEVLAKAVASWEEHRCEAPKAVWVGGPHYSKRATKRCLEGEACFGHIAPKYALDHLDEDLLRQMVERSFERPERAYVEKKSLKSELRLRVVKALEDLGLEVLVV | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 27362
Sequence Length: 245
EC: 3.1.1.96
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B1L7I3 | MSKRLALAYSKKDPAGSGMAREIKDMMGEEFEISDKRCELIEVDREILYINGSQFEGFDYLAVLSRHSGTPNHPIFTAHVSGNFGRARYGGDHFKLSIAIPSLMKEYLISVSKRAEEIGYWVGFEPTHHGPTLDIPTAFLEIGCDETAWRDERGLRAAAESVLEAIESWKDGKFVAAVAFGGPHINDHFTRVELFTRFAIGHAARKLDAEWVDGEMVKQAVSRNGEPTGVAIVDNKGLKGEDRERIEGALRDLGLEVIRVKKILRDELGEEEGEEI | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 30777
Sequence Length: 276
EC: 3.1.1.96
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A6UUZ4 | MKYLFINSSKDKAGINIRNNLEKLNNINNNCIIDFFETPKKLTELSKKDLPQDYDYYIFLSKHRSVSEKPTLTVHTSGNLTTDNSHGGNIEEVCCCDAILNTILLVNINKYNNLEKYKKLGFDVSFEAIHHAPTDLDVPSVFVEIGSSEKEWAIDEAGEIMANAIIDTISSIESKSYKKLDKVIAFGGGHYAPRFTKLSLSNKCFVGYIIPKYAKISEKVLQQLIQMQDFDYILFDWKGINSEDKKRYIEFFDKNNILWKKVKDLCY | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 30685
Sequence Length: 267
EC: 3.1.1.96
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P58850 | MTDTNPENVNNSKITIICSAPDLASQNIKKHLLALREWKPLELPENSGFSAVLESADGKFRLVDIEEIHVFQDGLDKKLEAAGLPAELIIFASKHRSKEEVKSLTVHCTGNSSNEARLGGHPKELAVSSPPAMKSILMEMKRLAKVKGLDYDVTLEVTHHGPTELNVPSLYAEIGSTEGQWEEPVPGEIVARAILTVSLEKVPTAVGFGGGHYAMRQTGLLLETAISFGHNFPKYQLEFVDEALIRQAVEKSNAEFAYFDRKSMKSADRKRISQILEKLGLKVLKESEIREKYGREE | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 32935
Sequence Length: 297
EC: 3.1.1.96
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A7IAL9 | MKVALIHSRDDVAGCTIRRHIEQCLDDAHGSANGRTYEFVEVGGRLINAEGVDATLDVNLVIFLSRHSSVNPVPVLTVHATGNFGAAELGGSPRTLAPAAPAMMQATLRALARYCPEGYRVSYEVTHHGPTGLSHPSFFVEIGSTEKEWVDPVAGRAVAEAVLGADPAGAVPLIGIGGTHYAPRETAIALSSRGAFGHIASSRLQVALLDRELVQAMVVQSRAVAAYIDRKAVLPGDVSRISAILDELGIPRLSETEITSLGHLAWEAYREVRALAATVGPQTRCFIHALEGTGPLVLVSLDPVLLSEAKRCDESALVQRFGPLPVAHLATEDNVLLPQFVAFERNSSKIINDLNTLCVKIIRNRESTATENDYLVIRKVRFDPQKARELGVPAGPAYRQLAAGQAVEYDGQIITPDRVSVATETRIHIPGLENYS | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 46842
Sequence Length: 436
EC: 3.1.1.96
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Q12UQ4 | MTEDNEVQIAGMSIVIVCSVVDPASQNIKEHLLKLRDWVEMSVPGGIFDDLSAVYQSGNFYIIEVTEHHIYQDGIDRKIEEAGLDCDLLIFASKHKSADGRRLLTAHFTGNPGSADFGGYPGELSMAAPFALRCLLRNMAELSESIGFDVSMESTHHGPSDLDVPSVYAEIGSSEVEWVDQDAGDIVARSILSVRSGFCPVGIGFGGGHYAARQSELVLGSDISFGHNFPNYQLQFVDVDMFRKAVERSGADLVYCDRKAMSSDEKKRINELADEFGLDVLRESDIKGMEGVCWDIFRIFWHKVRDEGLSGRVKVPVGLKDKLSENVCDIFDFDVSNVVTVVIDNELLKLVRSVDAGGVKRLLDMSNVVYSERDDATISNHFYTFWNRDAEDFLTFIVDECIKILKGRYDTEYVFEENVLYISDERFSPELARKWGVPSGPMFGELAKGQSVMIEGNTVLPEMVHERTQKSLVLRNVIF | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 53540
Sequence Length: 479
EC: 3.1.1.96
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Q2FPX3 | MTPKEQSPTTLLISSRKDPAGSLIHEELYSFLEDDKRAHSHIRHWHAEERLIYLDGPSLPHDADRILFLSRHASERPRPVLTVHVTGNFGSADYGGRPNTLTPAATGLMHALINRLIIHAPEGYEVMYEATHHGPTDIPLPSCFIELGSTEKEWNDRIAARAVAQAVLDALLMDTSSVIPLAGFGGTHYAQRQTEITKLTRGGFGHIMPTRDIPHLTDALFQDIISSTGAFAIYIDGKSMSGKEERMITGLADKHTIPILGQGDLMRLFDLPFSEYMSIRNLAESLIPGSSIVLHTILEMPAPVSLTIPGELVDEVMKVAAEEFISALDSFPIVHMTGRGKACHPVFITDAAFSGRISDELIHLCVTLLQDRYTCSFEGDSLIIKKLRFDPKKAKNLGIPSGPLYSELMAGKPVEVGDSVIYPEMVMTETEKRIHIPQRQAR | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 48825
Sequence Length: 442
EC: 3.1.1.96
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P58851 | MRRVVILWNPDDPASKNIAESLTEDAEKLDTEDLQHYTVETWERDGVRFHLTAALGDLIEEDEARELARKFDVIVFASRHESRTKKPSLTVHVPGNPTPEAKFGGKPLEVCTADPAGMKAALLELKRFRDKRGLDYDVCYEVTHHGPRDPGAPCFFIEIGSDEERWTDEEAGEACARAILAAVDPPDVKAVVGYGGGHYAPAHTDAALSNRKLAYGHIVPDYAVDHDYLRDQFREVVDKTPRAREIIVDDRNLDSGIVERLEDLVRDRGLRLRDVEEVK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 31379
Sequence Length: 279
EC: 3.1.1.96
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A2STU3 | MIIDILNSDSDPAGRNIRAAIDELLKNPPEGGFPLFDGNEVTFHTVSGRIIHAEKSAVNPDADLIIVVSRHSSVNPVPVLTVHPAGNFGIAGLGGNDRELGLTSPAWMKSILQNHAEFVPEGYRVSYEITHHGPTDFPVPFFFVEVGSTEKEWNDPAACIAAAKSVLYARPSPEIVPLIGFGGTHYAVRQTAIGLETKGAFGHMMHTRDVGSVSKEMVSQMIAKSCGVFAAHIDRKALSKQEISHIEGILAEVGLEEITEGDLRKMNAMSFSTWVAYRDLAALQAPGLKIFPHGRIFDGDPAVVELPSDLFSAAFLGYEEIFLAELDKMGNIFHTTGKGGRLMPTLLTSAKNRQKVSGDLIVLSVQQITRTQDSLVEGDQITIARRQFDPVLARTLGVPSGPLYGQLVAGKPVTLPDGRMITPDMVTKVVRTSIKIPGLENYS | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo.
Catalytic Activity: a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA + H(+)
Sequence Mass (Da): 47911
Sequence Length: 443
EC: 3.1.1.96
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Q65GR0 | MRLVVQRVTDASVSVGGETVGEIGLGLMVLVGVTHEDTSEDAAYLAEKLVNLRIFEDEGEKMNLSLLDVGGSVLSVSQFTLYGDTKKGRRPNFTKAAKPDQALQLYEEWNSMLRAKGVTVETGRFGEMMDVKLTNSGPVTFIMDSKA | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 16005
Sequence Length: 147
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
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Q8A2P0 | MRIVVQRVSHASVTIEGQCKSSIGKGMLILVGIEESDGQEDIDWLCKKIVNLRIFDDESGVMNKSILEDGGEILVISQFTLHASTKKGNRPSYIKAAKPEISVPLYERFCKDLSRALGKEIGTGTFGADMKVELLNDGPVTICMDTKNKE | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 16489
Sequence Length: 150
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
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Q8G4Q2 | MKVVLQRVSEASVDVVNELGTLDPTFEPQQIGPGFMILVGVTDGDGDKQIAWLAHKILNLRVFEDAQGKMNRSIQDIGGEILSISQFTLFADVHKGNRPSFIKAGKPEHADLMWIKFNEALRSGGVPVKEGRFGAHMRVGLVNDGPVTIVIDTEHDMPDGTR | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 17746
Sequence Length: 162
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
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Q88VQ3 | MRVIVQRSQQAQVSIDGKVRGTIDHGFVLLVGFQDGDGQAELDYIAHKILNLRVFSDADGKMNLNIQQVGGAILSISQFTLYAETRHGNRPSFTAAGNPELASKLYDTFNQQLAASGVTVATGEFGADMQVSLVNDGPVTICYDTDQR | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 16007
Sequence Length: 148
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
|
Q8E988 | MIALIQRVSRASVVVDNQTIGAIDKGLLVLLGVEREDNREKMEKLATKVMSYRVFSDENGKMNLNLTQAGGSLLVVSQFTLAADTERGLRPSFSGAGTPEQALGLYEEFVAFCRTKGVNTETGQFAADMKVELVNDGPVTFHLQV | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 15782
Sequence Length: 145
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
|
A0KRY8 | MIALIQRVSRASVVVDNQTIGAIDKGLLVLLGVEREDNREKMEKLATKVMSYRVFSDENGKMNLNLTQAGGSLLVVSQFTLAADTGRGLRPSFSGAGTPEQALGLYEDFVAFCRAQGVTTETGQFGADMKVELINDGPVTFNLQV | Function: An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
Catalytic Activity: glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala)
Sequence Mass (Da): 15630
Sequence Length: 145
Domain: A Gly-cisPro motif from one monomer fits into the active site of the other monomer to allow specific chiral rejection of L-amino acids.
Subcellular Location: Cytoplasm
EC: 3.1.1.96
|
B8NR70 | MVKNNAGIVNMFEKRRTQTTTIPIIEIMREKRSEDLETEIVQGLQFDSLQLPQELLWDDAGQILFDDLCNSSTYYLTKKEKEILQKYSTDMAATIPEGSTLIELGCGSLRKTGILLSALEKSHKAVTYYALDVSQDSLENGLAQLHKGLGCLDHVELRGLWGTYEDAIAWLADQHPINVHNGITFLWMGNSMTNMHLAQAQSLLSRMTKTCIGSGIPCQILVSVDSCSAEDIVMGAYDTDSQPLKDFIMNGLKSANRILGKDVFCASDWTFGTVLDRVRHEVQVFYAPTRDVTIHIDSHPCKITKGEKIAVISSGKWPEPYFRSMLEGIGLQVLDLWRDSDQFYCMNPLPLICSFPG | Function: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of the dimeric diketopiperazine alkaloid ditryptophenaline . The nonribosomal peptide synthase dtpA accepts L-tryptophan and L-phenylalanine as its substrates and forms the phenylalanyl-tryptophanyl cyclic dipeptide product cyclophenylalanyltryptophenyl . The N-methyltransferase dtpB is responsible for the N-methylation of cyclophenylalanyltryptophenyl to yield cyclo-N-methylphenylalanyltryptophenyl . The cytochrome P450 monooxygenase is responsible not only for pyrroloindole ring formation but also for concurrent dimerization of N-methylphenylalanyltryptophanyl diketopiperazine monomers into a homodimeric product .
Sequence Mass (Da): 39967
Sequence Length: 357
Pathway: Alkaloid biosynthesis.
EC: 2.1.1.-
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P36837 | MNTTTPMGMLQQPRPFFMIFFVELWERFGYYGVQGVLAVFFVKQLGFSQEQAFVTFGAFAALVYGLISIGGYVGDHLLGTKRTIVLGALVLAIGYFMTGMSLLKPDLIFIALGTIAVGNGLFKANPASLLSKCYPPKDPRLDGAFTLFYMSINIGSLIALSLAPVIADRFGYSVTYNLCGAGLIIALLVYIACRGMVKDIGSEPDFRPMSFSKLLYVLLGSVVMIFVCAWLMHNVEVANLVLIVLSIVVTIIFFRQAFKLDKTGRNKMFVAFVLMLEAVVFYILYAQMPTSLNFFAINNVHHEILGFSINPVSFQALNPFWVVLASPILAGIYTHLGNKGKDLSMPMKFTLGMFMCSLGFLTAAAAGMWFADAQGLTSPWFIVLVYLFQSLGELFISALGLAMIAALVPQHLMGFILGMWFLTQAAAFLLGGYVATFTAVPDNITDPLETLPVYTNVFGKIGLVTLGVAVVMLLMVPWLKRMIATPESH | Function: Proton-dependent permease that transports di- and tripeptides. Has a clear preference for dipeptides and tripeptides composed of L-amino acids, and discriminates dipeptides on the basis of the position of charges within the substrate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53575
Sequence Length: 489
Subcellular Location: Cell inner membrane
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B8NR71 | MKTPEYLAPLREELAAALKQADNAWSFDIFKHTPKLESFTKECLRVFTPSGKKPLQLRSTGRTLSPGTKFSLPAQQAHLDPDNYPNPNIFDGYRFCDPQSGACDIRGTITPSAKWLIFGIGTSACPARLLATRISQTLFFKVLRKYDLRLKLDNGQPEVVYAATNMFVNFNTQMYVKSASI | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of the dimeric diketopiperazine alkaloid ditryptophenaline . The nonribosomal peptide synthase dtpA accepts L-tryptophan and L-phenylalanine as its substrates and forms the phenylalanyl-tryptophanyl cyclic dipeptide product cyclophenylalanyltryptophenyl . The N-methyltransferase dtpB is responsible for the N-methylation of cyclophenylalanyltryptophenyl to yield cyclo-N-methylphenylalanyltryptophenyl . The cytochrome P450 monooxygenase is responsible not only for pyrroloindole ring formation but also for concurrent dimerization of N-methylphenylalanyltryptophanyl diketopiperazine monomers into a homodimeric product .
Sequence Mass (Da): 20313
Sequence Length: 181
Pathway: Alkaloid biosynthesis.
EC: 1.-.-.-
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P39276 | MKTPSQPRAIYYIVAIQIWEYFSFYGMRALLILYLTHQLGFDDNHAISLFSAYASLVYVTPILGGWLADRLLGNRTAVIAGALLMTLGHVVLGIDTNSTFSLYLALAIIICGYGLFKSNISCLLGELYDENDHRRDGGFSLLYAAGNIGSIAAPIACGLAAQWYGWHVGFALAGGGMFIGLLIFLSGHRHFQSTRSMDKKALTSVKFALPVWSWLVVMLCLAPVFFTLLLENDWSGYLLAIVCLIAAQIIARMMIKFPEHRRALWQIVLLMFVGTLFWVLAQQGGSTISLFIDRFVNRQAFNIEVPTALFQSVNAIAVMLAGVVLAWLASPESRGNSTLRVWLKFAFGLLLMACGFMLLAFDARHAAADGQASMGVMISGLALMGFAELFIDPVAIAQITRLKMSGVLTGIYMLATGAVANWLAGVVAQQTTESQISGMAIAAYQRFFSQMGEWTLACVAIIVVLAFATRFLFSTPTNMIQESND | Function: Proton-dependent permease that transports di- and tripeptides. Shows significantly higher specificity towards dipeptides than tripeptides. Has a preference for dipeptides with a C-terminal Lys residue. Can bind Ala-Lys, Lys-Ala, Ala-Ala. Can also transport alanine and trialanine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53055
Sequence Length: 485
Subcellular Location: Cell inner membrane
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P75742 | MNKHASQPRAIYYVVALQIWEYFSFYGMRALLILYLTNQLKYNDTHAYELFSAYCSLVYVTPILGGFLADKVLGNRMAVMLGALLMAIGHVVLGASEIHPSFLYLSLAIIVCGYGLFKSNVSCLLGELYEPTDPRRDGGFSLMYAAGNVGSIIAPIACGYAQEEYSWAMGFGLAAVGMIAGLVIFLCGNRHFTHTRGVNKKVLRATNFLLPNWGWLLVLLVATPALITILFWKEWSVYALIVATIIGLGVLAKIYRKAENQKQRKELGLIVTLTFFSMLFWAFAQQGGSSISLYIDRFVNRDMFGYTVPTAMFQSINAFAVMLCGVFLAWVVKESVAGNRTVRIWGKFALGLGLMSAGFCILTLSARWSAMYGHSSLPLMVLGLAVMGFAELFIDPVAMSQITRIEIPGVTGVLTGIYMLLSGAIANYLAGVIADQTSQASFDASGAINYSINAYIEVFDQITWGALACVGLVLMIWLYQALKFRNRALALES | Function: Probable proton-dependent permease that transports dipeptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54159
Sequence Length: 493
Subcellular Location: Cell inner membrane
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O94469 | MVQPELTQSVGYGIVVGLGLGFAALMIFVSWSLKKFNNENQTSEHFNTASHSVRTGLVASAVVSSWTWASTLLTSAQKTYQYGVSGAFWYASGACVQILLFTVLAIELKRKAPNAHTFLEVVRARCGPIAHGVFLVFAYITNILVMAMLLCGGSATISSVTGMNTVAVCFLLPVGVIIYTMFGGIKATFLTDYIHTVIILVILIMFSLATYSADKKIGSPGKLYDMLKEAGDAHPVAGNAQGSYLTMRSQEGAIFFIINLAGNFGTVFVDNGYWQKAIAANPASALPGYILGGLAWFAIPWLAATTMGLVALGLENKPYFPTYPNRMSDLEVSEGLVLPYAAIALMGRAGANATLLLVFMAVTSAASAELIAVSSIFTYDIYKQYVRPRATGKELLYTGHASLIVFGFAMSGFATGLYYGQVSMGYLYLLMGVLVCPAVVPATCVMLFSRVSTIAVTVSPVLGIISSIITWLVVARAEGGKTLTIETTGANNPMLAGNVVGLLSPALYILILSIIFPEKYDFNRLLATFAMHFSSEEDEIQQTKKLNRASVISKVAALIITAAFIILWPWPMYGTGYIFSKRFFTGWVVVGLIWIFFTVFAVGIFPLWEGRNDIYQVVSNMAASIFGRKVNDIVEDEGVVVETISIGSGSKEKVNFEKKDIESV | Function: Involved in active transport of urea.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71720
Sequence Length: 664
Subcellular Location: Membrane
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Q8TFG0 | MEPILNQGYGYGFALGLGAAFALLMAIITKVLTACMGQTQNSERFSTASRSVKSGLISSSTVSAWTWPATLLSSGAWSYTYGIMGGFMYGVGGTIQITLFLFLAIQIKKKAPAAHTVSECFFIRFGKLGHCVYLFYCISTNVLVSSLLLLGGSQGFSSTTGMNTVAACFLLPLGVMVYTTLGGLKATFISDWIHTVMIYIILIVTCYTVYCSSSLIGSPAKMYDMLKEVQEVYPATGGQSYLSFKNSEMMYLTWSVMIGGLSSVFGDPGYSQRAIASDAKSVFQGYLMGGLCWWIIPMALGSSAGLACRALLLNPASVTYPNVLSSVEISSGLPVIYGMASIFGKSGAAAGLVMLFMSITSATSAELIAFSSVTTYDIFRAYINPAANGKQLVRTAHLSVIGFSLFIGALSVGFNYAGVTAGWLLTFLGIILTPEVSAVTLCLFWNKMTRFSLVVGAPFGTITGVVCWLASTYSFCDGIVNKDTVMTSKACFVGNIVSMASSPLYIVLLSYIWPDKETFDLNQFRNITVGDDIDTTELNAIVSQLKDERILKLQTYWSIGINLFILIGCYVIIPTALLGSNHDLSKSSFSGLIIVCLIWILVAAIYIILFPLWQGRKSLANVISHIIRLKAPENILLDGLTPKQSSEDVGDATSFHMDKLDKEKEKSSELKTA | Function: Involved in active transport of urea.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72604
Sequence Length: 673
Subcellular Location: Endoplasmic reticulum membrane
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Q9URY6 | MTETVLNQGYGYGIVIGLGFAFAIVMILVTYVLKRYVGEVQDSEHFTTASRSVKTGLISSAVVSSWTWPGTLLTSAGMAYEYGVCGSMWYSFAFTVQITFFTVIALQVKRVAPGAHTIVEIVKARFGQASHAVFLFYALGTNIIVSAMLLLGGSQAISAITGMHVVAAGFLLPLGVWLYTVSGGLKSTFLSDWTHTVIVYIVILITLFVAYTSSVHIGSIDKMYDLLTEVSKTNPSTGYKGSYLTVTNRDAVFVGWNIVIGGFATVFCDPSYGQKAIAAKPISAMKGYFAGGLAWLIVPWAMGSAAALSCLALTNNPVSVTYPDPVSSKQVSEGMPLLYGMTALMGKNGAAAGVLILFMASTSATSAELVAFSSVMTYDVYRNYFRPNASGKELVRVTHVFVTIFAVCMGALAVLFNYIGITISWIITFIGIALGPAVFGITLTLFWKKMNKYGMIIGCPMGSITGVVCWVGSCYKFSNGVVNKTTLNTPYANAVGNFTGLFSGLIYIVLISYFFPNKSDDLNNLNEKFVLGDDATAEEIVDAETEKKQLDRSLRIGIFVSWIIFFILVIIVPLPMYGSKYIFSKLFFRGWIIVIIIWTLIAALYITFYPLYESRDTIVYLCKLAIGKAKAPEPMNYVDAVEVEIESLSDDDKEKKANDFL | Function: Involved in active transport of urea.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71966
Sequence Length: 661
Subcellular Location: Membrane
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F4KD71 | MATCPPFDFSTKYYDGDGGCQRQSSFFGGTTVLDQGVGYAVILGFGAFFAVFTSFLVWLEKRYVGARHTSEWFNTAGRNVKTGLIASVIVSQWTWAATILQSSNVAWQYGVSGPFWYASGATIQVLLFGVMAIEIKRKAPNAHTVCEIVKARWGTATHIVFLVFCLATNVVVTAMLLLGGSAVVNALTGVNLYAASFLIPLGVVVYTLAGGLKATFLASYVHSVIVHVALVVFVFLVYTSSKELGSPSVVYDRLKDMVAKSRSCTEPLSHHGQACGPVDGNFRGSYLTMLSSGGAVFGLINIVGNFGTVFVDNGYWVSAIAARPSSTHKGYLLGGLVWFAVPFSLATSLGLGALALDLPISKDEADRGLVPPATAIALMGKSGSLLLLTMLFMAVTSAGSSELIAVSSLFTYDIYRTYINPRATGRQILKISRCAVLGFGCFMGILAVVLNKAGVSLGWMYLAMGVLIGSAVIPIAFMLLWSKANAFGAILGATSGCVFGIITWLTTAKTQYGRVDLDSTGKNGPMLAGNLVAILTGGLIHAVCSLVRPQNYDWSTTREIKVVEAYASGDEDVDVPAEELREEKLRRAKAWIVKWGLVFTILIVVIWPVLSLPARVFSRGYFWFWAIVAIAWGTIGSIVIIGLPLVESWDTIKSVCMGMFTNDRVMKKLDDLNHRLRALTMAVPEAEKIYLLELEKTKKNDEEG | Function: High-affinity urea-proton symporter involved in the active transport of urea across the plasma membrane into root cells. May play an important role in urea uptake by plant cells at low external urea concentrations.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75913
Sequence Length: 704
Subcellular Location: Cell membrane
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P33413 | MGEFKPPLPQGAGYAIVLGLGAVFAGMMVLTTYLLKRYQKEIITAEEFTTAGRSVKTGLVAAAVVSSWIWCSTLLTSSTKEYADGIFGGYAYAAGACFQIIAFAILAIKTKQMAPNAHTYLELVRTRYGKIGHGCYLFYAIATNILVTSMLLTSGSAVFSDLTGMNTIASCFLLPVGVVVYTLFGGIKATFLTDYMHTCVIIIIVLVFAFKVYATSDVLGSPGKVYDLVREAAKRHPVDGNYQGEYMTMTSKSAGILLIINLIGNFGTVFLDNGYWNKAISASPAASLKAYAIGGLAWFAVPSLISLTMGLACLAVETSPNFPTYPDPLTSFQANSGLVLPAAAIAIMGKGGAVASLLMIFMAVTSAMSAELIAVSSVFTYDIYREYIDPRASGKKLIYTSHVACIFFGLAMSGFSVGLYYGGISMGYIYEMMGIIISSAVLPVVLTLCSKDMNLVAAVVSPILGTGLAIMSWLVCTKSLYKELTVDTTFMDYPMLTGNLVALLSPAIFIPILTYVFKPQNFDWEKMKDITRVDETAELVQADPDIQLYDAEANDKEQEEETNSLVSDSEKNDVRVNNEKLIEPNLGVVISNAIFQEDDTQLQNELDEEQRELARGLKIAYFLCVFFALAFLVVWPMPMYGSKYIFSKKFFTGWVVVMIIWLFFSAFAVCIYPLWEGRHGIYTTLRGLYWDLSGQTYKLREWQNSNPQDLHVVTSQISARAHRQSSHFGQVDEII | Function: Required for active transport of urea.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80617
Sequence Length: 735
Subcellular Location: Membrane
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P36504 | CKQSCSFGPFTFVCDGNTK | Function: Is a potent inhibitor of human phospholipase A2.
PTM: Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine or the formation of dialkylamine bonds with lysine. This is followed by membrane translocation and cleavage of the modified precursor.
Sequence Mass (Da): 2069
Sequence Length: 19
Subcellular Location: Secreted
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P36503 | CANSCSYGPLTWSCDGNTK | Function: Is a potent inhibitor of human phospholipase A2. Exhibits only a weak antibacterial activity against B.subtilis, and does not display antimicrobial activity against S.aureus, S.mitis, E.coli, K.pneumoniae, P.vulgaris and C.albicans.
PTM: Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine or the formation of dialkylamine bonds with lysine. This is followed by membrane translocation and cleavage of the modified precursor.
Sequence Mass (Da): 2007
Sequence Length: 19
Subcellular Location: Secreted
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Q9Y6W6 | MPPSPLDDRVVVALSRPVRPQDLNLCLDSSYLGSANPGSNSHPPVIATTVVSLKAANLTYMPSSSGSARSLNCGCSSASCCTVATYDKDNQAQTQAIAAGTTTTAIGTSTTCPANQMVNNNENTGSLSPSSGVGSPVSGTPKQLASIKIIYPNDLAKKMTKCSKSHLPSQGPVIIDCRPFMEYNKSHIQGAVHINCADKISRRRLQQGKITVLDLISCREGKDSFKRIFSKEIIVYDENTNEPSRVMPSQPLHIVLESLKREGKEPLVLKGGLSSFKQNHENLCDNSLQLQECREVGGGASAASSLLPQPIPTTPDIENAELTPILPFLFLGNEQDAQDLDTMQRLNIGYVINVTTHLPLYHYEKGLFNYKRLPATDSNKQNLRQYFEEAFEFIEEAHQCGKGLLIHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKGKRPIISPNLNFMGQLLEFEEDLNNGVTPRILTPKLMGVETVV | Function: Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 52642
Sequence Length: 482
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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Q9ESS0 | MPPSPLDDRVVVALSRPVRPQDLNLCLDSSYLGSASPGSGSHAPVLATAVVTLKAANLTYMPSSSGSARSLNCGCSSTSCCTVATYDKDHQAQTQAIAAGTATTAIGTSTTCPANQMVNNNENTGSVLSPSGGVGSPVSGTPKQLASIKIIYPNDLAKKMTKCSKSHLPSQGPVIIDCRPFMEYNKSHIQGAVHINCADKISRRRLQQGKITVLDLISCREGKDSFKRIFSKEIIVYDENTNEPSRVTPSQPLHIVLESLKREGKEPLVLKGGLSSFKQNHGNLCDNSLQLQECREVGGGASAASSMLPQSVPTTPDIENAELTPILPFLFLGNEQDAQDLDTMQRLNIGYVINVTTHLPLYHYEKGLFNYKRLPATDSNKQNLRQYFEEAFEFIEEAHQCGKGLLIHCQAGVSRSATIVIAYLMKHTRMTMTDAYKFVKGKRPIISPNLNFMGQLLEFEEDLNNGVTPRILTPKLMGMETVV | Function: Protein phosphatase involved in the inactivation of MAP kinases. Has a specificity for the MAPK11/MAPK12/MAPK13/MAPK14 subfamily. It preferably dephosphorylates p38.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 52532
Sequence Length: 483
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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