ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q9MA98 | MANEDDDGEKSRSLHQQIARKPKTQIVIGVPSYQEVLESSQTKSTPPSLFKPSQSFSQAFAFVKSSDVYSPPPPSSAAASSSQPSGASQVPHSSSQTHQTDGASSSSTPVATGSVPSNTTQNRNAILVSHRQKGNPLLKHIRNVKWVFSDIIPDYVLGQNSCALYLSLRYHLLHPDYLYFRIRELQKNFKLSVVLCHVDVEDTVKPLLEVTKTALLHDCTLLCAWSMTECARYLETIKVYENKPADLIQGQMDTDYLSRLNHSLTSIRHVNKSDVVTLGSTFGSLAHIIDASMEDLARCPGIGERKVKRLYDTFHEPFKRATSSYPSVVEPPIPEAPVEKDVNSEEPVEEDEDFVEDSRKRKKKEPEPEKTVKTALSAVFARYSDRLSKKKEKQKEKDTTTASDAETHQN | Function: Seems to be involved in nucleotide excision repair (NER) of damaged DNA (dark repair mechanism). The UVH1/RAD1-ERCC1/RAD10 complex may act as an endonuclease making DNA incision 5' to the lesion site. In vitro, is implicated in double strand breaks (DSBs) repair and is required for homologous recombination in the presence of non-homologous overhangs. In vitro, is involved in chromosomal recombination between tandem repeats in both direct and inverted orientations. May mediate the induction of a DNA-damage sensitive cell-cycle checkpoint during the G2 phase.
Sequence Mass (Da): 45748
Sequence Length: 410
Subcellular Location: Nucleus
EC: 3.1.-.-
|
Q1LZ75 | MDEEGVHKPAGPPTRKKFLIPTDEDVVPPPGAKPLFRSTRSLPTVETSPPPGPQTYAEYALSGPPGGAEATRPVGPEPLAEETPNQAPKPGAKSNSIIVSPRQRGNPVLRFVRNVPWEFGDVLPDYVLGQSTCALFLSLRYHNLHPDYIHQRLQSLGKSYALRVLLVQVDVKDPQQALKELAKMCILADCTLILAWSPEEAGRYLETYKAYEQKPADLLMEKLEQDFVSRVTECLTTVKSVNKTDSQTLLTTFGSLEQLIAASREDLSLCPGLGPQKARRLFDVFHEPFLKVPH | Function: Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. Also required for homology-directed repair (HDR) of DNA double-strand breaks, in conjunction with SLX4 (By similarity).
PTM: Ubiquitinated with both 'Lys-48' and 'Lys-63' linkages. Deubiquitinated by USP45.
Sequence Mass (Da): 32544
Sequence Length: 294
Subcellular Location: Nucleus
|
P07992 | MDPGKDKEGVPQPSGPPARKKFVIPLDEDEVPPGVAKPLFRSTQSLPTVDTSAQAAPQTYAEYAISQPLEGAGATCPTGSEPLAGETPNQALKPGAKSNSIIVSPRQRGNPVLKFVRNVPWEFGDVIPDYVLGQSTCALFLSLRYHNLHPDYIHGRLQSLGKNFALRVLLVQVDVKDPQQALKELAKMCILADCTLILAWSPEEAGRYLETYKAYEQKPADLLMEKLEQDFVSRVTECLTTVKSVNKTDSQTLLTTFGSLEQLIAASREDLALCPGLGPQKARRLFDVLHEPFLKVP | Function: Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. Also required for homology-directed repair (HDR) of DNA double-strand breaks, in conjunction with SLX4.
PTM: Ubiquitinated with both 'Lys-48' and 'Lys-63' linkages . Deubiquitinated by USP45 .
Sequence Mass (Da): 32562
Sequence Length: 297
Subcellular Location: Nucleus
|
P07903 | MDPGKDEESRPQPSGPPTRRKFVIPLEEEEVPCAGVKPLFRSSRNPTIPATSAHVAPQTYAEYAITQPPGGAGATVPTGSEPAAGENPSQTLKTGAKSNSIIVSPRQRGNPVLKFVRNVPWEFGEVIPDYVLGQSTCALFLSLRYHNLHPDYIHERLQSLGKNFALRVLLVQVDVKDPQQALKELAKMCILADCTLVLAWSAEEAGRYLETYKAYEQKPADLLMEKLEQNFLSRATECLTTVKSVNKTDSQTLLATFGSLEQLFTASREDLALCPGLGPQKARRLFEVLHEPFLKVPR | Function: Non-catalytic component of a structure-specific DNA repair endonuclease responsible for the 5'-incision during DNA repair. Responsible, in conjunction with SLX4, for the first step in the repair of interstrand cross-links (ICL). Participates in the processing of anaphase bridge-generating DNA structures, which consist in incompletely processed DNA lesions arising during S or G2 phase, and can result in cytokinesis failure. Also required for homology-directed repair (HDR) of DNA double-strand breaks, in conjunction with SLX4 (By similarity).
PTM: Ubiquitinated with both 'Lys-48' and 'Lys-63' linkages. Deubiquitinated by USP45.
Sequence Mass (Da): 32910
Sequence Length: 298
Subcellular Location: Nucleus
|
Q8W4M7 | MIFKIEDVTVYFPYDNIYPEQYEYMVELKRALDAKGHCLLEMPTGTGKTIALLSLITSYRLSRPDSPIKLVYCTRTVHEMEKTLGELKLLHDYQVRHLGTQAKILALGLSSRKNLCVNTKVLAAENRDSVDAACRKRTASWVRALSTENPNVELCDFFENYEKAAENALLPPGVYTLEDLRAFGKNRGWCPYFLARHMIQFANVIVYSYQYLLDPKVAGFISKELQKESVVVFDEAHNIDNVCIEALSVSVRRVTLEGANRNLNKIRQEIDRFKATDAGRLRAEYNRLVEGLALRGDLSGGDQWLANPALPHDILKEAVPGNIRRAEHFVHVLRRLLQYLGVRLDTENVEKESPVSFVSSLNSQAGIEQKTLKFCYDRLQSLMLTLEITDTDEFLPIQTVCDFATLVGTYARGFSIIIEPYDERMPHIPDPILQLSCHDASLAIKPVFDRFQSVVITSGTLSPIDLYPRLLNFTPVVSRSFKMSMTRDCICPMVLTRGSDQLPVSTKFDMRSDPGVVRNYGKLLVEMVSIVPDGVVCFFVSYSYMDGIIATWNETGILKEIMQQKLVFIETQDVVETTLALDNYRRACDCGRGAVFFSVARGKVAEGIDFDRHYGRLVVMYGVPFQYTLSKILRARLEYLHDTFQIKEGDFLTFDALRQAAQCVGRVIRSKADYGMMIFADKRYSRHDKRSKLPGWILSHLRDAHLNLSTDMAIHIAREFLRKMAQPYDKAGTMGRKTLLTQEDLEKMAETGVQDMAY | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD acts by forming a bridge between CAK and the core-TFIIH complex (By similarity). Essential during plant growth . May negatively regulate a common response program mediated by UV damage and heat stress, that leads to tissue death and reduced chloroplast function .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 86236
Sequence Length: 758
Subcellular Location: Nucleus
EC: 3.6.4.12
|
Q55G81 | MKFYIEDLLVYFPYSYIYPEQYSYMVALKRSLDNGGPCILEMPSGTGKTVSLLSLISSYQVKNPSIKLIYCSRTVPEIEQATEEARRVLQYRNSEMGEESPKTLCMSMSSRRNLCIQPRVSEERDGKVVDALCRELTSSWNRESPTSEKCKFFENFESNGKEILLEGVYSLEDLKEYGLKHQMCPYFLSRHMLNFANIVIFSYQYLLDPKIASLISSSFPSNSIVVFDEAHNIDNVCINALSINIDNKLLDTSSKNIAKINKQIEDIKKVDEKRLKDEYQRLVNGLARSGSTRADETTSDPVLPNDVIQEAVPGNIRKAEHFISLLRRVVDYLKSRLKSQMLLSESPLAFLQGLYHATQISSRTLRFCSSRLSSLLRTLRINDVNQFSGISLIADFATLVGTYNNGFLIIIEPYYQRQNNTYDQIFQFCCLDASIGMKPIFDKYRSVVITSGTLSPLDIYTKMLNFRPTVVERLTMSLNRNCICPCILTRGSDQISISTKFDVRSDTAVVRNYGALLVEVSAIVPDGIICFFTSYSYMEQIVSVWNEMGLLNNILTNKLIFVETSDPAESALALQNYKKACDSGRGAVLLSVARGKVSEGIDFDNQYGRCVILYGIPYINTESKVLRARLEFLRDRYQIRENEFLTFDAMRTASQCVGRVIRGKSDYGIMIFADKRYNRLDKRNKLPQWILQFCQPQHLNLSTDMAISLSKTFLREMGQPFSREEQLGKSLWSLEHVEKQSTSKPPQQQNSAINSTITTSTTTTTTTSTISETHLT | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. The ATP-dependent helicase activity of XPD/repD is required for DNA opening. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module CAK controls the initiation of transcription. XPD/repD acts by forming a bridge between CAK and the core-TFIIH complex.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 88278
Sequence Length: 776
Subcellular Location: Nucleus
EC: 3.6.4.12
|
Q9UQW6 | MVNTEVYIVSAVRTPMGSFGGSFASLPATKLGSIAIKGALERVNIKPSDVDEVFMGNVVSANLGQNPARQCALGAGLPRSIVCTTVNKVCASGMKATILGAQTIMTGNAEIVVAGGTESMSNAPYYAPKNRFGAKYGNVELVDGLLRDGLSDAYDGLPMGNAAELCAEEHSIDRASQDAFAISSYKRAQNAQATKAFEQEIVPVEVPVGRGKPNKLVTEDEEPKNLNEDKLKSVRAVFKSNGTVTAANASTLNDGASALVLMSAAKVKELGLKPLAKIIGWGEAAQDPERFTTSPSLAIPKALKHAGIEASQVDYYEINEAFSVVAVANTKILGLDPERVNINGGGVAMGHPLGSSGSRIICTLAYILAQKDAKIGVAAVCNGGGGASSIVIERV | Function: Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). Erg10 catalyzes the formation of acetoacetyl-CoA from acetyl-CoA (By similarity). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase eg10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hcs1 (Probable).
Catalytic Activity: 2 acetyl-CoA = acetoacetyl-CoA + CoA
Sequence Mass (Da): 40998
Sequence Length: 395
Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.3.1.9
|
P41338 | MSQNVYIVSTARTPIGSFQGSLSSKTAVELGAVALKGALAKVPELDASKDFDEIIFGNVLSANLGQAPARQVALAAGLSNHIVASTVNKVCASAMKAIILGAQSIKCGNADVVVAGGCESMTNAPYYMPAARAGAKFGQTVLVDGVERDGLNDAYDGLAMGVHAEKCARDWDITREQQDNFAIESYQKSQKSQKEGKFDNEIVPVTIKGFRGKPDTQVTKDEEPARLHVEKLRSARTVFQKENGTVTAANASPINDGAAAVILVSEKVLKEKNLKPLAIIKGWGEAAHQPADFTWAPSLAVPKALKHAGIEDINSVDYFEFNEAFSVVGLVNTKILKLDPSKVNVYGGAVALGHPLGCSGARVVVTLLSILQQEGGKIGVAAICNGGGGASSIVIEKI | Function: Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) . ERG10 catalyzes the formation of acetoacetyl-CoA from acetyl-CoA . The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 and HMG2 which are derived from a single ancestral HMGR gene by gene duplication .
Catalytic Activity: 2 acetyl-CoA = acetoacetyl-CoA + CoA
Sequence Mass (Da): 41729
Sequence Length: 398
Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.3.1.9
|
O65404 | MAFTNVCLWTLLAFMLTWTVFYVTNRGKKATQLADAVVEEREDGATDVIIVGAGVGGSALAYALAKDGRRVHVIERDLREPERIMGEFMQPGGRLMLSKLGLEDCLEGIDAQKATGMTVYKDGKEAVASFPVDNNNFPFDPSARSFHNGRFVQRLRQKASSLPNVRLEEGTVKSLIEEKGVIKGVTYKNSAGEETTALAPLTVVCDGCYSNLRRSLNDNNAEVLSYQVGFISKNCQLEEPEKLKLIMSKPSFTMLYQISSTDVRCVFEVLPNNIPSISNGEMATFVKNTIAPQVPLKLRKIFLKGIDEGEHIKAMPTKKMTATLSEKKGVILLGDAFNMRHPAIASGMMVLLSDILILRRLLQPLSNLGNAQKISQVIKSFYDIRKPMSATVNTLGNAFSQVLVASTDEAKEAMRQGCYDYLSSGGFRTSGMMALLGGMNPRPISLIYHLCAITLSSIGHLLSPFPSPLRIWHSLRLFGLAMKMLVPHLKAEGVSQMLFPVNAAAYSKSYMAATAL | Function: Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
Catalytic Activity: O2 + reduced [NADPH--hemoprotein reductase] + squalene = (S)-2,3-epoxysqualene + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56606
Sequence Length: 516
Pathway: Terpene metabolism; lanosterol biosynthesis; lanosterol from farnesyl diphosphate: step 2/3.
Subcellular Location: Membrane
EC: 1.14.14.17
|
Q4WP25 | MGNPRGRRTNGSIKTSKGTQRGTVSNLLSDQPLAARPKVSIVSNDDSQDSSDGGAFTTPSTTESTLKTTINGTDSTERNMSRKPSSPMAPAFMVSAPGKVIVYGEHAVVHGKAAMAAAISLRSYLLVTTLSKSQRTITMNFRDIGLDHTWNIDELPWDVFHHPSKKKFYYDLVTSLDPELVAAIQPHADAVSPDKPEDVRKIHRRSASAFLYLFLSLGSSQNPGAIYTLRSTIPIGAGLGSSASVCVCLSAALLLQIRTLAGPHPDQPPDEAEVQIERINRWAFVGEMCTHGNPSGVDNTVSAGGKAVVFRREDYSKPPTVTPLLNFPELPLLLVDTRQSRSTAVEVAKVGKLKDEYPVVTDSILEAIDQVTLAAQQKIQEISTNGISYRTLEDLGTLIRINHGFLVSLGVSHPRLERIRELVDYADIGWTKLTGAGGGGCAITLLRPDIKEEAVRELEEKLSAEGFVKYETTLGGDGIGVLWPAVLRNGTDEEGGEEIDQQKFENAVGTEGIERLVGVGVQEKREGWKFWKRSPRFS | Function: Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). Erg12 converts mevalonate into 5-phosphomevalonate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 (AFUA_4G07780) first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8 (AFUA_5G10680). The diphosphomevalonate decarboxylase mvd1 (AFUA_4G07130) then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 (AFUA_6G11160) then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase erg20 (AFUA_5G02450) catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
Sequence Mass (Da): 58457
Sequence Length: 538
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.36
|
A0A1D8PEL1 | MSQLPFIVGAPGKVIIFGEHAAVYGKPAIAAALSLRCYLLVSPSSDSNTIRLQFPDIKLDHSWNIKDLPWEEIKPYLTYDSANKPQIPSELVPEIVDKLSSFLNGFDNKMHYYACFCFLYLLMNLCDSKVSGMNFIVRSTLPIGAGLGSSASTSVCLSSALALMGGWINKPSLHENDKLDTADIPDLEFIDKWSLIGEKCFHGNPSGIDNAVATFGGAVMFQRTSTPEQPSIRTNMRNFPAIKLLLTNTKVPKSTADLVAGVGRLNAEFNSISTSILTAIEHLSQEAYKVMMNPMFGREETNVLRKLVNINHGLLVALGVSHPALETVKIIGDKHRIGATKLTGAGGGGCAITLVNDDVEESVIHNAIKEFEDSGYESFETSLGGKGVGILFHEDLDDATKFSESQFCNYVDRAAIEDSLGMANVKEWKFW | Function: Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). ERG12 converts mevalonate into 5-phosphomevalonate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
Sequence Mass (Da): 47035
Sequence Length: 431
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.36
|
Q09780 | MSKSLIVSSPGKTILFGEHAVVYGATALAAAVSLRSYCKLQTTNNNEIVIVMSDIGTERRWNLQSLPWQHVTVENVQHPASSPNLDLLQGLGELLKNEENGLIHSAMLCTLYLFTSLSSPSQGCTLTISSQVPLGAGLGSSATISVVVATSLLLAFGNIEPPSSNSLQNNKALALIEAWSFLGECCIHGTPSGIDNAVATNGGLIAFRKATAHQSAMKEFLKPKDTLSVMITDTKQPKSTKKLVQGVFELKERLPTVIDSIIDAIDGISKSAVLALTSESDKNSSAKKLGEFIVLNQKLLECLGVSHYSIDRVLQATKSIGWTKLTGAGGGGCTITLLTPECKEEEFKLCKESLLAHKNSIYDVQLGGPGVSVVTDSDSFFPQYESDFDFKKLNLLSKFNKYYI | Function: Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). Erg12 converts mevalonate into 5-phosphomevalonate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8. The diphosphomevalonate decarboxylase mvd1 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
Sequence Mass (Da): 43407
Sequence Length: 404
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.36
|
P07277 | MSLPFLTSAPGKVIIFGEHSAVYNKPAVAASVSALRTYLLISESSAPDTIELDFPDISFNHKWSINDFNAITEDQVNSQKLAKAQQATDGLSQELVSLLDPLLAQLSESFHYHAAFCFLYMFVCLCPHAKNIKFSLKSTLPIGAGLGSSASISVSLALAMAYLGGLIGSNDLEKLSENDKHIVNQWAFIGEKCIHGTPSGIDNAVATYGNALLFEKDSHNGTINTNNFKFLDDFPAIPMILTYTRIPRSTKDLVARVRVLVTEKFPEVMKPILDAMGECALQGLEIMTKLSKCKGTDDEAVETNNELYEQLLELIRINHGLLVSIGVSHPGLELIKNLSDDLRIGSTKLTGAGGGGCSLTLLRRDITQEQIDSFKKKLQDDFSYETFETDLGGTGCCLLSAKNLNKDLKIKSLVFQLFENKTTTKQQIDDLLLPGNTNLPWTS | Function: Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway . ERG12 converts mevalonate into 5-phosphomevalonate . The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase ERG12 first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase ERG8. The diphosphomevalonate decarboxylase MVD1/ERG19 then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase ERG20 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate .
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
Sequence Mass (Da): 48460
Sequence Length: 443
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.36
|
A0A1D8PTW6 | MVMTNSPQNIGIKGIEVYIPGQAVNQSDLEKFDGIPQGKYTIGLGQTNMAFVNDREDIYSISLTVLSRLIKNYSIDTNKIGRLEVGTETLLDKSKSVKSVLMQLFPGNNDIEGIDTVNACYGGTSSVINAINWIESSSWDGRDAIVVAGDIAIYDKGAARPTGGVGAIALLIGPDAPIVFDSIRGSFMEHAYDFYKPDFTSEYPVVDGHFSLSCYVKAVDNCYKNYSKKITGDANKTVGVYDHFDFSAFHVPTCKLVTKSYARLLYNDYVSNPSKFADLIDETTRKHIDGLTYDESLTDKILEKTFVGLAKDETKKRVQPALQVPTNTGNMYTASAWVSLASLLYYVGSDNLKNKRISIFSYGSGLASTLLSVTVKGDVSAITKVLDFDYKLGDGRKIQSPEDYLAAIELREKAHLQKSFKPQGSTDNLSQGTYYLTEIDDKFRRAYAIKE | Function: Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). ERG13 condenses acetyl-CoA with acetoacetyl-CoA to form hydroxymethylglutaryl-CoA (HMG-CoA) (By similarity). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase HMG1 finally reduces HMG-CoA to produce mevalonate (Probable).
PTM: Is a probable target for sumoylation.
Catalytic Activity: acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-methylglutaryl-CoA + CoA + H(+)
Sequence Mass (Da): 49755
Sequence Length: 451
Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
EC: 2.3.3.10
|
I1RY35 | MSSRPQNIGIKAIELYFPSQYVDQVELEKFDGVSAGKYTIGLGQTKMSFCDDREDIYSFALTATSKLLKNYNIDPNSIGFLEVGTETLLDKSKSVKSVLMQLFGDNTNIEGVDTINACYGGTNAVFNAINWVESSAWDGRDAIVVAGDIALYAKGNARPTGGAGAVALLIGPNAPIVAEPGLRGTYMQHAYDFYKPDLTSEYPYVDGHYSVNCYSKALDAAYRAYCKREAKQANGTNGVTNGDASTKTGLDRFDYMAFHSPTCKLVQKSYARLLYHDYLANADSPVFAEVAPELRDMDYEKSLTDKVVEKTFMTLTKKRFQERVNPAIQVATNCGNMYCGSVWSGLASLISVVDNKDLEGKRIGLFSYGSGLAASFLSFRINGSVDKISDVLNIPSRLESRRAVPPETYDQMCDLRKQAHLQKDYTPKGDPSTILPGTYYLTKVDDMFKREYAIKE | Function: Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (By similarity). ERG13 condenses acetyl-CoA with acetoacetyl-CoA to form hydroxymethylglutaryl-CoA (HMG-CoA) (By similarity). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10B that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 (Probable).
Catalytic Activity: acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-methylglutaryl-CoA + CoA + H(+)
Sequence Mass (Da): 50352
Sequence Length: 456
Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
EC: 2.3.3.10
|
P54874 | MSFDRKDIGIKGLVLYTPNQYVEQAALEAHDGVSTGKYTIGLGLTKMAFVDDREDIYSFGLTALSQLIKRYQIDISKIGRLEVGTETIIDKSKSVKSVLMQLFGDNHNVEGIDCVNACYGGVNALFNTIDWIESSAWDGRDGIVVAGDIALYAKGNARPTGGAGCVALLVGPNAPIVFEPGLRGTYMQHAYDFYKPDLTSEYPYVDGHFSLECYVKALDGAYANYNVRDVAKNGKSQGLGLDRFDYCIFHAPTCKQVQKAYARLLYTDSAAEPSNPELEGVRELLSTLDAKKSLTDKALEKGLMAITKERFNKRVSPSVYAPTNCGNMYTASIFSCLTALLSRVPADELKGKRVGAYSYGSGLAASFFSFVVKGDVSEIAKKTNLVNDLDNRHCLTPTQYEEAIELRHQAHLKKNFTPKGSIERLRSGTYYLTGIDDMFRRSYSVKP | Function: Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) . Hcs1 condenses acetyl-CoA with acetoacetyl-CoA to form hydroxymethylglutaryl-CoA (HMG-CoA) . The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase eg10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases hcs1 (Probable).
Catalytic Activity: acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-methylglutaryl-CoA + CoA + H(+)
Sequence Mass (Da): 49239
Sequence Length: 447
Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
EC: 2.3.3.10
|
P54839 | MKLSTKLCWCGIKGRLRPQKQQQLHNTNLQMTELKKQKTAEQKTRPQNVGIKGIQIYIPTQCVNQSELEKFDGVSQGKYTIGLGQTNMSFVNDREDIYSMSLTVLSKLIKSYNIDTNKIGRLEVGTETLIDKSKSVKSVLMQLFGENTDVEGIDTLNACYGGTNALFNSLNWIESNAWDGRDAIVVCGDIAIYDKGAARPTGGAGTVAMWIGPDAPIVFDSVRASYMEHAYDFYKPDFTSEYPYVDGHFSLTCYVKALDQVYKSYSKKAISKGLVSDPAGSDALNVLKYFDYNVFHVPTCKLVTKSYGRLLYNDFRANPQLFPEVDAELATRDYDESLTDKNIEKTFVNVAKPFHKERVAQSLIVPTNTGNMYTASVYAAFASLLNYVGSDDLQGKRVGLFSYGSGLAASLYSCKIVGDVQHIIKELDITNKLAKRITETPKDYEAAIELRENAHLKKNFKPQGSIEHLQSGVYYLTNIDDKFRRSYDVKK | Function: Hydroxymethylglutaryl-CoA synthase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) . ERG13 condenses acetyl-CoA with acetoacetyl-CoA to form hydroxymethylglutaryl-CoA (HMG-CoA) . The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 and HMG2 which are derived from a single ancestral HMGR gene by gene duplication .
Catalytic Activity: acetoacetyl-CoA + acetyl-CoA + H2O = (3S)-hydroxy-3-methylglutaryl-CoA + CoA + H(+)
Sequence Mass (Da): 55014
Sequence Length: 491
Pathway: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 2/3.
EC: 2.3.3.10
|
Q4V8Y6 | MSFDVRRFDIYRKVPKDLTQPTYTGAFISICCCVFMLFLFLSELTGFIATEIVNELYVDDPDKDSGGKIDVSLNISLPNLHCDLVGLDIQDEMGRHEVGHIENSMKVPLNNGHGCRFEGEFSINKVPGNFHVSTHSATAQPQSPDMTHIIHKLAFGAKLQVQHVQGAFNALGGADRLQSNALASHDYILKIVPTVYEELGGKQRFSYQYTVANKEYVAYSHTGRIIPAIWFRYDLSPITVKYTERRRPFYRFITTICAIIGGTFTVAGIIDSCIFTASEAWKKIQIGKMS | Function: Possible role in transport between endoplasmic reticulum and Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32529
Sequence Length: 290
Subcellular Location: Endoplasmic reticulum membrane
|
Q969X5 | MPFDFRRFDIYRKVPKDLTQPTYTGAIISICCCLFILFLFLSELTGFITTEVVNELYVDDPDKDSGGKIDVSLNISLPNLHCELVGLDIQDEMGRHEVGHIDNSMKIPLNNGAGCRFEGQFSINKVPGNFHVSTHSATAQPQNPDMTHVIHKLSFGDTLQVQNIHGAFNALGGADRLTSNPLASHDYILKIVPTVYEDKSGKQRYSYQYTVANKEYVAYSHTGRIIPAIWFRYDLSPITVKYTERRQPLYRFITTICAIIGGTFTVAGILDSCIFTASEAWKKIQLGKMH | Function: Possible role in transport between endoplasmic reticulum and Golgi.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32592
Sequence Length: 290
Subcellular Location: Endoplasmic reticulum membrane
|
Q9DC16 | MPFDFRRFDIYRKVPKDLTQPTYTGAIISICCCLFILFLFLSELTGFITTEVVNELYVDDPDKDSGGKIDVSLNISLPNLHCELVGLDIQDEMGRHEVGHIDNSMKIPLNNGAGCRFEGQFSINKVPGNFHVSTHSATAQPQNPDMTHTIHKLSFGDTLQVQNVHGAFNALGGADRLTSNPLASHDYILKIVPTVYEDKSGKQRYSYQYTVANKEYVAYSHTGRIIPAIWFRYDLSPITVKYTERRQPLYRFITTICAIIGGTFTVAGILDSCIFTASEAWKKIQLGKIH | Function: Possible role in transport between endoplasmic reticulum and Golgi.
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32562
Sequence Length: 290
Subcellular Location: Endoplasmic reticulum membrane
|
Q6NS19 | MPFDFRRFDIYRKVPKDLTQPTYTGAIISICCCLFITFLFLSELTGFIANEIVNELYVDDPDKDSGGKIDVTLNVTLPNLPCEVVGLDIQDEMGRHEVGHIDNSMKIPINNAYGCRFEGLFSINKVPGNFHVSTHSAIAQPANPDMRHIIHKLSFGNTLQVDNIHGAFNALGGADKLASKALESHDYVLKIVPTVYEDLNGKQQFSYQYTVANKAYVAYSHTGRVVPAIWFRYDLSPITVKYTERRQPMYRFITTVCAIIGGTFTVAGILDSFIFTASEAWKKIQLGKMQ | Function: Possible role in transport between endoplasmic reticulum and Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32533
Sequence Length: 290
Subcellular Location: Endoplasmic reticulum membrane
|
Q7T2D4 | MRRLNKKKALNFVRELDAFPKVPESYVETTASGGTVSLLAFTAMALLAFFEFFVYRDTWMKYEYEVDKDFTSKLRINIDITVAMRCQFVGADVLDLAETMVASDGLVYEPVVFDLSPQQRLWHRTLLLIQGRLREEHSLQDVLFKNVMKGSPTALPPREDDPNQPLNACRIHGHLYVNKVAGNFHITVGKAIPHPRGHAHLAALVSHETYNFSHRIDHLSFGEEIPGILNPLDGTEKVSADHNQMFQYFITIVPTKLQTYKVYADTHQYSVTERERVINHAAGSHGVSGIFMKYDISSLMVKVTEQHMPFWQFLVRLCGIIGGIFSTTGMLHNLVGFCVDVVCCRFKLGVYKPKSMSDFDGQINSLTPLLSENAEQ | Function: Possible role in transport between endoplasmic reticulum and Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42590
Sequence Length: 376
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
|
Q96RQ1 | MRRLNRKKTLSLVKELDAFPKVPESYVETSASGGTVSLIAFTTMALLTIMEFSVYQDTWMKYEYEVDKDFSSKLRINIDITVAMKCQYVGADVLDLAETMVASADGLVYEPTVFDLSPQQKEWQRMLQLIQSRLQEEHSLQDVIFKSAFKSTSTALPPREDDSSQSPNACRIHGHLYVNKVAGNFHITVGKAIPHPRGHAHLAALVNHESYNFSHRIDHLSFGELVPAIINPLDGTEKIAIDHNQMFQYFITVVPTKLHTYKISADTHQFSVTERERIINHAAGSHGVSGIFMKYDLSSLMVTVTEEHMPFWQFFVRLCGIVGGIFSTTGMLHGIGKFIVEIICCRFRLGSYKPVNSVPFEDGHTDNHLPLLENNTH | Function: Possible role in transport between endoplasmic reticulum and Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42549
Sequence Length: 377
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
|
Q803I2 | MDALNKLKQFDAYPKTLEDFRIKTCGGATVTIISGLIMLILFFSELQYYLTKEVHPELFVDTSRGDKLRINIDVIFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKQRLDKDGQPVTTEAEKHDLGKEEEGVFDPSTLDPDRCESCYGAETDDLKCCNTCDDVREAYRRRGWAFKTPDTIEQCKREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHDLQSFGLDNINMTHFIKHLSFGKDYPGIVNPLDDTNVAAPQASMMYQYFVKIVPTIYVKGDGEVVKTNQFSVTRHEKIANGLIGDQGLPGVFVLYELSPMMVKFTEKQRSFTHFLTGVCAIIGGVFTVAGLIDSLIYHSARAIQKKIELGKAS | Function: Possible role in transport between endoplasmic reticulum and Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43139
Sequence Length: 383
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
|
Q54DW2 | MLISQLKKFDAYPKTVDDFRVKTYTGAIVSIIGGVFILWLFFSQVTLYFSTDIHHELFVDTTRGEKLKINMDITFHHLPCAYLSLDAMDVSGEHQFDVAHNIFKKRLSPTGQPIIEAPPIREEEINKKESVKDNNDVVGCGSCYGAEDPSKGIGCCNTCEEVRVAYSKKGWGLDPSGIPQCIREGFTKNLVEQNGEGCQVYGFILVNKVAGNFHFAPGKSFQQHHMHVHDLQPFKDGSFNVSHTINRLSFGNDFPGIKNPLDDVTKTEMVGVGMFQYFVKVVPTIYEGLNGNRIATNQYSVTEHYRLLAKKGEEPSGLPGLFFMYDLSPIMMKVSERGKSFASFLTNVCAIIGGVFTVFGIFDSFIYYSTKNLQKKIDLGKTF | Function: Possible role in transport between endoplasmic reticulum and Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42921
Sequence Length: 383
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
|
Q9Y282 | MEALGKLKQFDAYPKTLEDFRVKTCGGATVTIVSGLLMLLLFLSELQYYLTTEVHPELYVDKSRGDKLKINIDVLFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKQRLDKDGIPVSSEAERHELGKVEVTVFDPDSLDPDRCESCYGAEAEDIKCCNTCEDVREAYRRRGWAFKNPDTIEQCRREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHDLQSFGLDNINMTHYIQHLSFGEDYPGIVNPLDHTNVTAPQASMMFQYFVKVVPTVYMKVDGEVLRTNQFSVTRHEKVANGLLGDQGLPGVFVLYELSPMMVKLTEKHRSFTHFLTGVCAIIGGMFTVAGLIDSLIYHSARAIQKKIDLGKTT | Function: Possible role in transport between endoplasmic reticulum and Golgi. Positively regulates trafficking of the secretory proteins SERPINA1/alpha1-antitrypsin and HP/haptoglobin .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43222
Sequence Length: 383
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
|
Q4R8X1 | MEALGKLKQFDAYPKTLEDFRVKTCGGATVTIVSGLLMLLLFLSELQYYLTTEVHPELYVDKSRGDKLKINIDVLFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKQRLDKDGTPVSSEAERHELGKVEVTVFGPDSLDPDRCESCYGAEAEDIKCCNTCEDVREAYRRRGAFKNPDTIEQCRREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHDLQSFGLDNINMTHYIQHLSFGEDYPGIVNPLDHTNVTAPQASMMFQYFVKVVPTVYMKVDGEVLRTNQFSVTRHEKVANGLLGDQGLPGVFVLYELSPMMVKLTEKHRSFTHFLTGVCAIIGGMFTVAGLIDSLIYHSARAIQKKIDLGKTT | Function: Possible role in transport between endoplasmic reticulum and Golgi. Positively regulates trafficking of the secretory proteins alpha1-antitrypsin/SERPINA1 and HP/haptoglobin (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42966
Sequence Length: 382
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
|
Q9CQE7 | MEALGKLKQFDAYPKTLEDFRVKTCGGATVTIVSGLLMLLLFLSELQYYLTTEVHPELYVDKSRGDKLKINIDVLFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKKRLDKDGVPVSSEAERHELGKVEVTVFDPNSLDPNRCESCYGAESEDIKCCNSCEDVREAYRRRGWAFKNPDTIEQCRREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHDLQSFGLDNINMTHYIKHLSFGEDYPGIVNPLDHTNVTAPQASMMFQYFVKVVPTVYMKVDGEVLRTNQFSVTRHEKVANGLLGDQGLPGVFVLYELSPMMVKLTEKHRSFTHFLTGVCAIIGGMFTVAGLIDSLIYHSARAIQKKIDLGKTT | Function: Possible role in transport between endoplasmic reticulum and Golgi. Positively regulates trafficking of the secretory proteins alpha1-antitrypsin/SERPINA1 and HP/haptoglobin (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43208
Sequence Length: 383
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
|
Q6NVS2 | MESLHRLRQFDAYPKTLEDFRVKTCGGALVTVISGLIMLILFFSELQYYLTKEIYPELFVDKSRGDKLKINIDVIFPHMPCAYLSIDAMDVAGEQQLDVEHNLFKQRLDKDKKPVTSEADRHELGKSEEHVVFDPKSLDPNRCESCYGAETDDFSCCNTCDDVREAYRRRGWAFKTPDSIEQCKREGFSQKMQEQKNEGCQVYGFLEVNKVAGNFHFAPGKSFQQSHVHVHDLQSFGLDNINMTHEIRHLSFGRDYPGLVNPLDGSSVAAMQSSMMFQYFVKIVPTVYVKVDGEVLRTNQFSVTRHEKMTNGLIGDQGLPGVFVLYELSPMMVKLTEKHRSFTHFLTGVCAIIGGVFTVAGLIDSLVYYSTRAIQKKIELGKAT | Function: Possible role in transport between endoplasmic reticulum and Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43621
Sequence Length: 384
Subcellular Location: Endoplasmic reticulum-Golgi intermediate compartment membrane
|
Q9P6K6 | MMSFGSFVYIACLLLNGANMLLQIFCVIMFSDLEMDYINPIDLCNKLNDLVMPEIISHTLVTLLLLLGKKWLLFLANLPLLVFHANQVIHKTHILDATEIFRQLGRHKRDNFIKVTFYLIMFFTLLYCMVMSLIQEE | Function: Regulates export of the secretory proteins from the endoplasmic reticulum in COPII-coated vesicles.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15990
Sequence Length: 137
Subcellular Location: Endoplasmic reticulum
|
P53173 | MGAWLFILAVVVNCINLFGQVHFTILYADLEADYINPIELCSKVNKLITPEAALHGALSLLFLLNGYWFVFLLNLPVLAYNLNKIYNKVQLLDATEIFRTLGKHKRESFLKLGFHLLMFFFYLYRMIMALIAESGDDF | Function: Could regulate export of the bud site and axial growth sites selection protein AXL2 and possibly other secretory proteins from the endoplasmic reticulum in COPII-coated vesicles. Seems to be required for axial budding pattern in haploid cells.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15930
Sequence Length: 138
Subcellular Location: Endoplasmic reticulum membrane
|
Q8GXX0 | MGEKPWQPLLQSFEKLSNCVQTHLSNFIGIKNTPPSSQSTIQNPIISLDSSPPIATNSSSLQKLPLKDKSTGPVTKEDLGRATWTFLHTLAAQYPEKPTRQQKKDVKELMTILSRMYPCRECADHFKEILRSNPAQAGSQEEFSQWLCHVHNTVNRSLGKLVFPCERVDARWGKLECEQKSCDLHGTSMDF | Function: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation . Oxidizes thioredoxin in vitro . Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space. Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine residues in MIA40 in an oxidized state (By similarity).
PTM: Contains three disulfide bonds; one catalytic disulfide (Cys-119 to Cys-122), one structural disulfide (Cys-148 to Cys-165), and one shuttle disulfide (Cys-177 to Cys-182).
Catalytic Activity: O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'
Sequence Mass (Da): 21600
Sequence Length: 191
Subcellular Location: Mitochondrion
EC: 1.8.3.2
|
Q10Q80 | MPPPAWGWGSNPLEPVVHTVAAFSRRLLIAPDAAPDEARLRPLLSLSLSPPPTPPSPPPPPPEVLKKDSKAAPLTKEEVGRATWMLLHTIAAQFPDEPTRQQRRDARELMAIISRLYPCKECAEHFKEVLKANPVQAGSQAEFSQWLCYVHNVVNRSLGKPIFPCQRVNARWGKLDCPERSCDLEGSNDIIPNR | Function: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation (By similarity). Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space. Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine residues in MIA40 in an oxidized state (By similarity).
PTM: Contains three disulfide bonds; one catalytic disulfide (Cys-119 to Cys-122), one structural disulfide (Cys-148 to Cys-165), and one shuttle disulfide (Cys-177 to Cys-182).
Catalytic Activity: O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'
Sequence Mass (Da): 21604
Sequence Length: 194
Subcellular Location: Mitochondrion
EC: 1.8.3.2
|
O14144 | MVFGKRYRDKETGIIYDENGRPCKTCNIFSSFRNVAQQPNSSTVPEVKSNTQLESKQSSIDCNTNAIPDSVSFPRLPDVAELGRSTWTFLHAMAANFPKNPTPTQQNDMSSFLYNFSKFYPCWSCAEDLRIWMAKYGNSPRVDSRESLCEWICEAHNDVNERLGKPLFNCQVWSKKASELAD | Function: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS) (By similarity).
Catalytic Activity: O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'
Sequence Mass (Da): 20769
Sequence Length: 182
Subcellular Location: Mitochondrion intermembrane space
EC: 1.8.3.2
|
P27882 | MKAIDKMTDNPPQEGLSGRKIIYDEDGKPCRSCNTLLDFQYVTGKISNGLKNLSSNGKLAGTGALTGEASELMPGSRTYRKVDPPDVEQLGRSSWTLLHSVAASYPAQPTDQQKGEMKQFLNIFSHIYPCNWCAKDFEKYIRENAPQVESREELGRWMCEAHNKVNKKLRKPKFDCNFWEKRWKDGWDE | Function: FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS). Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine residues in MIA40 in an oxidized state. Reduced ERV1 is reoxidized by cytochrome c. Required for the maturation of cytoplasmic, but not of mitochondrial Fe/S proteins.
Catalytic Activity: O2 + 2 R'C(R)SH = H2O2 + R'C(R)S-S(R)CR'
Sequence Mass (Da): 21639
Sequence Length: 189
Subcellular Location: Mitochondrion intermembrane space
EC: 1.8.3.2
|
Q9LJG3 | MADNLNLVSVLGVLLVLTIFHNPIIVYAGEGVPNVALFTFGDSYYDAGNKVFLSQRKDLPQTYWPYGKSRDYPNGKFSDGHIVPDFIADFISIPNGVLPPVLKPGVDISRGVSFAVADASILGAPVESMTLNQQVVKFKNMKSNWNDSYIEKSLFMIYIGTEDYLNFTKANPNADASAQQAFVTNVINRLKNDIKLLYSLGASKFVVQLLAPLGCLPIVRQEYKTGNECYELLNDLAKQHNGKIGPMLNEFAKISTSPYGFQFTVFDFYNAVLRRIATGRSLNYRFFVTNTSCCGVGTHNAYGCGKGNVHSKLCEYQRSYFFFDGRHNTEKAQEEMAHLLYGADPDVVQPMTVRELIVYPTGETMREYWEPNNLAIRRRPSRDFYLGLAAYY | Function: Represses or inhibits nitriles production from methionine-derived and from indol-3-ylmethyl glucosinolates. Favors isothiocyanate production.
Sequence Mass (Da): 44060
Sequence Length: 392
Subcellular Location: Secreted
EC: 3.1.1.-
|
Q9NQ30 | MKSVLLLTTLLVPAHLVAAWSNNYAVDCPQHCDSSECKSSPRCKRTVLDDCGCCRVCAAGRGETCYRTVSGMDGMKCGPGLRCQPSNGEDPFGEEFGICKDCPYGTFGMDCRETCNCQSGICDRGTGKCLKFPFFQYSVTKSSNRFVSLTEHDMASGDGNIVREEVVKENAAGSPVMRKWLNPR | Function: Involved in angiogenesis; promotes angiogenic sprouting. May have potent implications in lung endothelial cell-leukocyte interactions.
PTM: May contain intrachain disulfide bonds.
Sequence Mass (Da): 20095
Sequence Length: 184
Subcellular Location: Secreted
|
Q9QYY7 | MKSLLLLTTLLVPLHLGMAWSAKYAVDCPEHCDKTECRSSLRCKRTVLDDCGCCQVCAAGPGETCYRTVSGMDGVKCGPGLKCHFYSEEDDFGDEFGICKDCPYGTFGMECKETCNCQSGICDRVTGRCLDFPFFQYAAAKSPSRTSASHTERDSASGDGNAVREEIGEGNAARPSVMKWLNPR | Function: Involved in angiogenesis; promotes angiogenic sprouting. May have potent implications in lung endothelial cell-leukocyte interactions (By similarity).
PTM: O-glycosylated; contains chondroitin sulfate and dermatan sulfate.
Sequence Mass (Da): 20043
Sequence Length: 184
Subcellular Location: Secreted
|
P97682 | MKSLLLLTTLLIPLHLGMAWSAKYAVDCPEHCDNTECRSSLRCKRTVLDDCGCCQVCAAGPGETCYRTVSGMDGVKCGPGLKCHFYSEEDDFGDEFGVCKDCPYGTFGMDCKETCNCQSGICDRVTGRCLDFPFFQYAAAKSPSRTSASQTERDAASGDGNAVREEIGDRNAARPSVMKWLNPR | Function: Involved in angiogenesis; promotes angiogenic sprouting. May have potent implications in lung endothelial cell-leukocyte interactions (By similarity).
PTM: O-glycosylated; contains chondroitin sulfate and dermatan sulfate.
Sequence Mass (Da): 20075
Sequence Length: 184
Subcellular Location: Secreted
|
Q01068 | MVMEMSKTYQYRKVMKPLLERKRRARINKCLDDLKDLMVECLQQEGEHVTRLEKADILELTVDHMRKLKQRGGLSLQGVVAGVGSPPTSTSTAHVESFRSGYVHAADQITQVLLQTQQTDEIGRKIMKFLSTRLIELQTQLLQQQQQQQQHQQQQIPQSSGRLAFPLLGGYGPAAAAAAISYSSFLTSKDELIDVTSVDGNALSETASVSSQESGASEPVWRPW | Function: Transcriptional repressor of genes that require a bHLH protein for their transcription. May serve as a transcriptional regulator of the Achaete-scute complex (AS-C) genes. Belongs to notch signaling pathway and depends on Su(H) for transcriptional activation.
Sequence Mass (Da): 24983
Sequence Length: 224
Domain: Has a particular type of basic domain (presence of a helix-interrupting proline) that binds to the N-box (CACNAG), rather than the canonical E-box (CANNTG).
Subcellular Location: Nucleus
|
P13097 | MATKYEMSKTYQYRKVMKPLLERKRRARINKCLDELKDLMAECVAQTGDAKFEKADILEVTVQHLRKLKESKKHVPANPEQSFRAGYIRAANEVSRALASLPRVDVAFGTTLMTHLGMRLNQLEQPMEQPQAVNTPLSIVCGSSSSSSTYSSASSCSSISPVSSGYASDNESLLQISSPGQVWRPW | Function: Participates in the control of cell fate choice by uncommitted neuroectodermal cells in the embryo. Transcriptional repressor. Binds DNA on N-box motifs: 5'-CACNAG-3'.
Sequence Mass (Da): 20687
Sequence Length: 186
Domain: The orange domain and the basic helix-loop-helix motif mediate repression of specific transcriptional activators, such as basic helix-loop-helix protein dimers.
Subcellular Location: Nucleus
|
P13098 | MEYTTKTQIYQKVKKPMLERQRRARMNKCLDNLKTLVAELRGDDGILRMDKAEMLESAVIFMRQQKTPKKVAQEEQSLPLDSFKNGYMNAVNEVSRVMASTPGMSVDLGKSVMTHLGRVYKNLQQFHEAQSAADFIQNSMDCSSMDKAPLSPASSGYHSDCDSPAPSPQPMQQPLWRPW | Function: Participates in the control of cell fate choice by uncommitted neuroectodermal cells in the embryo . Transcriptional repressor . Binds DNA on N-box motifs: 5'-CACNAG-3' . Part of the Notch signaling pathway .
Sequence Mass (Da): 20303
Sequence Length: 179
Domain: The orange domain and the basic helix-loop-helix motif mediate repression of specific transcriptional activators, such as basic helix-loop-helix protein dimers.
Subcellular Location: Nucleus
|
Q8BK48 | MPLYKLLGWLNAVACGVLLLVLHVQGQDSASPIRNTHTGQVRGSLVHVKDTDIAVHTFLGIPFAKPPVGPLRFAPPEAPEPWSGVRDGTSHPNMCLQNDNLMGSEDLKMMNLILPPISMSEDCLYLNIYVPAHAHEGSNLPVMVWIHGGALTVGMASMYDGSMLAATEDVVVVAIQYRLGVLGFFSTGDQHAKGNWGYLDQVAALRWVQQNIVHFGGNPDRVTIFGESAGGTSVSSHVVSPMSQGLFHGAIMESGVAVLPDLISSSSEMVHRIVANLSGCAAVNSETLMCCLRGKNEAEMLAINKVFKIIPGVVDGEFLPKHPQELMASKDFHPVPSIIGINNDEYGWILPTIMDPAQKIEEITRKTLPAVLKSTALKMMLPPECGDLLMEEYMGDTEDPETLQAQFREMKGDFMFVIPALQVAHFQRSHAPVYFYEFQHRPSFFKDFRPPYVKADHGDEIFLVFGYQFGNIKLPYTEEEEQLSRRIMKYWANFARHGNPNSEGLPYWPVMDHDEQYLQLDIQPSVGRALKARRLQFWTKTLPQKIQELKGSQERHKEL | Function: Carboxylesterase that catalyzes the hydrolysis of pyrethroids pesticides. Hydrolyzes trans-permethrin at a rate about 22-fold higher than cis-permethrin. Also hydrolyzes trans-cypermethrin. Hydrolyzes retinyl esters (By similarity).
PTM: Glycosylated.
Catalytic Activity: (-)-trans-permethrin + H2O = (1S,3R)-3-(2,2-dichlorovinyl)-2,2-dimethylcyclopropanecarboxylate + (3-phenoxyphenyl)methanol + H(+)
Sequence Mass (Da): 62318
Sequence Length: 559
Subcellular Location: Microsome
EC: 3.1.1.88
|
G3V7J5 | MAQTRAWKSIMPLESLPGWLNAVVWGLLLLFCQVQGQDSASPIRNTHTGQVRGSFVHVKDTKSGVHTFLGIPFAKPPIGPLRFAPPEPPEPWSGVRDGTSHPAMCLQNIDGLNLENLKIKMSRSPVSMSEDCLYLSIYTPAHTHKDSNLPVMVWIHGGGLCWGMASTYDGSMLAAIEDVVVVTIQYRLGILGFFSTGDEHARGNWGYLDQVAALRWVQQNIVHFGGNPDRVTIFGESAGGISVSSHVVSPMSQGLFHGAIMESGVALLPNLISNTSEVIYTMVANLSGCEPVDSEALMSCLREKSEEEMLAINNIVRTISGVVDGKFLPRHPLELLASVDFHPVPSIIGINSDEYGWIIPMLHPDSTMKEINRETMRAVLKNTAVQMMLPPECSDLLMEEYMGDTEDSKTLQIQFNEMMGDFIFVIPALQVAHFQRSHAPVYFYEFQHQSNFLKDIRPPHVKADHGDELPYVIGYLFWDMKFVFTEEEKLLSRKMIKYWANFARHGNPNSEGLPYWPALDHDEQYLQLDIQPVVGRALKARRLKFWTKTLPQKIQELKGSQDNHTEL | Function: Carboxylesterase that catalyzes the hydrolysis of pyrethroids pesticides. Hydrolyzes trans-permethrin at a rate about 22-fold higher than cis-permethrin. Also hydrolyzes trans-cypermethrin (By similarity). Hydrolyzes retinyl esters .
Catalytic Activity: all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + H(+) + hexadecanoate
Sequence Mass (Da): 63583
Sequence Length: 567
Subcellular Location: Microsome
EC: 3.1.1.88
|
Q07085 | MGGFLSHLTPEQNVEALKASCGPVRGNIYKHDDVIVDGYLGIPYAKPPVGELRFKKPVTVDVWTEIKDCYKYGPACVQTGGFEQIAGPRTPTPEEAGCLTLNVFTPRNASSEFKNGRPVMVYIHGGGYELCASSDFCAYSLSGTLPLKDVVVVSINYRLGVFGFLTTGDNVCPGNFGLWDQTLALKWVQKHISSFGGDPNCVTVFGQSAGGASTDLLSLSPHSRDLFQRFIPISGTAHCDFAIRASENQAKIFREFAEFHGFSGRDSSALFKWYQEQSPETLSNVKGYKKSISGFLTFIPNLDGDFFPKPLDELRKEAPKKQMMTGVTEYEGLMLASMNPAFSPADVGLTLMPQGIYGKDVVSNPDEIQKIFYEKYVEGVDKSDELAMRKKLCEALGDEFFNVGVIQAAKNAAKHGNEVYFYTFEYVNPDSFGMWDGMMPFKAAVHCTELRYLLGEGVYSKFEPTEEDRKVMETTTTLFSNFAKYGNPNGKGATAEIWEKYSLNRPERHYRISYPKCEMRDVYHEGRIQFLEKIDGDSDKYQELVYGKKKSAKI | Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H(+)
Location Topology: Lipid-anchor
Sequence Mass (Da): 61825
Sequence Length: 554
Subcellular Location: Cytoplasm
EC: 3.1.1.1
|
P21370 | KLLTDQDMQDDIFTPFGPTVEPYLTEQCMIPKEPFEMARTAWGDRIDIMIGGTSEEGLLLLQKIKLHPELLSHPHLFLGNVPPNLKISMEKRIEFAAKLKQRYYPDSSPSMENNLGYVHMMSDRVFWHGLHRTILARGARSRARTFVYRICLDSEFYNHYRIMMIDPKLRGTAHADELSYLFSNFTQQVPGKETFEYRGLQTLVDVFTAFVINGD | Function: Overproduction of nonspecific esterases is a common mechanism of resistance to organophosphate insecticides.
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H(+)
Sequence Mass (Da): 24937
Sequence Length: 215
EC: 3.1.1.1
|
O00748 | MRLHRLRARLSAVACGLLLLLVRGQGQDSASPIRTTHTGQVLGSLVHVKGANAGVQTFLGIPFAKPPLGPLRFAPPEPPESWSGVRDGTTHPAMCLQDLTAVESEFLSQFNMTFPSDSMSEDCLYLSIYTPAHSHEGSNLPVMVWIHGGALVFGMASLYDGSMLAALENVVVVIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIMESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKPFKMIPGVVDGVFLPRHPQELLASADFQPVPSIVGVNNNEFGWLIPKVMRIYDTQKEMDREASQAALQKMLTLLMLPPTFGDLLREEYIGDNGDPQTLQAQFQEMMADSMFVIPALQVAHFQCSRAPVYFYEFQHQPSWLKNIRPPHMKADHGDELPFVFRSFFGGNYIKFTEEEEQLSRKMMKYWANFARNGNPNGEGLPHWPLFDQEEQYLQLNLQPAVGRALKAHRLQFWKKALPQKIQELEEPEERHTEL | Function: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs . Shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine . Hydrolyzes aspirin, substrates with large alcohol group and small acyl group and endogenous lipids such as triacylglycerol . Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins .
PTM: Glycosylated.
Catalytic Activity: cocaine + H2O = benzoate + ecgonine methyl ester + H(+)
Sequence Mass (Da): 61807
Sequence Length: 559
Subcellular Location: Endoplasmic reticulum lumen
EC: 3.1.1.84
|
Q53547 | MTEPLILQPAKPADACVIWLHGLGADRYDFMPVAEALQESLLTTRFVLPQAPTRPVTINGGYEMPSWYDIKAMSPARSISLEELEVSAKMVTDLIEAQKRTGIDASRIFLAGFSQGGAVVFHTAFINWQGPLGGVIALSTYAPTFGDELELSASQQRIPALCLHGQYDDVVQNAMGRSAFEHLKSRGVTVTWQEYPMGHEVLPQEIHDIGAWLAARLG | Function: Hydrolyzes carboxylic ester bonds with relatively broad substrate specificity.
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H(+)
Sequence Mass (Da): 23880
Sequence Length: 218
EC: 3.1.1.1
|
P14943 | QDSASPIRNTHTGQVRGSLVHVEGTDAGVHTFLGIPFAKPPLGPLRFAPPEPAEAWSGVRDGTSLPAMCLQNLAIMDQDVLLLHFTPPSIPMSEDCLYLNIYSPAHAREGSDLPVMVWIHGGGLTMGMASMYDGSALAAFEDVVVVTIQYRLGVLGFFSTGDQHATGNHGYLDQVAALRWVQKNIAHFGGNPGRVTIFGESAGGTSVSSHVLSPMSQGLFHGAIMESLVALLPGLITSSSEVVSTVVANLSRCGQVDSETLVRCLRAKSEEEMLAITQVFMLIPGVVDGVFLPRHPEELLALADFQPVPSIIGINNDEYGWIIPKLLLAIDPQEERDRQAMREIMHQATKQLMLPPALGDLLMDEYMGSNEDPKHLMAQFQEMMADAMFVMPALRVAHLQRSHAPTYFYEFQHRPSFTKDLRPPHVRADHGDEVVFVFRSHLFGSKVPLTEEEELLSRRVMKYWANFARNRNPNGEGLAHWPLFDLDQRYLQLNMQPAVGQALKARRLQFWTHTLPQRVQELRGTEQKHTEL | Function: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes of 2-arachidonoylglycerol and prostaglandins (By similarity).
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H(+)
Sequence Mass (Da): 59059
Sequence Length: 532
Subcellular Location: Endoplasmic reticulum lumen
EC: 3.1.1.84
|
Q6UWW8 | MERAVRVESGVLVGVVCLLLACPATATGPEVAQPEVDTTLGRVRGRQVGVKGTDRLVNVFLGIPFAQPPLGPDRFSAPHPAQPWEGVRDASTAPPMCLQDVESMNSSRFVLNGKQQIFSVSEDCLVLNVYSPAEVPAGSGRPVMVWVHGGALITGAATSYDGSALAAYGDVVVVTVQYRLGVLGFFSTGDEHAPGNQGFLDVVAALRWVQENIAPFGGDLNCVTVFGGSAGGSIISGLVLSPVAAGLFHRAITQSGVITTPGIIDSHPWPLAQKIANTLACSSSSPAEMVQCLQQKEGEELVLSKKLKNTIYPLTVDGTVFPKSPKELLKEKPFHSVPFLMGVNNHEFSWLIPRGWGLLDTMEQMSREDMLAISTPVLTSLDVPPEMMPTVIDEYLGSNSDAQAKCQAFQEFMGDVFINVPTVSFSRYLRDSGSPVFFYEFQHRPSSFAKIKPAWVKADHGAEGAFVFGGPFLMDESSRLAFPEATEEEKQLSLTMMAQWTHFARTGDPNSKALPPWPQFNQAEQYLEINPVPRAGQKFREAWMQFWSETLPSKIQQWHQKQKNRKAQEDL | Function: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows low catalytic efficiency for hydrolysis of CPT-11 (7-ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin), a prodrug for camptothecin used in cancer therapeutics.
PTM: N-glycosylated.
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H(+)
Sequence Mass (Da): 62282
Sequence Length: 571
Subcellular Location: Endoplasmic reticulum lumen
EC: 3.1.1.1
|
P94132 | MITIEREAMEFDVVIVGAGPAGLSAAIKIRQLAIENNLPDLSVCVVEKGSEVGAHILSGAVLEPRAINELFPNWKEEGAPLNVPVTEDKTYFLMSDEKSQEAPHWMVPKTMHNDGNYVISLGNVVRWLGQKAEELEVSIFPGFAAAEILYHADGTVKGIQTGDMGIGKDGEPTHNFAPGYELHAKYTLFAEGCRGHLGKRLINKFNLDQDADPQHYGIGIKELWEIDPAKHKPGLVMHGSGWPLSETGSSGGWWLYHAENNQVTLGMIVDLSYENPHMFPFMEMQRWKTHPLIKQYLEGGKRISYGARAVVKGGLNSLPKLTFPGGCLIGDDAGFLNFAKIKGSHTAMKSGMLCGEAVFEAIARGVDKGGDLAIARVVEGEDLFDKELTTYTQKFDKSWLKEELHRSRNFGPAMHKFGLWIGGAFNFVDQNIFKVPFTLHDLQPDYSALKTQDQATFKPNYPKPDGKLTFDRLSSVFVSNTVHEENQPSHLKLTDASIPVAVNLPRWDEPAQRYCPAGVYEIVDEGEGNKRFQINAANCVHCKTCDIKDPSQNITWVTPEGGGGPNYPNM | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 62996
Sequence Length: 570
EC: 1.5.5.1
|
Q2KIG0 | MQVLLARLACPVYQCFHAIKIKKNYLPLCATRWSSTSVVPRITTHYTVYPRDQDKRWEGVNMERFAEEADVVIVGAGPAGLSAAARLKQLAAQHEKDIRVCLVEKAAQIGAHTLSGACLDPRALQELFPDWKEKGAPLNTPVTEDRFGILTEKYRIPVPILPGLPMNNHGNYIVRLGHLVSWMGEQAEALGVEVYPGYAAAEVLFHEDGSVKGIATNDVGIQKDGAPKTTFERGLELHAKVTIFAEGCHGHLAKQLYRKFDLRANCEPQTYGIGLKELWVIDEKKWKPGRVDHTVGWPLDRHTYGGSFLYHLNEGEPLVALGFVVGLDYQNPYLSPFREFQRWKHHPSIQPTLEGGKRIAYGARALNEGGLQCIPKLTFPGGLLIGCSPGFMNVPKIKGTHTAMKSGILAAESIFNQLTNENLQSKTIGLDVTEYEDNLKKSWVWKELYAVRNIRPSCHSILGVYGGMIYTGIFYWIFRGMEPWTLKHKGSDSDKLKPAKDCTPIEYPKPDGQISFDLLSSVALSGTNHEHDQPAHLTLKDDSVPVNRNLSIYDGPEQRFCPAGVYEFVPVEQGDGFRLQINAQNCVHCKTCDIKDPSQNINWVVPEGGGGPAYNGM | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 68612
Sequence Length: 617
Subcellular Location: Mitochondrion inner membrane
EC: 1.5.5.1
|
Q11190 | MRISGVTLFRVSSQLRNVVNGQWTTTHYTVKDRSTDPRWKDVDLARESDVYDVVIVGGGPSGLSAAIRLRQLAEKAQKELRVCVVEKASVIGGHTLSGAVIETRALDELIPNWKELGAPVYQQVTSESIAILTESGRIPVPVLPGVPLANHGNYIVRLGKVVQWLGEQAEAAGVEVWPEIAASEVLYNEDGSVKGIATSDVGIGKDGAPKDGFARGMEFHAKCTIFAEGCRGHLSKQVLDKFDLRTHAMTYGIGLKELWEIDPAKHRPGYVEHTMGWPLNVDQYGGSFLYHIEDQGQPLVSVGFVVALDYANPNLNPYKEFQKYKTHPSISKQLEGGKRIGYGARALNEGGFQSIPKLHFPGGCLVGCSAGFLNVAKLKGTHNAMKSGMVAAESIFEDIQQKGEDVQTIDPATYDKNIRDTYVVKELKATRNIRPSFNTSLGYIGGLIYSGIFYVFGRGIEPWTLGHGKKDNEKLIPVKDAKEIDYPKPDGKLTFDLLTSVSLTGTNHTEDQPAHLTLKNDQVPLDVNLAVYGGPEARFCPAGVYEFVPSEADESKKRLQINAQNCIHCKTCDIKDPQQNINWVTPEGGGGPKYEGM | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 65335
Sequence Length: 597
Subcellular Location: Mitochondrion inner membrane
EC: 1.5.5.1
|
Q54XM6 | MLKSFSLIGKNITKNVSLSSSNKFLFGKNHQNMKSIYSSIRFFSSEQELPPRDSDQFDVVIVGAGPSGLSTAIRLKQLSEKAGKDLRVCVVEKGSEVGSHILSGAVMDPKALNELIPDWKEKGAPLITEVKQDKFYFLTENRSLRLPTPRLMHNEGNYIISLGNVVRWLGEQAESMGVEVYPSFAASEVLYHDNGAVRGIATNDMGIAKDGSLTSNFTRGMELNARLTIFAEGCRGSLTKGLFEKFNLRDECEPQTFGLGIKETWEIKPEKHQQGLVIHTLGYPLSDELLGGSFIYHAENNTVNLGLVVGLDYSNPYLNPYQEFQKLKLHPMVKDMLEGGTCIQYGARTINEGGFQSIPKLVFPGGALVGCTAGFVHVPKVKGSHYAMKTGILAAEAAFPQLISQQEKEQEQEQDKPSVEPLLINEYPEELKKSWVWKELREVRNYRPSLHWGTIPGLIYGALEMYIFRGHTPWTLSNGKPDNERLKPAAECKKIEYKKPDGQITFDLMTSVMRSGTNHEENQPIHLKVRDMEVAKKVNRDIYDGPEGRFCPAGVYEWVEGEKGEKELVRNSVFCLHCKTCDIKDPTQNIDFTVPEGGGGPKYGAM | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 67634
Sequence Length: 606
Subcellular Location: Mitochondrion inner membrane
EC: 1.5.5.1
|
Q16134 | MLVPLAKLSCLAYQCFHALKIKKNYLPLCATRWSSTSTVPRITTHYTIYPRDKDKRWEGVNMERFAEEADVVIVGAGPAGLSAAVRLKQLAVAHEKDIRVCLVEKAAQIGAHTLSGACLDPGAFKELFPDWKEKGAPLNTPVTEDRFGILTEKYRIPVPILPGLPMNNHGNYIVRLGHLVSWMGEQAEALGVEVYPGYAAAEVLFHDDGSVKGIATNDVGIQKDGAPKATFERGLELHAKVTIFAEGCHGHLAKQLYKKFDLRANCEPQTYGIGLKELWVIDEKNWKPGRVDHTVGWPLDRHTYGGSFLYHLNEGEPLVALGLVVGLDYQNPYLSPFREFQRWKHHPSIRPTLEGGKRIAYGARALNEGGFQSIPKLTFPGGLLIGCSPGFMNVPKIKGTHTAMKSGILAAESIFNQLTSENLQSKTIGLHVTEYEDNLKNSWVWKELYSVRNIRPSCHGVLGVYGGMIYTGIFYWILRGMEPWTLKHKGSDFERLKPAKDCTPIEYPKPDGQISFDLLSSVALSGTNHEHDQPAHLTLRDDSIPVNRNLSIYDGPEQRFCPAGVYEFVPVEQGDGFRLQINAQNCVHCKTCDIKDPSQNINWVVPEGGGGPAYNGM | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 68495
Sequence Length: 617
Subcellular Location: Mitochondrion inner membrane
EC: 1.5.5.1
|
P55932 | SDIGGSMDYDVVIVGAGGAGLSAAILKQVNP | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 2975
Sequence Length: 31
EC: 1.5.5.1
|
P55931 | MMVPLAKLASPAYQCFHALKIKKNYLPLCATRWSSTCKVPRITTHYTIYPRDQDKRWEGVNMERFAEEADVVIVGAGPAGLSAATRLKQLAAQHEKDLRVCLVEKAAHIGAHTLSGACLDPRAFEELFPDWKEKGAPLNTPVTEDRFGILTEKYRIPVPILPGLPMNNHGNYVVRLGHLVSWMGEQAEALGVEVYPGYAAAEILFHEDGSVKGIATNDVGIQKDGAPKTTFERGLELHAKVTIFAEGCHGHLAKQLYKKFDLRANCEPQTYGIGLKELWVIDEKKWKPGRVDHTVGWPLDRHTYGGSFLYHLNEGEPLLALGFVVGLDYQNPYLSPFREFQRWKHHPSIKPTLEGGKRIAYGARALNEGGFQSIPKLTFPGGLLIGCSPGFMNVPKIKGTHTAMKSGTLAAESIFNQLTSENLQSKTIGLHVTEYEDNLKNSWVWKELYSVRNIRPSCHGILGVYGGMIYTGIFYWIFRGMEPWTLKHKGSDSDQLKPAKDCTPIEYPKPDGQISFDLLSSVALSGTNHEHDQPAHLTLKDDSVPVNRNLSIYDGPEQRFCPAGVYEFVPLEQGDGFRLQINAQNCVHCKTCDIKDPSQNINWVVPEGGGGPAYNGM | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 68632
Sequence Length: 617
Subcellular Location: Mitochondrion inner membrane
EC: 1.5.5.1
|
P87111 | MSYLSRSALARSVGAKHLTGVLRKIGRRGGRSMHVLPLASPSTLLKISSQTLRQDFTVLGARNFHSSSVRLNELTDNLRKLDTIEREVEDVDVCIVGAGPAGLSAAIRIKQQAAKANRDIRVVVLEKAAEPGNHSVSGAVIQPTALDELLPNWRDDPPENCTAVTHDKMKFLIPKLHFPIPVPPAMKNHGNYVMSLAEFTRWLAAKAEEYGVEIYPSFAASEVLYNKDGSVIGVATNDFGVDSKGLPKDNFERGMAFHAPVTLFAEGAHGSLSKSIIKRFNLRGNCEPQTYGLGVKEVWRVPDENFRKGEVAHTLGWPMRNDTYGGGFMYQFGDNYVTVGLVVGLDYPNPYVSPALEFQRMKQNPFFAKVLKGGKCLEYAARALNEGGYQAIPKLVFPGGALIGCSAGFVNVAKIKGTHTAMKSGIVAADAIVDAFGRDAASKPLLLNDYEENLKNTYVFKELYSVRNIRPSFHSFLGNYGGMAYSAVEAYVLKGRVPWTLKHKGGDAKATKSASKYKPINYPKPDNVLSFDIPTSVSRSATMHAENQPCHLFDHRPKDRKSCFETYKGVENKFCPAGVYEYVNDEASSYGKRFVINSQNCVHCKTCDIKDPLQGIQWKTPQGGDGPKYTLT | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 69472
Sequence Length: 632
Subcellular Location: Mitochondrion inner membrane
EC: 1.5.5.1
|
Q08822 | MIKFTNENLIRGIRMTISAKSRHLALGTDMTRKFSLSCRFLNKANLTEEEKELLNEPRARDYVDVCIVGGGPAGLATAIKLKQLDNSSGTGQLRVVVLEKSSVLGGQTVSGAILEPGVWKELFPDEKSDIGIPLPKELATLVTKEHLKFLKGKWAISVPEPSQMINKGRNYIVSLNQVVGYLGEKAEEVGVEVYPGIAVSDLIYDENNAVKGVITKDAGISKSGKPKETFERGMEFWARQTVLAEGCHGSLTKQALAKYDLRKGRQHQTYGLGIKEVWEVKPENFNKGFAAHTMGYPLTNDVYGGGFQYHFGDGLVTVGLVVGLDYKNPYVSPYKEFQKMKHHPYYSKVLEGGKCIAYAARALNEGGLQSVPKLNFPGGVLVGASAGFMNVPKIKGTHTAMKSGLLAAESIFESIKGLPVLEEVEDEDAKMAMFDKEATINLESYESAFKESSIYKELYEVRNIRPSFSGKLGGYGGMIYSGIDSLILKGKVPWTLKFDEKNDGEILEPASKYKPIEYPKPDGVISFDILTSVSRTGTYHDDDEPCHLRVPGQDMVKYAERSFPVWKGVESRFCPAGVYEFVKDEKSPVGTRLQINSQNCIHCKTCDIKAPRQDITWKVPEGGDGPKYTLT | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 69634
Sequence Length: 631
Subcellular Location: Mitochondrion inner membrane
EC: 1.5.5.1
|
O22854 | MHRFLVKLSSSSSPFSNQLRSLKNQRLILPLLPSSKPFTSSSVSPPPSPLNASNRFGYPYSADLFRNLSPLNPNSRILGVNGITSSRCISSEAVRESIEYDVLIVGAGPAGLSAAIRLKQLSQEKNIDLSVCVVEKGAEVGGHIISGNVFEPLALDELLPHWRQEHAPIEIPASSDKFWFLTKDRAFSLPSPFDNKGNYVISLSQLVRWLGGKAEELGTEIYPGFSASEVLFDASDKVVGIATKDMGISKDGSKKENFQPGVDIKGRVTLFAEGCRGSLSERIIKKYKLREEVNAQHQTYALGIKEVWEIDESKHNPGEVIHTLGWPLDPKTYGGSFLYHMNDRQVALGLVVALNYHNPFLNPYEEFQKLKHHPAIKGILEGGTVLQYGARTLNEGGFQSIPYPVFPGGAIIGCSAGFLNVPKIKGTHTAMKSGMLAAEAAFGALHEGLNMNTYWDNLRDSWVWKELYAARNYRPAFEYGLLPGLAISAMEHYVLKGKVPFTLKHGKADHEATDLARKWTPIVYPKPDGVLSFDVPTSLYRSNTNHDHDQPSHLRLRDPKIPEKVNFPEYAAPESRYCPARVYEYIEDEEGKPKLQINAQNCLHCKACDIKDPKQNIEWTVPEGGGGPAYSLM | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Accepts electrons from ETF and reduces ubiquinone. May act downstream of IVD and D2HGDH in the degradation of phytol or chlorophyll during dark-induced senescence and sugar starvation.
Catalytic Activity: a ubiquinone + reduced [electron-transfer flavoprotein] = a ubiquinol + H(+) + oxidized [electron-transfer flavoprotein]
Sequence Mass (Da): 70128
Sequence Length: 633
Subcellular Location: Mitochondrion inner membrane
EC: 1.5.5.1
|
Q0AZ32 | MIFGFHPLEGGYDVPMRVVGANIPYEWLIYVIMLIPVSVFLFGFWKKLEVWLLAKGEIHRNDKIAQRIWSWFVFSFAQARVIRKPLAGWMHAFLFWGFLVLFLAAGIDAMHNMISWPHLEGNFYIGFSWVVDVLGFLALIGVMVLGFVRYFQKPERLNDTKSSDGWIILLIFAILLTGYFIEGLRIAAQIKLSTTMQQIAYERAASPFGWMFASFFGSMSVDAMLMWHRLLWWFHMAIAFLFIALVPFTKLWHIFASMLNYTFRDLEPSANRMVYNIEEAETFGVENIEDFGWKDLLDLDSCIRCGRCQENCPAYNTGKHLNPKITLIQNMKAHLDAKAPYLLAAKASGAEVEEMAMTEEAAAEEVNPMEQSLLYDVVGSETIWDCTNCRACMEHCPMFIEHIPKIVEMRRNLVMWQGDMPGEAQMAFTNMERNYNPWGVGWAGRAGWLDERGVREMVNLLPEDGKEFEYLLYAGCAVSFDDRYKRVGEALVRLLNKAGVSFGYLGTEEYCCGDSARRLGNEYLYQTLVSQNLESFNNYGVKKIIVVCPHGYTALKNEYPQMGGNYEVYHYTEILAKLVAEGKLKPSKPLGVKMTYHDSCFLGRHNGVYDQPRNVLKAAGGQVIEIEKAKEFGFCCGAGGGRMWLEEEAVLKDGIQYKRINDTRTDQLLVPNPEMIVTNCPFCLTMIADGVKAAEAEESTKVFDVAEVLWKAME | Cofactor: Binds 2 [4Fe-4S] clusters per subunit.
Function: Oxidoreductase involved in syntrophic growth of S.wolfei with butyrate. Is presumed to link the electron flow from butyryl-CoA dehydrogenases to the membrane, in conjunction with the electron transfer flavoprotein EtfAB. May transfer electrons to the menaquinone pool of the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81418
Sequence Length: 714
Pathway: Lipid metabolism; butanoate metabolism.
Subcellular Location: Cell membrane
EC: 1.18.-.-
|
Q8Y7U4 | MNEQELKQMIEGILTEMSGGKTTDTVAAVPTKSVVETVVTEGSIPDITEVDIKKQLLVPEPADREGYLKMKQMTPARLGLWRAGPRYKTETILRFRADHAVAQDSVFSYVSEDLVKEMNFIPVNTKCQDKDEYLTRPDLGREFDDEMVEVIRANTTKNAKLQIVVGDGLSSAAIEANIKDILPSIKQGLKMYNLDFDNIIFVKHCRVPSMDKIGEITGADVVCLLVGERPGLVTAESMSAYIAYKPTVGMPEARRTVISNIHSGGTPPVEAGAYIAELIHNMLEKKCSGIDLK | Cofactor: Binds between the large and small subunits.
Function: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12.
Catalytic Activity: ethanolamine = acetaldehyde + NH4(+)
Sequence Mass (Da): 32318
Sequence Length: 293
Pathway: Amine and polyamine degradation; ethanolamine degradation.
Subcellular Location: Bacterial microcompartment
EC: 4.3.1.7
|
Q02SJ2 | MNDKHLPDASAENPWLPLRQLTPARIALGRTGTSLPTRPQLDFQYAHAQARDAVHLPFDHAAISDGLRQRGRDSLLLHSAAADRHVYLQRPDLGRRLDEASVQRLREHAAGYDGQIDLAIVVADGLSALAVQRHTLPFLERLEEQALAEGWSLSPVVLVEQGRVAVADEIGELLRAKMSVILIGERPGLSSPDSLGLYFTWAPRVGLTDAYRNCISNVRLEGLSYGMAAHRLLYLMREACRRQLSGVNLKDEAEVQALEGEAPRTGNFLLARD | Cofactor: Binds between the large and small subunits.
Function: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12.
Catalytic Activity: ethanolamine = acetaldehyde + NH4(+)
Sequence Mass (Da): 30158
Sequence Length: 273
Pathway: Amine and polyamine degradation; ethanolamine degradation.
Subcellular Location: Bacterial microcompartment
EC: 4.3.1.7
|
C3K2P6 | MKEPPVQLDLPDNPWLELRRLTPARIALGRTGTSIPTNAQLDFQFAHAQARDAVHLPFDPAGLSSQLAERGRDSLLLHSAAADRHSYLQRPDLGRRLSDESAQALRDHASANPGGVDLAVVVADGLSALAVHKHTLPFLTRMEEQTHAEGWSLSPVILVEQGRVAVADEIGQLLGAKMVVILIGERPGLSSPDSLGLYFTYNPKVGLTDAYRNCISNVRLEGLSYGMAAHRLLYLMREACRRQLSGVNLKDEAQVQTLESDDPDLMKGNFLLSSPDD | Cofactor: Binds between the large and small subunits.
Function: Catalyzes the deamination of various vicinal amino-alcohols to oxo compounds. Allows this organism to utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12.
Catalytic Activity: ethanolamine = acetaldehyde + NH4(+)
Sequence Mass (Da): 30255
Sequence Length: 277
Pathway: Amine and polyamine degradation; ethanolamine degradation.
Subcellular Location: Bacterial microcompartment
EC: 4.3.1.7
|
P22794 | MPTDMEHTGHYLHLAFLMTTVFSLSPGTKANYTRLWANSTSSWDSVIQNKTGRNQNENINTNPITPEVDYKGNSTNMPETSHIVALTSKSEQELYIPSVVSNSPSTVQSIENTSKSHGEIFKKDVCAENNNNMAMLICLIIIAVLFLICTFLFLSTVVLANKVSSLRRSKQVGKRQPRSNGDFLASGLWPAESDTWKRTKQLTGPNLVMQSTGVLTATRERKDEEGTEKLTNKQIG | Function: May complex with itself or/and other proteins within the membrane, to function as part of a cell-surface receptor.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 26213
Sequence Length: 236
Subcellular Location: Membrane
|
P34910 | MDPKYFILILFCGHLNNTFFSKTETITTEKQSQPTLFTSSMSQVLANSQNTTGNPLGQPTQFSDTFSGQSISPAKVTAGQPTPAVYTSSEKPEAHTSAGQPLAYNTKQPTPIANTSSQQAVFTSARQLPSARTSTTQPPKSFVYTFTQQSSSVQIPSRKQITVHNPSTQPTSTVKNSPRSTPGFILDTTSNKQTPQKNNYNSIAAILIGVLLTSMLVAIIIIVLWKCLRKPVLNDQNWAGRSPFADGETPDICMDNIRENEISTKRTSIISLTPWKPSKSTLLADDLEIKLFESSENIEDSNNPKTEKIKDQVNGTSEDSADGSTVGTAVSSSDDADLPPPPPLLDLEGQESNQSDKPTMTIVSPLPNDSTSLPPSLDCLNQDCGDHKSEIIQSFPPLDSLNLPLPPVDFMKNQEDSNLEIQCQEFSIPPNSDQDLNESLPPPPAELL | Function: Required for granulocyte differentiation and functionality of hematopoietic progenitor cells through the control of cell cycle progression and survival of hematopoietic progenitor cells.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 48666
Sequence Length: 448
Subcellular Location: Membrane
|
O60447 | MVTNKMTAAFRNPSGKQVATDKVAEKLSSTLSWVKNTVSHTVSQMASQVASPSTSLHTTSSSTTLSTPALSPSSPSQLSPDDLELLAKLEEQNRLLETDSKSLRSVNGSRRNSGSSLVSSSSASSNLSHLEEDSWILWGRIVNEWEDVRKKKEKQVKELVHKGIPHHFRAIVWQLLCSAQSMPIKDQYSELLKMTSPCEKLIRRDIARTYPEHNFFKEKDSLGQEVLFNVMKAYSLVDREVGYCQGSAFIVGLLLMQMPEEEAFCVFVKLMQDYRLRELFKPSMAELGLCMYQFECMIQEHLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLALLQMNQAELMQLDMEGMLQHFQKVIPHQFDGVPDKLIQAAYQVKYNSKKMKKLEKEYTTIKTKEMEEQVEIKRLRTENRLLKQRIETLEKHKCSSNYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKRNNSLPDENNIARLQEELIAVKLREAEAIMGLKELRQQVKDLEEHWQRHLARTTGRWKDPPKKNAMNELQDELMTIRLREAETQAEIREIKQRMMEMETQNQINSNHLRRAEQEVISLQEKVQYLSAQNKGLLTQLSEAKRKQAEIECKNKEEVMAVRLREADSIAAVAELRQHIAELEIQKEEGKLQGQLNKSDSNQYIGELKDQIAELNHELRCLKGQRGFSGQPPFDGIHIVNHLIGDDESFHSSDEDFIDNSLQETGVGFPLHGKSGSMSLDPAVADGSESETEDSVLETRESNQVVQKERPPRRRESYSTTV | Function: Functions as a regulator of cell cycle progression by stabilizing the FBXO5 protein and promoting cyclin-A accumulation during interphase. May play a role in cytokinesis.
PTM: Probably phosphorylated by PLK1; may be required for degradation during mitosis.
Sequence Mass (Da): 92949
Sequence Length: 810
Subcellular Location: Nucleus
|
P97366 | MVTTKMTAAFRNPNRRQVATDKVAEKLSSTLSWVKNTVSHTVSQMASQVASPSASLHTTSSSTTLSTPTQSPSSPSKLSPDDLELLAKLEEQNRLIETDSKSLRSVNGSRRNSGSSLVSSSSASSNLSHLEEDSWILWGRIVNEWDDVRKKKEKQVKELVRKGIPHHFRAIVWQLLCNAQSMTIKDQYSELLKMTSPCEKLIRRDIARTYPEHNFFKEKDSLGQEVLFNVMKAYSLVDRELVTVRAVLSSLDCCCMQMPEEEAFCVFVKLMQDYRLRELFKPSMAELGLCMYQFECMIQEYLPELFVHFQSQSFHTSMYASSWFLTIFLTTFPLPIATRIFDIFMSEGLEIVFRVGLALLQMNQAELMQLDMEGMLQHFQKVIPHQFDGGPEKLIQSAYQVKYNSKKMKKLEKEYTTIKTKEMEEQGEIKRLRTENRLLKQRIETLEKHKCSSTYNEDFVLQLEKELVQARLSEAESQCALKEMQDKVLDIEKKNNSFPDENNIARLQEELIAVKLREAEAIMGLKELRQQVRTLEEHWQRHLARTSGRWKDPPKKNAVNELQDELMSIRLREAETQAEIREMKQRMMEMETQNQINSNQLRRAEQEVNSLQEKVCSLSVKNKGLLAQLSEAKRRQAEIECKNKEEVMAVRLREADSIAAVAELQQHIAELEIQKEEGKLQGQLNRSDSNQYIRELKDQIAELTHELRCLKGQRDFSSRPPFDGIHIVSHLIGDDELFHSSDEDFIDSSLQESAIGFPLHRKSGPMSLNPALADGSESEAEDGMLGPQESDPEAPQKQPPQRESYSTTV | Function: Functions as a regulator of cell cycle progression by stabilizing the FBXO5 protein and promoting cyclin-A accumulation during interphase. May play a role in cytokinesis (By similarity).
PTM: Probably phosphorylated by PLK1; may be required for degradation during mitosis.
Sequence Mass (Da): 92943
Sequence Length: 809
Subcellular Location: Nucleus
|
Q9UI08 | MSEQSICQARASVMVYDDTSKKWVPIKPGQQGFSRINIYHNTASNTFRVVGVKLQDQQVVINYSIVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQEGGPSSQRQVQNGPSPDEMDIQRRQVMEQHQQQRQESLERRTSATGPILPPGHPSSAASAPVSCSGPPPPPPPPVPPPPTGATPPPPPPLPAGGAQGSSHDESSMSGLAAAIAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQSDKPAEKKEDESQMEDPSTSPSPGTRAASQPPNSSEAGRKPWERSNSVEKPVSSILSRTPSVAKSPEAKSPLQSQPHSRMKPAGSVNDMALDAFDLDRMKQEILEEVVRELHKVKEEIIDAIRQELSGISTT | Function: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.
PTM: Phosphorylated by PKA; phosphorylation abolishes binding to SH3 domains of ABL and SRC.
Sequence Mass (Da): 44620
Sequence Length: 416
Domain: The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization.
Subcellular Location: Cytoplasm
|
P70429 | MSEQSICQARASVMVYDDTSKKWVPIKPGQQGFSRINIYHNTASSTFRVVGVKLQDQQVVINYSIVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQEGGPSTQRQVQNGPSPEEMDIQRRQVMEQQHRQESLERRISATGPILPPGHPSSAASTTLSCSGPPPPPPPPVPPPPTGSTPPPPPPLPAGGAQGTNHDESSASGLAAALAGAKLRRVQRPEDASGGSSPSGTSKSDANRASSGGGGGGLMEEMNKLLAKRRKAASQTDKPADRKEDESQTEDPSTSPSPGTRATSQPPNSSEAGRKPWERSNSVEKPVSSLLSRTPSVAKSPEAKSPLQSQPHSRVKPAGSVNDVGLDALDLDRMKQEILEEVVRELHKVKEEIIDAIRQELSGISTT | Function: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. EVL enhances actin nucleation and polymerization.
PTM: Phosphorylated by PKA; phosphorylation abolishes binding to SH3 domains of ABL and SRC.
Sequence Mass (Da): 44337
Sequence Length: 414
Domain: The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization.
Subcellular Location: Cytoplasm
|
Q64GL0 | MSEQSICQARASVMIYDDTSKKWVPIKPGQQGFSRINIYHNTANNTFRVVGVKLQDQQVVINYSLVKGLKYNQATPTFHQWRDARQVYGLNFASKEEATTFSNAMLFALNIMNSQDGGPAAQRQAQNIQNGPSPDDMEIQRRQMLEQQQRQETLERRTSTTVSTLQINVSSSPSHCQSPPPDYSNFSASPSTGAVPPPSYAKVISSAAASPELSSKSTNKSSNRTSEPPELQNSHCGSEPSTSQSSAFSPIRPSNGTVSRSIKQISLSPPPAPGSHSPLSLHQSVRHPSLSFSPCSSSPPVSVTSSVQKNISPQSPIPVVLPVIPVQNSRIRGCSDKMVQNPIVPQTGPSDQAEEPLTSQISLSSPRTQVKCVDRSFLSYIETVPVAQLPMITSPFGILTQASPQPFQSSTHPSQQSYQSMSHFVSLPPPYAAVSELTLPKRTTPYMTSSTITQFSPVLPPGHPSSAAMVASVGSAPAPASGPPPPPPPGPPPPSGGTPPPAPPLPAGGSQGVVYEESPASGLAAALAGAKLRKVQRPEDGSSSPCGATKTDANRTSSGGGGGGLMEEMNKLLAKRRKAASYTDKPGDKKEEECQNEDASLSSSPVTRGPTPQNSSDLGKKPWERSNSVEKPVPSLLSRMKPVSSSNDVSTDALDFDRMKQEILEEVVRELHKVKEEIIDAIRQELSRISTT | Function: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. Evl enhances actin nucleation and polymerization (By similarity).
Sequence Mass (Da): 73921
Sequence Length: 692
Domain: The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization.
Subcellular Location: Cytoplasm
|
F4J4C8 | MKTTATSFVTGERVVVFVVVSRILLSLPLSLISHGFSLFLLSLSAFLVEIRVETSPFLLSHFSSRRGASSGILLGAVTLPSVMISKLVQLSRAISIHEAEQDELAHVTMQYWAASASCCAILIYLSVIMSQVRKDESLSSSSIWLTRVSLTGTVLYGVACFVSLSMISHTGLNTSLKMLWMLFHGLAAVKLIRHLLCTFPSCASIGEALLVTSGLVLYFGDFLACTIAKIFEKLIPVDLVSISYGIKRTETGIIVQGLLLGLLLFPMVFRFVLHIYESSLRKRDARQRNCSDAAKSVLFFVSLLFFMVVAVPSWMQFVHDFNQHPFLWVLTFVFSEPLKRLSLCIYWILLIVVSVSRFYNISRSSKVERILLRKYYHLMAVLMFLPALVLQPKFLDLAFGAALAVFVALEIIRIWRIQPLGEPLHQFMNAFTDHRDSEHLIVSHFSLLLGCALPIWMSSGFNDRALSPFAGILSLGIGDTMASMVGHKYGVLRWSKTGKKTVEGTAAGITSMMAVCFVLVPILASMGYILSQGWWSLLVAVTATGMLEAYTAQLDNAFIPLVFYSLLCL | Function: Essential for pollen development. Involved in protein N-glycosylation in the endoplasmic reticulum (ER), especially in the female gametophyte. Mediates pollen tube (PT) reception in synergids through protein glycosylation.
Catalytic Activity: CTP + di-trans,poly-cis-dolichol = a dolichyl phosphate + CDP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63136
Sequence Length: 569
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.1.108
|
B8I3A9 | MNRVYSVSDINNYIKQLVSNDIILSDVSIRGEISNFKHHYTGHMYFTIKDKNSLLKCVMFRSQAVSLRFSPENGMKVIVSGYISVFERDGQYQLYASSMQPDGVGALHIAFEQLKEKLQREGLFDPENKKKIPVLPGSIGVVTSSTGAVIRDIINVTYRRNSKMKLVLYPVAVQGQQAAGQIAEAIKCLNEQNKVDVIIVARGGGSLEELWAFNEEIVARSIYASNIPVISAVGHETDFTICDFVSDMRAPTPSAAAELAVPDMEVLLYKLESYNMRMKSSLAKKVTTLKNQLQKLNARPFFAQPYDRVNQQRQTLDNLTKSMVRENQTIIKDKKSQFGMLAGKLDALSPLKILERGYSLVKNPQGYVVNNVKQINIGDKLEILMNDGLAECDVISVREGKIYE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 45244
Sequence Length: 404
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
A1AX20 | MFNIDEIYTISNFLFLCNKTIEDKIPTCWLQGEISNLTRPESGHWYFSLKDSKAQVYCVLFRFNQRHIKFNPKNGMEVLVHVTPTLYKARGNFQLIIQHLEPVGIGNLNLAFEQLKNKLVNEGLFDNIHKKPLPNIINTIGVISSSTGAVIQDIIKVLNNRYPFSDILLFDSMVQGQGSVKKLTNALNAADQSGKCDVIIIARGGGSLEDLWAFNEETLARAIFKASTPIISAIGHETDTTISDFVCDICAPTPSAAAMLVTPDRLELLANTDKLYMRLHQSYQQTLHDYQSVLNQLKLRIPISNKQIAFFSQKLDHVSINLNNHVKSTLVLNNAKLNSIFSALKQHSPIEAIKHIKILNQVSFAQLKHQIKQIININNSALYLANEKLKKAIATLTDKHKTTLSIQANSLHHLSPLNTLSRGFSITTNAKNQILSSITDIKINQAITTQLADGKLYSNIKKIEKN | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 52205
Sequence Length: 466
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
A9MHM3 | MLSSQTSSIFTVSRLNQTVRLLLEQEMGQVWISGEISNFTQPASGHWYFTLKDDTAQVRCAMFRNSNRRVTFRPQHGQQVLVRANITLYEPRGDYQIIVESMQPAGEGLLQQKYEQLKAKLQAEGLFDQQYKHPLPSPAYCVGVITSKTGAALHDILHVLKRRDPSLPVIIYPAAVQGEDAPGQIVRAITLANARKECDVLIVGRGGGSLEDLWSFNDERVARAIFASTIPVVSAVGHETDVTIADFVADLRAPTPSAAAEVVSRNQQELLRQMQTACQRLEMAMDYYLANRQRRFSQLYHRLQQQHPQLRLARQQTTLERLRQRMHLALENQLKQANQRQQRASQRLRQQNPQPRIHRAQSRIQQLEYRLAENFRARLSEQRERFGNTVTHLEAVSPLATLARGYSVSTATDGNVLKKVKQLKVGDMMTTRLKDGWVTSEVTAIKPVKKIRLG | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 51566
Sequence Length: 454
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
Q2S4K5 | MLSVAELTRGLSDLVEDRYDDVWVEGELSDFTRAASGHCYFSLKDEDAQIRCVMWKHLTQYVYFEPEEGMQVRVNGHASVYERRGDLQIQAQAMRQAGKGAQQKAFEELKQTLQAEGLFAPERKQALPAFPDTIGVVTSGQGAAIHDIQSGLARRFPPAEVVLCPVKVQGLDAPRAVADAVAAFNDLPADDAQRPDLLIVGRGGGSTEDLWAFNEEVVARALDASNLPVVSAVGHESDVTIADLVADERAATPSAAAERVVPDRRDVADRVRALHDRLRSRVTGRLQDARQRVDALVASRAFHAPARRLEQHRQHLDALVDRLGRGGARAVDRARTRLAHLRDRLHALDPEQPLRRGYVHLTQDGTSVQSAESLQDGDRVRLHFQDGRRDAEVLPDDG | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 43905
Sequence Length: 398
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
A9ANA4 | MAKTASPGATPPGNGAEPLPDNYETALAELETLVARMEGGALSLEDSLAAYRRGAALVAFCQQQLEKVEQQVRVLDGATLKPAAATDGEDDDL | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9672
Sequence Length: 93
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
Q8RAC8 | MEKEFNFEEDLKRLEEIVDTLEKGNLMLEESFNLFKEGVEISKRLEKMLKEVEGKITMLISEDEEIEFKEEENNV | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8987
Sequence Length: 75
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
Q3AAM6 | MTFEEAMNRLNEIVERLERGNVGLEESLALFEEGLKLHRFCSEKLKELELKLVEVQEDEAGEVTFEEIVEMEDDLPF | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9017
Sequence Length: 77
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
Q9K1A5 | MKKNAPKSFEEALSRLESLTQSMQGEMPLEDALAAYQEGNELVRYCQTKLAQVEQKLQVLDTDGLKELNLESDE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8375
Sequence Length: 74
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
Q82VD5 | MRKKSSSNKEETALHPPPENFETATAELEQIVAGMETGQMSLEDALSAYKRGVELLQYCQNILKNSQQQIKILEADMLKHFSPAEHDAS | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9976
Sequence Length: 89
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
B2IWI8 | MVKRKGASSSEEGWNYEAKVAEIEGIITRIEAGELELEAVFEQFASAVEYLRQCESFLQQRQQQVDLLIETLSEE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8583
Sequence Length: 75
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
Q8YW43 | MVKRKNSDNSDTVAHGNYEAKVAEIEAIISRIESGELELEAVFEQFANAVEYLRQCDTFLQQRQQQMDLLIETLNDEDNSEL | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9436
Sequence Length: 82
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
Q2G632 | MGTVPELASLSFEEALKELENVVRRLESGEAPLDESIELYARGDALRAHCQARLDAAQARIEAIVADRDGKAQGLRPFDETVG | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9037
Sequence Length: 83
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
Q30Z97 | MTGTGTTGFEEQLARLQEIVRRLETGELPLEEGVALYKEGLELAAGCRKRLQTARNDIKVFSDGVLKDFDMPEDSPAADD | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8814
Sequence Length: 80
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
Q6MDK5 | MNNPSDQEPTASFETALCRLEEILEKMNSGTVSLDESLKLYEEADQLIIICNKRLNDAERKIEILVKNRSGELTLGNDDKPIIQDFKIASTS | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 10357
Sequence Length: 92
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
Q8L1H9 | MSDIQTLSFEEAMRELEATVGKLETGEATLEDSIALYERGAALRAHCETRLREAEERVEKITLAANGQPSGTEPAEGL | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8492
Sequence Length: 78
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
Q6D842 | MPKKTEQPVSFESSLNELEKIVTRLESGELPLDDALNEFEHGIQLARQGQQKLQQAEQRVQILLSDDPDAPLSPFTPDNDTL | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9229
Sequence Length: 82
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
Q03FZ3 | MAEEKTFEENLQELQQVVSNLEQGDIPLEKALTEFQKGIQLSSELQETLKNAEKTLTKVMQDNGEETNLDLGTDGENE | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8784
Sequence Length: 78
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
A5D2Z3 | MAEKEMNFEEALARLEAVVKELEDGRLPLQKALELFAEGIGLSRICNRYLEDAEQRIAILTADEKGGVVLRELGPSPAAREDTNDEL | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 9670
Sequence Length: 87
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
B4RGV8 | MSEPADIAAMTFEQALAELEQIVARLESGQAPLEDSIRMYERGAALKAHCETRLEAARLRVEKIVMGAGGAPASEPAEFG | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
Sequence Mass (Da): 8559
Sequence Length: 80
Subcellular Location: Cytoplasm
EC: 3.1.11.6
|
Q6H676 | MAKSCTLVLLLVALVGLSLLVSPIACSRKLSKPKPKPKPSMKKPVVRAHNNYTGSPSVTVTTGWAAAGATYYGAPNGDGSDGGACGYQTAVGQRPFSSMIAAGSPSLYKGGKGCGACYEVKCTTNAACSGQPATVVITDECPGGICLAGAAHFDMSGTSMGAMAKPGMADKLRAAGILQVQYRRVPCKYSGVNIAFRVDQGANPFYFEVLIEFEDGDGDLNAVDLMEAGCGWTPMVQNWGALWRYNSNTGKALKAPFSLRLTSDSGKVLVANNVIPASWKPGVTYRSLVNYS | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 30500
Sequence Length: 292
Subcellular Location: Secreted
|
Q10G40 | MAAFEPHRLQLLYFIAITVLASVFQPCTSIELHRELSGWSNGIATWYGDPNGAGSEGGACGYQYAVDQPPFSSRIAAGSPYIYDSGKGCGSCYRVVCAGNEACSGIPVTVVITDQGPGGPCLEELVDGQCMNEAAHFDMSGTAFGAMARPGQADQLRGAGLLQIQYTRVECEWTGVGLTFVVDSGSNPNYLALLVEYDDNDSDLAAVDIMPIGAGASGSWIPMQQSWGAVWRLNSGSALQGPFSVRLTFSSGQMFVASNAIPAGWNPGMAYQPGGVAMRVRGRNGGRRGYEAVGMLGGLCHLLLLLLLMLFEL | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 33073
Sequence Length: 313
Subcellular Location: Secreted
|
Q6H677 | MALAAKLLPSIVAFVALACCVLRSSVASVDHHRKLSGWSIGGATWYGPANGSGTDGGACGYQGDVGQPPFNSMIAAGSPSIYESGKGCGSCYQVKCSGNPSCSGKPVTVVLTDLCPGGACLEEPVHFDLSGTAFGAMAKPGQDDQLRNAGKLPVQYARVPCKWQGVDIAFRVDAGSNQYYLAVLVEDEDGDGDLSAVDLMQSGGSGGGGSWAAMQQSWGAVWKYNSGPAPLQAPMSIRLTSGSGRTLVASNVIPAGWQPGGTYRSIVNFRRED | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28176
Sequence Length: 273
Subcellular Location: Secreted
|
Q0DZ85 | MAAFSSSSSAPMLIRSVLFVSLLSAAFVFDSGEAGAAHRVVDPEWHPATATWYGSADGDGSDGGACGYGTLVDVVPMKTRVGAVSPVLFKGGEGCGACYKVRCLDASICSRRAVTVIVTDECPGGVCAFGRTHFDLSGAAFARLAVAGHGGQLQNRGEISVVYRRTACKYGGKNIAFHVNEGSTTFWLSLLVEFEDGDGDIGSMQLKQANSAQWQDMKHIWGATWSLTPGPLVGPFSVRLTTLTTRQTLSAQDVIPKNWTPKATYTSRLNFA | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28841
Sequence Length: 272
Subcellular Location: Secreted
|
Q7X6J9 | MAAASSRSFSLCVLLLLLLLAPPISASFLFDGGKSKSAAAAAAVDMEWRPATATWYGDAEGDGSTGGACGYGSLVDVVPMKARVGSVSPVLFKDGEGCGACYKVKCLDHGICSRRAVTVIVTDECPGGLCAFGRTHFDLSGAAFSRMAVAGAGGHLRDRGQLSVVYRRTACKYGGKNIAFRVNEGSTNFWLSLLVEFEDGQGDIGSMQIKQANSVEWLDMKHVWGATWCLVRGPLVGPFSVRLTTLSAQKALTARDVIPRNWKPTATYTSRLNFEAAL | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 29529
Sequence Length: 278
Subcellular Location: Secreted
|
Q5W6Z9 | MNSKFQLILSTFVVIAAFTLLPRPCASIEFHRKLSSWSNGGATWYGAANGAGSDGGACGYQAAVDQAPFSSMIAAGSPSIYKSGLGCGSCYQVKCSGNSACSGNPVTVVLTDECPGGPCLSEPVHFDLSGTAFGAMANPGQADQLRAAGVLQIQYNRVPCNWGGVMLTFAVDAGSNPSYFAVLVKYENGDGDLSGMDLMQTGAGAAWTPMQQSWGAVWKLSAGAALQAPLSIRLTSSSGKTLVASNVIPSGWKPGASYTSTVNY | Function: May cause loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found. May be required for rapid internodal elongation in deepwater rice during submergence (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27153
Sequence Length: 264
Subcellular Location: Secreted
|
O52043 | MESLQQLQQQLGLMAWPLFICSALTVMLLAERLFQVLLSLTVGKGAIRHALQATSPKNPKQLAELTEHFASKRPVLYRGVAMLLAHHQFDKSLREDAAGIWLQEQRHQFNSGLRLLTLIGVISPLLGLLGTVLGLIEMFKGVAATTGSITPNVLADGLGVAMYTTAAGLLIAVPAVAGAQLLSLWADRTMAKLEHTLNYVNLWLEGMTLHADASLTVVTPQEATTENL | Function: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24684
Sequence Length: 228
Subcellular Location: Cell inner membrane
|
O67637 | MMEEIKELIDYGIMGTLLFMSFVALAVGIERYLSIRSTKVENFKSKAQLEKELTKRLYIIATVASNAPYVGLLGTVLGILLTFYIIGEKGIVNTKEIMVGLALALKATALGLIVAIPSTILYNFLVRKVREKLLDWEAIHGECSSSHE | Function: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16396
Sequence Length: 148
Subcellular Location: Cell membrane
|
P0ABU8 | MGNNLMQTDLSVWGMYQHADIVVKCVMIGLILASVVTWAIFFSKSVEFFNQKRRLKREQQLLAEARSLNQANDIAADFGSKSLSLHLLNEAQNELELSEGSDDNEGIKERTSFRLERRVAAVGRQMGRGNGYLATIGAISPFVGLFGTVWGIMNSFIGIAQTQTTNLAVVAPGIAEALLATAIGLVAAIPAVVIYNVFARQIGGFKAMLGDVAAQVLLLQSRDLDLEASAAAHPVRVAQKLRAG | Function: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26287
Sequence Length: 244
Subcellular Location: Cell inner membrane
|
Subsets and Splits
No saved queries yet
Save your SQL queries to embed, download, and access them later. Queries will appear here once saved.