ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
|
|---|---|---|
Q6MCA2 | MPSTKFKGYFITIEGGEGSGKSTLLNQLGDYFRNKGFEVIQTREPGGTKLGESIRHLLLNHEDSISIGHQAELLLFLAARAQHIEELIQPALKAGKIVLCDRFNDSTIAYQGAARGLNAKKIQEFCQLVCAEILPNWTLFLDVSPEIGLARTQKIQKVHAQMGQLDRIESEKIEFHERVRQAFLSLVQQEPQRIYRIDANESQSKVLQKALEFLEEQWSDSELKT | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 25495
Sequence Length: 225
EC: 2.7.4.9
|
A5D690 | MKGKFIVFEGVDGSGKTTQIKLLGEKLESMGCPVVYTREPGGTRVGERIREILLNPLYGELVPWAEALLYAAARAQHVAQVILPALREGKVVLCDRFTDSSLAYQGYGRGVDIEMLEQVNRPAAAGVVPDLVLVLDFDREGQTERMARSGRSADRIEREAQEFYRRVRSGYLALAARAPRRYRVIDASRAEKLVHLDVLKAAEEVLDAFLKGNSRA | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23990
Sequence Length: 216
EC: 2.7.4.9
|
Q8I4S1 | MTDDKKKGKFIVFEGLDRSGKSTQSKLLVEYLKNNNVEVKHLYFPNRETGIGQIISKYLKMENSMSNETIHLLFSANRWEHMNEIKSLLLKGIWVVCDRYAYSGVAYSSGALNLNKTWCMNPDQGLIKPDVVFYLNVPPNYAQNRSDYGEEIYEKVETQKKIYETYKHFAHEDYWINIDATRKIEDIHNDIVKEVTKIKVEPEEFNFLWS | Function: Catalyzes the phosphorylation of thymidine monophosphate (dTMP) to thymidine diphosphate (dTDP), the immediate precursor for the DNA building block dTTP . Can also phosphorylate dGMP and to a lesser extent GMP, dUMP and dIMP . Can use either ATP or dATP as phosphate donors in presence of Mg(2+) .
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24691
Sequence Length: 210
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.7.4.8
|
Q9CHU4 | MGQVHLHNRSFNKATSAGFLIALGIVYGDIGTSPLYAMQAIVRGQGGLANLSESFILGAVSLVIWTLTLITTVKYVLIALKADNHHEGGIFSLFTLVRRMRKWLIIPAMIGGATLLADGALTPAVTVTSAIEGLRGVTHVYSNQTAVMVTTLIILAFLFLIQRFGASLVGRLFGPIMFIWFGFLGVSGLINSFLDLSILKAINPYYAIHLLFSPENKAGFFILGSIFLVTTGAEALYSDLGHVGRGNIYVSWPFVKICIILSYCGQGAWLLAHRGEHIEKLNPFFAVLPDNMVIYVVILSTLAAIIASQALISGSFTLVSEAIRLKLLPLFKIYYPGQTLGQLYIPAVNFALWVTTSFFVLYFKTSEHMEAAYSLAITITMLMTTTLLTYFLIQKGTPKIAIAIISIGLFCIEGSFFAASLVQFINGAYIVVLIALAIIFVMFIWNKSHKIVMKYIKSLNINEYKNQLNALRHDESYDLYQTNVVYLTSKMDHEWIDRSILYSILDKRPKRAECYWFVNVKVTDEPYTSEYKVDMMDTDFIVRVNLYLGFRMRQEVPRYLRTIVTDLMESGRLPRQHQHYSITPGRKVGDFRFVVVEEKLMNARQMPGFERFVLQTKAQIKRITASPIRWFGLQFSEVTVETVPLVLSDVRNLEIHERLEQVDEAEASATH | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75477
Sequence Length: 671
Subcellular Location: Cell membrane
|
Q88SV0 | MRKQRIQERSLIGMLITLGVVYGDIGTSPLYVMNALINDAGQLKNATPDYVIGSVSLIFWTLMLITTVKYVLIALRADNHHEGGIFALYALVRHRAKWLIFVALIGGAALLADGTLTPAVTVTSAVEGLKGLPKLGAFSQYPWLVPLTVTVILLVLFMIQGFGTAVVGRSFGPMMLLWFTVIGIFGLINISQAPVILKAFSPVYAVQVLFNPANKMGIFILGSVFLATTGAEALYSDMGHVGKANIDATWPFVYTTLILNYLGQGAWMLTHYQDAAWRNATNVNPFYAMVPAGGQIAMIILATAAAIIASQALITGSYTLVDEAVGLKFLPRMIIKHPSNVRSQIYIGAINWLLCLVTLGIVWLFQTSAHMEAAYGLAITLTMLMTTILLSQWIHMKGHRALALALLFGFGALETVFLTASLTKFIHGGYLTLGLTLVIFLIMVVWFFGNRRRLRYNQANEQISLLDYRNQLIQLSHDDHLPVFATNLVYLAKVDHQHRVKRSILYSILDKRPKRAKVYWFITINETNRPYDCSYSIDMLGTRNIVEVQLNLGFRKSQHINLYLRQIVTNLIADHSIDPQYSRYGITQPRQVGDFKFVVQNQQIMDLASNPTMGQFDRLLIGGRVLLQNITPSPAIWYGLAFSDVLEETIPLFTKPATDATLTNLTVHHARTPQRNSRQP | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75704
Sequence Length: 680
Subcellular Location: Cell membrane
|
Q5ZTN5 | MMNESSTEKKNELSLSFAALGVVFGDIGTSPLYAFGQVIKYFPINDHNIYGILSLIFWSLIIIVSIKYLVIVFRADNDGEGGIIALAGLIRQKIKKPGGWLLFITLVGIGLIIGDGILTPAISILSAVEGLESLSPNLAKYVLPVTLIILFFLFKMQSIGTGKIGIYFAPVMLIWFITIGVLGFLQIIQNPKVLMAINPYYAIYFFMIHKYFALFILGGVFLVMTGGEALFADLGHFGKKAIRTGWFAVALPALLLCYFGQGAFVLMHIEYIKYPFFSLSPDWFLPVMIILATIATIIASQAIISAAFSILKQASLLNLIPRLKIIYTSKFEKGEVYLPLINFILALGTCSLVVIFKSSSNLADAYGIAVNLDMLITTVLVGIIAYYCWNWHAFKVMIFPLILVIELAFFAGNIPKLLTGGWIPILIAFLGFVVMYTWHCGFEKLRELHHRDALMDAFIIDELNQNKISRQSGMGLYIIDPYDCEGESLLHHLRLNRIFFENMIFVSIKIENKPYIPIEDKFELIKKAEGFYLIFIHYGFTENINLPNELDEMFKRVYLPFEIIKNKLIYFIEIVFVEMTRERQKHMYMWQKHLFSLMIRNAVPDIQFYRLPYNKTIAIGTYYQL | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71098
Sequence Length: 625
Subcellular Location: Cell inner membrane
|
Q2W905 | MSSHVPSFLRGTPDMTAHGGDGKSRNVAGLMLAAIGVVFGDIGTSPLYAMKETFSGPHAVAMDKGNILGVLSLVFWAITIIVSFKYVIIIMRADNRGEGGSLALLALVSHAAESNRRLSLMVSALGIFAAALFYGDSIITPAISVLSAVEGLQVAAPHLEQWVVPLTIVILFVLFAIQSHGTDLVGKMFGPVMLVWFLTLAILGIRNLSHAPSVLAALSPHYAISFLFREGWHAFLALGSVVLAVTGAEALYTDMGHFGRLPIRLAWYLLVLPALILNYFGQGALLIYNPEAIANPFFNLAPASLALPLVILATLATVIASQAVISGAFSVTRQAIQLGFLPRMEIIHTSEEEMGQIYLPFVNWLLMCMVMVLVVGFKTSSNLAAAYGVAVTGTMVIDALLVGTVMLLIWKWNPRKVKWLIGGFLVVDLAFFLANSIKIPDGGWFPLVVGGLLFTILTTWKDGRKRLLARLKADALPVEDFLASLSDRVPRVPGTAVFLTGTSEGVPIALLHNMKHNKIVHERVVLLTVIVEEVPFVPEERRLENRLLAPNFHRVFLRYGFMESPNIPKALAHARTDQLGFFYEPMSVSYFVSRETLLPTEKPGLRGLRDTLFATLARMATSAMDFFHLPSNRVVELGSQIEI | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70049
Sequence Length: 643
Subcellular Location: Cell inner membrane
|
Q122S7 | MSSKKSSLAALTLGAIGVVYGDIGTSVLYAIKEVFGSGHVPFTPGNIYGILSIFFWTLTVIVSIKYVVLVLRADNNGEGGLIAMLALASTAVKDKPKLRRILLIVGVFGTSLFYGDGVITPAISVLSAVEGLEVVSPAFKEGVIPITLVILFCLFALQKHGTAGIGRYFGPITLIWFVVIALLGISQIVTNPAILKAISPHYALLFMWHNPGTTFIILGAVVLCVTGAEALYADLGHFGKRPIRLAWFSVVMPSLVLNYFGQGALLLNNPAAVKNPFYLMAPEWALLPLVGLATMATVIASQAMITGAFSVTKQAVQMGYLPRLNIQHTSVKDTGQIYITFVNWSLFVAIVLAVVMFRSSSNLAAAYGIAVTLDMLITTTLTFFVIRYSWNYPLSLCIAATGVFFLVDLAFFASNLMKLFAGGWFPLLIGGAVFTLMMTWKEGRGLLNDKLRSDAIDLPSFLDAVFVSPPARVEGTAVFLTAEPGTVPNAMLHNLKHNKVLHQQNLFVTVRYHEVPWIGMNKRLEIESLGHDCWQVTVHYGFKNDLDLPKALQQIKGRGCELESMTTSYFLSRDTVVPTIGRGMASWREKLFAQMHHNASGAADFLNLPNNSVVELGSKIEI | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67676
Sequence Length: 622
Subcellular Location: Cell inner membrane
|
Q98KL7 | MDLASRDSEAETVEQSSHSGAEQHSTKVLMLGALGVVYGDIGTSPIYAFREALHASPGIDTRAQVLGVLSLIVWALTIIVTIKYVAFVLRADNKGEGGTLSLMSLARTAYPKGARLILAIGLCGAALFFGDSIITPAISVLSAVEGLRVVTPTLDPYVVPITLLILAILFSVQRFGTGKVAAVFGPVTALWFLAIGVAGLYHLLDDPSILLAINPYYAVTYLASTPTAAFVTVGAVFLAVTGAEALYVDLGHFGRKPIVLAWFSVVFPCLLLNYFGQGAFVLANGGRPTNPFFQMLPDWALMPMVGLATAATVIASQAVISGAFSLTRQAVQLNLLPRIEVQHTSEMQLGQIYMPRINLLVALGVMLLVVGFGSSSSLASAYGISVTGEMLMTTILLFVVMRKLWKWRLAVALPLTLLFGIIDSGFFLANIVKIFEGGWVSITVACLMGLIMWTWIRGTRYLFDKTRRNEIPLDFLAANLLKKKPHLVPGTAVFLTSDPLSAPTALMHSLKHYKVLHEQNVILSVVTAPQPVVSDSDRVKMETVNDLFMRVTLTFGYMEQPNIPRALAICRKRGWKFDIMTTSFFLSRRSLKASPNSGMPVWQDRLFIGLARTAADATEYFQIPTGRVVEIGTQVAI | Function: Transport of potassium into the cell. Likely operates as a K(+):H(+) symporter.
Catalytic Activity: H(+)(in) + K(+)(in) = H(+)(out) + K(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69094
Sequence Length: 637
Subcellular Location: Cell inner membrane
|
A9AWD5 | MSLIVDILIDDLRALIRDLGQNGGLMSPSVYDTSQALRLYPTPSEEHVWPAVNWLISQQQSDGGWGNPSMPLSRAVPTLAAILALRRHCQRRSTFDGLLEAKRFLRRQLEYWEKPLPDNLPVGMELLLPYMLEEAYREEHQDDIDDVPIKLRLNIPLAPYRELIALGEHKRSLIQQKKPRAGTAPVYSWEAWASHADPELIDGSGGIGHSPAATAAWLFAANHNPNLRNEIAGAENYLRQASLATSESAPCIMPTAWPIPRFEQSFSLYALVTGGILDFPSIQDVLKPQIADLHQALKPRGIGFSDDFMPDGDDTAAAVAVLIAAGYPVDLAILNQFEREPYFVAYHGELQPSISLTARAVHALDLAGVDISRWWKIFIDAQKLDGSWSGDKWNTSWLYTTCHVLIALKNSPYKTAMKEAVAALQVHQHPDGGWGIINRSTTVETAYAVLALQNLREAGLLDDDDIHMLQRGYNWLCIHYRPFRMKEYQCWLNKEIYCPQRIDRAYELSAMLAVTLGELKL | Function: Involved in the biosynthesis of (+)-O-methylkolavelool. Catalyzes the conversion of geranylgeranyl diphosphate into (+)-kolavenyl diphosphate.
Catalytic Activity: (2E,6E,10E)-geranylgeranyl diphosphate = (+)-kolavenyl diphosphate
Sequence Mass (Da): 58496
Sequence Length: 521
Domain: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic activity, presumably through binding to Mg(2+).
EC: 5.5.1.29
|
Q9XXD1 | MNSAIMQGAAMATSHGIARLNRHNAQRNHFHIPTANRLFYQLQTPCTSTEEERRTVQTDDVAEIGMQRPDYQMYCGEEEISEQFVKLNVGGQRFMLRKDTIRRRGVGRLLDLINKPVADSNADAFFSSTSEFYFERPPSLFHIVYQFYLNGVIHQPSNLCPVDIIEELEYWRIIPDQYLASCCCAQQIDDDDEEVEEQDKPNLFKTLRFGEIRRCVWNIIEEPASSGKAQAFAVCSVVFVLISISGLVLGSLPELQVATKQRNNLTGEEFTEMEPMPILGYIEYVCIVWFTMEYGLKMLVSAERSKTFRQLLNIIDLLAILPFIIEMLLLIFGISTEQLRDLKGAFLVIRILRVLRVIRVLKLGRYSSGLQMFGKTLKASFRQLGMMAMVVMTGVIFFSTLVYFLEKDEPASKFHSIPAACWWCIVTMTTVGYGDLTPVTVPGKLVATGAIACGVLVLALPITIIVDNFMKVAETERPAGGNRYRTSQYPKATKSEQMILKVT | Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56966
Sequence Length: 503
Domain: The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.
Subcellular Location: Cell membrane
|
P0DW45 | MQRNTYNKVGLYILSLAMLFVFIIILTAKIPFCFTSDCSFIGLKKLVLTNIVPIVCFVFFLFSIYFYNRLKNITKYNGQDSVKITSCQSESYESLTFLATYIVPFMGFSFEDMQKNIAYLLLVVVIGIIFIKTDKYYANPTLALFGFKLYRVNILHPGSGETKNLIAISNDVLKVDDNVYYSFFDEFVFIARKKI | Function: Component of antiviral defense system Kiwa, composed of KwaA and KwaB. Expression of Kiwa in E.coli (strain MG1655) confers resistance to phages lambda and SECphi18.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22507
Sequence Length: 195
Subcellular Location: Cell inner membrane
|
Q6P1M3 | MRRFLRPGHDPVRERLKRDLFQFNKTVEHGFPHQPSALGYSPSLRILAIGTRSGAIKLYGAPGVEFMGLHQENNAVTQIHLLPGQCQLVTLLDDNSLHLWSLKVKGGASELQEDESFTLRGPPGAAPSATQITVVLPHSSCELLYLGTESGNVFVVQLPAFRALEDRTISSDAVLQRLPEEARHRRVFEMVEALQEHPRDPNQILIGYSRGLVVIWDLQGSRVLYHFLSSQQLENIWWQRDGRLLVSCHSDGSYCQWPVSSEAQQPEPLRSLVPYGPFPCKAITRILWLTTRQGLPFTIFQGGMPRASYGDRHCISVIHDGQQTAFDFTSRVIGFTVLTEADPAATFDDPYALVVLAEEELVVIDLQTAGWPPVQLPYLASLHCSAITCSHHVSNIPLKLWERIIAAGSRQNAHFSTMEWPIDGGTSLTPAPPQRDLLLTGHEDGTVRFWDASGVCLRLLYKLSTVRVFLTDTDPNENFSAQGEDEWPPLRKVGSFDPYSDDPRLGIQKIFLCKYSGYLAVAGTAGQVLVLELNDEAAEQAVEQVEADLLQDQEGYRWKGHERLAARSGPVRFEPGFQPFVLVQCQPPAVVTSLALHSEWRLVAFGTSHGFGLFDHQQRRQVFVKCTLHPSDQLALEGPLSRVKSLKKSLRQSFRRMRRSRVSSRKRHPAGPPGEAQEGSAKAERPGLQNMELAPVQRKIEARSAEDSFTGFVRTLYFADTYLKDSSRHCPSLWAGTNGGTIYAFSLRVPPAERRMDEPVRAEQAKEIQLMHRAPVVGILVLDGHSVPLPEPLEVAHDLSKSPDMQGSHQLLVVSEEQFKVFTLPKVSAKLKLKLTALEGSRVRRVSVAHFGSRRAEDYGEHHLAVLTNLGDIQVVSLPLLKPQVRYSCIRREDVSGIASCVFTKYGQGFYLISPSEFERFSLSTKWLVEPRCLVDSAETKNHRPGNGAGPKKAPSRARNSGTQSDGEEKQPGLVMERALLSDERVLKEIQSTLEGDRGSGNWRSHRAAVGCSLSNGGAE | Function: Part of a complex with GPSM2/LGN, PRKCI/aPKC and PARD6B/Par-6, which may ensure the correct organization and orientation of bipolar spindles for normal cell division. This complex plays roles in the initial phase of the establishment of epithelial cell polarity.
PTM: Phosphorylated at Ser-653 by PRKCI. Phosphorylation is enhanced during cell polarization induced by calcium. Phosphorylation may occur during the cell-cell contact-induced cell polarization and may contribute to the segregation of LLGL2 from the PRKCI/aPKC and PARD6B/Par-6 complex.
Sequence Mass (Da): 113448
Sequence Length: 1020
Subcellular Location: Cytoplasm
|
A0A011QK89 | MESIEAVVIGAGVVGLACARELARRGFETVILERHGAFGTETSARNSEVIHAGLYYPTDSLKARLCVAGRQQLYAFCATHAISHQRCGKLVVATSPAQESRLAALQKQGEANGVDDLQRLSAAEARALEPGLACTAALLSPSTGIVDSHGLMLALLGDAETAGAALALHSPLLRGSLDANTPGIVLESGGADGLRFKARRVINAAGLWAPQVAASLAGFPRTLIPANFHAKGSYYALTGRTPFSRLVYPLPEAGGLGVHLTLDLGGQARFGPDVEWLPDPTPGQPIDEPDYRVDPARADAFYAEIRRYWPALPDAALTPAYAGIRPKIVGPGAPAADFLIQGPAQHGIAGLVNLFGIESPGLTACLAIAERAADAADGTRERQFRAHG | Function: Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG or(S)-2-hydroxyglutarate) to 2-oxoglutarate (alpha-ketoglutarate) (By similarity). Also displays some oxidase activity in vitro on L-2-hydroxyglutarate with O2 as the electron acceptor, but this activity is most likely not physiological .
Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 40540
Sequence Length: 388
EC: 1.1.99.2
|
A0A0M7LBC1 | MSVDVDCVVIGAGVVGLAIARALAQSGREVLVAEATEAIGTGTSSRNSEVIHAGIYYPAGSLKARLCVRGKHLLYSYCAERGVPYKRLGKLIVATTTEQAAQLEGIAQRARANGVDDLQFISGEDAMRLEPALRCTAALSSPSTGIVDSHALMLSFQGDAENAGAQCVFHTPLVSGRVRPEGGFELQFGGDDAMTLSCNVLINSAGLHAPALARRIDGLPASNIPKDYLCKGSYFTLSGRAPFSRLIYPVPQHAGLGVHLTLDLGGQAKFGPDTEWVETEDYTLDPARADVFYEAVRSYWPALPDDALAPGYTGIRPKISGPHEPAADFVIAGPAAHGVPGLVNLFGIESPGLTSSLALAEETLARLNG | Function: Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG or(S)-2-hydroxyglutarate) to 2-oxoglutarate (alpha-ketoglutarate) (By similarity). Also displays some oxidase activity in vitro on L-2-hydroxyglutarate with O2 as the electron acceptor, but this activity is most likely not physiological .
Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 38740
Sequence Length: 369
EC: 1.1.99.2
|
Q9LES4 | MKHKPETAAFSLIRPLEAWAANANKACNTKKMLPCLGRKWMRLSTRNLKPTWNLINVVDASKTIVRGISGGAETIAKERVDTVVIGAGVVGLAVARELSLRGREVLILDAASSFGTVTSSRNSEVVHAGIYYPPNSLKAKFCVRGRELLYKYCSEYEIPHKKIGKLIVATGSSEIPKLDLLMHLGTQNRVSGLRMLEGFEAMRMEPQLRCVKALLSPESGILDTHSFMLSLVEKSFDFMVYRDNNNLRLQGEAQNNHATFSYNTVVLNGRVEEKKMHLYVADTRFSESRCEAEAQLELIPNLVVNSAGLGAQALAKRLHGLDHRFVPSSHYARGCYFTLSGIKAPPFNKLVYPIPEEGGLGVHVTVDLNGLVKFGPDVEWIECTDDTSSFLNKFDYRVNPQRSEKFYPEIRKYYPDLKDGSLEPGYSGIRPKLSGPKQSPADFVIQGEETHGVPGLVNLFGIESPGLTSSLAIAEHIANKFLR | Function: Catalyzes the oxidation of (S)-2-hydroxyglutarate to 2-oxoglutarate. Is specific for the (S) enantiomer and possesses very poor activity toward (R)-2-hydroxyglutarate. Has no activity toward related 2-hydroxy acids, such as glycolate, L-lactate or D-lactate.
Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 53526
Sequence Length: 483
Subcellular Location: Mitochondrion
EC: 1.1.99.2
|
A7MBI3 | MVPALRYLGSVCGRARGIFPGGFSAAHTPASGKSRLLCQGGRRASTSSFDIVIIGGGIVGLASARALILRHPALSIGVLEKEKNLAVHQTGHNSGVIHSGIYYKPESLKAKLCVQGAALIYEYCNQKGISYKQCGKLIVAVEQEEIPRLQALYERGLQNGVQGLRLIQQEDIKKKEPYCRGLMAIDCPYTGIVDYRQVAFSFAKDFQEAGGSVLTNFEVEDIEMARESPSRSKDGMKYPIVIRNTKGEEVRCQYVVTCAGLYSDRISELSGCNPNPRIVPFRGDYLVLKPEKRYLVKGNIYPVPDSRFPFLGVHFTPRMDGNIWLGPNAILAFKREGYRPFDFSARDIMDIIIKSGLIKLVFQNFSYGVNEMYKACFLSATVKHLQKFIPEITISDVLRGPAGVRAQALDRDGNLIEDFVFDGGVGDIGNRILHVRNAPSPAATSSLAISGMIADEVQQRFKL | Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 51022
Sequence Length: 463
Subcellular Location: Mitochondrion
EC: 1.1.99.2
|
Q9N4Z0 | MLNRGTFQVFRGISGPPKKSVDLPKYDLVIVGGGIVGCATARQLLIEKPQLKVALIEKEKELAVHQSGHNSGVIHAGIYYTPGSLKAKLCVEGLDLSYEFFDKEKVPYKKTGKLIVAVEPEEVPRLDALFSRAQTNGCRDIEMIDSSKITELEPHCRGLKALWSPHTGIVDWGYVTKRFGEDFEKRGGKIYTSYPLEKISDNHDPGYPIRVSSGPALAEFETKNLITCAGLQSDRVAALSGCSTDPKIVPFRGEYLLLKPEKRHLVKTNIYPVPDPRFPFLGVHFTPRMNGDIWLGPNAVLAYKREGYSYFSISPSDLLESLSYSGMQKLVKKHFTFGIKELYRGVWIAAQVKQLQRFIPELKLSDVTRGPAGVRAQAMDSAGNLVDDFVFDSGTGKLSPLLMHVRNAPSPAATSSLAIAKMITSEAINRFKL | Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 47901
Sequence Length: 433
Subcellular Location: Mitochondrion
EC: 1.1.99.2
|
Q55GI5 | MKNSSSMLKGVKSFIGSGIYTNKPIYDVAIVGGGIVGLATGRELLKRNPKLKIVILEKENEIAPHQSSHNSGVIHCGIYYKPGSLRAKLCTKGSKLMYDYCNENQINYENCGKLIVATKKEEFQQLEQLYKRGIENGVPNIKLLESKEQLLSIEPFINGGLRAIHTPSTGIIDYKEVSKSFGNDITEKFGKDSKSEIKLNFNAKNFKYNSNDKLLLISTGDDDDDEEQQQSILTKYSIVCGGMNSDRIAKVAYGNDEPSIVPFRGSFLQFKPEFRHLIKGNVYPLPNASFPFLGVHFTKRINGEVWLGPNAVLSFDREGYKFTDFNLHDTIDLIKNPGLFKLAKKHWKYGLGELYRDFNKDHFIQLLKPYMPNITVDMLEYGGSGVRSQAISKSGDLIEDFIFDTPSDVPIIHVRNSPSPAATSSLAIAIEIVDLAQNNFKNLNSL | Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 49908
Sequence Length: 446
Subcellular Location: Mitochondrion
EC: 1.1.99.2
|
Q9H9P8 | MVPALRYLVGACGRARGLFAGGSPGACGFASGRPRPLCGGSRSASTSSFDIVIVGGGIVGLASARALILRHPSLSIGVLEKEKDLAVHQTGHNSGVIHSGIYYKPESLKAKLCVQGAALLYEYCQQKGISYKQCGKLIVAVEQEEIPRLQALYEKGLQNGVPGLRLIQQEDIKKKEPYCRGLMAIDCPHTGIVDYRQVALSFAQDFQEAGGSVLTNFEVKGIEMAKESPSRSIDGMQYPIVIKNTKGEEIRCQYVVTCAGLYSDRISELSGCTPDPRIVPFRGDYLLLKPEKCYLVKGNIYPVPDSRFPFLGVHFTPRMDGSIWLGPNAVLAFKREGYRPFDFSATDVMDIIINSGLIKLASQNFSYGVTEMYKACFLGATVKYLQKFIPEITISDILRGPAGVRAQALDRDGNLVEDFVFDAGVGDIGNRILHVRNAPSPAATSSIAISGMIADEVQQRFEL | Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 50316
Sequence Length: 463
Subcellular Location: Mitochondrion
EC: 1.1.99.2
|
S2DJ52 | MDFQVIIIGGGIVGLATGLKIKQRNPNIKVALLEKEEEVAKHQTGNNSGVIHSGLYYKPGSLKAKNCIEGYHELVRFCEEENIPFELTGKVVVATRKEQVPLLNSLLERGLQNGLKGTRSITLDELKHFEPYCAGVAAIHVPQTGIVDYKLVAEKYAEKFQILGGQVFLGHKVIKVETQNTASIIHTSKGSFSTNLLINCAGLYSDKVAQMNQKESLDVKIIPFRGEYYKIKKEREYLVKNLIYPVPDPNFPFLGVHFTRMMKGGVEAGPNAVLAFKREGYKKSQVNFSELAETLSWPGFQKVASKYWKTGMGELFRSFSKKAFTDALKELIPDIQESDLIEGGAGVRAQACDRTGGLLDDFCIREDQNAIHVLNAPSPAATSSLSIGGTVCEWALKRF | Function: Catalyzes the dehydrogenation of L-2-hydroxyglutarate (L2HG or(S)-2-hydroxyglutarate) to 2-oxoglutarate (alpha-ketoglutarate). Active in vitro with the artificial electron acceptor 2,6-dichlorophenolindophenol (DCPIP). Also displays a very low oxidase activity in vitro on L-2-hydroxyglutarate with O2 as the electron acceptor, but this activity is most likely not physiological.
Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 44131
Sequence Length: 399
EC: 1.1.99.2
|
Q91YP0 | MWPTLRYVGGVCGLARYCVAGGFLRASGPASGVPGLLCGGGRRSSSTSSFDIVIVGGGIVGLASARTLILKHPGLSIGVVEKEKDLALHQTGHNSGVIHSGIYYKPESLKAKLCVEGAALIYEYCNLKGIPYRQCGKLIVAVEQEEIPRLQALYERGLQNGVEGLRLIQQEDIKKKEPYCRGLMAIDCPYTGIVNYQQVALSFAQDFQEAGGSILRDFEVKGIEIAKENSSRSKDGMNYPIAVKNSKGKEIRCRYVVTCAGLYSDRISELSGCNPDPQIVPFRGDYLVLKPEKGYLVKGNIYPVPDSRFPFLGVHFTPRLDGTIWLGPNAVLAFKREGYRPFDFDARDVMEVILKSGFINLVFQHFSYGVNEMYKACFLSETVKHLQKFIPEITISDVLRGPAGVRAQALDRDGNLVEDFVFDGGTGEIADRVLHVRNAPSPAATSSLAISRMIAEEAQQRFKL | Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 50899
Sequence Length: 464
Subcellular Location: Mitochondrion
EC: 1.1.99.2
|
A7SMW7 | MLKTSFLLSKRNAVSLSRVLATGISGRNVRHLTLQPSEHYDVAIVGGGIVGLATARELILRHPKLTFCVLEKEKELSMHQSGHNSGVIHCGIYYTPGSLKAKLCVQGLDLTYQYCDEHNIPYKKCGKLIVAVEDKEIPLLNNLYERGKKNGVKDLTMVDKRGIKEIEPHCEGMFAIVSPNTGIVDWAQVALAYGDDFRKGGGDIFTGYEVTDFKCASESGKSQEKEAGLTHPVTVFSNNKQTIKCRYVITCGGLYSDRLAEKSGCNREPRIVPFRGDYLVLKPEKCHLVKGNIYPVPDPNFPFLGVHFTPRMDGSVWLGPNAVLAFAREGYNLLDINLRDLADALAFRGLRQLMFKYFSFGVGEYYRGLNHAAQVKQLQKYIPSVTADDVVSGPSGVRAQALDRDGNLVDDFVFDGGVGEIGSRVLHVRNAPSPAATSSLAIARMVADKAAERFTL | Catalytic Activity: (S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2
Sequence Mass (Da): 50175
Sequence Length: 456
Subcellular Location: Mitochondrion
EC: 1.1.99.2
|
Q24372 | MWRPSISNCVWSTLLLAIFVQQTLAQRTPTISYITQEQIKDIGGTVEFDCSVQYAKEYNVLFLKTDSDPVFLSTGSTLVIKDSRFSLRYDPNSSTYKLQIKDIQETDAGTYTCQVVISTVHKVSAEVKLSVRRPPVISDNSTQSVVASEGSEVQMECYASGYPTPTITWRRENNAILPTDSATYVGNTLRIKSVKKEDRGTYYCVADNGVSKGDRRNINVEVEFAPVITVPRPRLGQALQYDMDLECHIEAYPPPAIVWTKDDIQLANNQHYSISHFATADEYTDSTLRVITVEKRQYGDYVCKATNRFGEAEARVNLFETIIPVCPPACGQAYIAGAEDVSATSFALVGILAALLFAR | Function: Required for normal tracheal development and maintenance of the trans-epithelial diffusion barrier. Functions as a homophilic cell-adhesion molecule. May play a role in early neuronal differentiation and axon outgrowth.
Location Topology: Lipid-anchor
Sequence Mass (Da): 39939
Sequence Length: 359
Subcellular Location: Cell membrane
|
Q25092 | EGCKPCECDKSGSRLEQCNLYDGQCDCVDGRGGRDCSQCPEMSWGDPFLGCKSCTCNPDGARSLYCNKVTGQCECPRGVTGLNCDRCDRGTYGALPQCIPCGECFDNWDKLIAQLRDEAAAQLRIGTEIKLSGPPGAFAKEFEELEQVLMDMKSHVNSANVSSDQLENIDQELDNLSSKLKDLKPNLASHGSRTGEASVKISELYSRVLNLQSEFNKSSAKTKELRENALEIQEQDVSGAYASIQESLVKSSALQAKLTDAENSKNISVYFRTSVEHFLQNSNFSDANSENGNENSLDKVVEFMKAVDENVSSINTELCGGTGSPCHEDCGGAMCGKCGGELCGDGAVTKAVEAKNTSRKAEELIKSKYRSTSSTLSELENSNKQCKQATAEAKNNAHEA | Function: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Sequence Mass (Da): 43262
Sequence Length: 400
Domain: The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Subcellular Location: Secreted
|
P31242 | MMITLRKLPLAVAVAAGVMSAQALAVDFHGYARSGIGWTGSGGEQQCFKATGAQSKYRLGNECETYAELKLGQELWKEGDKSFYFDTNVAYSVNQEDDWESTSPAFREANIQGKNLIDWLPGSTLWAGKRFYQRHDVHMIDFYYWDISGPGAGLENVDLGFGKLSLAATRNSESGGSYTFSSDDTKKYAAKTANDVFDIRLAGLETNPGGVLELGVDYGRANPQDDYRLEDGASKDGWMWTGEHTQSIWGGFNKFVVQYATDAMTSWNSGHSQGTSIDNNGSMIRVLDHGAMDFNDDWGLMYVAMYQELDLDSKNGSTWYTVGVRPMYKWTPIMSTQLEIGYDNVKSQRTSENNNQYKITLAQQWQAGNSVWSRPAIRIFATYAKWDENWGYSNTSGLQTKDSSGSGAFTSSRGDDSEVTFGAQMEVWW | Function: Involved in the transport of maltose and maltodextrins. Does not act as a receptor for phages.
Catalytic Activity: beta-maltose(in) = beta-maltose(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47805
Sequence Length: 429
Subcellular Location: Cell outer membrane
|
Q65QT7 | MKKTLLAVAIGGAMFATSAAAVDFHGYARSGIGWTSGGGEQTALKVNGGGSKYRLGNETETYAEFKLGQELFKDGNKSIYLDSNIAYSIDQQVDWEATDPAFREINVQFKNFAEDLLPGATLWAGKRFYQRHDVHMNDFYYWDISGPGAGVENIDLGFGKLSLAVTRNTEGGGTATYGQDKVYYIDNNGQIQYRYEDRKADVYNDVFDIRLAELNVNPNGKLEIGFDYGNAHTKNGYHLEPGASKNGYMITLEHTQGEFFGGFNKFVAQYATDSMTSWNTGHSQGGSVNNNGDMLRLIDHGVVQFSPKVEMMYALIYEKTDLDNNQGKTWYSAGIRPMYKWNKTMSTLLEVGYDRIKEQSSGKKNDLAKVTLAQQWQAGDSIWARPAIRVFGTYGHWNDKFNITDRTNAGYKAKDAEFVAGVQFEAWW | Function: Involved in the transport of maltose and maltodextrins.
Catalytic Activity: beta-maltose(in) = beta-maltose(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47895
Sequence Length: 428
Subcellular Location: Cell outer membrane
|
Q6D2C3 | MKRKLLTTSIALSLAMLATPSYSVDFSGYFRSGVGVSNHGKQQTADKSYVGRLGNEDDTYGEIQLGQQLYNENGKTFYFDSMISMFSNSSNDNETTKNDDAEFGLRQLNLQAKGFVPGLPDATVWAGKRYYQRHDLHIIDTKYWNISGAGAGIENVKAGEGAFSFAWIRADAENMDVDCGNSLNSQECSSREDTYNDLNINYLDARYAGWKPWDGAWTEFGISYAMPNEADTQKNIFLAEGQKFDPKNSMMITGELSHYFSGLKSNQKLVLQYADKGLAHNMVDQGGGWYDVWSINDSAKGYRVIQAGDLPITDHISLSHVLTYGKADEISRWRDSTELLSAVGRGQYAWTKNQKTYLEAGTYQKKDSWKAGTETKYSGQKYTLAHAFSADIPMLTRPELRFFVSYLDGGNENRNRFNDDRSNTVNFGIQAEAWW | Function: Involved in the transport of maltose and maltodextrins.
Catalytic Activity: beta-maltose(in) = beta-maltose(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48922
Sequence Length: 435
Subcellular Location: Cell outer membrane
|
O87237 | MKEKNMKKNDTIELQLGKYLEDDMIELAEGDESHGGTTPATPAISILSAYISTNTCPTTKCTRAC | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. When present individually lacticin 3147 A2 exhibits weak activity towards L.lactis strain AM2 and L.lactis strain HP, and no activity towards L.lactis strain IFPL359, but when combined with lacticin 3147 A1 it displays strong activity towards all three strains.
PTM: Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor.
Sequence Mass (Da): 7080
Sequence Length: 65
Subcellular Location: Secreted
|
P83675 | MRNDVLTLTNPMEENELEQILGGGNGVLKTISHECNMNTWQFLFTCC | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Ruminococcin A is a broad spectrum bacteriocin exhibiting activity against a wide range of pathogenic clostridia and B.longum (By similarity).
PTM: Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor.
Sequence Mass (Da): 5346
Sequence Length: 47
Subcellular Location: Secreted
|
P83674 | MRNDVLTLTNPMEEKELEQILGGGNGVLKTISHECNMNTWQFLFTCC | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Ruminococcin A is a broad spectrum bacteriocin exhibiting activity against a wide range of pathogenic clostridia and B.longum.
PTM: Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor.
Sequence Mass (Da): 5360
Sequence Length: 47
Subcellular Location: Secreted
|
H2A7G5 | MMNATENQIFVETVSDQELEMLIGGADRGWIKTLTKDCPNVISSICAGTIITACKNCA | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. Macedovicin inhibits a broad spectrum of lactic acid bacteria, several food spoilage species (e.g. Clostridium spp.) and oral streptococci . The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
PTM: Maturation of macedovicin involves the enzymatic dehydration of Thr-33 and Thr-35 into dehydrobutyrine residues, that can form a beta-methyllanthionine bond with Cys-38 and Cys-57, respectively . This is followed by membrane translocation and cleavage of the modified precursor.
Sequence Mass (Da): 6250
Sequence Length: 58
Subcellular Location: Secreted
|
P36501 | MEKNNEVINSIQEVSLEELDQIIGAGKNGVFKTISHECHLNTWAFLATCCS | Function: Lanthionine-containing peptide antibiotic (lantibiotic) active on certain Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
PTM: Maturation of lantibiotics involves the enzymatic conversion of Thr, and Ser into dehydrated AA and the formation of thioether bonds with cysteine. This is followed by membrane translocation and cleavage of the modified precursor.
Sequence Mass (Da): 5666
Sequence Length: 51
Subcellular Location: Secreted
|
F1MVX2 | MAQRAFPNPYADYNKSLAEGYFDSAGRLTPEFSQRLNNKIRELLQQMERGLKSADPRDSTVYTGWAGIAVLYLHLYDVFGDPNYLQMAHGYVKQSLNSLSKHSITFLCGDGGPLAVAAVVHHKMNNEKQAEECITRLIHLNKIDPHAPSEMLYGRMGYISALLFVNKNFGEEKIPQSHIQQICETVLTSGEDLARKRRFTGKTPLMYEWYQEYYVGAAHGLAGIYYYLMQPSLQVSHAKLHNLVKPSVDYVCQLKFPSGNYPPCVDDSRDLLIHWCHGAPGVIYMLTQAYKVFKEERYLNDAYQCADVIWQYGLLKKGYGLCHGTAGNAYAFLSLYSLTQDAKYLYRACKFAEWCLDYGEHGCRTPDTPFSLFEGMAGTIYFLADLLVPTKARFPAFEL | Function: Functions as glutathione transferase. Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate. Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxidant defense mechanism (By similarity). May play a role in EPS8 signaling (By similarity). Binds glutathione .
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45309
Sequence Length: 399
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
Q90ZL2 | MSEQRALKNPYPDYTGLGCAQDLFDMQGNLTQHFATSISSKISELLAILENGLKNADPRDCTGYTGWAGIALLYLHLHSVFGDPTFLQRALDYVNRSLRSLTQRWVTFLCGDAGPLAIAAVVYHRLQKHQESDECLNRLLQLQPSVVQGKGRLPDELLYGRTGYLYSLIFVNQQFQQEKIPFQYIQQICDAILESGQILSQRNKIQDQSPLMYEWYQEEYVGAAHGLSGIYYYLMQPGLVAGQDRVFSLVKPSVNYVCQLKFPSGNYAPCVGDARDLLVHWCHGSPGVIYMLIQAFKVFGVRQYLEDALQCGEVIWQRGLLKKGYGLCHGAAGNAYGFLALYKITQDPKHLYRACMFADWCMNYGRHGCRTPDTPFSLFEGMAGTIYFLADLLQPARAKFPCFEV | Function: Functions as glutathione transferase. Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate (By similarity). Binds glutathione (By similarity).
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45752
Sequence Length: 405
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
O43813 | MAQRAFPNPYADYNKSLAEGYFDAAGRLTPEFSQRLTNKIRELLQQMERGLKSADPRDGTGYTGWAGIAVLYLHLYDVFGDPAYLQLAHGYVKQSLNCLTKRSITFLCGDAGPLAVAAVLYHKMNNEKQAEDCITRLIHLNKIDPHAPNEMLYGRIGYIYALLFVNKNFGVEKIPQSHIQQICETILTSGENLARKRNFTAKSPLMYEWYQEYYVGAAHGLAGIYYYLMQPSLQVSQGKLHSLVKPSVDYVCQLKFPSGNYPPCIGDNRDLLVHWCHGAPGVIYMLIQAYKVFREEKYLCDAYQCADVIWQYGLLKKGYGLCHGSAGNAYAFLTLYNLTQDMKYLYRACKFAEWCLEYGEHGCRTPDTPFSLFEGMAGTIYFLADLLVPTKARFPAFEL | Function: Functions as glutathione transferase. Catalyzes conjugation of the glutathione (GSH) to artificial substrates 1-chloro-2,4-dinitrobenzene (CDNB) and p-nitrophenyl acetate. Mitigates neuronal oxidative stress during normal postnatal development and in response to oxidative stresses probably through GSH antioxidant defense mechanism (By similarity). May play a role in EPS8 signaling. Binds glutathione .
Catalytic Activity: glutathione + RX = a halide anion + an S-substituted glutathione + H(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45283
Sequence Length: 399
Subcellular Location: Cytoplasm
EC: 2.5.1.18
|
Q9NS86 | MGETMSKRLKLHLGGEAEMEERAFVNPFPDYEAAAGALLASGAAEETGCVRPPATTDEPGLPFHQDGKIIHNFIRRIQTKIKDLLQQMEEGLKTADPHDCSAYTGWTGIALLYLQLYRVTCDQTYLLRSLDYVKRTLRNLNGRRVTFLCGDAGPLAVGAVIYHKLRSDCESQECVTKLLQLQRSVVCQESDLPDELLYGRAGYLYALLYLNTEIGPGTVCESAIKEVVNAIIESGKTLSREERKTERCPLLYQWHRKQYVGAAHGMAGIYYMLMQPAAKVDQETLTEMVKPSIDYVRHKKFRSGNYPSSLSNETDRLVHWCHGAPGVIHMLMQAYKVFKEEKYLKEAMECSDVIWQRGLLRKGYGICHGTAGNGYSFLSLYRLTQDKKYLYRACKFAEWCLDYGAHGCRIPDRPYSLFEGMAGAIHFLSDVLGPETSRFPAFELDSSKRD | Function: Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes.
PTM: Myristoylated. Essential for membrane association.
Sequence Mass (Da): 50854
Sequence Length: 450
Subcellular Location: Nucleus
|
Q9JJK2 | MGETMSKRLKFHLGEAEMEERSFPNPFPDYEAAASAAGLAAGSAEETGRVCPLPTTEDPGLPFHPNGKIVPNFIKRIQTKIKDLLQQMEEGLKTADPHDCSAYTGWTGIALLYLQLYRVTGDQTYLLRSLDYVKRTLRNLSGRRVTFLCGDAGPLAVGAVIYHKLKSECESQECITKLLQMHRTIVCQESELPDELLYGRAGYLYALLYLNTEIGPGTVGETAIKEVVSAIIESGKSLSREERKSERCPLLYQWHRKQYVGAAHGMAGIYYMLMQPEAKVDQETLTEMVKPSIDYVRHKKFRSGNYPSSLSNETDRLVHWCHGAPGVIHVLLQAYQVFKEEKYLKEAMECSDVIWQRGLLRKGYGICHGTSGNGYSFLSLYRLTQDKKYLYRACKFAEWCLDYGAHGCRIPDRPYSLFEGMAGAVHFLSDILVPETARFPAFELGFLQKD | Function: Necessary for abscisic acid (ABA) binding on the cell membrane and activation of the ABA signaling pathway in granulocytes.
PTM: Myristoylated. Essential for membrane association.
Sequence Mass (Da): 50777
Sequence Length: 450
Subcellular Location: Nucleus
|
Q8BSM7 | MAPTLKQAYRRRWWMACTAVVENLFFSAVLLGWASLLIMLKKEGFYSSLCPAENRTNTTQDEQHQWTSCDQQEKMLNLGFTIGSFLLSATTLPLGILMDRFGPRPLRLVGSACFAASCTLMALASRDTEVLSPLIFLALSLNGFAGICLTFTSLTLPNMFGNLRSTFMALMIGSYASSAITFPGIKLIYDAGVPFTVIMFTWSGLACLIFLNCALNWPAEAFPAPEEVDYTKKIKLIGLALDHKVTGDRFYTHVTIVGQRLSQKSPSLEEGADAFISSPDIPGTSEETPEKSVPFRKSLCSPIFLWSLVTMGMTQLRVIFYMGAMNKILEFIVTGGKERETNEQRQKVEETVEFYSSIFGVMQLLCLLTCPLIGYIMDWRIKDCVDAPTEGTLNENASFGDARDGASTKFTRPRYRKVQKLTNAINAFTLTNILLVGFGIACLIKNLHLQLLAFVLHTIVRGFFHSACGGLYAAVFPSNHFGTLTGLQSLISAVFALLQQLLFMAMVGPLHGDPFWVNLGLLLLSFLGFLLPSYLYYYRSRLQREYATNLVDPQKVLNTSKVAT | Function: Uniport that mediates the transport of neutral amino acids such as L-leucine, L-isoleucine, L-valine, and L-phenylalanine . The transport activity is sodium ions-independent, electroneutral and mediated by a facilitated diffusion .
Catalytic Activity: D-leucine(in) = D-leucine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62644
Sequence Length: 564
Subcellular Location: Cell membrane
|
Q1ELU5 | MKFSIIALALAVAFVCVAESRSEEEGYDVSEEIQAEELEEAERGGIDRKLMEVVNNLRKVQGREDSEEAGRGGINRKLMEMVNNLRKVQGREDSEEAGRGGINRKLMEMVNNLRKVQGREDSEEAGRGGINRKLMEMVNNLRKVQGREDSEEAGRGGINRKLMEMVNNLRKVQGREDTEEARGLKDKFKSMGEKLKQYIQTWKAKFG | Function: M-zodatoxin-Lt4a: Has antimicrobial activity against Gram-positive bacteria (A.globiformis VKM Ac-1112 (MIC=0.3 uM), and B.subtilis VKM B-501 (MIC=1.1 uM)), Gram-negative bacteria (E.coli DH5-alpha (MIC=4.5 uM), E.coli MH1 (MIC=3.2 uM), and P.aeruginosa PAO1 (MIC>35 uM)), and yeasts (P.pastoris GS115 (MIC=36 uM), and S.cerevisiae Y190 (MIC=18 uM)). Does not have hemolytic activity against rabbit erythrocytes. Causes paralysis, but is not lethal when injected into insect (M.domestica) larvae.
PTM: Cleavage of the propeptide depends on the processing quadruplet motif (PQM) (XXXR, with at least one of X being E) and the inverted PQM (RXXX, with at least one of X being E).
Sequence Mass (Da): 23509
Sequence Length: 207
Domain: M-zodatoxin-Lt4a: Probably forms an alpha-helix which disrupts target cell membranes.
Subcellular Location: Secreted
|
Q8N370 | MAPTLATAHRRRWWMACTAVLENLLFSAVLLGWGSLLIMLKSEGFYSYLCTEPENVTNGTVGGTAEPGHEEVSWMNGWLSCQAQDEMLNLAFTVGSFLLSAITLPLGIVMDKYGPRKLRLLGSACFAVSCLLIAYGASKPNALSVLIFIALALNGFGGMCMTFTSLTLPNMFGDLRSTFIALMIGSYASSAVTFPGIKLIYDAGVSFIVVLVVWAGCSGLVFLNCFFNWPLEPFPGPEDMDYSVKIKFSWLGFDHKITGKQFYKQVTTVGRRLSVGSSMRSAKEQVALQEGHKLCLSTVDLEVKCQPDAAVAPSFMHSVFSPILLLSLVTMCVTQLRLIFYMGAMNNILKFLVSGDQKTVGLYTSIFGVLQLLCLLTAPVIGYIMDWRLKECEDASEEPEEKDANQGEKKKKKRDRQIQKITNAMRAFAFTNLLLVGFGVTCLIPNLPLQILSFILHTIVRGFIHSAVGGLYAAVYPSTQFGSLTGLQSLISALFALLQQPLFLAMMGPLQGDPLWVNVGLLLLSLLGFCLPLYLICYRRQLERQLQQRQEDDKLFLKINGSSNQEAFV | Function: Uniporter that mediates the transport of the stereospecific L-phenylalanine, L-methionine and L-branched-chain amino acids, between the extracellular space and the cytoplasm and may control the transepithelial (re)absorption of neutral amino acid in kidney and small intestine . The transport activity is mediated through facilitated diffusion and is sodium ions-, chloride ions- and pH-independent .
PTM: Glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: L-leucine(in) = L-leucine(out)
Sequence Mass (Da): 62747
Sequence Length: 569
Subcellular Location: Cell membrane
|
A4IHK6 | MAPTLATAHRRRWWMACTAVVENLFFSAVLLGWGSLLIMLKSEGFYSYLCHYPDNTTYHNSTGNETNQELVMDMNGWLICKEQDEMLNLAFTVGSFLLSAISLPLGIIMDKYGPRKLRLSGSASFGVSCLLIAYGASNPNSLSVLIFVALCLNGFGGMCMTFTSLTLPNMFGDLRSTFIALMIGSYASSAVTFPFIKVIYDLGVSFITILIVWAACAGLVFFNCFFNWPLEPFPGPEDMDYTVKIKFSWLGFDHKITGKQFYKQVTTVGRRLSVGGSMKNPKELSALQNGNKLCLSTVDLEVKCQADNAATPSFMKSVFSPILLLSLITMCVTQLRLIFYMGAMNNILEFLVEGDMDTVSLYTSIFGVLQLLCLLTAPVIGYIMDWKLKDCDDGKEDADEKDTNTDGKKKKKRDRQIQKITNATRAFAFTNFLLVGFGITCLINNLPLQILSFILHTIVRGFIHSAVGGLYAAVYPSTHFGSLTGLQSLISALFALLQQPLFLAMMGPLEGDPLWVNVGLLGVSMFGFCLPLYLIFYKRSLERQRKQKIEDSKLYLKINGTPDHEAFV | Function: Uniporter that mediates the transport of the stereospecific L-phenylalanine, L-methionine and L-branched-chain amino acids, between the extracellular space and the cytoplasm and may control the transepithelial (re)absorption of neutral amino acid in kidney and small intestine. The transport activity is mediated through facilitated diffusion and is sodium ions-, chloride ions- and pH-independent.
PTM: Glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: L-leucine(in) = L-leucine(out)
Sequence Mass (Da): 63139
Sequence Length: 568
Subcellular Location: Cell membrane
|
Q1ELU9 | MKYCVVILALLVALVCITESRSTETGYAVAETLEDNDLDELQAYLEEIAEASEMEDFSNIEEARGFFGKMKEYFKKFGASFKRRFANLKKRLG | Function: Has antimicrobial activity against. Gram-positive bacteria (A.globiformis VKM Ac-1112 (MIC=1.1 uM), and B.subtilis VKM B-501 (MIC=0.6 uM)), Gram-negative bacteria (E.coli DH5-alpha (MIC=0.6 uM), E.coli MH1 (MIC=0.6 uM), and P.aeruginosa PAO1 (MIC=18 uM)), and yeasts (P.pastoris GS115 (MIC>37 uM), and S.cerevisiae Y190 (MIC>37 uM)). Also has a moderate hemolytic activity against rabbit erythrocytes. Causes paralysis, but is not lethal when injected into insect (M.domestica) larvae.
PTM: Cleavage of the propeptide depends on the processing quadruplet motif (XXXR, with at least one of X being E).
Sequence Mass (Da): 10632
Sequence Length: 93
Domain: The mature peptide (65-92) probably forms alpha-helices which disrupt target cell membranes.
Subcellular Location: Secreted
|
Q1ELU8 | MKYFVVALTLAVAFVCIEECKTVEIGYAVSEDFDQNEIDNEEARQAFKTFTPDWNKIRNDAKRMQDNLEQMKKRFNLNLEEARQAFQTFKPDWNKIRYDAMKMQTSLGQMKKRFNL | Function: Does not have antimicrobial activity against neither Gram-positive bacteria (A.globiformis VKM Ac-1112 (MIC>70 uM), and B.subtilis VKM B-501 (MIC>70 uM)), nor Gram-negative bacteria (E.coli DH5-alpha (MIC>70 uM), E.coli MH1 (MIC>70 uM), and P.aeruginosa PAO1 (MIC>70 uM)), nor yeasts (P.pastoris GS115 (MIC>70 uM), and S.cerevisiae Y190 (MIC>70 uM)). Does not have hemolytic activity against rabbit erythrocytes. However, it causes some conductance changes in planar bilayer membranes, without membrane rupture, suggesting a cytolytic function on other biological targets. It causes paralysis, but is not lethal when injected into insect (M.domestica) larvae.
PTM: Cleavage of the propeptide depends on the processing quadruplet motif (XXXR, with at least one of X being E).
Sequence Mass (Da): 13846
Sequence Length: 116
Domain: The mature peptides (45-79 and 84-116) probably form alpha-helices which disrupt target cell membranes.
Subcellular Location: Secreted
|
P0DJE4 | IVGTIAAAAMTVTHVASGRLNDYILKLEEPNGILLHFKAPLFSIIQEGYAVPKSSLVGTGTSNNEGLLDRNGVDEMLNEKYAVQYASETLFSKDLYNAASNPDSAVGFKLMESPEININERNDWPVASTLLRSSNVNVNLKNSDTPLNLAYFIDQGADINTRNGHLNIVKYLVEEEDLSVDGSKYGIDMTIRTALDIATDLK | Function: Presynaptic neurotoxin that causes massive release of neurotransmitters from vertebrate (but not invertebrate) nerve terminals and endocrine cells via a complex mechanism involving activation of receptor(s) and toxin insertion into the plasma membrane with subsequent pore formation. Binds to neurexin-1-alpha (NRXN1) in a calcium dependent manner, adhesion G protein-coupled receptor L1 (ADGRL1, also termed latrophilin-1 and calcium-independent receptor of latrotoxin (CIRL)), and receptor-type tyrosine-protein phosphatase S (PTPRS), also termed PTP sigma. NRXN1 and PTPRS are suggested to provide a platform for binding and subsequent pore formation events. In contrast, binding to ADGRL1 does not involve oligomerization and channel formation, but direct downstream stimulation of the synaptic fusion machinery.
PTM: Processed by furin-like proteases at both the N- and C-termini.
Sequence Mass (Da): 22054
Sequence Length: 202
Domain: The H8 helix is predicted to insert into membranes and form pores by assembling into tetramers. The helix is contained within a helical bundle domain that undergoes significant conformational changes during pore formation to allow exposure of the H8 transmembrane helix and transition of the toxin from a soluble monomer to a transmembrane tetramer.
Subcellular Location: Secreted
|
Q8MLV1 | MQHSPSTTTDHIHFAARFFDRNSYTMDRRLRRPRRTEDVSSGPLLAQSKQPSLLPVTRRTGSVTAAGATATATATAGPATRTRASPSRNKVVAPPSPDLGPRTRRSSRPRSSVGPLTGSGSGSSLPIKAAIKARTPIPEVSEVSSPIRLSTSNLPMTLTTNTSSGAPNKAFNTSSVNSGNSFSRTTTSSTTTTTERIEIRAEGDGEVDTDSIRKRITERLRRSVSKTISNLAGTPVTNTEEGSRYSRSVSRSVYDDEKSSKRSYSTGEEDIDEEDELEEDQFRSFNVTRKSATPAEISCRQLKAPREFGGWLGAFLFLLLLPTAVYYLTWSCTARNACQFKHLNLGILLDVNYLTRQVFQPRVVGAFAAYQVVVFLLVALLPGRRVHLTRETYKFNCLAVSLTLLIASGVAEYLKYPVVTFVLRHYLRFCIFGLVGAFVAAAWSYWLVDTAKYNVLRQTLTNDYGRTGSFVVDFALGRQLNPKWLGRVDWKQFQYRLSLVTTLIYATCYIYQTLVWPQKPQLGEQEGYLYQAKYYWNNVNYDPATLFSASCLLFYVLDAIIFEHHLSSSFELQHEGYGCLLLLRYAATPYLLTAVTKYFYEQRVPISCWYAPLAVAALLSLGLLVKRFSCAYKYKYRLNSQSPIFANIETIHTYQGSRLLLSGMWGWVRQPNYLGDIVALLALAAPMALRPAWPPVLGLSLIILLLLHRATRANARNQARYHSSWQRYSTQVRSYILPRVY | Function: Anchors the lamina and the heterochromatin to the inner nuclear membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83185
Sequence Length: 741
Subcellular Location: Nucleus inner membrane
|
Q14739 | MPSRKFADGEVVRGRWPGSSLYYEVEILSHDSTSQLYTVKYKDGTELELKENDIKPLTSFRQRKGGSTSSSPSRRRGSRSRSRSRSPGRPPKSARRSASASHQADIKEARREVEVKLTPLILKPFGNSISRYNGEPEHIERNDAPHKNTQEKFSLSQESSYIATQYSLRPRREEVKLKEIDSKEEKYVAKELAVRTFEVTPIRAKDLEFGGVPGVFLIMFGLPVFLFLLLLMCKQKDPSLLNFPPPLPALYELWETRVFGVYLLWFLIQVLFYLLPIGKVVEGTPLIDGRRLKYRLNGFYAFILTSAVIGTSLFQGVEFHYVYSHFLQFALAATVFCVVLSVYLYMRSLKAPRNDLSPASSGNAVYDFFIGRELNPRIGTFDLKYFCELRPGLIGWVVINLVMLLAEMKIQDRAVPSLAMILVNSFQLLYVVDALWNEEALLTTMDIIHDGFGFMLAFGDLVWVPFIYSFQAFYLVSHPNEVSWPMASLIIVLKLCGYVIFRGANSQKNAFRKNPSDPKLAHLKTIHTSTGKNLLVSGWWGFVRHPNYLGDLIMALAWSLPCGFNHILPYFYIIYFTMLLVHREARDEYHCKKKYGVAWEKYCQRVPYRIFPYIY | Function: Catalyzes the reduction of the C14-unsaturated bond of lanosterol, as part of the metabolic pathway leading to cholesterol biosynthesis . Plays a critical role in myeloid cell cholesterol biosynthesis which is essential to both myeloid cell growth and functional maturation (By similarity). Mediates the activation of NADPH oxidases, perhaps by maintaining critical levels of cholesterol required for membrane lipid raft formation during neutrophil differentiation (By similarity). Anchors the lamina and the heterochromatin to the inner nuclear membrane .
PTM: Phosphorylated by CDK1 in mitosis when the inner nuclear membrane breaks down into vesicles that dissociate from the lamina and the chromatin. It is phosphorylated by different protein kinases in interphase when the membrane is associated with these structures. Phosphorylation of LBR and HP1 proteins may be responsible for some of the alterations in chromatin organization and nuclear structure which occur at various times during the cell cycle. Phosphorylated by SRPK1. In late anaphase LBR is dephosphorylated, probably by PP1 and/or PP2A, allowing reassociation with chromatin.
Location Topology: Multi-pass membrane protein
Catalytic Activity: 5alpha-cholest-8,14-dien-3beta-ol + H(+) + NADPH = 5alpha-cholest-8-en-3beta-ol + NADP(+)
Sequence Mass (Da): 70703
Sequence Length: 615
Domain: The Tudor domain may not recognize methylation marks, but rather bind unassembled free histone H3.
Pathway: Steroid biosynthesis; cholesterol biosynthesis.
Subcellular Location: Nucleus inner membrane
EC: 1.3.1.70
|
A1XI29 | MIGLSYLLVQVVSFAGILVIDHRWKLAAFRAPAAAALAVTASVALLLTWDVLGVRSGVFFRGQTDFMTGLLVAPEIPFEEVVFLAFLSHLALVCAAGVSRAVDHARDSRAARASRPSRMTGERR | Function: Involved in the biosynthesis of C(50) beta-cyclic carotenoids . May have C(50) carotenoid beta-cyclase activity and produce the C(50) beta-cyclic carotenoid C.p.450 from the C(50) carotenoid dihydrobisanhydrobacterioruberin (DH-BABR) (Probable).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13367
Sequence Length: 124
Pathway: Carotenoid biosynthesis.
Subcellular Location: Cell membrane
EC: 5.5.1.-
|
A1XI30 | MTSLYTTLNLTMSIPVVAVALLAAWRLRGPERRRWLIGVGGALLILMILTAVFDNIMISAGLVAYDDSLTSGIRLGVAPIEDFAYAVAAAVFVPSVWALLTASPRVGAEVGSPTVSGRGDALLTRAPEPGDDDEVRTPERPGTPGLLTTLFWSSRPVSWVNTAAPFALAYFLATGGFDLVGVIGTIFFLVPYNLAMYGINDVFDYESDLRNPRKGGVEGSVLERSRHTATLVASAVTTVPFLVYLVLTGTVESSLWLAASAFAVIAYSAKGLRFKEIPFLDSLTSAFHFVSPAIVGWTIAGAELTGGVWACLIAFMLWGAASQAFGAVQDVRFDREADLKSVATVLGARAAVWFALACYVAAVVVLLAAAPWPASGAAFAILPYLATVAAYVGVTDADAERTNEGWKRFLVLNMLAGFCVTQIVLWSVLVWS | Function: Involved in the biosynthesis of C(50) beta-cyclic carotenoids . The elongase/hydratase domain catalyzes the elongation of lycopene by attaching a C(5) isoprene unit at C-2, as well as the hydroxylation of the previous end of the molecule (By similarity). The enzyme acts at both ends of the substrate, and catalyzes the conversion of lycopene to the C(45) intermediate dihydroisopentenyldehydrorhodopin (DH-IDR) and the conversion of isopentenyldehydrorhodopin (IDR) to the C(50) carotenoid dihydrobisanhydrobacterioruberin (DH-BABR) (By similarity). The beta-cyclase domain may produce the C(50) beta-cyclic carotenoid C.p.450 from the C(50) carotenoid dihydrobisanhydrobacterioruberin (DH-BABR) (Probable).
Catalytic Activity: all-trans-lycopene + dimethylallyl diphosphate + H2O = dihydroisopentenyldehydrorhodopin + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45929
Sequence Length: 432
Pathway: Carotenoid biosynthesis.
Subcellular Location: Cell membrane
|
Q6NYV8 | MVSPRGVCFLLFLLLGSVFGSVFMLGPLLPLMLLSPSRYRWITDRIVATWLTLPVALLELVLGVKVVVTGDGFIPGERSVIIMNHRTRLDWMFLWCCLLRYSYLRQEKICLKAALKSVPGFGWAMQVASFIFIQRRWEDDRTHMSNMLQYFCRIREPVQLLLFPEGTDLTENTRARSDEFAEKNGLQKYEYVLHPRTTGFTFIVDTLRGGDNLDAVHDITVAYPQNIPQTERHLLAGVFPREIHFHVQRFTVASVPAGAAGLQAWCQERWREKERRLQRFYETVPRRFDAPAVGVCVREPCCQSGQCVCVPRCKSEGRVRIILVASLLYWSVFITAACASLCLCPPAQFYFLFMVVFFLCQQRFTGGLELMELACHRYWSRRSADKQE | Function: Exhibits acyl-CoA:lysocardiolipin acyltransferase (ALCAT) activity; catalyzes the reacylation of lyso-cardiolipin to cardiolipin (CL), a key step in CL remodeling (By similarity). Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors (By similarity). Also exhibits 1-acyl-sn-glycerol-3-phosphate acyltransferase activity (AGPAT) activity; converts 1-acyl-sn-glycerol-3- phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3- phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities (By similarity). Required for establishment of the hematopoietic and endothelial lineages .
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44745
Sequence Length: 388
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.-
|
Q6UWP7 | MHSRGREIVVLLNPWSINEAVSSYCTYFIKQDSKSFGIMVSWKGIYFILTLFWGSFFGSIFMLSPFLPLMFVNPSWYRWINNRLVATWLTLPVALLETMFGVKVIITGDAFVPGERSVIIMNHRTRMDWMFLWNCLMRYSYLRLEKICLKASLKGVPGFGWAMQAAAYIFIHRKWKDDKSHFEDMIDYFCDIHEPLQLLIFPEGTDLTENSKSRSNAFAEKNGLQKYEYVLHPRTTGFTFVVDRLREGKNLDAVHDITVAYPHNIPQSEKHLLQGDFPREIHFHVHRYPIDTLPTSKEDLQLWCHKRWEEKEERLRSFYQGEKNFYFTGQSVIPPCKSELRVLVVKLLSILYWTLFSPAMCLLIYLYSLVKWYFIITIVIFVLQERIFGGLEIIELACYRLLHKQPHLNSKKNE | Function: Exhibits acyl-CoA:lysocardiolipin acyltransferase (ALCAT) activity; catalyzes the reacylation of lyso-cardiolipin to cardiolipin (CL), a key step in CL remodeling (By similarity). Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors (By similarity). Also exhibits 1-acyl-sn-glycerol-3-phosphate acyltransferase activity (AGPAT) activity; converts 1-acyl-sn-glycerol-3- phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3- phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone . Possesses both lysophosphatidylinositol acyltransferase (LPIAT) and lysophosphatidylglycerol acyltransferase (LPGAT) activities . Required for establishment of the hematopoietic and endothelial lineages (By similarity).
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48920
Sequence Length: 414
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.-
|
Q3UN02 | MVSWKGIYFILFLFAGSFFGSIFMLGPILPLMFINLSWYRWISSRLVATWLTLPVALLETMFGVRVVITGDAFVPGERSVIIMNHRTRVDWMFLWNCLMRYSYLRVEKICLKSSLKSVPGFGWAMQVAAFIFIHRKWKDDKSHFEDMIDYFCAIHEPLQLLIFPEGTDLTENNKARSNDFAEKNGLQKYEYVLHPRTTGFTFVVDRLREGKNLDAVHDITVAYPYNIPQTEKHLLLGDFPKEIHFHVQRYPADSLPTSKEDLQLWCHRRWEEKEERLRSFYQGEKNFHFTGQSTVPPCKSELRVLVVKLLSIVYWALFCSAMCLLIYLYSPVRWYFIISIVFFVLQERIFGGLEIIELACYRFLHKHPHLNSKKNE | Function: Exhibits acyl-CoA:lysocardiolipin acyltransferase (ALCAT) activity; catalyzes the reacylation of lyso-cardiolipin to cardiolipin (CL), a key step in CL remodeling . Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors . Also exhibits 1-acyl-sn-glycerol-3-phosphate acyltransferase activity (AGPAT) activity; converts 1-acyl-sn-glycerol-3- phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3- phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Possesses lysophosphatidylinositol acyltransferase (LPIAT) activity . Possesses lysophosphatidylglycerol acyltransferase (LPGAT) activity (By similarity). Required for establishment of the hematopoietic and endothelial lineages .
Catalytic Activity: a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphate + CoA
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44400
Sequence Length: 376
Domain: The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.1.-
|
Q8VY08 | MAESRSNRAAVQATNDDASASKLSCVKKGYMKDDYVHLFVKRPVRRSPIINRGYFSRWAAFRKLMSQFLLSGTSSKKQILSLGAGFDTTYFQLLDEGNGPNLYVELDFKEVTSKKAAVIQNSSQLRDKLGANASISIDEGQVLSDHYKLLPVDLRDIPKLRDVISFADMDLSLPTFIIAECVLIYLDPDSSRAIVNWSSKTFSTAVFFLYEQIHPDDAFGHQMIRNLESRGCALLSIDASPTLLAKERLFLDNGWQRAVAWDMLKVYGSFVDTQEKRRIERLELFDEFEEWHMMQEHYCVTYAVNDAMGIFGDFGFTREGGGERMSSSASSP | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A (PP2A) catalytic subunits to form alpha-leucine ester residues (Probable) . Involved in brassinosteroid (BR) signaling. Plays a negative role in BR signaling pathway. Functions as a positive regulator of BRI1 receptor-kinase degradation. Methylates PP2A, thus facilitating its association with activated BRI1. This leads to receptor dephosphorylation and degradation, and thus to the termination of BR signaling. May act upstream of ASK7/BIN2 . Involved in methylation of PP2A during environemental stress responses .
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37550
Sequence Length: 332
Subcellular Location: Cytoplasm
EC: 2.1.1.233
|
Q4WS57 | MSASQIPNLNTLRRGGGRGRLRGRGGFETGAPSEDRHGSRGLAAQDRVVQGTDNDASVSRLSAVEIGYLEDPFAKVLTPPGSGTRRLPIINRGTYVRTTAIDRLVARFLEGPSQTKKQIISLGAGSDTRVFRLLSSRSSASSSDLIYHEIDFSANTAAKIKFIRAAPLLQRTLGLGSAQNVAIPDSGDALHSPTYHLHPVDLRTLAASGSATTSRSPSSPNPAEKDQPPCPLQGVDPTLPTLLISECCLVYLSPREAADVVDYFTKTLFPASVPLGLIIYEPIRPDDAFGRTMVANLATRGIQLQTLHEYASLEAQRRRLREHGLHSGQAAADIDFIWERWVSEAEKERVARLEMLDEVEEWQLLARHYCVAWGWTSGAGEDTTVFDGWKEIDGQTGD | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 43370
Sequence Length: 398
EC: 2.1.1.233
|
P46554 | MDSEAVSSDSHVAAAIATRRRSNSVSDDYSVQRTNDDATQCKYFATQKGYWKDEFISRFANSSSNVSEARRFPEISMGYWARTAAIEKYVRDFLNEFDGNAQVVSLGCGFDTLFWRLVSSGAKLVKYVEVDFSSVTSKKIRHILKPIGPNSVDLKKSFESDAVVSHHADLHAGNYHLIGADLRQANELDQKLATCQLSHDIPTIFIAECVLVYMSADSSTALLKQIVSQFKQPAFVNYEQFRTSDAFTKVMEQNLGDRGIQLHGLEMCESAEKQEERFRNAGFKEVKVMDMNQIFNNFLDQKEVSRIREIEMLDEMELLQQLFAHYCVVSARI | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37816
Sequence Length: 333
EC: 2.1.1.233
|
Q5A387 | MLSPQDRQDKLVRATDLDALSCKYSINRNLYLNPPDEFVKDLVESYQRYLQYCVGYTGLSSSRALKGLFQEKKMPIINRGSYLRTRAIDQVVNKFIGEFKDRCQIVSLGSGSDTRAFQIFKSHANVIYHEIDFPESAKVKKLAILQNPVIRELVGTNETSPLINNKEQFESYSSELHTEKYHLHGIDLRTLKKPDSQIKGFQPEVPTLVISECVLCYLSPDEYQRTMNYWTEIADQNYMGFLIYEPMSLNDQFGETMTLNLQSRGLNLQTFSKYPDLISRKKFLEESCHLKNLRLTDMSYIGGYKVRQDGREWIDHKEMGRINKLEMIDEIEEIRLLLEHYCLIYGEYTEEKTLNFKGIDTWSWILS | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42896
Sequence Length: 367
EC: 2.1.1.233
|
P0CO56 | MTQCGDRRLLALIIYHGAIQTPPPTDPNAAPAHRPAPRPALGRCRPPHRRRRRLRPPVRPPVSLPVALTTRSSAAQLGYLQDPFASLLYRPPMPQPGAFAPQAVGRARKPPLINVGTHHRTWGIDRLVDRFLQRGGKQVVSLGAGSDTRFWRLMSRATPPDLARYVEIDFPHLTSPKAQRIARHRKLYQYLGPSSTAMPPPGHPYTVSKGGTQLSSPLYTLLPLDLRPSPSEPASSISAILSHHVLPQLDPRLPTLFLAECLFPYMSPEDSREIIKWFGETFCSCMGVVYEMVGLDDSFGNVMKRNLAVRNLSIPGSIFSTPESQAGRFTSPMLQGGKFDSAGAKTLWQIREEDVGPEELQRISKLEILDEIEELRLVLEHYVIAWGTKGECMSSISL | Function: Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.
Catalytic Activity: [phosphatase 2A protein]-C-terminal L-leucine + S-adenosyl-L-methionine = [phosphatase 2A protein]-C-terminal L-leucine methyl ester + S-adenosyl-L-homocysteine
Sequence Mass (Da): 44219
Sequence Length: 398
EC: 2.1.1.233
|
P76008 | MSLFHLIAPSGYCIKQHAALRGIQRLTDAGHQVNNVEVIARRCERFAGTETERLEDLNSLARLTTPNTIVLAVRGGYGASRLLADIDWQALVARQQHDPLLICGHSDFTAIQCGLLAHGNVITFSGPMLVANFGADELNAFTEHHFWLALRNETFTIEWQGEGPTCRAEGTLWGGNLAMLISLIGTPWMPKIENGILVLEDINEHPFRVERMLLQLYHAGILPRQKAIILGSFSGSTPNDYDAGYNLESVYAFLRSRLSIPLITGLDFGHEQRTVTLPLGAHAILNNTREGTQLTISGHPVLKM | Function: Releases the terminal D-alanine residue from the cytoplasmic tetrapeptide recycling product L-Ala-gamma-D-Glu-meso-Dap-D-Ala. To a lesser extent, can also cleave D-Ala from murein derivatives containing the tetrapeptide, i.e. MurNAc-tetrapeptide, UDP-MurNAc-tetrapeptide, GlcNAc-MurNAc-tetrapeptide, and GlcNAc-anhMurNAc-tetrapeptide. Does not act on murein sacculi or cross-linked muropeptides. The tripeptides produced by the LcdA reaction can then be reused as peptidoglycan building blocks; LcdA is thereby involved in murein recycling. Is also essential for viability during stationary phase.
Catalytic Activity: H2O + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl-D-alanine = D-alanine + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl
Sequence Mass (Da): 33567
Sequence Length: 304
Pathway: Cell wall biogenesis; peptidoglycan recycling.
Subcellular Location: Cytoplasm
EC: 3.4.17.13
|
Q9I2S7 | MYKDLKFPVLIVHRDIKADTVAGERVRGIAHELEQDGFSILSTASSAEGRIVASTHHGLACILVAAEGAGENQRLLQDVVELIRVARVRAPQLPIFALGEQVTIENAPAESMADLHQLRGILYLFEDTVPFLARQVARAARNYLAGLLPPFFRALVEHTAQSNYSWHTPGHGGGVAYRKSPVGQAFHQFFGENTLRSDLSVSVPELGSLLDHTGPLAEAEDRAARNFGADHTFFVINGTSTANKIVWHSMVGREDLVLVDRNCHKSILHSIIMTGAIPLYLTPERNELGIIGPIPLSEFSKQSIAAKIAASPLARGREPKVKLAVVTNSTYDGLCYNAELIKQTLGDSVEVLHFDEAWYAYAAFHEFYDGRYGMGTSRSEEGPLVFATHSTHKMLAAFSQASMIHVQDGGTRKLDVARFNEAFMMHISTSPQYGIIASLDVASAMMEGPAGRSLIQETFDEALSFRRALANVRQNLDRNDWWFGVWQPEQVEGTDQVGTHDWVLEPSADWHGFGDIAEDYVLLDPIKVTLTTPGLSAGGKLSEQGIPAAIVSRFLWERGLVVEKTGLYSFLVLFSMGITKGKWSTLVTELLEFKRCYDANLPLLDVLPSVAQAGGKRYNGVGLRDLSDAMHASYRDNATAKAMKRMYTVLPEVAMRPSEAYDKLVRGEVEAVPIARLEGRIAAVMLVPYPPGIPLIMPGERFTEATRSILDYLEFARTFERAFPGFDSDVHGLQHQDGPSGRCYTVECIKE | Function: Plays an essential role in lysine utilization by acting as a lysine decarboxylase.
Catalytic Activity: H(+) + L-lysine = cadaverine + CO2
Sequence Mass (Da): 82757
Sequence Length: 751
EC: 4.1.1.18
|
P52095 | MNIIAIMGPHGVFYKDEPIKELESALVAQGFQIIWPQNSVDLLKFIEHNPRICGVIFDWDEYSLDLCSDINQLNEYLPLYAFINTHSTMDVSVQDMRMALWFFEYALGQAEDIAIRMRQYTDEYLDNITPPFTKALFTYVKERKYTFCTPGHMGGTAYQKSPVGCLFYDFFGGNTLKADVSISVTELGSLLDHTGPHLEAEEYIARTFGAEQSYIVTNGTSTSNKIVGMYAAPSGSTLLIDRNCHKSLAHLLMMNDVVPVWLKPTRNALGILGGIPRREFTRDSIEEKVAATTQAQWPVHAVITNSTYDGLLYNTDWIKQTLDVPSIHFDSAWVPYTHFHPIYQGKSGMSGERVAGKVIFETQSTHKMLAALSQASLIHIKGEYDEEAFNEAFMMHTTTSPSYPIVASVETAAAMLRGNPGKRLINRSVERALHFRKEVQRLREESDGWFFDIWQPPQVDEAECWPVAPGEQWHGFNDADADHMFLDPVKVTILTPGMDEQGNMSEEGIPAALVAKFLDERGIVVEKTGPYNLLFLFSIGIDKTKAMGLLRGLTEFKRSYDLNLRIKNMLPDLYAEDPDFYRNMRIQDLAQGIHKLIRKHDLPGLMLRAFDTLPEMIMTPHQAWQRQIKGEVETIALEQLVGRVSANMILPYPPGVPLLMPGEMLTKESRTVLDFLLMLCSVGQHYPGFETDIHGAKQDEDGVYRVRVLKMAG | Function: Plays a role in lysine utilization by acting as a lysine decarboxylase.
Catalytic Activity: H(+) + L-lysine = cadaverine + CO2
Sequence Mass (Da): 80590
Sequence Length: 713
EC: 4.1.1.18
|
O34851 | MKGVFSLNYKPKALNKGDTVGVIAPASPPDPKKLDTALLFLEELGLQVKLGKALKNQHGYLAGQDDERLADLHEMFRDDEVKAVLCACGGFGTGRIAAGIDFSLIRKHPKIFWGYSDITFLHTAIHQNTGLVTFHGPMLSTDIGLDDVHPLTKASYKQLFQETEFTYTEELSPLTELVPGKAEGELVGGNLSLLTSTLGTPFEIDTRGKLLFIEDIDEEPYQIDRMLNQLKMGGKLTDAAGILVCDFHNCVPVKREKSLSLEQVLEDYIISAGRPALRGFKIGHCSPSIAVPIGAKAAMNTAEKTAVIEAGVSEGALKT | Function: May be involved in the degradation of peptidoglycan by catalyzing the cleavage of the terminal D-alanine residue from cytoplasmic murein peptides.
Sequence Mass (Da): 34596
Sequence Length: 319
Pathway: Cell wall degradation; peptidoglycan degradation.
Subcellular Location: Cytoplasm
EC: 3.4.16.-
|
Q9HTZ1 | MTSRPSSDQTWQPIDGRVALIAPASAIATDVLEATLRQLEVHGVDYHLGRHVEARYRYLAGTVEQRLEDLHNAFDMPDITAVWCLRGGYGCGQLLPGLDWGRLQAASPRPLIGFSDISVLLSAFHRHGLPAIHGPVATGLGLSPLSAPREQQERLASLASVSRLLAGIDHELPVQHLGGHKQRVEGALIGGNLTALACMAGTLGGLHAPAGSILVLEDVGEPYYRLERSLWQLLESIDARQLGAICLGSFTDCPRKEVAHSLERIFGEYAAAIEVPLYHHLPSGHGAQNRAWPYGKTAVLEGNRLRW | Function: Releases the terminal D-alanine residue from the cytoplasmic disaccharide-tetrapeptide GlcNAc-MurNAc-L-Ala-gamma-D-Glu-meso-Dap-D-Ala, which is a murein turnover product. Probably also act on free tetrapetide. May be involved in murein recycling.
Catalytic Activity: H2O + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl-D-alanine = D-alanine + N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-alanyl-D-glutamyl-6-carboxy-L-lysyl
Sequence Mass (Da): 33288
Sequence Length: 307
Pathway: Cell wall biogenesis; peptidoglycan recycling.
Subcellular Location: Cytoplasm
EC: 3.4.17.13
|
Q68F33 | MASAENLYQEKMQELQKQMNKVMQTINNHSKVEAFLNSPFGQYLDQHPFVTLSLLVFISLSAVPVGIFLTLIAGTAIAVCLAVLIIEGIVISVGGIALLCILCGLAVMSLGVAAVLCVSYVAGSSVLNYIHAYRVTVGTRGRSGPISLNHETTTAEKSYRSS | Function: Plays an important role in the formation of lipid droplets (LD) which are storage organelles at the center of lipid and energy homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17291
Sequence Length: 162
Subcellular Location: Endoplasmic reticulum membrane
|
P55796 | MYKFLVFSSVLVLFFAQASCQRFIQPTFRPPPTQRPITRTVRQAGQEPLWLYQGDNVPRAPSTADHPILPSKIDDVQLDPNRRYVRSVTNPENNEASIEHSHHTVDIGLDQPIESHRNTRDLRFLYPRGKLPVPTLPPFNPKPIYIDMGNRYRRHASEDQEELRQYNEHFLIPRDIFQE | Function: Antibacterial peptide.
PTM: O-glycosylation is important for the antibacterial activity of lebocin.
Sequence Mass (Da): 21013
Sequence Length: 179
Subcellular Location: Secreted
|
A9YWS7 | MALSNLKSNRTLSSSLITIFIISLFLQYHNIKSQSSWQSRQVPRSETVAFSITEFEKENPDIFLRGDTSISDGILRLTKTDQSGKPLPNTVGRATYLTPIHIWDKTSGELADFSTSFSFIVNTNDSDLHGDGFAFYLGPLHFDVPKNSSGGYLGLFDPENAFPPSKTPILAIEFDGFTNEWDPPSSFQSPHIGIDVGSIVSLEYAQWPINFVPRNALGEANINYNSESKRLSVFVAYPGTQWNSTRVSVVVDLRSVLPEWVRIGFSATTGELVETHDIINWSFESAL | Function: May be involved in arbuscular mycorrhizal (AM) symbiosis with AM fungi.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 31923
Sequence Length: 287
Subcellular Location: Membrane
|
P93114 | MAVPMDTISGPWGNNGGNFWSFRPVNKINQIVISYGGGGNNPIALTFSSTKADGSKDTITVGGGGPDSITGTEMVNIGTDEYLTGISGTFGIYLDNNVLRSITFTTNLKAHGPYGQKVGTPFSSANVVGNEIVGFLGRSGYYVDAIGTYNRHK | Function: Mannose-binding lectin . Preferentially binds mannose at concentrations ranging between 5 and 25 mM, but binds also glucose. Has a marked preference for methylated sugar derivatives, such as alpha-MeMan and alpha-MeGlc, at concentration down to 5 mM . Binds to N-glycans, but not to glycolipid-type or other type of glycans . Binds N-linked high-mannose-type glycans . Has a preference for smaller (Man(2)-Man(6)) high-mannose-type glycans to larger (Man(7)-Man(9)) ones. Recognizes both alpha1-6 extended and alpha1-3 extended monoantennary glycans. The addition of alpha1-2Man to the Man-alpha1-3Man-beta branch results in a significant loss of affinity, but beta1-2GlcNAc has some affinity. Has less affinity for biantennary glycans . However, affinity is significant for the biantennary complex-type N-glycans with bisecting GlcNAc . No affinity is observed for tri- and tetra-antennary glycans . Binds bisected glycans of the mouse brain. Selectively binds to bisecting N-glycans which are in back-fold conformation, and does not favor a glycan with an extend conformation . Has hemagglutinating activity against rabbit erythrocytes at 0.3 ug/ml and against trypsin-treated human erythrocytes at 5 ug/ml. Has mitogenic activity in murine cells .
PTM: Not glycosylated.
Sequence Mass (Da): 16063
Sequence Length: 153
Subcellular Location: Cytoplasm
|
P06027 | GCCPTFWTSFGSNCYRFFAVSLTWAEGEQFCQSFSVPSRGDIDSIGHLVSIHSETEQNFVYHYFETSTKDDTTPEMWLGFNDRTTEGNFQWTDGSPNDFTAWVGSNPDNYGSGEDCTQMVMGAGLNWIDLPCSSTRHYLICKLPLWE | Function: Role in the defense system of the organism against microorganisms. This lectin is specific for Gal-GalNAc.
PTM: The identity of the saccharide is not reported in PubMed:3571253, and it is unlikely to be N-acetylgalactosamine. The sugar attached to Ser-38 is represented simply as Hex.
Sequence Mass (Da): 16661
Sequence Length: 147
Subcellular Location: Secreted
|
D4AL26 | MKLLHFTILLQVSLFPASSLAQAGGNNTEVQVQQTLPGTGIAAVNSVNLLRIYSQDTSGGIREARFEGYWSGGLANDTIAKARANSSIAAASDDLELYKSSSSTNFLLKIRVYYLLPNNTLGEAASDSQSRWYTGSLNQYNFQVASHSRLAAVFVPSTQRPRLRIYAQLGDNTIQEFGYDVSPLSQLEPMFANYLKVGRGWQRLANFGPALPGTGIAALTYTTGLRRSTTRVYFQTTDRRVVERVYDNRSWSDGGTVVRTAKPRTPLAATSFLLTPGNPQSVRVYYGTEDNRILEKGTEGGTYWYDGAFEHSAIPDSQVAAVDWGNGGVFNIRLYIQDGAFKNGISEWAWFRRSWRRGILAIPPA | Function: Probable L-fucose-binding lectin.
Sequence Mass (Da): 40297
Sequence Length: 365
Domain: Adopts the six-bladed beta-propeller fold and contains six binding sites per monomer, each located between two adjacent blades (By similarity). The six binding sites that are non-equivalent, and owing to minor differences in amino-acid composition they exhibit a marked difference in specific ligand recognition (By similarity).
Subcellular Location: Secreted
|
Q8NC56 | MAGLSDLELRRELQALGFQPGPITDTTRDVYRNKLRRLRGEARLRDEERLREEARPRGEERLREEARLREDAPLRARPAAASPRAEPWLSQPASGSAYATPGAYGDIRPSAASWVGSRGLAYPARPAQLRRRASVRGSSEEDEDARTPDRATQGPGLAARRWWAASPAPARLPSSLLGPDPRPGLRATRAGPAGAARARPEVGRRLERWLSRLLLWASLGLLLVFLGILWVKMGKPSAPQEAEDNMKLLPVDCERKTDEFCQAKQKAALLELLHELYNFLAIQAGNFECGNPENLKSKCIPVMEAQEYIANVTSSSSAKFEAALTWILSSNKDVGIWLKGEDQSELVTTVDKVVCLESAHPRMGVGCRLSRALLTAVTNVLIFFWCLAFLWGLLILLKYRWRKLEEEEQAMYEMVKKIIDVVQDHYVDWEQDMERYPYVGILHVRDSLIPPQSRRRMKRVWDRAVEFLASNESRIQTESHRVAGEDMLVWRWTKPSSFSDSER | Function: Nuclear lamina-associated inner nuclear membrane protein that is involved in nuclear structure organization, maintenance of nuclear envelope (NE) integrity and NE reformation after mitosis . Plays a role as transmembrane adapter for the endosomal sorting complexes required for transport (ESCRT), and is thereby involved in ESCRT-mediated NE reformation . Promotes ESCRT-mediated NE closure by recruiting CHMP7 and downstream ESCRT-III proteins IST1/CHMP8 and CHMP2A to the reforming NE during anaphase . During nuclear reassembly, condenses into a liquid-like coating around microtubule spindles and coassembles with CHMP7 to form a macromolecular O-ring seal at the confluence between membranes, chromatin, and the spindle to facilitate early nuclear sealing . Plays a role in the organization of heterochromatin associated with the NE and in the maintenance of NE organization under mechanical stress (By similarity). Required for embryonic development and involved in regulation of several signaling pathways such as MAPK and AKT (By similarity). Required for myoblast differentiation involving regulation of ERK signaling (By similarity). Essential for cardiac homeostasis and proper heart function (By similarity).
PTM: Phosphorylated; strongly phosphorylated in mitosis compared to G1/S.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56975
Sequence Length: 503
Domain: The LEM domain is required for inner nuclear membrane (INM) localization and contains a BANF1 conserved binding motif which allows localization to chromatin . In late anaphase, as the reforming nuclear envelope (NE) surrounds the chromatin disk, both the LEM domain and the disordered regions are necessary for localization to the NE core .
Subcellular Location: Nucleus inner membrane
|
P94565 | MRKINFFDTTLRDGEQSPGVNLNTQEKLAIAKQLERLGADIIEAGFPASSRGDFLAVQEIARTIKNCSVTGLARCVKGDIDAAWEALKDGAQPRIHVFIATSDIHLKHKLKMTREQVIERAVGMVKYAKERFPIVQWSAEDACRTELPFLAEIVEKVIDAGASVINLPDTVGYLAPAEYGNIFKYMKENVPNIHKAKLSAHCHDDLGMAVANSLAAIENGADQIECAVNGIGERAGNAALEEIAVALHTRKDFYQVETGITLNEIKRTSDLVSKLTGMAVPRNKAVVGDNAFAHESGIHQDGFLKEKSTYEIISPELVGVTADALVLGKHSGRHAFKDRLTALGFQFDSEEINKFFTMFKELTEKKKEITDEDLVSLILEEKVTDRKIGYEFLSLQVHYGTSQVPTATLSLKNQENAQLIQEAATGAGSVEAIYNTLERCIDKDVELLDYRIQSNRKGEDAFAQVYVRVLVNGKESAGRGIAQDVLEASAKAYLNAVNRQLVFQSNMSGLKNHTAVGS | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 56912
Sequence Length: 518
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
Q89A49 | MTQKIIIFDTTLRDGEQSLKMSLSVKKKLKIAFALEKLGVDVIEAGFPISSPGDFESVKKISERIKDAKICSLARCIDGDIDIAAKAMKKANSFRIHIFLGTSALHVQSKLKKTFDQIIDMMVSSVKRAQKYTDDVEFSCEDAGRTSLDDLCRIIELAIDLGVKTINIPDTVGYTIPYEFSNIISSIYKKVPNIDKAIISVHCHDDLGMAVANSISAIQVGARQIEGTITGVGERAGNAALEEILMAIKIRKDILNFKTNIKYQEIYSTCRVISSICNIPVPVNKAIIGSNAFSHSSGIHQDGILKDKKTYEIIVPESIGFVSQPLNLTSRSGRAAVKYRMKKIGYKDSDYNIDILYSRFLKLADKKGRVSDSDLKQLVCFNNKLKNLKD | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 43227
Sequence Length: 390
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
Q9HXK5 | MSMLKDPSQKYRPFSAINLPDRTWPSKTITEVPIWCSSDLRDGNQSLIEPMDAAKKMRFFKTLVQVGLKQIEVAFPSASDTDFNFVRELIEGNHIPDDVTIQVLTQAREDLITRTFESLRGAKKAIVHVYNATAPSFRRIVFNQDKQGVVDIATNAAKLIKKLAAEQPETQWSFQYSPEIFSSTELEFSVEVCNAVIDVWQPTPDNKIILNLPATVECATPNVYADQIEWFGRHVDKRDSVIISLHTHNDRGTGVAATELGLMAGADRVEGCLFGNGERTGNVDLVTLALNMYTQGLHPQLDFSDIDAVRKVVEECNQLPVHPRHPYVGDLVHTAFSGSHQDAIRKGFAQQKEDAIWEVPYLPIDPADIGRDYEAVIRVNSQSGKGGITFLLEQEYGISLPRRMQIEFSQVVQGETDRLGLEMTAQQIYSLLENEYLKATSPYVLASHRLQEENGTSAVDLEVSFDGEKQHWRGIGKGPLEALVAALPVKAEIMDYHEHAIGAGANAKAAAYIEIRLEGQRPLHGIGIDENITTASFRALFSALNRAVTQAEAKAA | Function: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate).
Catalytic Activity: 3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+)
Sequence Mass (Da): 61727
Sequence Length: 556
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4.
Subcellular Location: Cytoplasm
EC: 2.3.3.13
|
P56933 | MKKNYRIAVLSGDGIGPEVMQEACKILNVLKKYFFLSLEIQKFNIGGIAIEREGVALPKTTLLGCENSDSILLGSVGGKKWDNLPVEQRPERAALLPLRKHFNLFSNLRPAKLYPELKCLSPLRSDIVKNGFDILCVRELTGGIYFGEPKGFVNKNNTKYAFDTEIYHEYEIIRIAHLAFKLARSRKKKVCSIDKSNVLQSSILWREVVESVSKKYPDVHLSHLYIDNAAMQIIKDPNQFDVLLCSNLFGDIISDECATITGSIGMLPSASFNEKNFGLYEPAGGSAPDIEGKNIANPIAQILSLSMLVRYGMNLNQIADKIDKAVNNVLKKGYRTSDISHDNNFLKTDEMGDLIVDSLINGE | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH
Sequence Mass (Da): 40479
Sequence Length: 363
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.1.1.85
|
Q9AQC8 | NQFDILLCSNLFGDIISDECAVITGSIGMLPSASFNEKNFGLYEPAGGSAPDIAGKNIANPIAQILSLSMLVRYGMKLKKIADKIDKSVASALKAGYRTADISNNNSYLKTNEMGDVISDFLINGK | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate (By similarity).
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH
Sequence Mass (Da): 13438
Sequence Length: 126
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.1.1.85
|
B1VZ57 | MSRSIDLAVIPGDGIGQEVVAQGLKVLNAVLPQDVKLETKEYDLGAQRWHRTGDTLPDAELEALKGHDAILLGAIGDPSVPSGVLERGLLLKLRFAFDHFINLRPSKLFPNTATPLAGRPDIDFVVVREGTEGPYTGNGGSLRTGTPAEVATEVSLNTAYGVERVVRDAFERAAARPRKKLTLVHKNNVLVYAGHLWKNTFDKVAAEYPQVSTDYLHVDAATIFFVTQPERFDVIVTDNLFGDILTDLAAAVSGGIGLAASGNINPTGAFPSMFEPVHGSAPDIAGQGKADPTATVLSVALLLRHLGYEAEAARIEDAVSADLAERDGSVARTTDEIGDALAVRVAS | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH
Sequence Mass (Da): 36867
Sequence Length: 347
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.1.1.85
|
Q8DTG3 | MKKIVTLAGDGIGPEIMAAGLEVFDAVAQKINFDYEIEAKAFGGAGIDASGHPLPDDTLAAAKTADAILLAAIGSPQYDKAPVRPEQGLLAIRKELNLFANIRPVRIFDALRHLSPLKAERIAGVDFVVVRELTGGIYFGQHTLTENSACDINEYSASEIRRIMRKAFAIARGRSKKVTSIDKQNVLATSKLWRQIAEEVAKEYSDVTLEHQLVDSAAMVMITNPACFDVVVTENLFGDILSDESSVLPGTLGVMPSASHSESGPSLYEPIHGSAPDIAGKGIANPISMILSVAMMLRDSFGETAGAEMIEHAVNKTLTQGILTRDLGGLANTKQMTAAIIANL | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH
Sequence Mass (Da): 36700
Sequence Length: 344
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.1.1.85
|
Q30RK2 | MKTYKIALIKGDGIGPEIIDEAVKVLDAVASCCDLEFSYEEALMGGCAYDITGDPLPQETINISLNSDAVLFGAIGGAKWDNLPREKRPESGLLRFRKELGVYANLRPANVFDELINASSLKAEVIKGVDLMVVRELIGGIYFGEPKGRDENRGWNTMVYTREEIVRIAHQAFKIAMSRSKRVCSIDKANVLDVSQLWREVVIEVAKEYPEVELTHMYVDNAAMQLIRDPRQFDVMLTGNIFGDILSDEASMLSGSIGLLPSASVGAKIGVYEPIHGSAPDIAGQGIANPIATILSASMMLRYALGEHGAADKIDAAVKRALKEGYRTKDLAQYDAKEVCSTSEMGSIIANYAAK | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH
Sequence Mass (Da): 38671
Sequence Length: 355
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.1.1.85
|
P50455 | MGFTVALIQGDGIGPEIVSKSKRILAKINELYSLPIEYIEVEAGDRALARYGEALPKDSLKIIDKADIILKGPVGESAADVVVKLRQIYDMYANIRPAKSIPGIDTKYGNVDILIVRENTEDLYKGFEHIVSDGVAVGMKIITRFASERIAKVGLNFALRRRKKVTCVHKANVMRITDGLFAEACRSVLKGKVEYSEMYVDAAAANLVRNPQMFDVIVTENVYGDILSDEASQIAGSLGIAPSANIGDKKALFEPVHGAAFDIAGKNIGNPTAFLLSVSMMYERMYELSNDDRYIKASRALENAIYLVYKERKALTPDVGGNATTDDLINEIYNKLG | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH
Sequence Mass (Da): 36964
Sequence Length: 337
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.1.1.85
|
Q67JY2 | MAQPTYHIACLPGDGIGPEVTRGAVTVLQAAAAAYGFRLEFSEYLVGGAAYDAVGTPFPDETRDACDRADAILFGAVGGPRYEGLPWDLRPEAGLLAIRKRYDLYANLRPILLYPPLKDASPLKNEIIGGGVDFIIVRELVGGIYFGEPRGIETLPDGTRRGVNTEVYTDAEIARIARMGFEIARGRRRRLTSVDKGNVMEAGKLWRTVVDEVAREFPDVEVEHLLADNAAMQILRRPGDFDVMLASNLFGDFLSDEAAMLTGSIGLLPSASLGAARNRFGLPKGFYEPIHGSAPDIAGQDRANPLAAILCGAMLLRHSLGREDAARAVEQAVAAVLEEGLRTADITVPGTAVLGTAAMARAVADRVH | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Catalytic Activity: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl-2-oxopentanoate + CO2 + NADH
Sequence Mass (Da): 39411
Sequence Length: 368
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 3/4.
Subcellular Location: Cytoplasm
EC: 1.1.1.85
|
P49601 | MAPKTLYEKIFDSHLVHEEADGTCLIYIDRHLVHEVTSPQAFEGLRNANRKVRRTDCTLATVDHNIPTASRKSYRDTKSFVEQVDSRTQCMTLEENVKAFGLTFFGLSDNRQGIVHIIGPEQGFTLPGATIVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLLQKRAKNMLIQVDGELSQGVTSKDIILHIIGLIGTAGGTGHVIEYAGSTIRSLSMEARMSICNMSIEAGARAGLIAPDEITYEYIKGRPLAPKQGEAWDQALAYWKTLPSDEGAQYDTVIKIDAKDIPPTVTWGTSPQDVVAITGTVPDPKNASNEAEAKAWTRALEYMGLEAGTPMEKIKIDKVFIGSCTNARIEDLRAAARVLHGRKVADGLYCMLVPGSGLVKKQAEAEGLDKIFQAAGFDWREAGCSMCLGMNPDQLAPGERCASTSNRNFEGRQGAGGRTHLMSPAMAAACAVTGYLTDVRKVVGHSSAKVGSDAAKPAFEIEVSDAKSYLVDATPAPAPTNVAAAGAGALTDEDALRDVPASHISSSGGGMEKFTTLTGIAAPLERSNVDTDLIIPKQFLKTIKRTGLGSALFWPLRYDAKTGEPDPAFVLNQKPYDQSKILVVTGPNFGCGSSREHAAWSLLDFGIRAVIAESFGDIFRNNLTKNGQLPVVLSRAQIQRLTQDAKAGKQITVDLVDQLVITADGKEKFSFETPEFTRHCLINGLDDIALTLQRDAQIGAFERNRSTHTPWLDGFGYHANSNSSSLLDSAKPLVNNVTATDW | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
Catalytic Activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Sequence Mass (Da): 83224
Sequence Length: 773
Pathway: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4.
EC: 4.2.1.33
|
Q2L247 | MATKLTERQQEILDLIRQTVARTGFPPTRAEIAQALGFRSPNAAEDHLKALARKGAIELTAGASRGIRLKDAEPTPSPILASLSQLLLPLVGRVAAGSPILAAEHVEREVGVDPSLFSQAPDYLLKVRGMSMRDAGILEGDLLAVKKSSEARNGQIIVARLGDDVTVKRLQRHGSRIELLPENPEFSPILVAPDDEFALEGVAVGLIRTHALH | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 22906
Sequence Length: 213
EC: 3.4.21.88
|
Q7WCK0 | MATKLTERQQEILDLIRQTVARTGFPPTRAEIAQALGFRSPNAAEDHLKALARKGAIELTAGASRGIRLKVPDSATPSAQLTHPLLAQLVLPLVGRVAAGSPILASEHVEREVGVDPGLFAQTPDYLLKVRGMSMRDAGILEGDLLAVKRAAEARNGQIVVARLGDEVTVKRLQRQNGRIELLPENPDFAPIVVANTDEFALEGIAVGLIRTQPLH | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 23217
Sequence Length: 216
EC: 3.4.21.88
|
A6X0K7 | MLTRKQHELLLFIHERLKETGIPPSFDEMKEALDLASKSGIHRLITALEERGFIRRLPNRARALEVLRLPDSIAPGLNAQKKFAPSVIEGSLGKTPPPPARPAPVATNDDTSGTVSVPVMGRIAAGVPISAIQNQTHSLSLPPEMIGAGEHYALEVRGDSMIDAGIFDGDTVIIKRGDSANPGEIVVALVDDEEATLKRFRRKGASIALEAANPAYETRIFGPDRVRVQGKLVGLIRRY | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 25920
Sequence Length: 239
EC: 3.4.21.88
|
P61612 | MDDSNDSSSAGPDGRLHAVDPSLTERQRTILNVIRSSVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRGVDDDVAAPATEVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGDGTLFLLKVVGDSMVEAAICDGDWVVVRQQHVADNADIVAAMIDGEATVKTFKRAGGQVWLMPHNPAFDPIPGNDATVLGKVVTVIRKV | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 24661
Sequence Length: 232
EC: 3.4.21.88
|
A0QVY5 | MSDDTGEFTDGSTESPADADGAGRRRAVDNGLTERQRTILEVIRASVTSRGYPPSIREIGDAVGLTSTSSVAHQLRTLERKGYLRRDPNRPRAVDVRAADDPAAAAVVTTDVAGSDALPEPTFVPVLGRIAAGGPILAEEAVEDVFPLPRELVGEGSLFLLKVVGDSMVDAAICDGDWVVVRQQNVADNGDIVAAMIDGEATVKTFKRARGQVWLMPHNPAYDPIPGNEAAVLGKVVTVIRKI | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 25778
Sequence Length: 243
EC: 3.4.21.88
|
Q1D406 | MEELTERQREILSFIVKETETRGFPPTIREIGEHMDIRSTNGVNDHLKALERKGYLNRGEQQSRSLVATKRARLLLGLGARKDSGMVEIPLLGKVAAGAPLLAQENMEDSVKIDSFLLGGVNGREVFALRVKGQSMIDDGIHDGDYLFVKKTPSAQPGEIVVALIEDEATVKRYYPEGDRIRFQPANATMQPIYVSRAEFRSTMILGQVVGVYRKLQGGRTP | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 24712
Sequence Length: 222
EC: 3.4.21.88
|
Q2G6Q5 | MLTRKQHELLTFIQTRLEDSGISPSFEEMKEALDLKSKSGVHRLISALEERGFIRRLPNRARALEVLRQPDSAVGKAAPVSQREAANTNSALPPLRAAPKAAPAPANDVIELPLHGKIAAGVPIEALETTATLPVPAALLGAGEHYALEVSGDSMVEAGIFDGDYALVRKTDVARDGEIVVALVRGEEATLKYLHREKGMVRLDPANAAYDPQYYRPEEVAVQGKLAGLLRRYH | Function: Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.
Catalytic Activity: Hydrolysis of Ala-|-Gly bond in repressor LexA.
Sequence Mass (Da): 25414
Sequence Length: 234
EC: 3.4.21.88
|
Q8JHF2 | MLKTYRGKVVVSLAGATVTCLGFLLFLSQHQRIQADGMQNESEVGLRSLQSLGDSETDDGAQPEQNAKKGFSAYFSKLTRSRREADKPSEAPGAATDAPPAEDISADDIFIAVKTTKKFHRSRLDLLLDTWISRNMRQTYIFTDGEDEELKKKIGSHAINTNCSAAHSRQALSCKMAVEYDKFIESGKKWFCHVDDDNYVNTKTLVKLLSNYPHTQDMYIGKPSLDRPIEATERLGDNKMRPVNFWFATGGAGFCISRGLALKMSPWASGGHFMNTAEKIRLPDDCTIGYIIESVLGVSLTRSSLFHSHLENLQQVSKSEVHKQITLSYGMFENKRNIINMKGAFSVEEDPSRFKSVHCLLYPDTPWCPPQVAY | Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Involved in the correct formation of boundaries in the somites and hindbrain (By similarity). Required for Delta-Notch-mediated induction of hypochord cells at the lateral borders of the midline precursor domain .
PTM: A soluble form may be derived from the membrane form by proteolytic processing.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: 3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP
Sequence Mass (Da): 41882
Sequence Length: 374
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.222
|
O09010 | MLQRCGRRLLLALVGALLACLLVLTADPPPTPMPAERGRRALRSLAGSSGGAPASGSRAAVDPGVLTREVHSLSEYFSLLTRARRDADPPPGVASRQGDGHPRPPAEVLSPRDVFIAVKTTRKFHRARLDLLFETWISRHKEMTFIFTDGEDEALAKLTGNVVLTNCSSAHSRQALSCKMAVEYDRFIESGKKWFCHVDDDNYVNLRALLRLLASYPHTQDVYIGKPSLDRPIQATERISEHKVRPVHFWFATGGAGFCISRGLALKMGPWASGGHFMSTAERIRLPDDCTIGYIVEALLGVPLIRSGLFHSHLENLQQVPTTELHEQVTLSYGMFENKRNAVHIKGPFSVEADPSRFRSVHCHLYPDTPWCPRSAIF | Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 . Decreases the binding of JAG1 to NOTCH2 but not that of DLL1 (By similarity). Essential mediator of somite segmentation and patterning. During somite boundary formation, it restricts Notch activity in the presomitic mesoderm to a boundary-forming territory in the posterior half of the prospective somite. In this region, Notch function activates a set of genes that are involved in boundary formation and in anterior-posterior somite identity . Ectopically expressed in the thymus, Lfgn inhibits Notch signaling which results in inhibition of T-cell commitment and promotes B-cell development in lymphoid progenitors . May play a role in boundary formation of the enamel knot .
PTM: A soluble form may be derived from the membrane form by proteolytic processing.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: 3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP
Sequence Mass (Da): 41952
Sequence Length: 378
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.222
|
A0R5K5 | MSTCIEGTPSTTRTPTRAWVALAVLALPVLLIAIDNTVLAFALPLIAEDFRPSATTQLWIVDVYSLVLAALLVAMGSLGDRLGRRRLLLIGGAGFAVVSALAAFAPSAELLVGARALLGVFGAMLMPSTLSLIRNIFTDASARRLAIAIWASCFTAGSALGPIVGGALLEHFHWGAVFLVAVPILLPLLVLGPRLVPESRDPNPGPFDPVSIVLSFTTMLPIVWAVKTAAHDGLSAAAAAAFAVGIVSGALFVRRQNRSATPMLDIGLFKVMPFTSSILANFLSIIGLIGFIFFISQHLQLVLGLSPLTAGLVTLPGAVVSMIAGLAVVKAAKRFAPDTLMVTGLVFVAVGFLMILLFRHNLTVAAIIASFVVLELGVGVSQTVSNDTIVASVPAAKSGAASAVSETAYELGAVVGTATLGTIFTAFYRSNVDVPAGLTPEQTGAAAESIGGAAAVAADLPAATATQLLDSARAAFDSGIAPTAVIAAMLVLAAAAVVGVAFRR | Function: Energy-dependent efflux pump that contributes to drug resistance . Catalyzes the efflux of norfloxacin and several related fluoroquinolones (FQ) . Contributes significantly to the intrinsic MICs for ethidium bromide and acriflavine . Overexpression confers low-level resistance to hydrophilic FQ such as ciprofloxacin, ofloxacin and levofloxacin, and to ethidium bromide, acridine, acriflavine, rhodamine 123 and some quaternary ammonium compounds . May contribute to resistance to certain beta-lactams . Probably uses the proton motive force .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51524
Sequence Length: 504
Subcellular Location: Cell inner membrane
|
A3DES1 | MPVFRLTDKLVFPHPSLADEDGILAVGGDLSCERLLLAYKNGIFPWFSEDEPILWWSPNPRCVLFPKDIKISRSMRKFLKKQLYEVTFDTCFRHVIAMCAKLREGNTWITPEIIESYSKLHDLGFAHSVETWYEGRLVGGLYGVSLGKCFFGESMFSTMDNASKTALITLCQKLEEKGFLLIDCQVYSKHLESLGAVNIDRDLFLKYLEAGLSHETLRGNWKFFNEQKQVRNN | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 26818
Sequence Length: 233
Subcellular Location: Cytoplasm
EC: 2.3.2.6
|
Q6FDS1 | MILPSMYVFPDPPEADPEGQGLICIGADLEPSTLFEAYTHGLFPWFNEGDPICWWSPEPRCVIYPEQYQPSKTLIRSMKKYDYQITMNRAFEKVIRSCALPRNYTNETWISEDIVQGYVELFKAGYAYSVEVWENDQLIGGLYGVNIGKGCFGESMFSLRTDTSKIAFYTLMLIGQENQVPWVDCQLVNDHLISLGACTLSRQAYLKSLQDVIIQPPINWKRYQERVFSSKRIAQNAKLTE | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 27699
Sequence Length: 241
Subcellular Location: Cytoplasm
EC: 2.3.2.6
|
A0KJE0 | MSRYLTQLDDELCWFPDPEHALEEPNGLLAIGGDLSPARLLAAYHKGIFPWNEPHQPLLWWSPDPRGVIRPEQLHIGRTLRKFIRGTSFDISIDRAFNEVIAACAAPRRSASGTWISTPMIDAYRQLHRLGHAHSIEIWQEGQLQAGLYGLSLGRVFCGESMFSRIDNGAKLAMVALCQHFARHDGALIDCQMQNDFLATLGIEEWPRRQFLTTLAQLSRQPLAANCWQTGSILL | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 26498
Sequence Length: 235
Subcellular Location: Cytoplasm
EC: 2.3.2.6
|
Q8UFR8 | MAGRRSRNNDITVDILLRAYSAGLFPMADSADDPELFWVEPEIRGIIPLDDFHVSKSLAKAMRKKPFAIRFNTAFEDVMAGCAAEAADRPSTWINATIRRLYTELHQIGHAHSVEAWEGDELVGGLYGVSLGAAFFGESMFSRRTNASKICLVHLVERLNAKGFVLLDTQFTTEHLKTFGAIDVPKLDYARMLDLAVNRPSLQF | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 22762
Sequence Length: 204
Subcellular Location: Cytoplasm
EC: 2.3.2.6
|
B2UNS0 | MNDRLTPELVLSAYCQGCFPMADPETGEISFYEPDPRALIPLDDRFHIPHGLKRALNKKPFELRMDTAFPEVVHACARTDQPEEQWIDGQIEEAYGKLHEMGFAHSVECWDEEGLQGGLYGVALGKAFFGESMFHRKTDASKIALVALVQYLRAHRFLFLDTQWTTPHLLKFGTYEVPAKEYRKLLKRALEEQ | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 22173
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 2.3.2.6
|
C4XT58 | MPVFALIDEPVFPSPHLAEPGGLLAVGGDLSVARLLAAYRRGIFPWYDDESPILWWSPDPRPILVPGHVRVSKRLERTIRSGKFTVTLDTDFAGVIRGCAAVPRDADNGTWIVPDMIEGYERLHAAGHAHSVEAWQNGELVGGAYGVAIGKAFFGESMFHRATDASKVAFVTLCRFLDRHEFRFIDCQQATGHLLRFGAVQVRRNEFLRRLEAAREEEGMVGKWVLPRTTRCASPQPTSESSPSAKQ | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 27380
Sequence Length: 247
Subcellular Location: Cytoplasm
EC: 2.3.2.6
|
Q30TE4 | MIPKLLKHELTFPHPNDATEDGIVAWGGDLNPSRLIRAYQNGIFPWYGKNDPIIWWSPNPRLIMELDDFKLSRSLRKSMKKFEYRFDTNFINVMKNCQNIKRVKQDGTWIQDEIIEAYSVLHDMGIAHSVESYLDGELVGGLYGVAVGGLFCGESMFTLVNDASKSAYAVLINHLKIWGYDFIDAQVPTEHLKNLGAKEVSRDYFLDRLHKVNMNIINHKWELLHVNT | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 26283
Sequence Length: 228
Subcellular Location: Cytoplasm
EC: 2.3.2.6
|
Q2LQL0 | MPICPLGKVIVFPPVSLAMEDGLLAVGGDLSPYRLLEAYRQGIFPWYSPGEPILWWAPQPRFVLFPDEILLSRSMRQILRKKHFQVTLDRNFDAVIHACATIGRPAQEGTWITEEMQEAYSILHELGYAHSVEVWRDRGLIGGLYGVSLGGCFFGESMFSRESNASKAALIFLSSLLKILRFTLIDCQVYTSHLALLGARFIPRETFTALIRKSLRRPTLRGNWSTHPETADKLPGHEF | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 27019
Sequence Length: 239
Subcellular Location: Cytoplasm
EC: 2.3.2.6
|
A0LE95 | MPVFRLTEELIFPPSYLAERDGLLAVGGDLSAERLLLAYRQGIFPWYTEKTPILWWSPDPRLVLFPAELKISISLRRVLRKNVFSVTFDRAFADVIRRCAEVRRARDDSTWIVPGMVTAYSRLHRLGYAHSVESWHEGELVGGLYGVALGRVFYGESMFTRKTDASKVALVHLVDLLTRGGFQLIDCQVTTAHLQSMGAREISRRRFLTLLAENIPEVVHGESWEGESCCGKRP | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 26567
Sequence Length: 234
Subcellular Location: Cytoplasm
EC: 2.3.2.6
|
Q2JWL1 | MQVDIGAILTGYAQGYFLMADEETGSLAWYGTEQHALIPLDERFHCPRSLRPLVRGSCFQVRINGAFEQVVEGCAARPQTWISSELKQIYLALHQAGFAHSFETWQGDTLAGGILGIALGAAFIGESMFYRIPNASKVALVKLVEHLRERGFRLFDAQLMNPHLARFGAFLMDGRDYQELLQQCLRIPCRFD | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = H(+) + N-terminal L-leucyl-L-lysyl-[protein] + tRNA(Leu)
Sequence Mass (Da): 21585
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 2.3.2.6
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.