ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9A716 | MRKLGLIAGGGALPVELASHCEAAGRAFAVMRLRSFADPSLDRYPGADVGIGEFGKIFKALRAEGCDVVCFAGNVSRPDFSALMPDARGLKVLPSLIVAARKGDDALLRRVLDEFEKEGFEIEGAHEVMGEMTLPRGRLGKVSPAPEHMADIDKALDVAREIGRLDIGQGAVVCEGLVLAVEAQEGTDAMLRRVADLPEAIRGRAERRLGVLAKAPKPIQETRVDLPTIGVATIHRAARAGLAGIVGEAGRLLVVDREAVIAAADDLGLFVLGVDPQERP | Cofactor: To a lesser extent, can also use Mn(2+) or Co(2+).
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to form 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the beta-P atom. Involved in the biosynthesis of lipid A, a phosphorylated glycolipid tha... |
B7J512 | MTLRQTLEQQWQDGGALATALRPLGALTGKVARWRRRHIQGRAASIPTIVVGNLGVGGSGKTPLVAALARQLTVAGWRVAIVSRGYGARPPHWPYRVQRDDSPQQAGDEPLLLAQEQGQTQAVYLCPDRHRAIAAAAADGYNLALLDDGFQHLALQPSLRLLVLSGPRPLGNGHCLPAGPLRECPDAMLHADALLMDAAAAAAIPERNGPPRFLFRIQPKDLVAVNDPCRSRSLDSLQGQHVTAVTGIARPQRFVASLEGLGAIPDPRFFPDHHSFCASDIAHLPRPLVMTAKDAVKCREFAQADDWTLRIEAELEASSQ... | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36036
Sequence Length: 332
P... |
Q8UHI5 | MVSEAPPFWWQKAGWQAWLLSPFSLLYGKVAGRRMRTAKRANVPVPVICIGNFTVGGAGKTPTAIAIARAAVARGMKPGFLSRGYGGTLDVTTLVDAQHHRAAAVGDEPLLLAREAVTVISRRRVEGAHRLVKEGVNLIIMDDGFQSARLTLDYALVVIDTVRGIGNGHLVPGGPVRAPLAEQMRQMTGLLKVGKGHAADPLVRQAAKAAKPVFVAAIMPQEPEDFRGKRVLAFAGIADPAKFYRTVEALGGDIVLSRSFPDHHHFSDDEIDDLLKDARKENLQLVTTAKDAVRLNGHHGRAEELLWNSQVIEIDMVFDD... | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 37690
Sequence Length: 348
P... |
Q9PPA9 | MNEEKNYELWLDNYFFKPNFWQKCLAFILLPLSVLYAFFAILNTFFRKKIVFKKPVISVGNLSFGGNGKTPLCKAIAREFDGVFIVLRGYKRKSKGLFVVKNQNEILCTLTQSGDEAMEYAFEENIKGVIVSEDRVKGIEKAFELGAKIVVLDDAFSKFHIKKFDILLESKIKPYFNFTLPSGAYRLPKFYEKRADFIALEGRDFVRYSFVKENPKAVLVTAIAKPFRLYEHFIKARACYFFKDHYEFKKEELENLLKKHNCDTLMLTFKDFVKVKDFGFKCQIIELNIELKDSLREKIKTYIKEFEQ | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36228
Sequence Length: 308
P... |
P58184 | MKLGTPRWWYVKSGAPAPVTRALLTPLSWLWADTTRRRIARATPAIVGAPVICVGNVTMGGAGKTPIVRELLLTLTQRGVAAHGLSRGYGGKLKGPVRVDTIRHTAADVGDEPLMLAQDFPMWIAADRVAGAKAAVRAGASAIVMDDGHQNPSVKKALSLVVVDGETRGGEWPFGDGRVFPAGPMREPLKVGLSRADAVIVLLPVDVEQPDFDLLVAFGDMPVLVARLEAAAPVPKGPQVGFAGIAKPWKVEKALTAAGCQLVDFAPFPDHGAYSESTLKMLADRAEVYEAGLVTTEKDWVRLPPAWRERVTPWPVRARF... | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 35775
Sequence Length: 335
P... |
Q3J6I0 | MRPPAFWFTPPDSPALAARLLAPLGQAYAAATARRLRAPGHRAGVPVICIGNLNAGGTGKTPTAIALMQRLAARGIEAHVVSRGYGGRLEGPVEVDARRHRAADVGDEPLLLAAFGRAWVARDRAAGVRAAEAAGAQAILLDDGFQNPSVVKDLSLIVVDAAVGFGNGRCLPAGPLREPVEAGLARADLLLSIGGPEAQRRFATDWPALPVPRLTGRLATLQMGMDWQGARVLAFAGIGRPEKFFASLRAEGAELLRAEALDDHQPLGEALMKRLEIEAMALGAQLVTTEKDAVRLPPSFRQKVLTLPVRLEFDDATALD... | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 35058
Sequence Length: 332
P... |
B3EG23 | MSNPLSPLLKPAAALYRTVVRMRNLGFEKKLFKTWKAPLPVVSIGNISAGGTGKTPLADWIINYCLSVGSEPALLSRGYGRTTKGVQLVSDGQRILLDSREAGDETSMLAARNPGIIVVVAEKRKEGVEFILKRFGTRMPSLIILDDAFQHRQIARDLDIVIINAAEPYCNARMLPEGRLREPLGNIRRAGLIVLNKITDRNAADAIACDLKKTGIPVVLAKTEAGELVPFGEDAGERNMNGIRAFAFAGIGSPEGFLGSLKEKGIQVEAHRFFRDHEPYSGDKLLPILLEAEKKGLSLVTTEKDYFRLLGEHELTATLS... | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 38464
Sequence Length: 350
P... |
Q9ZCL0 | MIKLLYPQFWQERNIIAYLLLPISLIYQFLSYLRASLAYPVILPAQVICVGNCSVGGTGKTQIVIYLAKLLKAKNVPFVIITKAYGSHIKSTTIIQKGHTALEVGDEGIMLARYGTVIAAKYVKDILPLINELKPDVIIVDDFLQNPYLHKDFTIVSVDSQRLFGNRFLIPAGPLRQNPKQVLDAADLIFLVSSNQDQIPNELTPYIDKLINAQIVPSNNIDKNKNYFAFSGIGNPQRFFLTLENYRLNIVGYKIFPDHYNYLQADLENLYSLAKEHNAILITTRKDYVKFNYLNDEIICLDVELSINNPDLLNEKIFKK... | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36971
Sequence Length: 325
P... |
A1AXA3 | MNLNIRGIINYSLLPISGIFYLVSVFRKWLYRVNFFKVQKFKYPVIVVGNITVGGTGKTPIVIALAQYFKQQGKQVGIVSRGYGGAHHQGSLLVNKDTNVYLSGDEPLLIALQTDLPVMINKNRAKAVKDLINQCQVDLIISDDGLQHYKMDRDVEIVVIDGIKRFGNGFFLPLGPLRESITRLKSVDFVINNAGLCAGEFSVKLTLKMFVNVKTGEEKSLNYFKGKYCHGVAGIGHPERFFNALIRLGINLEHHIFADHYIYQQSDLVFEDNHPILMTAKDCVKCTQFENDQMWYLQVEADLSDDFLKKLDAKL | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 35640
Sequence Length: 315
P... |
Q21J10 | MSAALAKAIERRWYSRPGILWLLYPLALLFRLLSYFRRRSQTQSSVKFAVPVCIVGNIAIGGTGKTPTIIALVHALAEQGITAGVVARGYGASLAKDEVRVLDANATAAMVGDEPLLIYKRTGCVVAVGSNRVAACETLLKSHAVDVILSDDGMQHYKLGRDLELALVDGERVFGNGQLLPVGPLREHPKRLQSVNWLLVNGGSAEHVNARLQALEAINAAELSSKPNKLNKTPAPVFAQLEAVKLVNLATGKTLLLQNITELGAFVAVAGIGNPARFFKTLQSTGITGFDTFSYPDHHKFTSADFRQFDNKAIVMTEKD... | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 39190
Sequence Length: 361
P... |
Q8BZT5 | MKVTRFMFWLFSMLLPSVKSQASETEVPCNFSRRNYTLIPEGISTNVTILDLSYNRITLNAADSRVLQMYSLLTELYLMENNIIALYNSSFRNLLNLEILNICGNSISVIQQGSFVGLNELKQLFLCQNKILQLNPDTFVPLNNLKVLNLQGNLIRLFDAPQLPHLEILTLDGNPWNCTCGLLELHNWLNTSNVTLENENMTMCSYPDELKHDSIKSAPFTTECHSTFISTITEDFQSTRNSSFNSSSHNLTWTSEHEPLGKSWAFLVGVVATVLLTSLLIFIAIKCPVWYNILLSYNHHRLEEHEAETYENGLTRNPSS... | Function: Pathogen-recognition receptor which mediates the activation of TRAF2- and TRAF6 NF-kappa-B signaling pathways and induces the expression of pro-inflammatory cytokines . In kidney, prevents infection by uropathogenic bacteria by inducing the production of cytokines, chemokines and antimicrobial substances . In... |
Q8MII8 | MGGPLMWALLLPLLLHQAGSQTSSCSVLSGYMDWTKEYFDTCLNFSGKILTQLPQNQSLRARSVQLLDLSANGLQRLPWSFFRDLEQLQLLIVTNNSLDFVDRALXXXGCGLELLADCSCALLDWHTDRQDNCSGPELPRCLDVPTGAWHNLSVFLDVSCPSGLTKIAIGALAASGSLLLVLAIAGPVLAWRFCRHRMDQNLSKTWASQDGSRSGSGRQPRYSSQGRRPKSPANTPPRSSTPDYENVFVGPPAARHQWDELRSPPSEGGDFYMTYDSLQHESQPVYCNLQSLSQVPLDDEEYVVPGR | Function: Plays a role in the inhibition of RLR-mediated type I interferon signaling pathway by targeting RIGI for autophagic degradation. Interacts specifically with ISG15-associated RIGI to promote interaction between RIGI and the autophagic cargo receptor p62/SQSTM1 to mediate RIGI degradation via selective autophag... |
Q8N386 | MGGTLAWTLLLPLLLRESDSLEPSCTVSSADVDWNAEFSATCLNFSGLSLSLPHNQSLRASNVILLDLSGNGLRELPVTFFAHLQKLEVLNVLRNPLSRVDGALAARCDLDLQADCNCALESWHDIRRDNCSGQKPLLCWDTTSSQHNLSAFLEVSCAPGLASATIGAVVVSGCLLLGLAIAGPVLAWRLWRCRVARSRELNKPWAAQDGPKPGLGLQPRYGSRSAPKPQVAVPSCPSTPDYENMFVGQPAAEHQWDEQGAHPSEDNDFYINYKDIDLASQPVYCNLQSLGQAPMDEEEYVIPGH | Function: Plays a role in the inhibition of RLR-mediated type I interferon signaling pathway by targeting RIGI for autophagic degradation. Interacts specifically with ISG15-associated RIGI to promote interaction between RIGI and the autophagic cargo receptor p62/SQSTM1 to mediate RIGI degradation via selective autophag... |
Q2I0M4 | MRGPSWSRPRPLLLLLLLLSPWPVWAQVSATASPSGSLGAPDCPEVCTCVPGGLASCSALSLPAVPPGLSLRLRALLLDHNRVRALPPGAFAGAGALQRLDLRENGLHSVHVRAFWGLGALQLLDLSANQLEALAPGTFAPLRALRNLSLAGNRLARLEPAALGALPLLRSLSLQDNELAALAPGLLGRLPALDALHLRGNPWGCGCALRPLCAWLRRHPLPASEAETVLCVWPGRLTLSPLTAFSDAAFSHCAQPLALRDLAVVYTLGPASFLVSLASCLALGSGLTACRARRRRLRTAALRPPRPPDPNPDPDPHGCA... | Function: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Required for the conversion of BK alpha channels from a high-voltage to a low-voltage activated channel type in non-excitable cells. These are characterized by negative membrane voltages and constant low le... |
Q91W20 | MRGSFFSRLPPQLSLLLLLSLRRVWTQEDIGTAPSKSPVAPECPEACSCSLGGKANCSALALPAVPADLSWQVRSLLLDHNRVSALPPGAFANAGALLYLDLRENRLRSVHARAFWGLGVLQWLDLSSNQLETLPPGTFAPLRALSFLSLAGNRLALLEPSILGPLPLLRVLSLQDNSLSAIEAGLLNNLPALDVLRLHGNPWTCNCALRPLCTWLRKHPRPASETETLLCVSPRLQTLSLLTAFPDAAFKQCTQSLAARDLAVVYALGPVSFLASLAICLALGSVLTACGARRRRRRRTTVRHLLRRQLDPEGPPSLED... | Function: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Required for the conversion of BK alpha channels from a high-voltage to a low-voltage activated channel type in non-excitable cells. These are characterized by negative membrane voltages and constant low le... |
Q9JMH2 | MWVALGMLWLLALGGPHQAWSFCPSQCSCSLHILSDGSKARTVVCSDPDLTLPPASIPPDTCKLRLERTAIRRVPGETFRPLSRLEQLWLPYNALSELSTLMLRGLRRLRELRLPGNHLVTFPWAALKDTPQLQLLDLQANRLSTLPPEAVHFLENLTFLDLSNNQLMRLPEELLDTWAHLKTGPYLSSRRTRLVLGLQDNPWVCDCRLYDLVHLLDGWASNLIFIEARLRCGSPRSLAGVAFSQLELRKCQSPELRPGVTSIISPLGSTVLLRCGATGIPGPEMSWRRANGRPLNGTVHQEVSSDGSSWTLLDLPVVSL... | Function: Possible role in phototransduction.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 68417
Sequence Length: 623
Subcellular Location: Endoplasmic reticulum membrane
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Q3SXY7 | MHLFACLCIVLSFLEGVGCLCPSQCTCDYHGRNDGSGSRLVLCNDMDMNELPTNLPVDTVKLRIEKTVIRRISAEAFYYLVELQYLWVTYNSVASIDPSSFYNLKQLHELRLDGNSLAAFPWASLLDMPLLRTLDLHNNKITSVPNEALRYLKNLAYLDLSSNRLTTLPPDFLESWTHLVSTPSGVLDLSPSRIILGLQDNPWFCDCHISKMIELSKVVDPAIVLLDPLMTCSEPERLTGILFQRAELEHCLKPSVMTSATKIMSALGSNVLLRCDATGFPTPQITWTRSDSSPVNYTVIQESPEEGVRWSIMSLTGISS... | Function: Plays a role in the synapse formation and synaptic transmission between cone photoreceptor cells and retinal bipolar cells (By similarity). Required for normal transmission of a light-evoked stimulus from the cone photoreceptor cells to the ON-bipolar cells and ON-ganglion cells in the inner retina . Required... |
P93604 | MSKLLVIALLLLPLINHGIYLATAWDDQDFFKYCPPSKCSQHGPMIRYPLCLESSNTSSSSSCGCAGRSIWKLACSGQDTILVHPVLGPYSVSAIDYRRSSMKITPLVDPCLVLQQKLIISRSSSSPQVDVINDEKPSFDENFFESSSATIVHCSREFTPAAAHADSIAGPVSCLSNTTHFFYLVNSDEDMSILPLDCKVVPVSDRGGISLPHMLKDQMFYNFTETAKKIPSFAETAVSWDEGDCRECELSGRRCAFSSQRDREFCMPDPHGSHIKVIAATSSVAAFVALLLTVATVLYLSLKTRYNAEIHMKVEMFLKT... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 71023
Sequence Length: 636
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9M3D8 | MACRLYLALIFSCVYLICLSSQQETGFVYNGFEQADLFIDGIAKILPDGLLQLTNTTELQMGHAFFKKPFDFDPSSSLSFYTHFVCALVPPKLGADGGHGIVFVVSPSIDLSHAYATQYLGVFSNLTNGTSSSHLLAIELDTVKTVEFNELEKPHVGIDLNSPISVESALPSYFSNALGKNISINLLSGEPIQVWVDYDGSFLNVTLAPIEIKKPNQPLISRAINLSEIFQEKMYVGFSSSTGNLLSNHYILGWSFSRRKEQLQSLNLSTLPRVPLPKEEKKKLSPLLIGLVILLVIPVVMVLGGVYWYRRKKYAEVKEW... | Function: Involved in resistance response to the pathogenic fungus Alternaria brassicicola.
PTM: Autophosphorylated on Ser and Thr residues.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 73910
Sequence Le... |
Q9LSS0 | MIRGLLLGIIWMIFCVCSSFQQETPFVYNNFGHVDHLHLDGSARIIPSGGILQLTNATNSQIGHVFYEKPIEFKSSESVSFSTYFVCALLPAGDPSGHGMTFFVSHSTDFKGAEATRYFGIFNRNGSTSTRVLAVELDTSLASDVKDISDNHVGIDVNSAESITSANASYFSDKEGKKIDIKLLSGDPIQVWVDYEGTTLNVSLAPLRNKKPSRPLLSSTSINLTDILQGRRMFVGFSGSTGSSMSYQYILGWSFSKSMASLPNIDISKLPKVPHSSTKKKSTSPVLSVLLGLIAFIVLGILVVAYLYRRNLYSEVREEW... | Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 73955
Sequence Length: 668
Subcellular ... |
Q9M021 | MGTQRSMFIVSFLFKLFLFLSVHVRAQRTTTNFAFRGFNGNQSKIRIEGAAMIKPDGLLRLTDRKSNVTGTAFYHKPVRLLNRNSTNVTIRSFSTSFVFVIIPSSSSNKGFGFTFTLSPTPYRLNAGSAQYLGVFNKENNGDPRNHVFAVEFDTVQGSRDDNTDRIGNDIGLNYNSRTSDLQEPVVYYNNDDHNKKEDFQLESGNPIQALLEYDGATQMLNVTVYPARLGFKPTKPLISQHVPKLLEIVQEEMYVGFTASTGKGQSSAHYVMGWSFSSGGERPIADVLILSELPPPPPNKAKKEGLNSQVIVMIVALSAV... | Function: Involved in negative regulation of abscisic acid response in seed germination.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 75868
Sequence Length: 682
Subcellular Location: Cell membrane
EC: 2.... |
Q66GN2 | MGRAKSMVSLLLVLFLVRAHVATTETTTEFIFHGFKGNQSEIHMQGDSTITSNGLLRLTDRNSDVVGTAFYHKPVRLLDSNSTNTTVRSFSTSFIFIIPSSSTSNGGFGFTFTLSPTPNRTDADPEQYMGLLNERNDGNSSNHVFAVEFDTVQGFKDGTNRIGNHIGLNFNSLSSDVQEPVAYFNNNDSQKEEFQLVSGEPIQVFLDYHGPTKTLNLTVYPTRLGYKPRIPLISREVPKLSDIVVDEMFVGFTAATGRHGQSSAHYVMGWSFASGGEHPLAAMLDISQLPPPPPNKAKKRGYNGKVIALIVALSTVISIM... | Function: Involved in negative regulation of abscisic acid response in seed germination.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 76735
Sequence Length: 691
Subcellular Location: Cell membrane
EC: 2.... |
Q9S9U1 | MKALLFLLTLFLILPNPISAIDFIFNGFNDSSSNVSLFGIATIESKILTLTNQTSFATGRALYNRTIRTKDPITSSVLPFSTSFIFTMAPYKNTLPGHGIVFLFAPSTGINGSSSAQHLGLFNLTNNGNPSNHIFGVEFDVFANQEFSDIDANHVGIDVNSLHSVYSNTSGYWSDDGVVFKPLKLNDGRNYQVWIDYRDFVVNVTMQVAGKIRPKIPLLSTSLNLSDVVEDEMFVGFTAATGRLVQSHKILAWSFSNSNFSLSNSLITTGLPSFVLPKDSIVKAKWFVFVLVLICFLVVALVGLVLFAVVRKRLERARKR... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 76693
Sequence Length: 686
Subcellular Location: Cell membrane
EC: 2.7.11.1
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O49445 | MFSKVSILLFSLASLLLFRSTTGIEFIYNSNFTTTNTLLLGNATVKSPPSILTLTNQTTFSIGRGLYPSRINASSSSASPLPFATSFIFSMAPFKHLSPGHGFAFVFLPFSETSAASSSQHLGLFNFTNNGDPNSRIFAVEFDVFANQEFNDINDNHVGVDVNSLTSVASETAGFYGGRDGQRFTELKLNSGENYQAWIEFNGSAINVTMARASSRKPIRPLISIPLNLTGVLLDDMFVGFTASTGQLVQSHRILSWSFSNSNFSIGDALITRNLPSFKLSGDSVLKSKGFIAGVSSGVVLLVSVIGLLCFYVVRRRRQR... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 75711
Sequence Length: 681
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
Q9LYX1 | MLKLPPRFFSVYSTLIHILASFLCSSDVRGDFPATRFDLGTLTLSSLKLLGDAHLNNGTIKLTRELSVPTSTAGKALYGKPVKFRHPETKSPASFTTYFSFSVTNLNPSSIGGGLAFVISPDEDYLGSTGGFLGLTEETGSGSGFVAVEFDTLMDVQFKDVNGNHVGLDLNAVVSAAVADLGNVDIDLKSGNAVNSWITYDGSGRVLTVYVSYSNLKPKSPILSVPLDLDRYVSDSMFVGFSGSTQGSTEIHSVDWWSFSSSFEESSESPPPMPNSPPPSSPSSSITPSLSTVRRKTADPSSSCRNKLCKKSPAAVAGVV... | Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 77120
Sequence Length: 711
Subcellular ... |
Q9LSL5 | MLYFIFCQNLSSSSSMSNSILFLSLFLFLPFVVDSLYFNFTSFRQGDPGDIFYHGDATPDEDGTVNFNNAEQTSQVGWITYSKKVPIWSHKTGKASDFSTSFSFKIDARNLSADGHGICFFLAPMGAQLPAYSVGGFLNLFTRKNNYSSSFPLVHVEFDTFNNPGWDPNDVGSHVGINNNSLVSSNYTSWNASSHSQDICHAKISYDSVTKNLSVTWAYELTATSDPKESSSLSYIIDLAKVLPSDVMFGFIAAAGTNTEEHRLLSWELSSSLDSDKADSRIGLVIGISASGFVFLTFMVITTVVVWSRKQRKKKERDIE... | Function: Promotes hydrogen peroxide H(2)O(2) production and cell death.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 75295
Sequence Length: 675
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9M9E0 | MSWQWRRRQWPSPLLLILIVLHLVSSSSAIDFLYNSFSSVTNRTDVILIEDSRVESTVISLINDSDPLSFGRVFYPQKLTIIPDPTRNPTRLSSFSTSFVFSILPDISTSPGFGLCFVLSNSTSPPNAISSQYFGLFTNATVRFNAPLLAVEFDTGRNSEVNDIDDNHVGIDLNNIESTTSVTAGYYDSVNGSFVRFNMRNGNNVRAWIDFDGPNFQINVSVAPVGVLRPRRPTLTFRDPVIANYVSADMYAGFSASKTNWNEARRILAWSLSDTGALREINTTNLPVFFLENSSSSLSTGAIAGIVIGCVVFVALIGFG... | Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici and to the pathogenic bacteria Pseudomonas syringae.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequenc... |
Q9M2S4 | MSQTFAVILLLLIFLTHLVSSLIQDFSFIGFKKASPNLTLNGVAEIAPTGAIRLTTETQRVIGHAFYSLPIRFKPIGVNRALSFSTSFAIAMVPEFVTLGGHGLAFAITPTPDLRGSLPSQYLGLLNSSRVNFSSHFFAVEFDTVRDLEFEDINDNHVGIDINSMESSISTPAGYFLANSTKKELFLDGGRVIQAWIDYDSNKKRLDVKLSPFSEKPKLSLLSYDVDLSSVLGDEMYVGFSASTGLLASSHYILGWNFNMSGEAFSLSLPSLPRIPSSIKKRKKKRQSLILGVSLLCSLLIFAVLVAASLFVVRKVKDED... | Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici and to the pathogenic bacteria Pseudomonas syringae.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequenc... |
Q9FG33 | MRFSLAWKLLFLILTCKIETQVKCLKFDFPGFNVSNELELIRDNSYIVFGAIQVTPDVTGGPGGTIANQAGRALYKKPFRLWSKHKSATFNTTFVINISNKTDPGGEGLAFVLTPEETAPQNSSGMWLGMVNERTNRNNESRIVSVEFDTRKSHSDDLDGNHVALNVNNINSVVQESLSGRGIKIDSGLDLTAHVRYDGKNLSVYVSRNLDVFEQRNLVFSRAIDLSAYLPETVYVGFTASTSNFTELNCVRSWSFEGLKIDGDGNMLWLWITIPIVFIVGIGAFLGALYLRSRSKAGETNPDIEAELDNCAANPQKFKL... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 72868
Sequence Length: 652
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9FHX3 | MNHHHYSLVIFHLILFLSLDFPTLSHRFSPPLQNLTLYGDAFFRDRTISLTQQQPCFPSVTTPPSKPSSSGIGRALYVYPIKFLEPSTNTTASFSCRFSFSIIASPSCPFGDGFAFLITSNADSFVFSNGFLGLPNPDDSFIAVEFDTRFDPVHGDINDNHVGIDVSSIFSVSSVDAISKGFDLKSGKKMMAWIEYSDVLKLIRVWVGYSRVKPTSPVLSTQIDLSGKVKEYMHVGFSASNAGIGSALHIVERWKFRTFGSHSDAIQEEEEEKDEECLVCSGEVSENPKEIHRKGFNFRVTVVGLKIPVWSLLPGLAAIV... | Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici and to the pathogenic bacteria Pseudomonas syringae.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequenc... |
Q9FHG4 | MSLSRKLLVIFFTWITALSMSKPIFVSSDNMNFTFKSFTIRNLTFLGDSHLRNGVVGLTRELGVPDTSSGTVIYNNPIRFYDPDSNTTASFSTHFSFTVQNLNPDPTSAGDGLAFFLSHDNDTLGSPGGYLGLVNSSQPMKNRFVAIEFDTKLDPHFNDPNGNHIGLDVDSLNSISTSDPLLSSQIDLKSGKSITSWIDYKNDLRLLNVFLSYTDPVTTTKKPEKPLLSVNIDLSPFLNGEMYVGFSGSTEGSTEIHLIENWSFKTSGFLPVRSKSNHLHNVSDSSVVNDDPVVIPSKKRRHRHNLAIGLGISCPVLICL... | Function: Involved in resistance response to the pathogenic oomycetes Phytophthora infestans and Phytophthora capsici.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 75842
Sequence Length: 681
Subcellular ... |
Q9C6K9 | METVSVLLFFFLFLLAAEARSTKRTGCKDFTCGEHDFKFPFFRTDMPSRCGLFKLNCSANIPEIQLEKDGKWYTVKSVSQANTITIIDPRLNQSLTTGGCSDLSSFSLPDSPWLKLNTLYKCNNSSRKNGFSYANCRGEGSSLYYNLGDDHDVSGCSPIKTPESWVTPKNGNLSDVNATFSLHIELPGNCFRCHNNGGECTKVKNNYRCVGANTEPNNYHAEMRLGLGIGGSVILIIILVALFAVIHRNYRRKDGSELSRDNSKSDVEFSQVFFKIPIFSYKELQAATDNFSKDRLLGDGGFGTVYYGKVRDGREVAVKR... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 70856
Sequence Length: 629
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
P0C5E2 | MNPSTPSLLYTSIFFYFTIIATQTLSLDPKFKACEPKSCGKGPQISYPFYLSGKQESFCGYPSFELTCDDEEKLPVLGISGEEYVIKNISYLTQSFQVVNSKASHDPCPRPLNNLTLHRTPFFVNPSHINFTILYNCSDHLLEDFRTYPLTCARNTSLLRSFGVFDRKKLGKEKQIASMSCQKLVDVPVLASNESDVMGMTYVEILKRGFVLNWTANSCFRCITSGGRCGTDQQEFVCLCPDGPKLHDTCTNGKNDKRRRVIVKVLIGASAAVVGLIAASIFWYVYHRRKTKSYRNSSALLPRNISSDPSAKSFDIEKAE... | Function: Probable receptor-like serine/threonine-protein kinase involved in abscisic acid (ABA) signaling. Acts as a positive regulator of abiotic stress response.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass... |
Q8VYG0 | MFSPVLFRFSKPNSFLVLLFFLSYIHFLPCAQSQREPCDTLFRCGDLTAGFPFWGVARPQPCGHPSLGLHCQKQTNSTSLIISSLMYRVLEVNTTTSTLKLVRQDFSGPFCSASFSGATLTPELFELLPDYKTLSAYYLCNPSLHYPAKFICPNKGVGSIHQDDLYHNHCGGIFNITVPIGYAPEEGALNVTNLESVLKKGFEVKLSIDERPCQECKTNGGICAYHVATPVCCKTNSSSEVNCTPMMPSGSSAHAGLSKKGKIGIGFASGFLGATLIGGCLLCIFIRRRKKLATQYTNKGLSTTTPYSSNYTMSNTPTST... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 75294
Sequence Length: 686
Subcellular Location: Cell membrane
EC: 2.7.11.1
|
O75074 | MEKRAAAGLEGAPGARAQLAVVCLVNIFLTGRLSSAVPALAACSGKLEQHTERRGVIYSPAWPLNYPPGTNCSWYIQGDRGDMITISFRNFDVEESHQCSLDWLLLGPAAPPRQEAFRLCGSAIPPAFISARDHVWIFFHSDASSSGQAQGFRLSYIRGKLGQASCQADEFRCDNGKCLPGPWQCNTVDECGDGSDEGNCSAPASEPPGSLCPGGTFPCSGARSTRCLPVERRCDGLQDCGDGSDEAGCPDLACGRRLGSFYGSFASPDLFGAARGPSDLHCTWLVDTQDSRRVLLQLELRLGYDDYVQVYEGLGERGDR... | Function: Probable receptor, which may be involved in the internalization of lipophilic molecules and/or signal transduction. Its precise role is however unclear, since it does not bind to very low density lipoprotein (VLDL) or to LRPAP1 in vitro.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da... |
Q98931 | MCRPALARLLLLQLLLLKLYLGKGAMKECDKDQFQCRNERCIPAVWACDEDNDCSDNSDEADCPKKTCAETDFACDNGHCIPDRWKCDGEEECSDGSDESEAACTKQVCPAEKISCGDLSNKCIPSSWRCDGQKDCESGIDEAGCAPACSPDEFQCSNKTCISINFVCDGYNNCGDGSDEKKCSPLTCSPNEFQCNNSVCIPQLWVCDNQADCEDHSDESIERCGYDAKAFNTCAAHEFQCGNGECILLNWKCDGDEDCKDKSDEQDCPLVTCRPDEFQCGDGTCIHGAKQCDKVHDCPDNSDEAGCVQESACESPSKFQ... | Function: Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. Also binds alpha2-macroglobulin. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (V... |
Q14114 | MGLPEPGPLRLLALLLLLLLLLLLQLQHLAAAAADPLLGGQGPAKDCEKDQFQCRNERCIPSVWRCDEDDDCLDHSDEDDCPKKTCADSDFTCDNGHCIHERWKCDGEEECPDGSDESEATCTKQVCPAEKLSCGPTSHKCVPASWRCDGEKDCEGGADEAGCATLCAPHEFQCGNRSCLAAVFVCDGDDDCGDGSDERGCADPACGPREFRCGGDGGGACIPERWVCDRQFDCEDRSDEAAELCGRPGPGATSAPAACATASQFACRSGECVHLGWRCDGDRDCKDKSDEADCPLGTCRGDEFQCGDGTCVLAIKHCNQ... | Function: Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands . LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 ... |
Q924X6 | MGRPELGALRPLALLLLLLLQLQHLSAADPLPGGQGPVKECEEDQFRCRNERCIPLVWRCDEDNDCSDNSDEDDCPKRTCADSDFTCDNGHCIPERWKCDGEEECPDGSDESKATCSSEECPAEKLSCGPTSHKCVPASWRCDGEKDCEGGADEAGCPTLCAPHEFQCSNRSCLASVFVCDGDDDCGDGSDERGCSDPACPPREFRCGGGGTCIPERWVCDRQFDCEDRSDEAAELCGRAGQGTTATPAACAPTAQFTCRSGECIHLGWRCDGDRDCKDKSDEADCSPGPCRENEFQCGDGTCVLAIKRCNQERDCPDGS... | Function: Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 t... |
D4A7P2 | MGLHFKWPLGAPMLAAIYAMSVVLKMLPALGMACPPKCRCEKLLFYCDSQGFHSVPNATDKGSLGLSLRHNHITALERDQFASFSQLTWLHLDHNQISTVKEDAFQGLYKLKELILSSNKIFYLPNTTFTQLINLQNLDLSFNQLSSLHPELFYGLRKLQTLHLRSNSLRTIPVRLFWDCRSLEFLDLSTNRLRSLARNGFAGLIKLRELHLEHNQLTKINFAHFLRLSSLHTLFLQWNKISNLTCGMEWTWSTLEKLDLTGNEIKAIDLTVFETMPNLKILLMDNNKLNSLDSKILSSLRSLTTVGLSGNLWECSPRVC... | Function: Involved in the development and maintenance of excitatory synapses in the nervous system. Regulates surface expression of AMPA receptors and instructs the development of functional glutamate release sites. Acts as a ligand for the presynaptic receptors NRXN1-A and NRXN1-B.
Location Topology: Single-pass type ... |
Q86VH5 | MGFNVIRLLSGSAVALVIAPTVLLTMLSSAERGCPKGCRCEGKMVYCESQKLQEIPSSISAGCLGLSLRYNSLQKLKYNQFKGLNQLTWLYLDHNHISNIDENAFNGIRRLKELILSSNRISYFLNNTFRPVTNLRNLDLSYNQLHSLGSEQFRGLRKLLSLHLRSNSLRTIPVRIFQDCRNLELLDLGYNRIRSLARNVFAGMIRLKELHLEHNQFSKLNLALFPRLVSLQNLYLQWNKISVIGQTMSWTWSSLQRLDLSGNEIEAFSGPSVFQCVPNLQRLNLDSNKLTFIGQEILDSWISLNDISLAGNIWECSRNI... | Function: Exhibits a limited synaptogenic activity in vitro, restricted to excitatory presynaptic differentiation (By similarity). May play a role in the development and maintenance of the vertebrate nervous system.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 65896
Sequence Length: 581
Su... |
Q80XG9 | MGFRLITQLKGMSVFLVLFPTLLLVMLTGAQRACPKNCRCDGKIVYCESHAFADIPENISGGSQGLSLRFNSIQKLKSNQFAGLNQLIWLYLDHNYISSVDEDAFQGIRRLKELILSSNKITYLHNKTFHPVPNLRNLDLSYNKLQTLQSEQFKGLRKLIILHLRSNSLKTVPIRVFQDCRNLDFLDLGYNRLRSLSRNAFAGLLKLKELHLEHNQFSKINFAHFPRLFNLRSIYLQWNRIRSVSQGLTWTWSSLHTLDLSGNDIQAIEPGTFKCLPNLQKLNLDSNKLTNVSQETVNAWISLISITLSGNMWECSRSIC... | Function: May play a role in the development and maintenance of the vertebrate nervous system. Exhibits strong synaptogenic activity, restricted to excitatory presynaptic differentiation (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 67148
Sequence Length: 590
Subcellular Lo... |
Q04087 | MTTLLQLLSNYYKAKLDSERIYNEYVQSQYEFASLDKLNNNKGDPKKVVDETLFLQRQIAQLNKQLQLSFQENEKLLSVQKNQKALYQSKLSSKDAFIDDLKLKLKVEQISVDKHNKERTPSTGRDEQQRNSKAAHTSKPTIHLLSPIVNRDKPNNQTNDRGGNDPDSPTSQRRSRGLRSLLSSGKNTIFDSISKNLDDEINENAHIRNDTTSSKIAGKSPSRLSALQKSPELRKERNNMILKEHILRSKDDQNITSSRKLDNIELSSIGDSTAMTSRSSTVNANDILGNEENDGITKLKRVNKLTSSPVKRDCSTNKKR... | Function: Component of the monopolin complex which promotes monoorientation during meiosis I, required for chromosome segregation during meiosis. Involved in rDNA silencing.
PTM: Phosphorylated by CDC5. This phosphorylation is required for the location to the kinetochores during late pachytene.
Sequence Mass (Da): 3935... |
A0A0P0VIP0 | MPPRCRRLPLLFILLLAVRPLSAAAASSIAAAPASSYRRISWASNLTLLGSASLLPGAAGVALTTPSRDGVGAGRALFSEPVRLLLPQDAAASASASRAATPASFSTRFTFRITPSPTYGDGLAFLLTSSRTFLGASNGFLGLFPSSSASDEGELRDVSTVAVEIDTHLDVALHDPDGNHVALDAGSIFSVASAQPGVDLKAGVPITAWVEYRAPRRRLNVWLSYSPSRRPEKPALSADVDLSGLLRTYMYAGFSASNGNGAALHVVERWTFRTFGFPNSSYAPPPTKYIGPMPPNNQPLPPPPSPSPSPPPPSPPPPPH... | Function: Legume-lectin receptor-like kinase required for normal pollen development and male fertility . Regulates pollen exine assembly and aperture development . Plays a critical role in annulus formation, and may participate in the formation of the fibrillar-granular layer underneath the operculum . May function by ... |
Q6UWE0 | MPLFFRKRKPSEEARKRLEYQMCLAKEAGADDILDISKCELSEIPFGAFATCKVLQKKVLIVHTNHLTSLLPKSCSLLSLATIKVLDLHDNQLTALPDDLGQLTALQVLNVERNQLMQLPRSIGNLTQLQTLNVKDNKLKELPDTVGELRSLRTLNISGNEIQRLPQMLAHVRTLEMLSLDASAMVYPPREVCGAGTAAILQFLCKESGLEYYPPSQYLLPILEQDGIENSRDSPDGPTDRFSREELEWQNRFSDYEKRKEQKMLEKLEFERRLELGQREHTQLLQQSSSQKDEILQTVKEEQSRLEQGLSEHQRHLNAE... | Function: E3 ubiquitin-protein ligase that mediates monoubiquitination of TSG101 at multiple sites, leading to inactivate the ability of TSG101 to sort endocytic (EGF receptors) and exocytic (HIV-1 viral proteins) cargos . Bacterial recognition protein that defends the cytoplasm from invasive pathogens . Localizes to s... |
B0R160 | MEKITEKILLEKSSTKTNKLDQIKTLNLSRMSLKSEDLPVPLLSKLCRLEKLDLSGNMLQKIPKGLRLPCLKILNCSNNDMEDVLSLEALTNLEELRLEDNLYLTVNDEHKVIFLLPNLRMFNGKDISSTAHHIRHGSTEILRKRVIGVWERDFSLPDPISAKSLAAVEKSFVNAACTQVKYGPNSLSDYTKWRVEKIAKEYLKSLTSSEEEERVADTTPTKENKTKACDVGGNSITSPQKRTRNNTDVVAEASPRKSSRLVSAAPVEASPRKSARVLNTPQKTQPVVSSPRKHARLTSAETPESSPRKSSRLENVTQKA... | Function: Required for G1/S transition. Recruits and stabilizes the origin recognition complex (ORC) onto chromatin during G1 to establish pre-replication complex (preRC) and to heterochromatic sites in post-replicated cells. Binds a combination of DNA and histone methylation repressive marks on heterochromatin. Requir... |
Q9UFC0 | MGPLSARLLMQRGRPKSDRLGKIRSLDLSGLELLSEHLDPKLLCRLTQLQELDLSNNHLETLPDNLGLSHLRVLRCANNQLGDVTALCQFPKLEELSLEGNPFLTVNDNLKVSFLLPTLRKVNGKDASSTYSQVENLNRELTSRVTAHWEKFMATLGPEEEAEKAQADFVKSAVRDVRYGPESLSEFTQWRVRMISEELVAASRTQVQKANSPEKPPEAGAAHKPRARLAALKRPDDVPLSLSPSKRACASPSAQVEGSPVAGSDGSQPAVKLEPLHFLQCHSKNNSPQDLETQLWACAFEPAWEEGATSQTVATCGGEA... | Function: Required for G1/S transition. Recruits and stabilizes the origin recognition complex (ORC) onto chromatin during G1 to establish pre-replication complex (preRC) and to heterochromatic sites in post-replicated cells. Binds a combination of DNA and histone methylation repressive marks on heterochromatin. Binds ... |
B0JZ65 | MSKITADVLLKEGLPKSIHLKDLKKLNLSKMHLEMKDIDPKLFSQMVNLDELDISHNTLSELPDNLGLHNLRILNFADNHVEDVTVLKQFPNLEEVIYEDNIYLTVSDNYKVFCLLPKLRRLNNKDITSLANHVRFVNHRELSNRVEAHWDSKFKDNLPDKPSSQKINAVAKDFIKSVVNNIKYGPSSLKEFVRWKALGCSGKKRDSADDCTEGSPTKRTRIQHELQSIPLSPRKSNRLQNSPLSLTPIKRKQETSTQGTPSKSTETKSPKVALKSTPSKKQSNESSAKINGKQKLSLTPKIIQKALDNIEPLHFLQCHS... | Function: Required for G1/S transition. Recruits and stabilizes the origin recognition complex (ORC) onto chromatin during G1 to establish pre-replication complex (preRC) and to heterochromatic sites in post-replicated cells. Binds a combination of DNA and histone methylation repressive marks on heterochromatin. Requir... |
O65375 | MLFPPLRSLFLFTLLLSSVCFLQIKADHDDESDLGSDIKVDKRLKFENPKLRQAYIALQSWKKAIFSDPFNFTANWNGSDVCSYNGIYCAPSPSYPKTRVVAGIDLNHADMAGYLASELGLLSDLALFHINSNRFCGEVPLTFNRMKLLYELDLSNNRFVGKFPKVVLSLPSLKFLDLRYNEFEGKIPSKLFDRELDAIFLNHNRFRFGIPKNMGNSPVSALVLADNNLGGCIPGSIGQMGKTLNELILSNDNLTGCLPPQIGNLKKVTVFDITSNRLQGPLPSSVGNMKSLEELHVANNAFTGVIPPSICQLSNLENFT... | Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization. Together with LRX2, component of the extracellular mechanism regulating root hair morphogenesis and elongation.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 80994
Sequ... |
Q9T0K5 | MKKTIQILLFFFFLINLTNALSISSDGGVLSDNEVRHIQRRQLLEFAERSVKITVDPSLNFENPRLRNAYIALQAWKQAILSDPNNFTSNWIGSNVCNYTGVFCSPALDNRKIRTVAGIDLNHADIAGYLPEELGLLSDLALFHVNSNRFCGTVPHRFNRLKLLFELDLSNNRFAGKFPTVVLQLPSLKFLDLRFNEFEGTVPKELFSKDLDAIFINHNRFRFELPENFGDSPVSVIVLANNRFHGCVPSSLVEMKNLNEIIFMNNGLNSCLPSDIGRLKNVTVFDVSFNELVGPLPESVGEMVSVEQLNVAHNMLSGKI... | Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 82246
Sequence Length: 760
Subcellular Location: Secreted
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Q9LHF1 | MKNNTTQSLLLLLLFFFFFFEISHSLSISSNAPLSDTEVRFIQRRQLLYYRDEFGDRGENVTVDPSLIFENPRLRSAYIALQAWKQAILSDPNNITVNWIGSNVCNYTGVFCSKALDNRKIRTVAGIDLNHADIAGYLPEELGLLTDLALFHVNSNRFCGTVPHKFKQLKLLFELDLSNNRFAGKFPTVVLHLPSLKFLDLRFNEFEGTVPKELFSKNLDAIFINHNRFRFELPENFGDSPVSVIVLANNHFHGCIPTSLVEMKNLNEIIFMNNGLNSCLPADIGRLKNVTVFDVSFNELVGPLPESVGGMVEVEQLNVA... | Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 54703
Sequence Length: 494
Subcellular Location: Secreted
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Q9LUI1 | MREDTFFFQWWFLVSGLSFIFLLPQAFTYHTPPINPCFAHPFLPPITNPRLLKAFTALQAWKFTITSDPNGFTSNWCGPNVCNYTGVFCAPALDNPYVLTVAGIDLNHANIAGYLPLELGLLTDLALFHINSNRFQGQLPKTLKCLHLLHELDVSNNKLSGEFPSVIFSLPSLKFLDIRFNEFQGDVPSQLFDLNLDALFINDNKFQFRLPRNIGNSPVSVLVLANNDLQGSCVPPSFYKMGKTLHEIIITNSQLTGCLNREIGLLNQLTVFDVSYNNLVGSLPETIGDMKSLEQLNIAHNKFSGYIPESICRLPRLENF... | Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 52335
Sequence Length: 470
Subcellular Location: Secreted
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Q4PSE6 | MRIYQPTLLIFTTVVLLSISAVAPGGSRQLLYTRDDPITIPPYLIFENVRLERAYVALQAWKRAMISDPWNLTTNWFGSRVCDYNGVVCSESLDDPLVKTVSGVDLNQGDIAGHLPEELGLLTDIALFHVNSNRFCGTLPVGFSQLSLLFELDLSNNRFAGKFPEVVIGLPKLKYLDLRYNEFEGELPESLFDKDLDALFLNSNRFRSKIPVNMGNSPVSVLVLASNRFEGCIPPSFGKMGKTLNEIILMDNGLQSCIPNDMGLLQNVTVLDISYNWLVGELPKSMGQMENLEVLNVERNMLSGLIPDELCSLEKLRDFR... | Function: Modulates cell morphogenesis by regulating cell wall formation and assembly, and/or growth polarization.
PTM: Hydroxylated on proline residues in the S-P-P-P-P repeat.
Sequence Mass (Da): 48088
Sequence Length: 433
Subcellular Location: Secreted
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Q8ND56 | MSGGTPYIGSKISLISKAEIRYEGILYTIDTENSTVALAKVRSFGTEDRPTDRPIPPRDEVFEYIIFRGSDIKDLTVCEPPKPQCSLPQDPAIVQSSLGSSTSSFQSMGSYGPFGRMPTYSQFSPSSLVGQQFGAVGVAGSSLTSFGTETSNSGTLPQSSAVGSAFTQDTRSLKTQLSQGRSSPQLDPLRKSPTMEQAVQTASAHLPAPAAVGRRSPVSTRPLPSASQKAGENQEHRRAEVHKVSRPENEQLRNDNKRQVAPGAPSAPRRGRGGHRGGRGRFGIRRDGPMKFEKDFDFESANAQFNKEEIDREFHNKLKL... | Function: Essential for formation of P-bodies, cytoplasmic structures that provide storage sites for translationally inactive mRNAs and protect them from degradation . Acts as a repressor of mRNA translation . May play a role in mitotic spindle assembly .
Sequence Mass (Da): 50530
Sequence Length: 463
Domain: The LSM14... |
Q9Y802 | MMDLSSKDALSDVLKDTHAQSSDPSLWAIFGHQSSDNVHEGGNESVSVEQEIFDLSQLSERPVSETVSKASIPTNINGLSQVKPSALEKSQEVLSLQKLPIKGRRPAGRRGRPALNTSNSLERNGTRYVSAEAPISVKSSIPAIPRVTFERLCYESAIASNLPPNALSPLEAEMLSEILENPTWLSLYLSIRNGICYLWHRNPTLYVSFNEALGIVREKKAFPLASLAFEFLSRNGHINYGCIYIISSLKLDESLSQKTVAIIGAGMAGISCARQLTNLFAQYEQDFLSRGEKPPRIVIYEASERLGGHIYTHMVPLSDN... | Function: Catalytic component of the SWM histone demethylase complex that specifically demethylates H3K9me2, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Has a role i... |
Q9VW97 | MKPTQFGGSSSKMTEPIEYVTLISDDSDGEPTPKRNVNHPPSALSAPNPGQKQKHPDEDSNDAPATSDERRTSRRNRPKVDYSNRPSGSGDTASNDKSGSASMGPNNQQAERRSQSQTRKSEANATSSSVSGPSAGNSRPSQNGDSKDRDAGTPTVLSGQEGAVFQSRLPFNKMTPNEEACFPDISRSGILGHRVFLNIRNSLLHMWVDNPKIQLSFEIALKNLPPPFDSEPSLVRRVHSFLERHGFINFGIFKRLKPIPAKKLGKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNSYIADVGAMVV... | Function: Probable histone demethylase that specifically demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for heterochromatic gene silencing. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subseque... |
Q53353 | MAHFPQTPGFSGTLRPLRIEGDILDIEIEGEVPPQLNGTFHRVHPDAQFPPRFEDDQFFNGDGMVSLFRFHDGKIDFRQRYAQTDKWKVERKAGKSLFGAYRNPLTDDASVQGMIRGTANTNVMVHAGKLYAMKEDSPCLIMDPLTLETEGYTNFDGKLQSQTFCAHPKIDPVTGNLCAFAYGAKGLMTLDMAYIEISPTGKLLKEIPFQNPYYCMMHDFGVTEDYAVFAVMPLLSSWDRLEQRLPFFGFDTTLPCYLGILPRNGDARDLRWFKTGNCFVGHVMNAFNDGTKVHIDMPVSRNNSFPFFDVHGAPFDPVAG... | Cofactor: 1 Fe(2+) ion per subunit.
Function: Catalyzes the cleavage of the interphenyl double bond (C alpha-C beta) of lignin-derived polyphenolic diaryl-propane type compounds (Stilbene).
Catalytic Activity: 1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene + O2 = 2 vanillin
Sequence Mass (Da): 54436
Sequence Length: 485
EC... |
F4J117 | MAFLQQISGLGALERSCPSIMIGSSFRSGNGRVFDGRGIAYLGSREKFGFNRRRRVVLRVVAMSSSSTPFKMNLNEYMVTLEKPLGIRFALSADGKIFVHAIKKGSNAEKARIIMVGDTLKKASDSSGGTLVEIKDFGDTKKMLVEKTGSFSLVLERPFSPFPIQYLLHLSDLDLLYNRGRVSFVTWNKNLLSSNLRASSQGSGNSGYAAFSSKFFTPQGWKLLNRQSNSFQSGTKKNILSPPISPLVSVFSEDVPGDGEWGYGNFPLEEYIKALDRSKGELSYNHALGMRYSKITEQIYVGSCIQTEEDVENLSEAGIT... | Function: Starch granule-associated phosphoglucan phosphatase involved in the control of starch accumulation. Participates in the regulation of the initial steps of starch degradation at the granule surface. May release a different set of phosphate groups from those removed by DSP4.
Sequence Mass (Da): 65741
Sequence L... |
Q9SRK5 | MSVIGSKSCIFSVARYTRENEKSSCFTSINKKSSLDLRFPRNLAGVSCKFSGENPGTNGVSLSSKNKMEDYNTAMKRLMRSPYEYHHDLGMNYTLIRDELIVGSQPQKPEDIDHLKQEQNVAYILNLQQDKDIEYWGIDLDSIVRRCKELGIRHMRRPAKDFDPLSLRSQLPKAVSSLEWAVSEGKGRVYVHCSAGLGRAPGVSIAYMYWFCDMNLNTAYDTLVSKRPCGPNKGAIRGATYDLAKNDPWKEPFESLPENAFEDIADWERKLIQERVRALRGT | Function: Starch-associated phosphoglucan phosphatase that selectively dephosphorylates the glucan C3 position. Probably participates in the regulation of starch degradation.
Sequence Mass (Da): 32087
Sequence Length: 282
Subcellular Location: Plastid
EC: 3.1.3.-
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Q9SHS8 | MGKNEKTSLGRALVKHHNHMIQETKEKGKSYKDQHKKVLESVTEVSDIDAIIEQAEEAERLFAIHHDSATPVPINMDTGSSSSGITAKEWKEQRMREEALHASSLQVPRRPHWTPKMNVEKLDANEKQAFLTWRRKLASLEENEKLVLTPFEKNLDIWRQLWRVLERSDLIVMVVDARDPLFYRCPDLEAYAQEIDEHKKTMLLVNKADLLPSYVREKWAEYFSRNNILFVFWSAKAATATLEGKPLKEQWRAPDTTQKTDNPAVKVYGRDDLLDRLKLEALEIVKMRKSRGVSATSTESHCEQVVVGFVGYPNVGKSST... | Function: GTPase that might be redundant with LSG1-2 for ribosome biogenesis (Probable). Binds to 23S rRNA .
Sequence Mass (Da): 60758
Sequence Length: 537
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutation of the GTPase motifs described by a G4-G1-G3 pattern.
Subc... |
Q9SJF1 | MGKSEKTSLGRSLVKHHNHMIQESKDKGKYYKNLQKKVLESVTEVSDIDAIIEQAEEAERLYTINHSSSTPLSINLDTNSSSSVIAAEEWREQQKIEEALHASSLQVPRRPPWTPEMSVEELDANEKQAFLNWRRMLVSLEENEKLVLTPFEKNLDIWRQLWRVLERSDLIVMVVDARDPLFYRCPDLEAYAQEIDEHKKIMLLVNKADLLPTDVREKWAEYFRLNNILFVFWSAIAATATLEGKVLKEQWRQPDNLQKTDDPDIMIYGRDELLSRLQFEAQEIVKVRNSRAASVSSQSWTGEYQRDQAVVGFVGYPNVG... | Function: GTPase involved in ribosome biogenesis (Probable). Binds to 23S rRNA and associates with 60S pre-ribosomes . Involved in early cotyledon and leaf development .
Sequence Mass (Da): 66743
Sequence Length: 589
Domain: In contrast to other GTP-binding proteins, this family is characterized by a circular permutati... |
Q2YDM7 | MGRRRAPEGGTLGRALIRQQVQRSRSHRHTDSWLHTSELNDGYDWGRLNLQSVTEQSSLDDFLATAELAGTEFVAEKLNIKFVPPEARTGLLSFEENQRIKKLHEENKQFLCIPRRPKWDQKTSPEELKQAEKDNFLEWRRQLVWLEEEQNLILTPFERNLDFWRQLWRVIERSDIVVQIVDARNPLLFRCEDLECYVKTIDDNKENVILINKADLLTAEQRSAWAEFFKKENVKVIFWSALAEAIKLMGNSKGDVNGDTGEAITAEFENSSCDEAEILHKETEHLSLGEAASSEEDESEYEDCQEEEEDWQTCLEDSSS... | Function: GTPase required for the XPO1/CRM1-mediated nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm (By similarity).
Sequence Mass (Da): 74249
Sequence Length: 652
Domain: In contrast to other GTP-binding protein... |
Q5ZJD3 | MGKKRGTGLGRSLQRQRGSERRGASSWLHASEVVGESGPERRSAVEQSPLEEFLATAELAGTRFVAERLNIQFVSAQSRTGLLTAQEAQHVRQLHEENRQFLRIPRRPYWDRTTSSEDLKQAERESFLEWRRQLAHLEEEKKLILTPFERNLEFWRQLWRVIERSDIVVQIVDARNPLLFRCQDLESYVKEVSNDKENMILINKADLLSEEQRAAWAQFFEKEGVKVVFWSALAECRRLSGEVKELDADSVADDLSDSEEESSSQEEDVTAEDSAESTSTGSALQTENQCLLSDDDSSDEYEDCEDEEEDDWQTCSEDEG... | Function: GTPase required for the XPO1/CRM1-mediated nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm (By similarity).
Sequence Mass (Da): 73831
Sequence Length: 653
Domain: In contrast to other GTP-binding protein... |
Q9W590 | MGKKNKGGAPNLGRQLIKDRFGHTQRRKVDNDTMLHTTELQDGYDWGRLNLSSVTEESSFQAFLRTAELAGTEFQAEKLNITFVNPKQRVGLLSKTQEQRMHQKHDEHRDQLKIPRRPKWTKETSAEELVRAENEAFLDWRRDLALLQEDEEILMTPYEKNLEFWRQLWRVVERSDVVVQIVDARNPLLFRSADLERYVKEVEPSKMNMILVNKSDLLTEEQRRHWAEYFDSEGIRTAFYSATLVEEELKREAEECLDSFPEVQQLRRAVEEIKQSLDSVEDALNVIEQKYKTIPETQNDELPRLPGDKNSPRLLSRLEL... | Function: GTPase required for the nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of Nmd3 from the 60S ribosomal subunit after export into the cytoplasm. Regulator of body size; acts in serotonergic neurons to regulate insulin signaling and thus exerts global growth control.
Sequence... |
Q9H089 | MGRRRAPAGGSLGRALMRHQTQRSRSHRHTDSWLHTSELNDGYDWGRLNLQSVTEQSSLDDFLATAELAGTEFVAEKLNIKFVPAEARTGLLSFEESQRIKKLHEENKQFLCIPRRPNWNQNTTPEELKQAEKDNFLEWRRQLVRLEEEQKLILTPFERNLDFWRQLWRVIERSDIVVQIVDARNPLLFRCEDLECYVKEMDANKENVILINKADLLTAEQRSAWAMYFEKEDVKVIFWSALAGAIPLNGDSEEEANRDDRQSNTTKFGHSSFDQAEISHSESEHLPARDSPSLSENPTTDEDDSEYEDCPEEEEDDWQT... | Function: GTPase required for the XPO1/CRM1-mediated nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm (Probable).
Sequence Mass (Da): 75225
Sequence Length: 658
Domain: In contrast to other GTP-binding proteins, th... |
Q3UM18 | MGRRRAPGGGSLGRVLIRQQTQRSRSHRHTDSWLHTSELNDGYDWGRLNLQSVTEQSSLEDFLATAELAGTEFVAEKLNIKFVPPEARTGLLSFEESQRIKKLHEENRQFLCIPRRPNWDRKTSPEELKQAEKDNFLKWRRQLVRLEEEQKLILTPFERNLDFWRQLWRVIERSDIVVQIVDARNPLLFRCEDLECYVKEIDAAKENVILINKADLLTAEQRFAWAVHFEKEGVKVIFWSALAETDHLNGDLKEEVDSVAGDTNKTESESSSLDANEIPHRDLISLSEESASDSGDSKYEDCQEDEEEDWQTCSEEDSVP... | Function: GTPase required for the XPO1/CRM1-mediated nuclear export of the 60S ribosomal subunit. Probably acts by mediating the release of NMD3 from the 60S ribosomal subunit after export into the cytoplasm (By similarity).
Sequence Mass (Da): 73157
Sequence Length: 644
Domain: In contrast to other GTP-binding protein... |
Q88W75 | MWIYLILMVALVIIDQVIKAAIVSHIALGASTSIVTGLLSLTNLHNNGAAWSILEGKMWFFYLISVIALIVMGYLLWRLRGKWLYEVGISLMIAGTLGNFIDRLRIGYVVDMFQLDFINFPIFNFADSCLTVGVIFILIGVLRDDSFEK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q38X31 | MLLYIILGLLILVGDQLLKGWIVANVSYGALHTVIPNILGLTYVQNDGAAWSMLAGQQWFFYIVTIIAVGVIGYLFYTSERSEKLYRIGLTLMLAGALGNFIDRLHLKYVVDMFQLEFINFPIFNVADTALTCGVICVFIAILLKEKVTHD | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q6AE72 | MATSRTAPTRAPSLRSSPALEASPSRTKASVGALVILAVVALCVYLMDQITKALVVSNLSEGQQVAVLGQLLQLHFVKNPGAAFSIGSGSTWIFSLVGVGVLGFVIWYAPRIRSTAWAILFGLLLGGLLGNLTDRLFREPGFGVGHVIDFLQIPLLTAIFNLADVAIVFSMGLFLLLTLRGIGLDGRRQRDEGAGVSSASPAGDESAADKPENLSA | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q72PS8 | MKYFEKRFLDVYRPIYLGVIFLGIVLDLVTKFLVILYFQPHRYLEVFGSFFRMTLTFNTGFVFGAFQDNAIPSLIATGVAIVFLIGYRWKNHDLGNPWGWNLVMAGAFGNFLDKFFVKIPGTGFRFGFQPNMGEYIGVVDFLDFDWPDFLLFSRWPAFNVADSCVTIGLTILIFTMKLEEEK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q1WTX7 | MWLYIPMIIILIIADQGLKFWISVNIKLGTSQVILPNVLALTNVRNDGAAWSVLSGQQWFFTVITIVALGLMGYFFWKLRSDNLYMLAISLLIAGTLGNFIDRIRLGYVVDMFETLFMNFPIFNVADMCLTFGVIIVIIALIKDEKDE | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q8EWS0 | MIKQFFSNVYEGIKHYSNYLWELSKKQLIKIYLNKKHLIWKISIILICAFIVLLTSFLTRNSILNATQSYWELIPGFLVINITGNTGVSFGTLGDSNPSLVYFVQSIPIVLGFFVLLFSSNYLLDIGVSLVFFGGLSNIIDRSIVDNYKYLSGISTNNAVVDYFQFPFIKNSAIFNFPDTFVIIGMIFVGIQIIISFVKDYKKEKDSEENKKPIKDVVLDEERNKTKKEPIKKPIVIQKS | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
C6BV90 | MNKYFLAGIISVVTLVLDQVTKIAVREKMVLWTSETVIPGFFNLVHVVNKGAAFGFLNRADITWQRNFFVVVTIIALGAIGMLLKSAEEKDKFQILGLGFVLGGAIGNLIDRILYHQVTDFLDFYYGSHHYPAFNVADIAICLGAFAMIVSFYKNK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
C5BQX3 | MHKLNVLAALKWYGVALLVILLDQITKNVASHMLVLHQPEPITSFFNFTLRHNFGAAFSMFHDAGGWQRWFLALLAAGVSVLLIFWIAKLPKQKWMEALALALVLGGALGNLYDRMLLGYVVDFIVVHYKEHEWPAFNIADSAICIGAALLVWDSLFGTKVAKYGDAK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
B5YJT2 | MSLKLYKTSISIFLILLIDQITKYLAIKFLSPDGIVKLLPFLNLVYVENTGTAFGMFKFLGSGFFIIIALVVTGFLVYMYFKDTQNWFIYSLIIAGALGNIIDRLIYGYVIDFIDLHLKNLHWPAFNVADSAISIGIVLFVYKNLKK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
C4LD11 | MMSLLTGTGLRWMWLAVFAIVLDQAAKLAIMQHIPYGHGVVITPFFNLVHVYNTGAAFSFLADAEGWQRWLFSGLAIVISGVLAVAMAKAPAKCSLSNLAYSLVIGGAIGNLIDRVVYGHVVDFLDFHWQDLYHFAAFNVADMAISCGAVFIILDGFIKKPADK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q73JG0 | MNNKKDYYLPFLLTAIVIVVDQVTKILVVQYMSVNEVIPVIGDLVNLRFVYNTGAAFSLGAGFGEIARKILLVFLPFLLLIALTGAYLKSAELTRAQRWFICGILGGGFGNLIDRFFRSEGVVDFIDVKFFGILGMERWPTFNAADSFIVCCGIGLGVNLILQGIKQKKLKDS | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
O83943 | MKLTRIQKEKWIPLFAAGLVVVLDQCAKLLVGAYVPTNTSGVRVLGDFVRIVHVYNVGAAFSIGHQLNQVLRTLVLGIVPLIIMFLIVFSYFRTDAFCPVQRWAVSGIIGGGIGNLIDRFLRPNGVLDFIDVKFFGIFGFERWPAFNIADAVIMTCGLLLIISFIKQEKEISSQPSCNETGGVFRT | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q83G22 | MTTRTLRFYALVGFLVFLDQVTKYLAHAYLARDFIVIPNLFRLTLAKNSGAAFSFGTGFSWLFFLLGIIALIFIGWFLPRTTGSIVFLALLQGGIAGNVFDRLFKPPYFGNGEVVDFLNTPLLSGVVFNIADLFILAGVFGTFLFLKGSK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q9KU46 | MSNSSLALKQSGLRWLWLALLVFIADITIKLIVMDNMGYGWANRIEVLPFFNLLYVHNYGAAFSFLSDQEGWQRWLFTGIAFVVTGMLAYWMRRLPASDKWNNIAYALIIGGAVGNVFDRIVHGFVVDYLDFYWGTYHWPAFNLADSTICIGAAMIILDGFRAKKSAPSQS | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q8D2R1 | MKTKSNLIIISIFLIDFFTKKWILNNYEIFDSIKIFPMIKITYIRNYGIALGLFQSYSNLIRILIIVISIFILLFIFYMKNLCKDLLSNLGYSIIIGGSFGNIFDRIFYGSVIDFIDIYIYKWHFPVFNFADISIFIGFLILIYNKKIFIVNT | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q7M9M1 | MRIALFRSLGLFVLVFAIDQAIKALILGGFRWESEALSITLAFNKGVAFSMFAFLEGWLKYIQLGMLGGILLFLAYDRSFFVAHYLPLSILLAAGFSNILDRFIHGGVVDYVYWHYGFEFAIFNFADVMIDVAVALFLWQTFFKQK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q8ZKP9 | MHVTLVEINVHDDKVEQFIDVFRQNHLGSIKEPGNLRFDVLQDPQVLTRFYIYEAYVDEQAVAFHKTTPHYKTCVEQLEPLMTGPRTKKVFMGLMP | Function: Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the conversion of (4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione (P-DPD) to 3-hydroxy-5-phosphonooxypentane-2,4-dione (P-HPD).
Catalytic Activity: (2S)-2-hydroxy-3,4-dio... |
A1JJ50 | MHVTLVEINVKEDKVEQFVEVFRANHQGSLLEPGNLRFDVLQDESIPTRFYIYEAYVDEAAVAAHKKTPHYLRCVEELEGLMTGPRKKTTFIGLMP | Function: Involved in the degradation of phospho-AI-2, thereby terminating induction of the lsr operon and closing the AI-2 signaling cycle. Catalyzes the conversion of (4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione (P-DPD) to 3-hydroxy-5-phosphonooxypentane-2,4-dione (P-HPD).
Catalytic Activity: (2S)-2-hydroxy-3,4-dio... |
Q8GYS8 | MKIGVVLVLLTVFVVVMSSTSVSAQSDEDECLKETGQMQLNCFPYLTDNRIHTPSFACCSEVYTVGKTYVDCFCQFINNGGPSFGIVVSQKLLDLPELCGVYGACGNGKNFKNTSL | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 12580
Sequence Length: 116
Subcellular Location: Cell membrane
|
F4HZB9 | MILAILALVIATFLYGGATTVQAGCRDTLTSLSPCLYYLNGGSSSPSWSCCRQFSTVVQSSPECLCSVVNSNESSFYGFKFNRTLALNLPTACNVQTPSPSLCNTGGNVPTTLPANTPVGSPRSAPSPSGTTSPANTPSGSKKFPLSNESSSKSNVIILSFVSIALVLAII | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 17664
Sequence Length: 171
Subcellular Location: Cell membrane
|
Q9LJ85 | MSKIISLVVAMIAVLALPIRGQQQPLSQCTPSMMTTVSPCMGFITNSSSNGTSPSSDCCNSLRSLTTGGMGCLCLIVTGTVPFNIPINRTTAVSLPRACNMPRVPLQCQANIAPAAAPGPAATFGPSMSPGPETDPIVPEPTPAAQTPQSDTTRPFTPSVDGGAPTSDDGGSTSRPSETPSSAYALSPSLLFFSIALVALKFY | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20779
Sequence Length: 203
Subcellular Location: Cell membrane
|
Q1G2Y5 | MNSNSFLISAALIFSLLSSNSPTSILAQINTPCSPSMLSSVTGCTSFLTGGGSFPTSDCCGALKSLTGTGMDCLCLIVTAGVPISIPINRTLAISLPRACGIPGVPVQCKASAAPLPTPGPASFGPTTSPTDSQTSDPEGSASFRPPTSPTTSQTPNDKDLSGSGNGGDPMGFAPPPPSSSPSSSHSLKLSYLLFAFAFTIIKFI | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20621
Sequence Length: 205
Subcellular Location: Cell membrane
|
Q9M2G1 | MARFMAYNQNPQMLALCITVAVMFLGVRSELSQDIKGCQDAMSDLYSCLPFVTNKAKAPDSTCCSTLKVKIDKGQTRKCLCTLVKDRDDPGLGFKVDANRAMSLPSACHVPANISQCPDLLHLLPDSPASQIFKQFTESSSQTVGHKAVSTSSSIKGRDNKQFGLMMAGALSIWYIM | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 19291
Sequence Length: 177
Subcellular Location: Cell membrane
|
Q2PE60 | MKPSFVLLSIVLLLSSSLSDAADFGSPSQPPSMAPTPQPSNSTDCSSVIYSMVDCLSFLTVGSTDPSPTKTCCVGVKTVLNYSPKCLCSALESSREMGFVLDDTKALAMPKICNVPIDPNCDVSTPAASTPVSPPVESPTTSPSSAKSPAITPSSPAVSHSPPPVRHSSPPVSHSSPPVSHSSPPTSRSSPAVSHSSPVVAASSPVKAVSSSTASSPRAASPSPSPSPSISSSGILLVSKLFIAVVMVSSFLYILA | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25907
Sequence Length: 256
Subcellular Location: Cell membrane
|
Q9STH5 | MAQTTTLILLLATLLVAATTVSGQGPHIPLAPSPSVNEAMNCAAGLAVCLPAITQRGPPSQECCTAVETALTTQLSCLCGFIKSPMLLIPFNVTDFNALFSKTCGLTTDPNLCSETAAQAPLPKTAAPVPGAPKSDKDAASKLAGTGLVGIVVITIAAMFY | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 16330
Sequence Length: 161
Subcellular Location: Cell membrane
|
F4JIG1 | MATKITGVFILILTITFSSSSAVTATQQAPSSSPPVLTCTEELVMFSPCLPYVSSPPNNMSETPDPICCSVFTSSVHSSTGNCLCYLLRQPMILGFPLDRSRLISLSQICTDQNSEESFESLCSVSESPELPPLQSIQFTNPFVSGNNVSASPQSVDLAPEVSPSSDLFSPETATLAPPPPPPPLPVLQYFSSDSLKIRNFWFPSTIIMTFATSILARI | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23547
Sequence Length: 219
Subcellular Location: Cell membrane
|
O49644 | MAYTNKVAVAVGAAVVFLAVVMNPRWTEAQTYPKLDRLCVMMIPDILEECFTHDRLKPTEDCCNDLKNATMTQVDCLCDNFLESLSFSDLSRTFSAGVLKKCDVSHKYMCQAAKNRGEAKGGRNSTTTCDNSITNTSVGGKNKVATSMSAFGLVAILLFVMF | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 17730
Sequence Length: 162
Subcellular Location: Cell membrane
|
Q1G3I0 | MAYTNQISAVVFLAVAIAPLLAEPQSTMFPEMTPECATVMPDLLEKCFATGSVTPTEDCCTDLKSATSTQVTCLCDNYIANPAVSNITGPYSKAITTKCGVFDKYSCDGTSKGGEEKKGGSSSSNGKDNGKSEGNGGRANSVAASMAMFGLLASLVFVMF | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 16587
Sequence Length: 160
Subcellular Location: Cell membrane
|
Q9FY78 | MAYFSTATSLLLLVLSVSSPYVHGASDCDTLVITLFPCLPFISIGGTADTPTASCCSSLKNILDTKPICLCEGLKKAPLGIKLNVTKSATLPVACKLNAPPVSACDSLPPASPPTANGQAPVWGSGWAPAPSPSKGNSLIPISGFSFVIVTALAMFRI | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 16164
Sequence Length: 158
Subcellular Location: Secreted
|
Q9FFY3 | MMMGMKFFSFYVVLLLVAASSGMRINGQSVSCLNQLAPCLNYLNGTKEVPQVCCNPLKSVIRNNPECLCRMISNRWSSQAERAGIDVNDAQMLPARCGEHVNPIACLTRSRGGSTNSDRSSSIGNTFSQSYWMTTLAIAATVLSYCHHIIS | Function: Lipid transfer protein that promotes the number of phloem (pro)cambial and pericycle cells.
Location Topology: Lipid-anchor
Sequence Mass (Da): 16532
Sequence Length: 151
Subcellular Location: Cell membrane
|
Q8VYI9 | MATHSSFTATTPLFLIVLLSLSSVSVLGASHHHATAPAPSVDCSTLILNMADCLSFVSSGGTVAKPEGTCCSGLKTVLKADSQCLCEAFKSSASLGVTLNITKASTLPAACKLHAPSIATCGLSVAPSTAPGLAPGVAAAGPETAGFLAPNPSSGNDGSSLIPTSFTTVLSAVLFVLFFSSA | Function: Probable lipid transfer protein (By similarity). Proteoglycan-like factor that exhibits xylogen activity consisting in mediating local and inductive cell-cell interactions required for xylem differentiation .
Location Topology: Lipid-anchor
Sequence Mass (Da): 17972
Sequence Length: 182
Subcellular Location: ... |
O49645 | MAYTNKVTISAAVATMMLFLAVTIVDAQSMPPMPKFNPVCALADLPNIVQLCYFNLDLTPSEECCNDLKSSSTIQVNCLCDNFIAHPSNGNISQARYDLVNSACGVADKFACKGGDASGGSTNKIAASMVLLGLVASLFF | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 14753
Sequence Length: 140
Subcellular Location: Cell membrane
|
Q9SUV6 | MAVAVTAVLFLAVVIAPQWTETKKPPRPSDTSDTSGTSGRDRRTMCPLSIPGIVQNCYATLNAFPSKECCKDLKTASKREVTCLCNNVIAHPDPLYTNTNQVNKACGVLDKYACDAGNSNGGATKKIVASMGLFGVVASLFF | Function: Probable lipid transfer protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 15077
Sequence Length: 142
Subcellular Location: Cell membrane
|
A4F2N8 | MQLSSYHDVIKAAERLEGFANRTPVFTSRTLDAETGAQVFIKCENLQRTGSFKFRGAFNALSRFDEAQRKAGVVAFSSGNHAQGIALAARLLQMPATIVMPTDAPAAKVAATREYGATVVFYDRITEDREQIGRTLAEQHGMTLIPSYDHPDVLAGQGTAAKELLEFTGPLDALFVGLGGGGMLSGTALATRALSPDCLLYGVEPEAGNDGQRSFQTGSIVHIDTPATIADGAQTQHLGNHTFPIIRENVNDILTVSDAELVESMRFFMQRMKMVVEPTGCLGLAALRNLKQQFRGQRVGIIVTGGNVDIEKYASLLKG | Cofactor: Requires a divalent metal cation such as Mn(2+), Mg(2+), or Ca(2+).
Function: Catalyzes the deamination of L-threo-3-hydroxyaspartate to oxaloacetate and ammonia. Shows a high specificity towards L-threo-3-hydroxyaspartate as other 3-hydroxyaminoacids, i.e. D,L-erythro- and D-threo-3-hydroxyaspartate, D-threo... |
P36007 | MIVPTYGDVLDASNRIKEYVNKTPVLTSRMLNDRLGAQIYFKGENFQRVGAFKFRGAMNAVSKLSDEKRSKGVIAFSSGNHAQAIALSAKLLNVPATIVMPEDAPALKVAATAGYGAHIIRYNRYTEDREQIGRQLAAEHGFALIPPYDHPDVIAGQGTSAKELLEEVGQLDALFVPLGGGGLLSGSALAARSLSPGCKIFGVEPEAGNDGQQSFRSGSIVHINTPKTIADGAQTQHLGEYTFAIIRENVDDILTVSDQELVKCMHFLAERMKVVVEPTACLGFAGALLKKEELVGKKVGIILSGGNVDMKRYATLISGK... | Cofactor: Requires a divalent metal cation such as Mn(2+), Mg(2+), or Ca(2+).
Function: Catalyzes the deamination of L-threo-3-hydroxyaspartate to oxaloacetate and ammonia. Shows a high specificity towards L-threo-3-hydroxyaspartate as other 3-hydroxyaminoacids, i.e. D,L-erythro- and D-threo-3-hydroxyaspartate, D-threo... |
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