ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q83906 | MSGTSESELKNLISSLHLNNGFLGIFDCRFPGFLQKSKIQTAIINTGPREQGGIHWITLALEPISYKLFIFDPLGWKDTQLIKFYNFSLNSLIKRSALNNSDRCITVERNTQSVQCTCAGSCGLFCIFFLYCFHFYKQNVFKSWLFQKLNGSTPSLIPCEPHLLHENQTFLYDFLNAKSVYFRKNYRTFIENTKTGLIKTH | Function: Cleaves viral precursor proteins (pTP, pIIIa, pVI, pVII, pVIII, and pX) inside newly assembled particles giving rise to mature virions. Protease complexed to its cofactor slides along the viral DNA to specifically locate and cleave the viral precursors. Mature virions have a weakened organization compared to ... |
P0DOI1 | MGNSPSYNPPAGISPSDWLNLLQSAQRLNPRPSPSDFTDLKNYIHWFHKTQKKPWTFTSGGPASCPPGKFGRVPLVLATLNEVLSNDEGAPGASAPEEQPPPYDPPAVLPIISEGNRNRHRAWALRELQDIKKEIENKAPGSQVWIQTLRLAILQADPTPADLEQLCQYIASPVDQTAHMTSLTAAIAAEAANTLQGFNPKMGTLTQQSAQPNAGDLRSQYQNLWLQAWKNLPTRPSVQPWSTIVQGPAESYVEFVNRLQISLADNLPDGVPKEPIIDSLSYANANKECQQILQGRGLVAAPVGQKLQACAHWAPKTKQP... | Function: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus.
PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding,... |
P49860 | MPEIVKTLSFDETEIKFTGDGKQGIFEGYASVFNNTDSDGDIILPGAFKNALANQTRKVAMFFNHKTWELPVGKWDSLAEDEKGLYVRGQLTPGHSGAADLKAAMQHGTVEGMSVGFSVAKDDYTIIPTGRIFKNIQALREISVCTFPANEQAGIAAMKSVDGIETIRDVENWLRDSVGLTKSQAVGLIARFKSAIRSESEGDGNEAQINALLQSIKSFPSNLGK | Function: Protease involved in virion assembly and maturation.
PTM: Cleaves itself autocatalytically to yield the mature form of the protease.
Sequence Mass (Da): 24392
Sequence Length: 225
Subcellular Location: Virion
|
Q01267 | MKKHAIGIAALNALSIDDDGWCQLLPAGHFSARDGRPFDVTGGQGWFIDGEIAGRLVEGVRALNQDVLIDYEHNQLRKDKGLPPEQLVAAGWFNADEMQWREGEGLFIHPRWTAAAQQRIDDGEFGYLSAVFPYDTATGAVLQIRLAALTNDPGATGMKKLTALAADLPDILQQENKPMNETLRKLLARLGVTVPENADITDEQATAALTALDTLEINAGKVAALSAELEKAQKAAVDLTKYVPVESYNALRDELAQATAQSATASLSAVLDKAEQEGRIFKSERTYLEQLGGQIGVAALSAQLEKKQPIAALSAMQTTT... | Function: Protease I is involved in virion assembly and maturation. Protease I cleaves the portal protein to yield mature procapsids competent for DNA packaging (Probable). Isoform scaffold protein Z probably helps the capsid proteins to assemble into a functional capsid (Probable).
PTM: The N-terminus is acetylated.
S... |
Q6QGD7 | MTQAAIDYNKLKSAPVHLDAYIKSIDSESKEGVVKIRGFANTISKDRAGDVIPASAWKTSNALTNYMKNPIILFGHDHRRPIGKCIDLNPTEMGLEIECEINESSDPAIFSLIKNGVLKTFSIGFRCLDAEWDEATDIFIIKDLELYEVSVVSVPCNQDSTFNLAKSMNGHDYTEWRKSFTAISSKAVPAQERNLSELEKLAIALGYVKE | Function: Serine protease involved in capsid assembly and maturation. Cleaves the major capsid protein, the decoration protein, the portal protein to yield mature procapsids competent for DNA packaging (Probable). Acts as a trigger for assembly of the capsid protein.
PTM: Cleaves itself autocatalytically to yield the m... |
P10274 | MGQIFSRSASPIPRPPRGLAAHHWLNFLQAAYRLEPGPSSYDFHQLKKFLKIALETPARICPINYSLLASLLPKGYPGRVNEILHILIQTQAQIPSRPAPPPPSSPTHDPPDSDPQIPPPYVEPTAPQVLPVMHPHGAPPNHRPWQMKDLQAIKQEVSQAAPGSPQFMQTIRLAVQQFDPTAKDLQDLLQYLCSSLVASLHHQQLDSLISEAETRGITGYNPLAGPLRVQANNPQQQGLRREYQQLWLAAFAALPGSAKDPSWASILQGLEEPYHAFVERLNIALDNGLPEGTPKDPILRSLAYSNANKECQKLLQARGH... | Function: The matrix domain targets Gag, Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus.
PTM: Specific enzymatic cleavages by the viral protease yield mature proteins. The polyprotein is cleaved during and after budding,... |
Q13523 | MAAAETQSLREQPEMEDANSEKSINEENGEVSEDQSQNKHSRHKKKKHKHRSKHKKHKHSSEEDKDKKHKHKHKHKKHKRKEIIDASDKEGMSPAKRTKLDDLALLEDLEKQRALIKAELDNELMEGKVQSGMGLILQGYESGSEEEGEIHEKARNGNRSSTRSSSTKGKLELVDNKITTKKRSKSRSKERTRHRSDKKKSKGGIEIVKEKTTRSKSKERKKSKSPSKRSKSQDQARKSKSPTLRRRSQEKIGKARSPTDDKVKIEDKSKSKDRKKSPIINESRSRDRGKKSRSPVDLRGKSKDRRSRSKERKSKRSETD... | Function: Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF.
PTM: Phosphorylated by Clk1.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 116987
Sequence Length: 1007
Subcellular Location: Nucleus
EC: 2.7.11.1
|
O33071 | MNILSRIFARTPSLRTRVVVATAIGAAIPVLIVGTVVWVGITNDRKERLDRKLDEAAGFAIPFVPRGLDEIPRSPNDQDAIITVRRGNLVKSNFDITLPKLTNDYADTYLRGVRYRVRTVEIPAPEPTSIAVGATYDATVAETNNLHRRVLLICGFAIAAAAVFAWLLAAFAVRPFKQLAQQTRSVDAGGEAPRVEVHGATEAVEIAEAMRGMLQRIWNEQNRTKEALASARDFAAVSSHELRTPLTAMRTNLEVLATLDLADDQRKEVLGDVIRTQSRIEATLSALERLAQGELSTSDDHVPVDITELLDRAAHDATRS... | Function: Member of the two-component regulatory system PrrB/PrrA that is involved specifically in early intracellular multiplication of Mycobacterium and is essential for its viability. Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the cons... |
Q6J4G7 | MGKLLLILGSVIALPTFAAGGGDLDASDYTGVSFWLVTAALLASTVFFFVERDRVSAKWKTSLTVSGLVTGIAFWHYMYMRGVWIETGDSPTVFRYIDWLLTVPLLICEFYLILAAATNVAGSLFKKLLVGSLVMLVFGYMGEAGIMAAWPAFIIGCLAWVYMIYELWAGEGKSACNTASPAVQSAYNTMMYIIIFGWAIYPVGYFTGYLMGDGGSALNLNLIYNLADFVNKILFGLIIWNVAVKESSNA | Function: Light-driven proton pump.
PTM: Contains one covalently linked retinal chromophore per subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27308
Sequence Length: 250
Subcellular Location: Cell membrane
|
Q66GI4 | MLRLTCFTPSFSRACCPLFAMMLKVPSVHLHHPRFSPFRFYHTSLLVKGTRDRRLILVERSRHLCTLPLAAAKQSAASPSENLSRKAKKKAIQQSPEALLKQKLDMCSKKGDVLEALRLYDEARRNGVQLSQYHYNVLLYVCSLAEAATESSPNPGLSRGFDIFKQMIVDKVVPNEATFTNGARLAVAKDDPEMAFDMVKQMKAFGIQPRLRSYGPALFGFCRKGDADKAYEVDAHMVESEVVPEEPELAALLKVSMDTKNADKVYKTLQRLRDLVRQVSKSTFDMIEEWFKSEVATKTGVKKWDVKKIRDAVVSGGGGW... | Cofactor: Binds 2 Mg(2+) or Mg(2+) ions per subunit.
Function: Endonuclease RNase P responsible for the 5' maturation of tRNA precursors. Preferentially cleaves at the unusual cleavage site, but also able to cleave at the classical cleavage site. Also involved in the maturation of mRNAs in mitochondria.
Catalytic Activ... |
Q680B9 | MAASDQHRSRRHDESSSRPNKKKKVSRNPETNLLFNLNSCSKSKDLSAALALYDAAITSSEVRLSQQHFQTLLYLCSASITDISLQYLAIDRGFEIFDRMVSSGISPNEASVTSVARLAAAKGNGDYAFKVVKEFVSVGGVSIPRLRTYAPALLCFCEKLEAEKGYEVEEHMEAAGIALEEAEISALLKVSAATGRENKVYRYLHKLREYVGCVSEETLKIIEEWFCGEKAGEVGDNGIGSDVGMLREAVLNNGGGWHGHGWVGEGKWTVKKGNVSSTGRCLSCSEQLACVDTNEVETQKFVDSLVALAMDRKTKMNSCE... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Endonuclease RNase P responsible for the 5' maturation of tRNA precursors . Preferentially binds precursor tRNAs containing short 5' leaders and 3' trailers . Also involved in the maturation of mRNA and small nucleolar RNA (snoRNA) .
Catalytic Activity: Endonucleolyt... |
F4JKB6 | MKLKKPSLPSSLLCAVPPCLSQIRLLIPRRVRVSSSTFANAKLVTLRNHTVNLHIYYCSMAGTDNRRSRHDDESPKNPNKKKKGNRNPEKSLLINLHSCSKRKDLSAALALYDAAITSSDIRLNQQHFQSLLYLCSAFISDPSLQTVAIDRGFQIFDRMVSSGISPNESSVTAVARLAAAKGDGDYAFKLVKDLVAVGGVSVPRLRTYAPALLCFCDTLEAEKGYEVEDHMDASGIVLEEAEISALLKVSAATGRENKVYRYLQKLRECVGCVSEETSKAIEEWFYGVKASEVSDNGIGSDIELLRAAVLKNGGGWHGLG... | Cofactor: Binds 2 Mg(2+) or Mg(2+) ions per subunit.
Function: Endonuclease RNase P responsible for the 5' maturation of tRNA precursors. Also involved in the maturation of mRNA and small nucleolar RNA (snoRNA).
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Seque... |
P81264 | MKAVGAWLLCLLLLGLALQGAASRAHQHSMEIRTPDINPAWYAGRGIRPVGRFGRRRAAPGDGPRPGPRRVPACFRLEGGAEPSRALPGRLTAQLVQE | Function: Stimulates prolactin (PRL) release and regulates the expression of prolactin through its receptor GPR10. May stimulate lactotrophs directly to secrete PRL.
PTM: Amidation of C-terminus is required for receptor interaction.
Sequence Mass (Da): 10544
Sequence Length: 98
Subcellular Location: Secreted
|
Q01939 | MTAAVTSSNIVLETHESGIKPYFEQKIQETELKIRSKTENVRRLEAQRNALNDKVRFIKDELRLLQEPGSYVGEVIKIVSDKKVLVKVQPEGKYIVDVAKDINVKDLKASQRVCLRSDSYMLHKVLENKADPLVSLMMVEKVPDSTYDMVGGLTKQIKEIKEVIELPVKHPELFESLGIAQPKGVILYGPPGTGKTLLARAVAHHTDCKFIRVSGAELVQKYIGEGSRMVRELFVMAREHAPSIIFMDEIDSIGSTRVEGSGGGDSEVQRTMLELLNQLDGFETSKNIKIIMATNRLDILDPALLRPGRIDRKIEFPPPS... | Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity).
PTM: N-acetylated by NAT1.
Sequence Mass (Da): 45272
Sequence Length: 405
Subcellular Location: Cyt... |
Q81U45 | MKKAMLALAATSVIALSACGTSSSDKIVTSKAGDITKDEFYEQMKTQAGKQVLNNMVMEKVLIKNYKVEDKEVDKKYDEMKKQYGDQFDTLLKQQGIKEETLKTGVRAQLAQEKAIEKTITDKELKDNYKPEIKASHILVKDEATAKKVKEELGQGKSFEELAKQYSEDTGSKEKGGDLGFFGAGKMVKEFEDAAYKLKKDEVSEPVKSQFGYHIIKVTDIKEPEKSFEQSKADIKKELVAKKSQDGEFMNDLMMKEIKKADVKVDDKDLKDLFEEKKADAKKEEKK | Function: Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins. Important for the secretion of the protective antigen. The three PsrA proteins in this organism show different but overlapping substrate specificities.
Catalytic Activity: [protein]-... |
P60750 | MNKTWKKAATVLAFAGIALSATACSGGKAVVTYKGGKITESQYYDKMKESQAGQSTLASMIVSDALESQYGKDVTQKQVDKEYNKYKKQYGSQFDSVLEQNGMTASTFKDNLKTNLLTEAALKHIKKITPAQEKKAWKNYQPEVTVQHILVSKKSTAEDVIKQLQDGGDFKKLAKKYSTDTATKNDAGKLPAFDSTDSTLDSSFKTAAFKLKTGEITTTPVKTQYGYHVIKMIKHPAKGTFKEHKKQIDNQIYQSMSEDQNVMRSVIATVLKRADVSIKDKDLKNVLSQYVSSDSLSK | Function: Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Location Topology: Lipid-anchor
Sequence Mass (Da): 33048
Sequence Length: 298
Subcell... |
Q88X05 | MKKWLIALAGVLLTFTLAGCGSKTVASTSGGKITESQYYSSMKGTSSGKQVLQQMILNKVLEKDYGSKVSTKQVTKQYNTYKSQYGSSFSTVLSQNGLTTKTFKEQLRSNLLLKEAVKDKVKITDKALKKQWKSYEPKVTVQHILVAKSATADKVLDALKKDSSQANFTKLAKKYSTDTTTKNDGGKLSAFDNTNTSYSSKFLTAAFKLKNGEYTTSAVKTSNGYEIIRMIKNPGKGKMSDHTADLKKQIWDNDMSDSTVLQNVVSKVLKGGNVSIKDNDLKDILSSYLSTSSSSSSN | Function: Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Location Topology: Lipid-anchor
Sequence Mass (Da): 32619
Sequence Length: 298
Subcell... |
Q92BR2 | MTKLKKVMISLVAATLLLLAGCGSSAVVKTDAGNVTQDELYEAMKTTYGNEVVQQLTFKKILEDKYTVTEKEVNAEYKKYEEQYGDSFESTLSSNNLTKTSFKENLEYNLLVQKATEANMNVSESKLKTYYKTWEPNITVRHILVDDEATAKEIQTKLKNGEKFADLAKEYSTDTATSTNGGLLDPFGPGEMDETFEKAAYALKNKDDVSGIVKSTYGYHLIQLVKKTEKGTYAKEKANVKAAYIKSQLTSENMTAALKKELKAANIDIKDSDLKDAFADYTSTSSSSSTSTSN | Function: Plays a major role in protein secretion by helping the post-translocational extracellular folding of several secreted proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Location Topology: Lipid-anchor
Sequence Mass (Da): 32552
Sequence Length: 294
Subcell... |
Q99405 | MKKPLGKIVASTALLISVAFSSSIASAAEEAKEKYLIGFNEQEAVSEFVEQIEANDDVAILSEEEEVEIELLHEFETIPVLSVELSPEDVDALELDPTISYIEEDAEVTTMAQSVPWGISRVQAPAAHNRGLTGSGVKVAVLDTGISTHPDLNIRGGASFVPGEPSTQDGNGHGTHVAGTIAALNNSIGVLGVAPSAELYAVKVLGASGSGSVSSIAQGLEWAGNNGMHVANLSLGSPSPSATLEQAVNSATSRGVLVVAASGNSGAGSISYPARYANAMAVGATDQNNNRASFSQYGAGLDIVAPGVNVQSTYPGSTYA... | Cofactor: Binds 2 calcium ions per subunit.
Function: Alkaline serine protease that cleaves various substrates, including N-succinyl-Ala-Ala-Pro-Phe-pNA, N-succinyl-Ala-Ala-Pro-MetpNA, oxidized insulin B chain, casein, hemoglobin and scleroproteins, such as keratin, alpha-keratin and elastin.
Sequence Mass (Da): 38881
... |
P24158 | MAHRPPSPALASVLLALLLSGAARAAEIVGGHEAQPHSRPYMASLQMRGNPGSHFCGGTLIHPSFVLTAAHCLRDIPQRLVNVVLGAHNVRTQEPTQQHFSVAQVFLNNYDAENKLNDVLLIQLSSPANLSASVATVQLPQQDQPVPHGTQCLAMGWGRVGAHDPPAQVLQELNVTVVTFFCRPHNICTFVPRRKAGICFGDSGGPLICDGIIQGIDSFVIWGCATRLFPDFFTRVALYVDWIRSTLRRVEAKGRP | Function: Serine protease that degrades elastin, fibronectin, laminin, vitronectin, and collagen types I, III, and IV (in vitro) . By cleaving and activating receptor F2RL1/PAR-2, enhances endothelial cell barrier function and thus vascular integrity during neutrophil transendothelial migration . May play a role in neu... |
A9YWT8 | MQIQNNNYKGLIPPYILQNIYKNTSESEKDNVLMTLNHTQSLMLDSVIKTSDSIDNTDDEVVSDTLHRSIYDAKNETKLPGTLVRDEGDPDNGDVAVDNAYKYLEATYNFYKEVFNRNSLDDKGMKLIATVHYGKEYMNAYWGRGQMVFGDGDGKVFNNFTTSIDVIGHELSHGVIEKTADLIYFFQSGALNESIADVFGSLVRQHYLKQKADEASWVVGEELLAKGIKGVGIRSMKEPGKAYDDPLLGKNPQPGHMDDFKDYPIYRDNGGVHVNSGIPNKAFYNLAIKLGGYAWEKAGKIWYNTLLDKDLARDTTFLSF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Metalloprotease involved in the inhibition of insect antibacterial peptides. Reduces the antibacterial activity of G.mellonella hemolymph by 50%. Reduces the antibacterial activity of cecropin A by 80% and completely inhibits cecropin B.
Sequence Mass (Da): 41773
Sequen... |
Q7NFT6 | MSTTPQEREKPVRVLVDNDPVPTSTEKWGKPGWFERNLARGPKTTTWIWDLHALAHDFETHTSDKEEISRKIFSAHFGHLAVVCVWLSGMFWHGAYFSNFTAWMENPLGLKPSAQTVWPVFGQEILNDPSTVAKGFEQGGIVITSGLFHLWRAVGFTTTGQLAAMSIAMLIIAALFLFAGWFHYHKRAPKLEWFQNVESMLNHHLAGLFGLGSLFWTGHLIHVALPVKAQLDAGIAPAQVNPFAGLDYGLMGQYFPKGFGPNGGLGAFFTLNWGQFTDFLTFKGGLEPATGALYLTDIAHHHLAIATLFIIAGHMYRTNW... | Cofactor: PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX... |
Q9XQV3 | MKLFFRYVNSRVWSQAGSSHFNKALAKGPKTTTWIWSLHADAHDFQQSSSESTAASVGAKVFSSGLAHFSIVFFWLGGMHFHGAYFSNYSAWLKDPKTPGSQLVWSLVGQDILNQDLGGYFQSIRVTSGFFQLWRAEGIVTQVHLKYAAAAALIGSIATLWAAYFHMHISWSSSLRTMGSLSSYNAGQLAILAGLGSISWAGHQIHIALPINRLLDSGVDPSQLPSPQDLLFKDLMQVIFPGFGVGPAVDFSIYLNQKGAASEVGLNPSTGSIYLGQIASHHFFVGITCIISGIIALLVKRSKAGSFQDAAAFNNSWHSR... | Cofactor: P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
Function: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocy... |
Q9MUK1 | XIMVEKDPVKTSFEKWAQPGHFSKALAKGPSTTTWIWNLHADAHDFDSHTNDLEDISRKIFSAHFGQLGIIFIWLSGMYFHGARFSNYEAWLNDPTHVKPSAQVVWPIVGQEILNGDVGGGFQGIQITSGFFQLWRASGITSELQLYCTAIGGLIFAGLMFFAGWFHYHKAAPKLAWFQNVESMLNHHLAGLLGLGSLAWAGHQIHVSLPINQLLDAGVDPKEIPLPHEFILNRELMAQTFPSFAKGLIPFFTLDWSEYSDFLTFRGGLNPVTGGLWLTDTAHHHLAIAVLFLVAGHMYRTXXXXXXXXXXXXXXXXXXX... | Cofactor: P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
Function: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocy... |
Q0P3K2 | MATKFPKFSQGLASDPTTRRIWFGIATAHDFETHDGMTEEKLYQKIFASHFGQLAIIFLWTSGNLFHVAWQGNFEKWGEDPLHVRPIAHTIWDPHFGQPAVEAFTRGGASAPVNIAYSGVYQWWYTIGMRTNVDLYNGSLFLLFVAGLFLFAGWLHLQPTFAPAVSWFKNAESRLNHHLSGLFGVSSLAWTGHLVHVAIPASRGETVRWDNFLTTLPHPAGLAPFFTGQWAVYAQNPDTAGHIFGTSEGAGTAILTFLGGFHPQTQSLWLTDMAHHHLAIAVVFIIAGHQYRTNFGIGHSMKEILEAHTAPSGRLGAGHT... | Cofactor: P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
Function: PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocy... |
P12185 | MTASYLPSIFVPLVGLIFPAITMASLFIYIEQDEIL | Function: May help in the organization of the PsaL subunit.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4018
Sequence Length: 36
Subcellular Location: Plastid
|
Q0P3K0 | MAASLLPSIFVPLVGLVFPAVAMASLFLYIEKEQVS | Function: May help in the organization of the PsaL subunit.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3853
Sequence Length: 36
Subcellular Location: Plastid
|
P17230 | MRDFKTYLSVAPVLSTLWFGSLAGLLIEINRFFPDALTFPFFSF | Function: May help in the organization of the PsaE and PsaF subunits.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5077
Sequence Length: 44
Subcellular Location: Plastid
|
Q31NU0 | MDGLKRYLSSAPILATIWFAITAGILIEFNRFFPDLLFHPL | Function: May help in the organization of the PsaE and PsaF subunits.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4710
Sequence Length: 41
Subcellular Location: Cellular thylakoid membrane
|
A0T0V1 | MNDFQKYLSTAPVLLTLWMTFTAGFIIEVNRFFPDMLGLYF | Function: May help in the organization of the PsaE and PsaF subunits.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4853
Sequence Length: 41
Subcellular Location: Plastid
|
A9WSI0 | MTQQFYVSPEQVMKDRADFARKGIARGRSVVVVSSLEGIALVAENPSPSLHKIGEIYDKIAFAAVGKYNEFESLRQAGVRYADVRGYSYDRDDVTARGLASVYAQSLGAVFTAEQKPFEVELAVAEVGENQDQDHLYRLTFDGSIADETGFIAMGGQVDSVHQVVAAGWASGSSLADVVGLAVGALGAGREPVVELDAANLEIAVLDRDSETSRGVARAFRRLNANEVNDLLSPRGSGSPAE | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Sequence Mass (Da): 25828
Sequence Length: 242
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
Subcellular Location: Cytoplasm
|
B1W307 | MSTPFYVSPQQAMADRAEYARKGIARGRSLVVLQYADGIVFVGENPSRALHKFSEIYDRIGFAAAGKYNEYENLRIGGVRYADLRGYTYDRDDVTARGLANVYAQTLGTIFSSAAEKPYEVELVVAEVGSEPEGDQIYRLPHDGSIVDEHGSVAVGGNSEQISTFLDQRHRDGMTLAEALKLAVQALSREPGGGEREIPAERLEVAVLDRTRPQQRKFKRIVGRQLARLLDTEAAGSTPTDAPSDTEDGDSTDGTDRADGTTDSTEETEK | Function: Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation.
Sequence Mass (Da): 29525
Sequence Length: 270
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
Subcellular Location: Cytoplasm
|
Q2TBP0 | MAAVSVYERPVGGFSFDNCRRNAVLEADFAKKGYKLPTARKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKKLVSEAIAAGIFNDLGSGSNIDLCVISKSKLDFLRPYSVPNKKGTRFGRYRCEKGTNAVLTEKVTTLEIEVLEETVQTMDTS | Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus p... |
Q54QR2 | MENLNRGGFDFDLCNRNNVLEKTGLRMKGFMKTGTTIVGVVYKGGVVLGADTRATEGPIVADKNCEKIHYIADNIYCCGAGTAADTESATALISSKLKLHKLSTGKQTRVITALTMLKQMLFKYQGHISAALILGGIDINGPSLHTIYPHGSTDQLPYVTMGSGSLAAMAVFEAKYKNDMTKEEAIALVAEAISSGIFNDLGSGSNVDVTVIEPSGVTVLRNYQTPNERKFRNNPYIFKQGTTPVLKQDIAPLSTKVVIEDIMMGQ | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Catalytic Activity: Cleavage ... |
Q99436 | MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS | Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus p... |
P70195 | MAAVSVFQPPVGGFSFDNCRRNAVLEADFAKKGFKLPKARKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLTTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKKLVSEAIAAGIFNDLGSGSNIDLCVISKSKLDFLRPFSVPNKKGTRLGRYRCEKGTTAVLTEKVTPLEIEVLEETVQTMDTS | Function: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus p... |
Q3T112 | MALLDVCGAPGGQRGDWAVPLAGSRQRSDPGHYGFSLRSPELALPRGMQPTEFFRSLGGNGESKVQIEMAHGTTTLAFKFQHGVIVAVDSRASAGNYIATLKVNKVIEINPYLLGTMSGCAADCLYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNSHAYGVMDSGYRPDLSIEEAYDLGRRAIVHATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLMHQYREASQ | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processin... |
P28062 | MALLDVCGAPRGQRPESALPVAGSGRRSDPGHYSFSMRSPELALPRGMQPTEFFQSLGGDGERNVQIEMAHGTTTLAFKFQHGVIAAVDSRASAGSYISALRVNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMCQYRGMGLSMGSMICGWDKKGPGLYYVDEHGTRLSGNMFSTGSGNTYAYGVMDSGYRPNLSPEEAYDLGRRAIAYATHRDSYSGGVVNMYHMKEDGWVKVESTDVSDLLHQYREANQ | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processin... |
P28063 | MALLDLCGAARGQRPEWAALDAGSGGRSDPGHYSFSAQAPELALPRGMQPTAFLRSFGGDQERNVQIEMAHGTTTLAFKFQHGVIVAVDSRATAGSYISSLRMNKVIEINPYLLGTMSGCAADCQYWERLLAKECRLYYLRNGERISVSAASKLLSNMMLQYRGMGLSMGSMICGWDKKGPGLYYVDDNGTRLSGQMFSTGSGNTYAYGVMDSGYRQDLSPEEAYDLGRRAIAYATHRDNYSGGVVNMYHMKEDGWVKVESSDVSDLLYKYGEAAL | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processin... |
Q29576 | RLYYLRNGARISVSAASKLXSNMMYQYRGMGLSMGSMICGWDKKGPGLYYVDENGTRLSGNMFSTGSGNTYAYGVMDSGHRYDLSIEEAYDLGRRAIVHATHRD | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processin... |
P28065 | MLRAGAPTGDLPRAGEVHTGTTIMAVEFDGGVVMGSDSRVSAGEAVVNRVFDKLSPLHERIYCALSGSAADAQAVADMAAYQLELHGIELEEPPLVLAAANVVRNISYKYREDLSAHLMVAGWDQREGGQVYGTLGGMLTRQPFAIGGSGSTFIYGYVDAAYKPGMSPEECRRFTTDAIALAMSRDGSSGGVIYLVTITAAGVDHRVILGNELPKFYDE | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processin... |
P28076 | MLRAGAPTAGSFRTEEVHTGTTIMAVEFDGGVVVGSDSRVSAGTAVVNRVFDKLSPLHQRIFCALSGSAADAQAIADMAAYQLELHGLELEEPPLVLAAANVVKNISYKYREDLLAHLIVAGWDQREGGQVYGTMGGMLIRQPFTIGGSGSSYIYGYVDAAYKPGMTPEECRRFTTNAITLAMNRDGSSGGVIYLVTITAAGVDHRVILGDELPKFYDE | Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit is involved in antigen processin... |
A8W3E7 | MGLPWYRVHTVVLNDPGRLLSVHIMHTALVAGWAGSMALYELAVFDPSDPVLDPMWRQGMFVIPFMTRLGITNSWGGWGIAGGTVTNPGLWSYEGVAGAHIAFSGLCFLAAIWHWVYWDLEVFYDERTGKPSLDLPKIFGIHLFLSGVACFGFGAFHVTGLYGPGIWVSDPYGLTGKVQPLKPAWGAEGFDPFVPGGIASHHIAAGTLGILAGLFHLSVRPPQRLYKGLRMGNIETVLSSSIAAVFFAAFVVAGTMWYGSATTPIELFGPTRYQWDQGYFQQEIYRRVSAGLAENQSLSETWSKIPEKLAFYDYIGNNPA... | Cofactor: Binds multiple chlorophylls. PSII binds additional chlorophylls, carotenoids and specific lipids.
Function: One of the components of the core complex of photosystem II (PSII). It binds chlorophyll and helps catalyze the primary light-induced photochemical processes of PSII. PSII is a light-driven water:plasto... |
P48187 | MKILYSLRRFYHVETLFNGTFVLAGRDQETTGFPWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGSGGEVLDTFPYFVSGVLHLISSAVLGFGGIYHALLGPETLEESFPFFGYVWQDRNKMTTLLGIHLILLGLGAFLLVLKALYFGGVYDTWAPGGGDVRKITNLTLSPGVIFGYLLKSPFGGEGWIVSVDDLEDIIGGHVWLGSICVLGGIWHILTKPFAWARRAFVWSGEAYLSYSLGALSVFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVR... | Cofactor: Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids.
Function: One of the components of the core ... |
P06414 | MKILYSQRRFYPVETLFNGTLALGGRDQETTGFAWWAGNARLINLSGKLLGAHVAHAGLIVFWAGAMNLFEVAHFVPEKPMYEQGLILLPHLATLGWGVGPGGEIVDTFPYFVSGVLHLISSAVLGFGGIYHALIGPETLEESFPFFGYVWKDKNKMTTILGIHLILLGAGAFLLVFKALYFGGIYDTWAPGGGDVRKITNLTLSPGVIFGYLLKSPFGGEGWIVSVDNLEDIIGGHVWLGSICIFGGIWHILTKPFAWARRALVWSGEAYLSYSLGAIAVFGFIACCFVWFNNTAYPSEFYGPTGPEASQAQAFTFLVR... | Cofactor: Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids.
Function: One of the components of the core ... |
Q8CM25 | MTIAIGRAPAERGWFDILDDWLKRDRFVFVGWSGILLFPCAYLALGGWLTGTTFVTSWYTHGLASSYLEGCNFLTVAVSTPANSMGHSLLLLWGPEAQGDFTRWCQLGGLWTFIALHGAFGLIGFMLRQFEIARLVGVRPYNAIAFSAPIAVFVSVFLIYPLGQSSWFFAPSFGVAAIFRFLLFFQGFHNWTLNPFHMMGVAGVLGGALLCAIHGATVENTLFQDGEGASTFRAFNPTQAEETYSMVTANRFWSQIFGIAFSNKRWLHFFMLFVPVTGLWMSAIGVVGLALNLRSYDFISQEIRAAEDPEFETFYTKNLL... | Cofactor: The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. There is also a Cl(-1) ion associated with D1 and D2, which is r... |
Q85C42 | MSGNTGERPFADIITSIRYWVIHSITIPSLFIAGWLFVSTGLAYDVFGSPRPNEYFTENRQEVPLITGRFNSLEQVDEFTRSF | Cofactor: With its partner (PsbF) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids.
Function: This b-type cytochrome is tightly associated with the reaction center of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electr... |
Q2MI72 | MATQTVENSSRSGPRRTAVGDLLKPLNSEYGKVAPGWGTTPLMGVAMALFAVFLSIILEIYNSSVLLDGISMN | Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consi... |
Q2PMQ6 | MATQTVEDNSRSGPRRTVVGDLLKPLNSEYGKVAPGWGTTPLMGVAMALFAIFLSIILEIYNSSILLDGISMN | Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consi... |
P05146 | MATQTVESSSRSRPKPTTVGALLKPLNSEYGKVAPGWGTTPLMGVAMALFAVFLSIILEIYNSSVLLDGISMN | Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consi... |
Q2JUV4 | MAIRTKLGDLLRPLNSEYGKVAPGWGTTPLMAVFMVLFGIFLLIILQIYNKSLLLEDINVSWESLSF | Function: One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consi... |
Q8DJZ6 | METLKITVYIVVTFFVLLFVFGFLSGDPARNPKRKDLE | Cofactor: PSII binds multiple chlorophylls, carotenoids and specific lipids.
Function: One of the components of the core complex of photosystem II (PSII). May be required for formation of PSII dimers but not their subsequent stability . PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to... |
Q85CD4 | MANTTGRIPLWLIGTIAGILVIGLVGIFFYGSYSGLGSSL | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures ... |
Q85X72 | MPVIFNICLDDAFIHSNNPFFGKLPEAYAIFDPIVDVMPIIPVLSFLLAFVWQAAVSFR | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures ... |
P41598 | MFNIFLDDAFIHSNNPFFGKLPEAYAISDPIVDVMPIIPVLSFLLAFVWQAAVSFR | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures ... |
Q6YXL7 | MTQPNPNKQSVELNRTSLYWGLLLIFVLAVLFSNYFFN | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures ... |
A2CBT5 | MPVNNFGFLATLLFVAVPMLFLIGLYIQTNSNKS | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures ... |
Q7VDL9 | METTNFGFIISLLFVGIPTIFLVGLYISTSDGEKSSFFSDSSKGKLGPKS | Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures ... |
Q7V340 | MQTLSSAPDPAVSVAVTILAVLLALTGFGLWTAFGPKAAKLTDPWDDHDD | Function: May play a role in photosystem I and II biogenesis.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 5225
Sequence Length: 50
Subcellular Location: Cellular thylakoid membrane
|
Q85BG5 | MEALVYTFLLVGTLGIIFFAIFFRDPPKVPSKGVPSKGKK | Function: Seems to play a role in the dimerization of PSII.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 4413
Sequence Length: 40
Subcellular Location: Plastid
|
P37256 | MEALVYTFLLVGTLGIIFFSIFFRDPPRMIK | Function: Seems to play a role in the dimerization of PSII (By similarity). Essential to maintain photosynthetic activity under adverse growth conditions.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 3636
Sequence Length: 31
Subcellular Location: Plastid
|
P32095 | MLLFTFTFQALVLALIIFSFILVLTLPVIFASPKGWENNKSRIWLACRFWFFLVFLIGILDGIFL | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 7586
Sequence Length: 65
Subcellular Location: Plastid
|
A0ZZ32 | MTIAFQLAVFALIATSSILLISVPVVFASPDGWLSNKNIVFSGTSLWIGLVFLVGILNSLIS | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6567
Sequence Length: 62
Subcellular Location: Plastid
|
Q6B8V1 | MTIIVQLLVFILVIFSTLLVVGIPVTFASPGQWEKSKNLIYTGAGIWTGLVLITGLVNSFIN | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6721
Sequence Length: 62
Subcellular Location: Plastid
|
O78503 | MVTILQLLVSILILLSFALVVGVPVILVSPGEWERSKNLVYASAGLWFGLVIVTAAFNSFVI | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6689
Sequence Length: 62
Subcellular Location: Plastid
|
Q06RD4 | MTLVFQLAVFALIATSSILLISVPVVFASPDGWSSNKNVVFSGTSLWIGLVFLVGILNSLIS | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6555
Sequence Length: 62
Subcellular Location: Plastid
|
Q332Y1 | MTLAFQLAVFALIATSSILLISVPVVFASPDGWSSNKNVVFSGTSLWIGLVFLVGILNSLIS | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6527
Sequence Length: 62
Subcellular Location: Plastid
|
Q5IHA9 | MTIAFQLAVFALIATSSILLISVPVVFASSDGWSSNKNVVFSGTSLWIGLVFLVAILNSLIS | Function: Controls the interaction of photosystem II (PSII) cores with the light-harvesting antenna.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 6531
Sequence Length: 62
Subcellular Location: Plastid
|
O00231 | MAAAAVVEFQRAQSLLSTDREASIDILHSIVKRDIQENDEEAVQVKEQSILELGSLLAKTGQAAELGGLLKYVRPFLNSISKAKAARLVRSLLDLFLDMEAATGQEVELCLECIEWAKSEKRTFLRQALEARLVSLYFDTKRYQEALHLGSQLLRELKKMDDKALLVEVQLLESKTYHALSNLPKARAALTSARTTANAIYCPPKLQATLDMQSGIIHAAEEKDWKTAYSYFYEAFEGYDSIDSPKAITSLKYMLLCKIMLNTPEDVQALVSGKLALRYAGRQTEALKCVAQASKNRSLADFEKALTDYRAELRDDPIIS... | Function: Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose ... |
Q84V22 | MKPRFPQNVYFLARYSYLRRFQHSQRRTFSSFLNNIRSNYSGARASPLGGSSGAGAGAGGGGTGDSKGNAFLVPGATMATILMLGALHARRLYEDKKIEEKREKGIELEFHPDIKASFLGVLPLRSISRAWGSFMSLEIPVWMRPYAYKAWARAFHSNLEEAALPLEEYTSLQDFFVRSLKEGCRPIDPDPCCLVSPVDGTVLRFGELKGNRGMIEQVKGHSYSVPALLGNNSLLPMEPEGKNESKEEAVGDKSDKSWLRVSLASPKLRENVSASPMKGLYYCVIYLKPGDYHRIHSPADWNATVRRHFAGRLFPVNERA... | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. Contributes only to a minor proportion of PtdEtn ... |
A0L627 | MEKSGLVAKEGYPFMAIFIGVAAVSSALSWYGIVQFVLWVLAGWCIWFFRDPERHSDAPEDAVIAPADGRVVAIREMEKGPLTDEPVRMVSIFMNVFNVHVNRAPIAGTVTKISYHPGKFVNADLDKASIENERNVLLMESPAGVKMAFQQVAGLVARRIVCRINEGTVLQRGERFGLIRFGSRVDLFFPMDAEISVKLGEMTHSGVTQMGRLKGKES | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as a... |
Q2W9R7 | MRGEAVQAQQISLTKYLWFPINREGWPFVGLFALGALLLGQIWGPLGWAGALLTCWCAWFFRDPDRVTPTRDGLVISPADGVVQMVGMVAPPPELDMGDAPRMRISVFMSVFSVHINRCPVDGTIVKCSYRPGKFLDASLDKASADNERMSVRMSRADGREIAFVQIAGLVARRIKCDLKDGQQVRAGQRFGLIRFGSRVDVYLPDGVAPLVSLGQSIIAGETVLADLDSTEGARQGEIR | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as a... |
Q65RD9 | MNSLEKKQITYGQRLKIAFQYAMPQIYLTQIAGWFANKRWGAVTHFVIKMFAKKYNVHMAEAAKPNFSDYATFNEFFIRQLKEYARPINQNTDALCLPADGKISQCGHIDDELLLQAKGHSFSLRDLLAGDEELTRLFKDGEFVTTYLSPRDYHRVHMPCNGTIRKMIYVPGELFSVNPFLNTHIPNLLARNERVICLFDTDFGPMVQILVGATITASISTVWEGVINPPRTGDIRTWTYEGQSAVSLAKGQEMGAFQLGSTVINLFPKNAVKLADYLQVDTVTRVGEILAYKK | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as a... |
A1U4D6 | MLDKLFVLSQYVTPQLAVSRLAGRLADSESTPALKNRVIKWFIGRYGVNMSEAAEPDFTAYPTFNAFFTRALKPGARTIDPAPETLTSPVDGAISQIGQISTDRVFQAKGQSFSLTELLGGDDERAEPFREGEFATIYLSPKDYHRIHMPMAGTLKEMVYVPGKLFSVNPVTAENVPNLFARNERVACLFDTEAGPMAMVLVGAMIVGSVETTWAGVVAPNSGKVTQWQYRGDDAVQFEKGQEMGRFRLGSTVVLVMPKGAVKWQPNQVAEKTVQLGEAFGKLNVK | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as a... |
B2HQP4 | MARRPRRSDSSSAEPTLSPQHLLALVRSTIPPIHPAGRPFIAAGLAVAGVGYRHRWARRTGLLAAGACAGFFRHPPRVPPSRAGAIVAPADGVICVIDTAAPPAELSMGDAPLPRVSIFLSVFDAHVQRAPVSGEVVAVQHRPGRFGSADLPAASDDNERNSVRIRTANGAEVVAVQVAGLVARRIVCDAHVGDKLAIGDTYGLIRFGSRLDTYLPPGTEPVVRVGQRTIAGETILADLP | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as a... |
Q5GSL0 | MCFSLPSINKEGYLFIVVSFIVTCIAFSISWGFGVTCLFPTLLCTYFFRDPARIIPGNKDLVLSPADGVISKIEEVSYPLSTNNGEEKKFTLVSIFLSVLNVHVNRIPISGTVKEMHYKKGKFVSAMSDRSSNENEKQVIVIEYTKGKEIIVEQIAGLIARRIVCNLRVSQSVKAGERFGIIRFGSRVNIYVPTDVEIRVSEGQTVVGGETIIANLNKENTQEKLTFDLV | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as a... |
Q8PJ17 | MSLVTSLTYVLPHRLLSSLARALAYSQTPSTKQWLIDTVTRKFGVDLSEAQEPDPHAYPTFNAFFTRALKPGARVPDADPSAVLMPADGRISQLGPVENGRIFQAKGQSFTAAELLGDEAAAAPFNDGVFATVYLSPKDYHRVHMPWTGTLRETVHVPGRLFSVGPDAVRKVPRLFARNERLVCHFDTEFGPMASVMVGALLVSGVETVWSGVEIPRYGDRITRKDYRGKGVVLEKFAEMARFNYGSTVIVLLPPGVATLDGGLAAETSVRLGQALARRQ | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
PTM: Is synthesized initially as a... |
Q7YSJ4 | MKYLFIAIILILYCSFTKADQKKFLVNMYDNDPLFSPDFENANGAQTGLVKKKLGSDGKPIPANYDMKDPNGNYYIKNATTFKSWFNEVAGVSILVPFELVLTQTAGSQNYYSYSNTSFFPLNELGWYNPSIKGDYEFKKYQDSNKKEQNFHFCMHASFIMSTNCKEVFKFKGDDDVWVFINDVLVLDIGGVHGVQDGTVDMANLPEKIHDSTNSKLGNCKNGTYPFDFFYCERHTKASNCLFETNMGFTCSYYDYCGICNGKGECCTDVKLNQCYTKKCPLPNSLPNGATNYQDYMTIVPTNTCGGTDKCKIYSCNNST... | Function: Acts as a quorum sensing protein regulating discoidin gene expression during growth and development. D.discoideum is a single-celled amoebae and switches to multicellular development when food becomes limited. As the growing cells reach a high density, they begin expressing discoidin genes. The ability of psi... |
P0DPA7 | MIAVLFSFVIAGCIYYIVSRRVRRSRLPPGPPGIPIPFIGNMFDMPEESPWLTFLQWGRDYNTDILYVDAGGTEMVILNTLETITDLLEKRGSIYSGRLESTMVNELMGWEFDLGFITYGDRWREERRMFAKEFSEKGIKQFRHAQVKAAHQLVQQLTKTPDRWAQHIRHQIAAMSLDIGYGIDLAEDDPWLEATHLANEGLAIASVPGKFWVDSFPSLKYLPAWFPGAVFKRKAKVWREAADHMVDMPYETMRKLAPQGLTRPSYASARLQAMDLNGDLEHQEHVIKNTAAEVNVGGGDTTVSAMSAFILAMVKYPEVQ... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product . The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD . 4-hydroxy-L-tryptophan is accepted as substra... |
P0DPA8 | MAFDLKTEDGLITYLTKHLSLDVDTSGVKRLSGGFVNVTWRIKLNAPYQGHTSIILKHAQPHMSTDEDFKIGVERSVYEYQAIKLMMANREVLGGVDGIVSVPEGLNYDLENNALIMQDVGKMKTLLDYVTAKPPLATDIARLVGTEIGGFVARLHNIGRERRDDPEFKFFSGNIVGRTTSDQLYQTIIPNAAKYGVDDPLLPTVVKDLVDDVMHSEETLVMADLWSGNILLQLEEGNPSKLQKIYILDWELCKYGPASLDLGYFLGDCYLISRFQDEQVGTTMRQAYLQSYARTSKHSINYAKVTAGIAAHIVMWTDFM... | Function: 4-hydroxytryptamine kinase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product . The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD . 4-hydroxy-L-tryptophan is accepted as substrate ... |
P0DPA9 | MHIRNPYRTPIDYQALSEAFPPLKPFVSVNADGTSSVDLTIPEAQRAFTAALLHRDFGLTMTIPEDRLCPTVPNRLNYVLWIEDIFNYTNKTLGLSDDRPIKGVDIGTGASAIYPMLACARFKAWSMVGTEVERKCIDTARLNVVANNLQDRLSILETSIDGPILVPIFEATEEYEYEFTMCNPPFYDGAADMQTSDAAKGFGFGVGAPHSGTVIEMSTEGGESAFVAQMVRESLKLRTRCRWYTSNLGKLKSLKEIVGLLKELEISNYAINEYVQGSTRRYAVAWSFTDIQLPEELSRPSNPELSSLF | Function: N-methyltransferase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product . The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD . 4-hydroxy-L-tryptophan is accepted as substrate by psiD... |
P61289 | MASLLKVDQEVKLKVDSFRERITSEAEDLVANFFPKKLLELDSFLKEPILNIHDLTQIHSDMNLPVPDPILLTNSHDGLDGPTYKKRRLDECEEAFQGTKVFVMPNGMLKSNQQLVDIIEKVKPEIRLLIEKCNTVKMWVQLLIPRIEDGNNFGVSIQEETVAELRTVESEAASYLDQISRYYITRAKLVSKIAKYPHVEDYRRTVTEIDEKEYISLRLIISELRNQYVTLHDMILKNIEKIKRPRSSNAETLY | Function: Subunit of the 11S REG-gamma (also called PA28-gamma) proteasome regulator, a doughnut-shaped homoheptamer which associates with the proteasome. 11S REG-gamma activates the trypsin-like catalytic subunit of the proteasome but inhibits the chymotrypsin-like and postglutamyl-preferring (PGPH) subunits. Facilita... |
Q9GP84 | MRFISIFLIIVALCVSSSWAFNFTDQPNSFRISGTGCGSGTTTVYFSTDGRCNSACGGSIRIKGEGNNVPNQQFTLNDYSKNVTNCSGTSNVASFRCPALVNTTSPTFTVNVGNSAYHVTCQYAQVTETPAGNSADKVAVGIAIIFGALISLLAL | PTM: The GPI-like-anchor contains a phosphoceramide group, rather than a phosphatidyl group.
Location Topology: Lipid-anchor
Sequence Mass (Da): 16273
Sequence Length: 155
Subcellular Location: Cell membrane
|
P23857 | MFKKGLLALALVFSLPVFAAEHWIDVRVPEQYQQEHVQGAINIPLKEVKERIATAVPDKNDTVKVYCNAGRQSGQAKEILSEMGYTHVENAGGLKDIAMPKVKG | Function: The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspE catalyzes the sulfur-transfer reaction from thiosulfate to cyanide, to form sulfite and thiocyanate. Also able to use dithiol (dithiothreitol) as an al... |
P32696 | MLELLFVIGFFVMLMVTGVSLLGIIAALVVATAIMFLGGMLALMIKLLPWLLLAIAVVWVIKAIKAPKVPKYQRYDRWRY | Function: Effector of the phage shock response.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 9023
Sequence Length: 80
Subcellular Location: Cell inner membrane
|
P94512 | MKAVFFDLDDTLLWDEKSVRTTFAETCLQAEKKYGLAPEEFEAAVREAARELYMSYETYPYTVMIGINPFEGLWSNFSEPISEGFQKLNKIVPEYRRNAWTNGLKALGIDDPAYGEYLGEFFAAERRKRPFVYDETFAVLDQLKGKYELLLLTNGDPSLQKEKLAGVPELAPYFNEIVISGAFGKGKPDVSIFEHCLKLMNIEKDDAIMVGDNLNTDILGASRAGIKTVWINRTDKKNETDVKPDYIISSLHDLFPILEK | Function: Catalyzes the last step of the phosphorylated serine biosynthetic pathway, i.e. dephosphorylation of O-phospho-L-serine to form L-serine. To a lesser extent, is also able to dephosphorylate phosphothreonine, phosphoethanolamine, and histidinol phosphate in vitro.
Catalytic Activity: H2O + O-phospho-L-serine =... |
Q72H00 | MKLLLLDLDDTLLQDLPVSRAVLEDLGRKAGVEGFFARVKARAEALFREAPFYPWAEAIGHSALEALWARYSTPGLEALAAWAGPFRERVFREALEEAGGAPERARELAEAFFRERRRYPLYPEAEAFLAEARRRGLALALLTNGVPDLQREKLVGAGLAHHFSLVLISGEVGIGKPDPRLFRMALCAFGVAPEEAAMVGDNPQKDVRGARLAGVRAVWVDRGLRPEDPEASPDLRVGDLREVFLAEAL | Function: Catalyzes the last step of the phosphorylated serine biosynthetic pathway, i.e. dephosphorylation of O-phospho-L-serine to form L-serine. Is also able to dephosphorylate O-phospho-D-serine with similar efficiency. Displays a poor activity on L-phosphothreonine, and cannot use L-phosphotyrosine, pyridoxal phos... |
G4YRX5 | MRLTYVLLVAVTTLLVSCDATKPSTEATAVSKRLLRFVEAADEEERRIDFSPEKLRKMLGDETYRLKKFGKWDSDGHTFDGLKHYLLLSDSSMVKLRNMYKAWLEQ | Function: Secreted effector that possesses RNA silencing suppression activity by inhibiting the biogenesis of small RNAs in the host plant to promote enhanced susceptibility of host to the pathogen during infection . Interferes with secondary siRNA production by associating with host nuclear protein PINP1 that acts as ... |
Q07800 | MGFISSILCCSSETTQSNSNSAYRQQQSSSLNKNRSVKHSNTKSRTRGVHQTNSPPSKTNSAATFSSTERSTGKSGISTNDNEKKKPSSPTAAVTATTTNNMTKVEKRISKDDLYEEKYEVDEDEEIDDEDNRRSRGIVQEKGDAVKDTSRQKKQQQQQQQQSQPQPQPQSQSQSQSQSQSQQRGPTVQVSSDHLIQDMNLSRVSSSSQASETSNDADDEDDEDEEYIDLTLLQQGQYHAPGYNTLLPPQDESTKGKKCLILDLDETLVHSSFKYLRSADFVLSVEIDDQVHNVYVIKRPGVEEFLERVGKLFEVVVFTA... | Function: Has phosphatase activity in vitro. Involved in the response to sodium and lithium ion stress (but not to potassium or sorbitol stress) by inducing transcription of the sodium pump ENA1/PMR2. Acts through a calcineurin-independent pathway and is functionally redundant with PSR2. Also involved in the general st... |
D0NRS4 | MGCRYAVLALAVAYFAGSIAANDSQIVAVKGPASIRFTPAIHVVRGRFLRAANTADERNEDRGINLKSMPGFEKIASLFTKKNTPGPLLSWFEKKKSPDYVFLKLKINKGKQQLFDHPDWNVWVQYTTSVVKSDPEEAMIAALRTHYTDDILSKLLESAKNVPKTSGLATKMQMEHWVASKTPSQMFQFLRLDKVRNGVLDDPTLSIWINYMKLYNSKPVNKKQQVTLVSMLTTHYKDRGVLDIIEAAKKVPKTAPAARQLEMEQIQFWLKNGKSPDELLTVLSLDKAGNQLLASPRFKFWSKYVDNYNRDFPDEATTVM... | Function: Secreted effector that possesses RNA silencing suppression activity by inhibiting the biogenesis of small RNAs in the host plant to promote enhanced susceptibility of host to the pathogen during infection . Interferes with secondary siRNA production by associating with host dsRNA-binding protein DRB4 (By simi... |
G5ADB3 | MRLQCVVLFAALTLVAATHAPPNVKTVLSAEQHDIPVKRLLRPGNPAGKEDEERGINFSSVPGFEKLANLLKPKPGLKKLLKWADAKKPPETVFTRLRLDKTGTQLFDNTDFPVWAAYTRSVAQTDSEASAVMLKTLVSRYSDEVLSGMIAAAKKSSKTESIATKLETEQMRTWLAAKKTPDDMFLVFKLNKAGDDILSSPLLSAWTNYMKLSNKENPKAQTTLIATMTKHYGDSGVSQILAAARKSPATQSTAKRLEAEQVQLWLKKGRTPDDTFTLLSLDRAGDDLLASPQFNTWMKYINYYNKENPDEKTTVLAKLM... | Function: Secreted effector that possesses RNA silencing suppression activity by inhibiting the biogenesis of small RNAs in the host plant to promote enhanced susceptibility of host to the pathogen during infection . Interferes with secondary siRNA production by associating with host dsRNA-binding protein DRB4 . Inhibi... |
Q07949 | MGFIANILCCSSDTSKTHRQRQPPETNHNRNRNRKHSSNKAQTQGRKQKATPNGDKMQYSTPEILLSSSDSGSNAGSKTMQENGNSGNGKLAPLSRDHSNNSYDEEKEYEDYNEGDVEMTEVNNAGEEEEEDDEAKEKQDHVVHEYNVDADRNSSINDEAPPQQGLYQVGQEDMNPQYVASSPDNDLNLIPTTEEDFSDLTHLQPDQYHAPGYDTLLPPKLQEFQQKKCLILDLDETLVHSSFKYMHSADFVLPVEIDDQVHNVYVIKRPGVDEFLNRVSQLYEVVVFTASVSRYANPLLDTLDPNGTIHHRLFREACYN... | Function: Probable phosphatase. Involved in the response to sodium and lithium ion stress (but not to potassium or sorbitol stress) by inducing transcription of the sodium pump ENA1/PMR2. Acts through a calcineurin-independent pathway and is functionally redundant with PSR1. Also involved in the general stress response... |
P31075 | METTMTRRDFLKSAGAAGAAGLVWSQTIPGTLGALEKQEIKGSAKFVPSICEMCTSSCTIEARVEGDKGVFIRGNPKDKSRGGKVCARGGSGFNQLYDPQRLVKPIMRVGERGEGKWKEVSWDEAYTFIAKKLDEIKQKHGAHTVAFTARSGWNKTWFHHLAQAYGSPNIFGHESTCPLAYNMAGRDVFGGSMNRDFAKAKYIINMGHNVFEGIVISYVRQYMEAIENGAKVVTLEPRLSVMAQKASEWHAIKPGHDLPFVLGFMHTLIFENLYDKKFVQKYCTGFEELKASIEPCTPEKMALECDIPADTIKRLAREFA... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Component of the phosphorylative electron transport system with polysulfide as the terminal acceptor.
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Sequence Mass (Da): 84751
Sequence Length: 763
|
P08456 | MVESDEDFAPQEFPHTDTDVIVNEHRDENDGYASDEVGGTLSRRASSIFSINTTPLAPPNATDIQKFTSDEHHFSMMRNLHMADYITMLNGFSGFYSIVSCLRFTLTGKPHYVQRAHFFILLGMCFDFLDGRVARLRNRSSLMGQELDSLADLVSFGVAPAAIAFAIGFQTTFDVMILSFFVLCGLARLARFNVTVAQLPKDSSTGKSKYFEGLPMPTTLALVLGMAYCVRKGLIFDNIPFGIFREDQILEFHPIILVFFIHGCGMISKSLKIPKP | Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30805
Sequence Length: 276
Pathway: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-d... |
Q12355 | MQLHSLIASTALLITSALAATSSSSSIPSSCTISSHATATAQSDLDKYSRCDTLVGNLTIGGGLKTGALANVKEINGSLTIFNATNLTSFAADSLESITDSLNLQSLTILTSASFGSLQSVDSIKLITLPAISSFTSNIKSANNIYISDTSLQSVDGFSALKKVNVFNVNNNKKLTSIKSPVETVSDSLQFSFNGNQTKITFDDLVWANNISLTDVHSVSFANLQKINSSLGFINNSISSLNFTKLNTIGQTFSIVSNDYLKNLSFSNLSTIGGALVVANNTGLQKIGGLDNLTTIGGTLEVVGNFTSLNLDSLKSVKGG... | Function: Has a partially redundant function to ECM33 in cell wall integrity. May be involved in a repair mechanism activated in response to cell wall damage.
PTM: Extensively N- and O-mannosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 45777
Sequence Length: 444
Subcellular Location: Cell membrane
|
Q39195 | MASMTMTATFFPAVAKVPSATGGRRLSVVRASTSDNTPSLEVKEQSSTTMRRDLMFTAAAAAVCSLAKVAMAEEEEPKRGTEAAKKKYAQVCVTMPTAKICRY | Function: May be a component of the oxygen-evolving complex.
PTM: The maturation of the PSII-T precursor to its final form occurs through a two step process. First, a stromal intermediate is formed, which, upon translocation into the thylakoid membrane, is processed to the mature protein (By similarity).
Sequence Mass ... |
B3EWI4 | MASITMMSSFLGGSTVAPAKVPSANRRGVVMVKAMHEGENNVVISKNEESKNSGRRELFFAMAAAAACSVAKTAMADEEPKRGTPEAKKKYSSVCVTNPTARICRY | Function: May be a component of the oxygen-evolving complex.
PTM: Disulfide bond.
Sequence Mass (Da): 11317
Sequence Length: 106
Subcellular Location: Plastid
|
P9WG11 | MSPSMSIEALDQPVKPVVFRPLTLRRRIKNSVATTFFFTSFVVALIPLVWLLWVVIARGWFAVTRSGWWTHSLRGVLPEQFAGGVYHALYGTLVQAGVAAVLAVPLGLMTAVYLVEYGTGRMSRVTTFTVDVLAGVPSIVAALFVFSLWIATLGFQQSAFAVALALVLLMLPVVVRAGEEMLRLVPDELREASYALGVPKWKTIVRIVAPIAMPGIVSGILLSIARVVGETAPVLVLVGYSHSINLDVFHGNMASLPLLIYTELTNPEHAGFLRVWGAALTLIIVVATINLAAAMIRFVATRRRRLPL | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33498
Sequence Length: 308
Subcellular Location: Cell membrane
|
P0A627 | MGESAESGSRQLPAMSPPRRSVAYRRKIVDALWWAACVCCLAVVITPTLWMLIGVVSRAVPVFHWSVLVQDSQGNGGGLRNAIIGTAVLAIGVILVGGTVSVLTGIYLSEFATGKTRSILRGAYEVLSGIPSIVLGYVGYLALVVYFDWGFSLAAGVLVLSVMSIPYIAKATESALAQVPTSYREAAEALGLPAGWALRKIVLKTAMPGIVTGMLVALALAIGETAPLLYTAGWSNSPPTGQLTDSPVGYLTYPIWTFYNQPSKSAQDLSYDAALLLIVFLLLLIFIGRLINWLSRRRWDV | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32236
Sequence Length: 301
Subcellular Location: Cell membrane
|
P07654 | MAMVEMQTTAALAESRRKMQARRRLKNRIALTLSMATMAFGLFWLIWILMSTITRGIDGMSLALFTEMTPPPNTEGGGLANALAGSGLLILWATVFGTPLGIMAGIYLAEYGRKSWLAEVIRFINDILLSAPSIVVGLFVYTIVVAQMEHFSGWAGVIALALLQVPIVIRTTENMLKLVPYSLREAAYALGTPKWKMISAITLKASVSGIMTGILLAIARIAGETAPLLFTALSNQFWSTDMMQPIANLPVTIFKFAMSPFAEWQQLAWAGVLIITLCVLLLNILARVVFAKNKHG | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32322
Sequence Length: 296
Subcellular Location: Cell inner membrane
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.