lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Specifically dephosphorylates nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Displays high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP.
Sequence:
MRDAALRYPNILFDLDGTLTDPREGITRSVQFALARLGIDEPDLARLEHFIGPPLLQCFMQTYGFDEARAWEAVNHYRERFRVTGLYENRVFDGIPELLEALVGRGHTLYVATSKPGVFAREIARHFAFDRHFKAIYGSELDGTRTHKEELIRHLLDSEGLAAEHCLMIGDRMHDLLGASRNGVACIGVGYGFGSEDELRAHQPTHYCADLAALRQVLESH
The following text describes a protein:
Function:
Transfers mannose from Dol-P-mannose to Ser or Thr residues on proteins; Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. Coexpression of both POMT1 and POMT2 is necessary for enzyme activity, expression of either POMT1 or POMT2 alone is insufficient. Essentially dedicated to O-mannosylation of alpha-DAG1 and few other proteins but not of cadherins and protocaherins.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MWGFLKRPVVVTADINLSLVALTGMGLLSRLWRLTYPRAVVFDEVYYGQYISFYMKQIFFLDDSGPPFGHMVLALGGYLGGFDGNFLWNRIGAEYSSNVPVWSLRLLPALAGALSVPMAYQIVLELHFSHCAAMGAALLMLIENALITQSRLMLLESVLIFFNLLAVLSYLKFFNCQKHSPFSLSWWFWLTLTGVACSCAVGIKYMGVFTYVLVLGVAAVHAWHLIGDQTLSNVGADVQCCMRPACMGQMRMSQGVCVFCHLLARAVALLVIPVVLYLLFFYVHLILVFRSGPHDQIMSSAFQASLEGGLARITQGQPLEVAFGSQVTLRNVFGKPVPCWLHSHQDTYPMIYENGRGSSHQQQVTCYPFKDVNNWWIVKDPRRHQLVVSSPPRPVRHGDMVQLVHGMTTRSLNTHDVAAPLSPHSQEVSCYIDYNISMPAQNLWRLEIVNRGSDTDVWKSILSEVRFVHVNTSAVLKLSGAHLPDWGYRQLEIVGEKLSRGYHGSTVWNVEEHRYGASQEQRERERELHSPAQVDVTRNLSFMARFSELQWRMLALRSDDSEHKYSSSPLEWVTLDTNIAYWLHPRTSAQIHLLGNIVIWVSGSLALAIYALLSLWYLLRRRRNVHDLPQDAWLRWVLAGALCAGGWAVNYLPFFLMEKTLFLYHYLPALTFQILLLPVVLQHISDHLCRSQLQRSVFSALVVAWYSSACHVSNTLRPLTYGDKSLSPHELKALRWKDSWDILIRKH
The following text describes a protein:
Function:
Involved in the degradation of triuret (carbonyldiurea), an impurity in agricultural urea fertilizer, and an intermediate of uric acid oxidation endogenously found in human urine and in prokaryotic metabolism. Catalyzes the hydrolysis of triuret to 1-carboxybiuret and ammonia. The product, carboxybiuret, channels into biuret metabolism and is spontaneously decarboxylated to biuret. Extremely specific for triuret with four, three and two orders of magnitude less activity with biuret, 1-nitrobiuret and formylurea, respectively. No activity with tetrauret, pentauret or nonplanar compounds methylene diurea or succinamide.
Sequence:
MIRIDATPYPYQFHPRSTALVVIDMQRDFIEEGGFGSALGNDVRPLAAIVPTVAALLQLAREAGMLVVHTRESHLPDLSDCPRSKRLRGNPTLGIGDVGPMGRILVQGEPGNQILPQLAPVEGELVIDKPGKGAFYATDLHAQLQERRITHLLVAGVTTEVCVQTSMREANDRGYECLVIEDACASYFPDFHRITLEMLTAQGGIVGWRTPLAQLQAGVAAYTGENP
The following text describes a protein:
Function:
Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis. Required for global lipid homeostasis in liver and cholesterol homeostasis in fibroblasts. Involved in the regulation of pro-inflammatory response and neutrophil trafficking. Modulates neuronal autophagy via phosphoethanolamine production which regulates accumulation of aggregate-prone proteins such as APP. Seems to play a role in establishing neuronal contact sites and axonal maintenance.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type III membrane protein; Cytoplasmic side.
Sequence:
MDALVTYKEIFLQYLNKIRNVVNEKSAGTEPWQLIASTVVATLLLVWLYTFLFQPESLTSRFKKWFFRFIRKLPFIGTEIQKQMNKTMDDMASGLSFLQDKKRYIKTLPAKGLSQPEVLKMMKEYNAMGDVHWEDGKVSGTVYSGEEKLTNLLVKVYQEFAWSNPLHPDIFPGLRKMEAEVVRMACTLFHGGPNSCGTMTSGGTESILMACKAYRNLAYEKGIKYPEMLVPQSVHAAFDKAAHYFGMKIVHIPLTKSMQVDVKAMKRAISKNTAMLVCSAPQFPHGVMDPIEEVAKLAVKYDIPFHVDACLGGFLIVFMEKAGFPLKHPFDFQVEGVTSISADTHKYGYAPKGSSVILYRDTKYRHHQFFIAPDWQGGIYASPTIAGSRPGGLIAACWATLIHIGEDGYVEATWKIISTARYLESELRKIDNIFILGNPEVCVLALGSDTFDIYQLSNMLLTKGWNLNTLQFPPSIHICLTLLHTKPGVAEQLLNDIRECVKEIMKDPKAKTTGMGAIYGMAQTIPDRSMISEIAGGYLDCLYCTDVPSSANAQMNGSPSHH
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MTIKKDKKKMTDRIVNHALEIIFLLTGEEYIIMKKNAPQSIHLLTGEVHIKSGDAAVYFSTEEWEYIESHKESYKDVMMETIGSSGIPNNKTFGKIVTKVAFEKEQKEESYAIRRLDTKVQKISGYASPGEINEVVSDIENKGEQYADSSLEDTMQIICVNADSGESSSVDILEESQPATCISDEEVENEIGKINPEVATDMEEKVKQCAVRCLDDEDDEDEEVCMSSGSGGSWNRRMSEEYQTNVCIAHELVKYESSVFHGLQSDNSKGNLTLWKQGEAIFASQPYQCKENALALNEKFDYISDDALQEAIKHNNKEKKVCAKLSSGKSGCEYYTLAEDTPFNYSDSNNPYVTTQQMAHTDDRLYECTEGEKHFPYDSIFNRHQIIHKKEEPCTSADFDKSFSPHKVTHYMDSSGEKPFSCNDCGQCFTRRSSLLRHGKFHSGDNPYTCLVCGKCFSNKSHLVAHRRIHEGEKPYSCPECGKCFANRSYLSVHKRTHTGEKPYSCPECGKRFTAMQSVVRHRRSHTGEKPYACGECGKRFTRRSCLNRHNRSHMRVKPFPCSECGQCFTNKGLLDAHKITHTGVKLYSCTECGKCFTQMAALIGHHRSHIEENP
The following text describes a protein:
Function:
Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase (By similarity); May play a role in tissue reorganization.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Domain:
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Sequence:
MQLTLFCFVCLLPGHLALPLSQEAGDVSAHQWEQAQNYLRKFYPHDSKTKKVNSLVDNLKEMQKFFGLPMTGKLSPYIMEIMQKPRCGVPDVAEYSLMPNSPKWHSRIVTYRIVSYTSDLPRIVVDQIVKKALRMWSMQIPLNFKRVSWGTADIIIGFARRDHGDSFPFDGPGNTLGHAFAPGPGLGGDAHFDKDEYWTDGEDAGVNFLFAATHEFGHSLGLSHSSVPGTVMYPTYQRDYSEDFSLTKDDIAGIQKLYGKRNTL
The following text describes a protein:
Function:
May play a role in vesicle trafficking.
Sequence:
MAIADEKDGKVWGLFKLPFRNAQSTSTTTTSRSSSHNTTTHHYRTQQNQSLGSTSLDDGSIPRTNSSSSVSSVARSLLPARRRLKLDPSNKLYFPYEPGKQVRSAIKIKNSSKSHVAFKFQTTAPKSCFMRPPGAILAPGESIIATVFKFVEHPENNEKPMDQKSKVKFKIMSLKVKGPMDYVPELFDEQKDQVAVEQILRVIFLDVERPSPAFEKLKRQLAEADAALEARKKPAEDTGPKIIGEGLVIDEWKERRERYLARQQVEGVDSV
The following text describes a protein:
Function:
Involved in the final steps of cholesterol and steroid degradation. Opens the last steroid ring of cholesterol by catalyzing the hydrolysis of (3E)-2-(2-carboxylatoethyl)-3-methyl-6-oxocyclohex-1-ene-1-carboxyl-CoA (COCHEA-CoA) to 6-methyl-3,7-dioxodecanedioyl-CoA (MeDODA-CoA).
Sequence:
MSTRAEVCAVACAELFRDAGEIMISPMTNMASVGARLARLTFAPDILLTDGEAQLLADTPALGKTGAPNRIEGWMPFGRVFETLAWGRRHVVMGANQVDRYGNQNISAFGPLQRPTRQMFGVRGSPGNTINHATSYWVGNHCKRVFVEAVDVVSGIGYDKVDPDNPAFRFVNVYRVVSNLGVFDFGGPDHSMRAVSLHPGVTPGDVRDATSFEVHDLDAAEQTRLPTDDELHLIRAVIDPKSLRDREIRS
The following text describes a protein:
Function:
Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIM8-TIM13 complex is non essential and only mediates the import of few proteins, while the predominant TIM9-TIM10 70 kDa complex is crucial and mediates the import of much more proteins.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Domain:
The twin CX3C motif contains 4 conserved Cys residues that form 2 disulfide bonds in the mitochondrial intermembrane space.
Sequence:
MEPVDVDNFLQHQEQFTHAHNPTHSNMDSLGASGMSAFPNDPKTQIMRQIQQEAAMQNARLLVEKLNEHCFERCVPKPNASLSKGEETCFTSCMEKYMGAWNTVSKQYVARIQRESQNGVQNI
The following text describes a protein:
Function:
Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Sequence:
MEKTTSSLSDVCAFWNHLDEEKIISYVSPEKDVDGFHPTNVGNLAMRGREPSFIPCASKSCVELLLRNDVKIKGKNVVVVGRSKLGGLPTSLLIQRHHATVTTVHAFTGNPEQVTCGADILVSDIGVPNMIRGHWLKPGVIVVDMGANSVEDTGSLQGHRLVVDVCYEEAIVKASAITPVPGVVSGPTYAHLDNSNAYLLPLFSIGYGYNHNILRSKFILFQLRKSTYLSG
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).
Sequence:
MPAESISADSVPDFRSTNRPVSRVAVLGATGSIGVAALDVIENLNRCDPDFAWEVSSMSGHSQIDPLIELAGGCHTPPKCVVVSDAEMEAQAAKALRTASTQTSSRLTERCRLDVGPDALVRAATENDVDVVVAAIVGRAGLESTLAAVHAGKRVALANKETLVVAGPVVTRAAANNGAQLLPVDSEHSAIFQCLAESRARQSQYATAKQSIQPESVRATDPPSSTTDSPAKTHWPGVRRLILTASGGPFRDWTTAQMREATIEQALAHPTWKMGAKITIDSASMMNKALEVIEAKWLFDVPADKIEVVVHPQSLIHSLVEFEDGSLIAQVSPPDMRIPIQYALTYPRRLPCPAPELDRSQAWDMSLCPADPDRFPALALGFEVARVGGTAGAVVNAANETAVDLFLHGQIRFTDIPEICRRTLLDHDHESSPTLERLLKLDVWARARARELAQI
The following text describes a protein:
Function:
Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers. Probably facilitates sialidase-negative bacteria to compete successfully for limited amounts of extracellular Neu5Ac, which is likely taken up in the beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses. Forms linear aceneuramate during interconversion of Neu5Ac anomers.
Subcellular Localization:
Periplasm.
Sequence:
MNKTITALAIMMASFAANASVLPETPVPFKSGTGAIDNDTVYIGLGSAGTAWYKLDTQAKDKKWTALAAFPGGPRDQATSAFIDGNLYVFGGIGKNSEGLTQVFNDVHKYNPKTNSWVKLMSHAPMGMAGHVTFVHNGKAYVTGGVNQNIFNGYFEDLNEAGKDSTAIDKINAHYFDKKAEDYFFNKFLLSFDPSTQQWSYAGESPWYGTAGAAVVNKGDKTWLINGEAKPGLRTDAVFELDFTGNNLKWNKLAPVSSPDGVAGGFAGISNDSLIFAGGAGFKGSRENYQNGKNYAHEGLKKSYSTDIHLWHNGKWDKSGELSQGRAYGVSLPWNNSLLIIGGETAGGKAVTDSVLITVKDNKVTVQN
The following text describes a protein:
Function:
Facilitates protein transport into the nucleus. Interacts with various nucleoporins and with Ran-GDP. Could be part of a multicomponent system of cytosolic factors that assemble at the pore complex during nuclear import; Has a role in nuclear-cytoplasmic transport of proteins and mRNAs.
Subcellular Localization:
Cytoplasm. Nucleus. Nucleus envelope.
Sequence:
MAAQMDPDAVAKAFVEHYYSTFDNNRVGLGGLYQEASMLTFEGQKIQGVQSIVTKLTSLPFQQCKHNISTVDCQPSGPASGMLVFVSGNLQLAGEEHALKFSQMFHLMPTPQGSFYVFNDIFRLNYA
The following text describes a protein:
Function:
Required for vesicular transport from the ER to the Golgi complex. Functions as a SNARE involved in the docking process of ER-derived vesicles with the cis-Golgi membrane.
Subcellular Localization:
Endomembrane system; Single-pass type IV membrane protein. Endoplasmic reticulum membrane; Single-pass membrane protein. Golgi apparatus, cis-Golgi network membrane.
Sequence:
MDRGGMKHREGGPRTEMSGYSVYEEENERLTENLKMKASALKSLSIDIGNEVKYHNKMLGEMDSDFDSTGGLLGATMGRLRILSRGSQAKLLCYMMLFALFVFFVIYWFIKLR
The following text describes a protein:
Function:
Transmembrane (T) component of an energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MMDKMILGRYIPGNSWLHRIDPRAKITAVMAFIAIVFLANNWLTYALMFVYVLYLVLTSKVPFLFFIKGLQPIFWLILITLLLQVFFTKGGTVLVDLGLLQITTLGLANGAMMFCRFVLIIFMTTLLTLTTSPIELTDGLEKILAPFRLVHLPVHELALMLSISLRFIPTLMDETEKILKAQKARGVEFTSGKWSDRIKAIIPLLVPLFISAFKRAEDLAIAMEARGYRGGKGRTRFRLLRWRFADTFLLISLAVLSGLLFWLRS
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Involved in the interferon/all-trans-retinoic acid (IFN/RA) induced cell death. This apoptotic activity is inhibited by interaction with viral IRF1. Prevents the transactivation of STAT3 target genes. May play a role in CARD15-mediated innate mucosal responses and serve to regulate intestinal epithelial cell responses to microbes; Complex I functions in the transfer of electrons from NADH to the respiratory chain. Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein; Matrix side.
Sequence:
MAASKVKQDLPPSGGYGPVDYKRNLPRRGLSGYSMFAVGVGVMLFGYWSIFRWNRERRRLQIEDLEARVALLPLFQAETDRRILRMMRQNLEEEATIMKDVPGWKVGESTFHTDRWVTPTLNELYNLKPKEELIKKKYGFQWYV
The following text describes a protein:
Function:
Catalyzes the oxidation of D-2-hydroxyglutarate (D-2-HG) to alpha-ketoglutarate. Also catalyzes the oxidation of other D-2-hydroxyacids, such as D-malate (D-MAL) and D-lactate (D-LAC). Exhibits high activities towards D-2-HG and D-MAL but a very weak activity towards D-LAC.
Sequence:
MLLQNEDVINYNVDWLRRFRGNSRLVLRPKTTEHISKILKYCNERRLAVVPQGGNTGLVGGSVPLFDEIILSTQLMNEIINFDCNSGVLTCQSGCVLENLSANVSEHGYMMPLDLGSKGSCNIGGNISTNAGGIRLIRFGSLHGSTLGLEAVTADGSVIDCLTSMRKDNVGYHLKHLFIGSEGTLGIVTKVSILCPKAPSSVNLALLGCSNFDDVLKILALTKSNLGEILSAFEFLDAVSMRCSERYLSQKCPIQSAPFYVLIETSGSNDDHDQEKLGGLLEAVSSSGLIVDGTLATDLSKISTLWKLRESITLGLLEDGFCYKYDVSLPLSSFYDIVTLMEDKLKELPYLKVCGYGHVADGNLHFNVTSRIYDERISGTIEKELYKFVASAGGSISAEHGVGQFKRDHMTDVKSPEVLSLMRNIKSIMDPHCILNPYKVIP
The following text describes a protein:
Function:
Has no flavonol 3-O-glucoside (1->6) rhamnosyltransferase activity in vitro.
Miscellaneous:
MISCELLANEOUS: Flavonol glycosides (FGs) having rhamnose at the 6''-position of glucose or galactose that is bound to the 3-position of kaempferol are present in cv. Koganejiro, whereas FGs of cv. Kitakomachi are devoid of rhamnose; MISCELLANEOUS: In contrast to cv. Koganejiro, FG2 of cv. Kitakomachi has a two-base deletion that generates a truncated polypeptide devoid of enzymatic activity.
Sequence:
MPSELAMNNDELHVVMFPFLAFGHISPFVQLSNKLFSHGVHVTFLSAASNIPRIRSTLNLNPAINVISLKFPNGITNTAELPPHLAGNLIHALDLTQDQVKSLLLELKPHYVFFDFAQHWLPKLASEVGIKSVHFSVYSAISDAYITVPSRFADVEGRNITFEDLKKPPPGYPQNSNISLKAFEAMDFMFLFTRFGEKNLTGYERVLQSLGECSFIVFKTCKEIEGPYLDYIETQFRKPVLLSGPLVPEPSTDVLEEKWSKWLDGFPAKSVILCSFGSETFLSDYQIKELASGLELTGLPFILVLNFPSNLCQS
The following text describes a protein:
Function:
Acts as a receptor of SCOOP peptides from Brassicaceae plants regulating multiple processing including plant growth, development and stress responses. Perception of SCOOP peptides induces the association of MIK2 with the coreceptors BAK1/SERK3 and SERK4 and relays the signaling through the activation of receptor-like cytosolic kinases (RLCKs) BIK1 and PBL1. Also able to detect SCOOP-like proteins (SCOOPL) present in fungal Fusarium spp. and bacterial Comamonadaceae to elicit various immune responses, including growth inhibition, ROS production, calcium Ca(2+) influx, MAPK activation and MYB51 promoter activation in roots, thus being required for resistance to several root pathogens. Involved in the pollen tube perception of the female signal. Required to trigger defense responses toward generalist herbivores such as Spodoptera littoralis, probably via the activation of jasmonate and indole glucosinolate biosynthesis.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MNKTNPERKISLTSFKERMACKEKPRDLQVLLIISIVLSCSFAVSATVEEANALLKWKSTFTNQTSSSKLSSWVNPNTSSFCTSWYGVACSLGSIIRLNLTNTGIEGTFEDFPFSSLPNLTFVDLSMNRFSGTISPLWGRFSKLEYFDLSINQLVGEIPPELGDLSNLDTLHLVENKLNGSIPSEIGRLTKVTEIAIYDNLLTGPIPSSFGNLTKLVNLYLFINSLSGSIPSEIGNLPNLRELCLDRNNLTGKIPSSFGNLKNVTLLNMFENQLSGEIPPEIGNMTALDTLSLHTNKLTGPIPSTLGNIKTLAVLHLYLNQLNGSIPPELGEMESMIDLEISENKLTGPVPDSFGKLTALEWLFLRDNQLSGPIPPGIANSTELTVLQLDTNNFTGFLPDTICRGGKLENLTLDDNHFEGPVPKSLRDCKSLIRVRFKGNSFSGDISEAFGVYPTLNFIDLSNNNFHGQLSANWEQSQKLVAFILSNNSITGAIPPEIWNMTQLSQLDLSSNRITGELPESISNINRISKLQLNGNRLSGKIPSGIRLLTNLEYLDLSSNRFSSEIPPTLNNLPRLYYMNLSRNDLDQTIPEGLTKLSQLQMLDLSYNQLDGEISSQFRSLQNLERLDLSHNNLSGQIPPSFKDMLALTHVDVSHNNLQGPIPDNAAFRNAPPDAFEGNKDLCGSVNTTQGLKPCSITSSKKSHKDRNLIIYILVPIIGAIIILSVCAGIFICFRKRTKQIEEHTDSESGGETLSIFSFDGKVRYQEIIKATGEFDPKYLIGTGGHGKVYKAKLPNAIMAVKKLNETTDSSISNPSTKQEFLNEIRALTEIRHRNVVKLFGFCSHRRNTFLVYEYMERGSLRKVLENDDEAKKLDWGKRINVVKGVAHALSYMHHDRSPAIVHRDISSGNILLGEDYEAKISDFGTAKLLKPDSSNWSAVAGTYGYVAPELAYAMKVTEKCDVYSFGVLTLEVIKGEHPGDLVSTLSSSPPDATLSLKSISDHRLPEPTPEIKEEVLEILKVALLCLHSDPQARPTMLSISTAFS
The following text describes a protein:
Function:
Mediates glycerol diffusion across the cytoplasmic membrane via a pore-type mechanism.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signature motif Asn-Pro-Ala (NPA).
Sequence:
MMNELFGEFLGTLILILLGNGVVAGVVLPKTKSNSSGWIVITMGWGIAVAVAVFVSGKLSPAHLNPAVTIGVALKGGLPWASVLPYILAQFAGAMLGQILVWLQFKPHYEAEENAGNILATFSTGPAIKDTVSNLISEILGTFVLVLTIFALGLYDFQAGIGTFAVGTLIVGIGLSLGGTTGYALNPARDLGPRIMHSILPIPNKGDGDWSYAWIPVVGPVIGAALAVLVFSLF
The following text describes a protein:
Function:
Centriole-enriched microtubule-binding protein involved in centriole biogenesis. In collaboration with CEP295 and POC1B, is required for the centriole-to-centrosome conversion by ensuring the formation of bona fide centriole wall. Functions as a linker component that maintains centrosome cohesion. Associates with CROCC and regulates its stability and localization to the centrosome.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, spindle pole. Midbody.
Sequence:
MATGDVQGNVDRLRLELRSVRYNEEIDVQGLRDGNPAAFLPLLHYCFLGYSRLLARHLSGLGHELYAKSDLRFVESVFKILRDEFAYRSTLTIAQFLSRGFAERKLILLYDIVQFCKRKHNELWKESQPAKVLKVHKTPPAEEREANVRVVRETPPAPPASTSNQATSSGRDATARNGTSEPGADIGTTSKVAALAARFRSPTEPPPLPQALQKQRRRVSHPTNNPPPAVASSSRPHNPMLRPQTATPSDHRPMPQAASARPQTSFADVNRVQIDASSRPMSEILRHSGGVASGADRPPLPEDDRTRAERIAESGGPSERRVQWADRENSLVDNLDANDFSDGDADRKEMSGVEPEQLLAALQRQLDASGNLVDAGRRFGQDDVGRASFSSDEDGPLSSRRLQEFAAKNEEQVEELRSTVRSLEEKYDKMEQEAVKVKENLQARITLLEGRIRFLEAAQDKKGKGALTAASPQRAGPSTASTSYTGRFLGASPVRQTSLPKRATSQGQPAAVIPQRSIRDVTNTESVPPAQVHGPKTVETSPIKANRGTKDFIEKMRARFEATQKLLQESDGLAA
The following text describes a protein:
Function:
Probably involved in the antiviral immune response. May have a role in controlling viral load in the adult fat body, after infection with viruses such as the Drosophila C virus.
Subcellular Localization:
Secreted. Note=Expressed in hemolymph.
Sequence:
MESISSMIYLVAMMSLIIGGSQAIPYRPSAYLYNQQYCMDTLTGRQLYIGEVFTREDQCVRIQCLETLQLWEDSCQVPKLTQGNCTPVPSTNPHAEYPRCCPLYECKSYESNSGGTLEQTNIYDHYGTLRSSHLTEMIVIDGRTPPRGEIHTASARKYQV
The following text describes a protein:
Function:
TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.
Subcellular Localization:
Nucleus.
Sequence:
MANHPPQSQGQCFSVCLAEADANKKFAVLKFPPSNKVDFTLCTAGAKLERENNLKEFKSAYDIDVLPKFGAGSEYGKEQREEARKKMYGIKIKKYDPQDQPWLLKLGSGKQIKRFRGTRNGGVTKNASYYIFMPMSDSKFIAQPVEEWYDFIPQAKYKALNAEEAEEEFSRRDRTLNHFAIMMKKRIDKHENDGNIEEGAGGKKSKKKDKSFLVSEFDEMSNEDDDLDSECEVDKDENANEGKPKKRGNKMKRSNLVKKRKGTDDEAEEESDEMDEGQEVDYMSGSSSDDEGMYDDGKRDEGDTYKDASVVEEEALRKLVNSDDDEDDEENKKDDDNEDDDIMENDKTKDGKAGRESDAESSSSSSDIDEENDQLHISGKSASAVKQTESDVSTVDLTNKKRKMDPLATSLLAKKVKLDSSLSQRTTQSFSSNSDASMEETLKRYLLRKPITPRDLLQKLHSKHNKINRLSKNQLEACLADILKKLNPEVNKIDGKMYLSLKPALTVSNNTEI
The following text describes a protein:
Function:
May act as a link between DNA replication, transcription and chromatin remodeling during flower development. May participate in the repression of LHP1-targeted genes during flower development by direct interaction with LHP1. May be involved in the polar growth of plant cells via transportation of RNAs (Probable).
Miscellaneous:
MISCELLANEOUS: Plants with reduced expression of DUF7 show a slight delay in flowering.
Subcellular Localization:
Nucleus.
Sequence:
MLLTTGRKEKLSVSKGSEIEISSQEYEYGSGNVWYCVILEENLAKSKRKKLSVRHLDPLLKYDYSPPLIKTTVHRFMRPVPPPDPFPEVDFEEGDVVDAAYKGGWCSGSVVKVLGNRRFLVYLRFQPDVIELLRKDLRPHFVWKDEEWFRCEKQQLIESDFSAGKSVEVRTKVDKLGDVWAPAMVIKEDEDGTMLVKLKTLKEEEVNCTKISVSYSEIRPSPLPIGLRDYKLMENVDALVESGWCPGVVSKVLAGKRYAVDLGPNRESKEFSRLQLRPSIEWKDGIWHRKEKVSGSEESSHAVEETAASTRIRITVRTALKEKKALGTGINVRTTRSSSGAMHNPLPASFNGGDVAEAGRVSVTVNETPLFETAALSGELGNSLADVVMNESAPVTSQPEIAAPKEFHPSVVLGVAAAVKTQGKTTPKKKLQAMKNQKSSTNDSVGEKVSVNKRKRGQPRKFIVAEPKQKIGVSGNNSKAATIEHADMTDDDRPLASWVHTGNSSSGQSVSRTPDIGLNTVVEKHVDIVETPPGRESTMVLPFVKKSQLWKVLESMEVFKVVPQSPHFSPLLESEEECREGDAIGRMVMFSSLLEKVNNLQVDDPISSINRIDECFLKLEKHGFNVTTPRSRIAKILSIKERQTCALEELKAVEEKITENDNKRRKYEEDIVELQRQEVLMKEAKVTLDNEIARMQSQAAVLDQEVQNVDHEFQAILAAPWK
The following text describes a protein:
Function:
Plant-specific actin binding protein. May be part of a membrane-cytoskeletal adapter complex.
Subcellular Localization:
Cytoplasm, cytoskeleton. Nucleus membrane.
Domain:
The NAB domain, also called NAB (NET actin-binding) domain, is sufficient for F-actin binding.
Sequence:
MVMDSSKWWWIGNHNTTNFSPWLHSTLSELDEKTKEMLRVIDEDADSFAARAEMYYKKRPELIAMVEEFYRSHRSLAERYDLLRPSSVHKHGSDSESHEKSSTCDESSWSEACETHEEYAESEIDNGESKWVDESEIDGIVEEIEPSEVVYSEGNGNSEMMKIEIERLREENKVYSEMVREKDEEKREAIRQMSVAIQMLKEENSELKKRVTNTVVARRNKEGGDSQRKQQMWKPFEFKKIKLEGLWGKGFGNWALPNTDSTSKELMTL
The following text describes a protein:
Function:
Plays a role in the DNA damage response (DDR) pathway by regulating postreplication repair of UV-damaged DNA and genomic stability maintenance. The SLF1-SLF2 complex acts to link RAD18 with the SMC5-SMC6 complex at replication-coupled interstrand cross-links (ICL) and DNA double-strand breaks (DSBs) sites on chromatin during DNA repair in response to stalled replication forks. Promotes the recruitment of SLF2 and the SMC5-SMC6 complex to DNA lesions.
Subcellular Localization:
Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Relocalizes with RAD18 to nuclear foci in response to DNA damage. Colocalizes with RAD18 in the nucleus and to centrosomes (By similarity). Associates with chromatin. Accumulates with RAD18 and the SMC5-SMC6 complex at replication-coupled DNA interstrand repair and DNA double-strand breaks (DSBs) sites on chromatin in a ubiquitin-dependent manner.
Domain:
BRCT domains are necessary for its targeting to ionizing radiation-induced nuclear foci.
Sequence:
MEDGTPKHIIQMTGFKMEEKEALVKLLLKLDCTFIKSEKYKNCTHLIAERLCKSEKFLAACAAGKWILTKDYIIHSAKSGRWLDETTYEWGYKIEKDSRYSPQMQSAPKRWREELKRTGAPGAFHRWKVVLLVRTDKRSDSLIRVLEAGKANVILPKSSPSGITHVIASNARIKAEKEKDNFKAPFYPIQYLGDFLLEKEIQNDEDSQTNSVWTEHSNEETNKDFRKDAGFLEMKGALRETMYRTQKEMQNHEDVNVGSILIQHHKKEKFSGSSKDLKFVKMRNTFGSHTYENQKEIKKKDEDIQRSYTLRRKRKKGKESNCKKGVEHEKIKSTLRRHIYNRDQKEMKNSIFAEYAKESKAMAIKTDVDVVEIKNTLRKHIYRAQAVRYNCIRIDKQPVYNVEVKNAEFPRGVLNLIESLIEGHFFKEAIEELSTLQAHYIPPVCVLHALLENVLQDNIDTFSGRYFHILSALLHLHPPWKSPAMSRYYLELFQCPTCMKGAWSLVEVLIRSCLFNESFCHQISENIGSKVLHLTLLKFFFNLIESEVQHLSQKLYDWSDSQNLKITGKAMLLEIFWSGSETSGLLTKPVNMLLEWTIYSHKEKFKSNDVFKHELAYLLAGILGAAIDYWIFLGLKMGRNVMRHMSDDLGSYVSLSCDDFSSQELEIFICSFSSSWLQMFVAEAVFKKLCLQSSGSVSSEPLSLQKMVYSYLPALGKTGVLGSGKIQVSKKIGQRPCFDSQRTLLMLNGTKQKQVEGLPELLDLNLAKCSSSLKKLKKKSEGELSCSKENCPSVVKKMNFHKTNLKGETALHRACINNQVEKLILLLSLPGIDINVKDNAGWTPLHEACNYGNTVCVQEILQRCPEVDLLTQVDGVTPLHDALSNGHVEIGKLLLQHGGPVLLQQRNAKGELPLDYVVSPQIKEELFAITKIEDTVENFHAQAEKHFHYQQLEFGSFLLSRMLLNFCSIFDLSSEFILASKGLTHLNELLMACKSHKETTSVHTDWLLDLYAGNIKTLQKLPHILKELPENLKVCPGVHTEALMITLEMMCRSVMEFS
The following text describes a protein:
Function:
Is required for correct transcription of 5S RNA genes by RNA polymerase III. Also binds the transcribed 5S RNA's. Initiates transcription of the 5S ribosomal RNA gene.
Subcellular Localization:
Nucleus.
Sequence:
MCHFNELSIEIESKNLRSAKKIFHCPYEECGKKYSRPSLLEQHLRTHSNERPFVCDYTGCSKAFYRKSHLKIHKRCHTNVKPFSCHYDGCDAQFYTQQHLERHIEVHRKPKPYACTWEGCDECFSKHQQLRSHISACHTHLLPYPCTYQDCELRFATKQKLQNHVNRAHEKIISYSCPHESCVGHEGFEKWSQLQNHIREAHVPSCSICGRQFKTAAHLRHHVVLHQTTLEERKTYHCPMEGCKKSFTRSSALKKHISVIHEGNMAFHCDSCGTKFGYKHMLQRHLERGTCKKAHKPYINECGIKHDGIEGVAIHDQKEKELSSNLVSDVAKKIINEVTGHGYKEAREYSCSFPECNYRFKRLYDMHRHLNSHH