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RFC1_DICDI
ID   RFC1_DICDI              Reviewed;        1401 AA.
AC   Q54MH9;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Probable replication factor C subunit 1;
DE   AltName: Full=Activator 1 subunit 1;
GN   Name=rfc1; ORFNames=DDB_G0285961;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- FUNCTION: The elongation of primed DNA templates by DNA polymerase
CC       delta and epsilon requires the action of the accessory proteins
CC       proliferating cell nuclear antigen (PCNA) and activator 1. Subunit 1
CC       binds to the primer-template junction (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Heteropentamer of various rfc subunits that forms a complex
CC       (RFC) with PCNA in the presence of ATP. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000082; EAL64515.1; -; Genomic_DNA.
DR   RefSeq; XP_638011.1; XM_632919.1.
DR   AlphaFoldDB; Q54MH9; -.
DR   SMR; Q54MH9; -.
DR   STRING; 44689.DDB0232230; -.
DR   PaxDb; Q54MH9; -.
DR   PRIDE; Q54MH9; -.
DR   EnsemblProtists; EAL64515; EAL64515; DDB_G0285961.
DR   GeneID; 8625362; -.
DR   KEGG; ddi:DDB_G0285961; -.
DR   dictyBase; DDB_G0285961; rfc1.
DR   eggNOG; KOG1968; Eukaryota.
DR   HOGENOM; CLU_254323_0_0_1; -.
DR   InParanoid; Q54MH9; -.
DR   OMA; RLYYVPM; -.
DR   PhylomeDB; Q54MH9; -.
DR   Reactome; R-DDI-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-DDI-6782135; Dual incision in TC-NER.
DR   Reactome; R-DDI-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-DDI-69091; Polymerase switching.
DR   PRO; PR:Q54MH9; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0005663; C:DNA replication factor C complex; ISS:dictyBase.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0003689; F:DNA clamp loader activity; ISS:dictyBase.
DR   GO; GO:0006272; P:leading strand elongation; ISS:dictyBase.
DR   GO; GO:0006298; P:mismatch repair; ISS:dictyBase.
DR   Gene3D; 3.40.50.10190; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR013725; DNA_replication_fac_RFC1_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF00533; BRCT; 1.
DR   Pfam; PF08519; RFC1; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00292; BRCT; 1.
DR   SUPFAM; SSF48019; SSF48019; 1.
DR   SUPFAM; SSF52113; SSF52113; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50172; BRCT; 1.
PE   3: Inferred from homology;
KW   Activator; ATP-binding; DNA replication; DNA-binding; Nucleotide-binding;
KW   Nucleus; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..1401
FT                   /note="Probable replication factor C subunit 1"
FT                   /id="PRO_0000330464"
FT   DOMAIN          637..727
FT                   /note="BRCT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT   REGION          1..639
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..829
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1334..1401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..134
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..257
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        303..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..426
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        461..480
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        481..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..518
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..542
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..560
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        743..829
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1350..1366
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1367..1390
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         898..905
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1401 AA;  153582 MW;  1F4328D06524FFD9 CRC64;
     MAKKANKEQS PKKTSPTSSQ GSTATKKKTK TSEPAGTDIR NFFAVIKPST SGENVKNDLF
     SKAKEDSNKE FSLSDKENDD VKIISNKKDT TNNDKKKPSE NKSPKKKEPS KSIDLTSDED
     KSSSEEDKKK PSSSSSKKKP SSSSSSLPNK KKSTLKRLKK KRDDSSSSSS SSESDFDSGS
     DLDIESIDQK PKTITKKKNL KRKSKPDSSS SSEDETKHQK DKKIKLKTPE KKIEEPEKKV
     EIPSSTSSIS SSQKKIVYSF EDSEDSDADK PIPPSKKPSA VVVNAPSTKT FEKKKENTDI
     PPSPSKTKET TSTTTDTKPI KSPSKSNKST TPTTTTPITT EKKKIAQLEF ESPIVSITAI
     DTEKKKDGNK DNKNKEKDKD SSPFDEMEIE ESKSKTIMPN NNNNNKSKES SSSTTNSKNN
     TSMNDDLIFD DFAFSPIKSG SNKTTPSKST SSPSKETTPI KTRSKTVESK FDDDSIFDSP
     DKKTTTTTAS NTKTKTPPSK KDKFNHDIIF EESDTPLNRA IEDSIVKRSL SGLNNIDKDS
     KTTTTTTTEK KQKLKSDPFD TETEEETEDE GDEPLYKQQS SSFGSGSINP TATPTTPTKK
     PAATSTNATP TKKPNPFMYM NGRPTPPNKG SKPRPQGKEN CLRGKVFLVS GVMDCFERDE
     MHDIIKRWGG KVAKSAVKLL NYLVSGKDVG EKKLEGAKKV GAKIITEDEF LEMINKTLPK
     PVSTTETTHI SLPTPTPTPT PTPASSSSSS TTTTTTTTTT TTNSTGIKGP SLPVRSGSGG
     SSTGIKGPSL PVRSGSGGTT SSSPPLTFTS SPPTSTTTAT TTTTSSPPIS MASVIVPKSI
     STIPKGHDIL WVEKYRPKVI EDIVGNPGIF QEFGKWLDQW NSTAPRDASK KNAVLLSGPP
     GIGKTSAALL ICKQKGFEAI ELNASDARSK SEIKRLLSGV SDNQNITKFF GTTNQDTGKD
     VQANKKIKTA IILDEIDGSS GNSDRGGIAE IIGLIKKSKM PFICLCNDYY SSKVTSLRNH
     CMDLKLRKPT LNQVSSRLLA IAKHEGMKVS SYMIEKVYTS SHSDIRQSIN TLQMMSRSKR
     DYNNDNVTQS LQEKDFDISP FTAAELILRE DNSNINKKLD YFFSDFSLVP LIIQENYLKT
     RPYGGGSQSK YNDCELISMA ADALSDSDQF GRAIGKEMAW NLLPTYGVTS CIIPSGYIRG
     SPPMPLSFPS YLGKYSNASK QQRFVRELQL HMRSTSNTFV NRDETRLYYV PMLKHHLIQP
     LVQDDNDGIE NVINVMDEYG LTEDDRNNII ELSTWGKEDP LKDVKTQVKS AFTRKFRSTS
     HAIYDVSLLS SKGSGGGGTN IAEGYEEVEG ESQNQIEEED EETEEKDSLP NLVKKSSVKS
     KSDTKPKSTK SKSTTTKSKK K
 
 
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