ID A0A150GSV0_GONPE Unreviewed; 1187 AA.
AC A0A150GSV0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=GPECTOR_8g236 {ECO:0000313|EMBL:KXZ52854.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ52854.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
CC -!- SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can
CC form a complex with RFC1. {ECO:0000256|ARBA:ARBA00011480}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR036578}.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000256|ARBA:ARBA00006116, ECO:0000256|PIRNR:PIRNR036578}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXZ52854.1}.
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DR EMBL; LSYV01000009; KXZ52854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150GSV0; -.
DR STRING; 33097.A0A150GSV0; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
DR GO; GO:0005663; C:DNA replication factor C complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003689; F:DNA clamp loader activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00009; AAA; 1.
DR CDD; cd17752; BRCT_RFC1; 1.
DR CDD; cd18140; HLD_clamp_RFC; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 InterPro; IPR012178; RFC1.
DR InterPro; IPR047854; RFC_lid.
DR PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1.
DR PANTHER; PTHR23389:SF6; REPLICATION FACTOR C SUBUNIT 1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08519; RFC1; 1.
DR PIRSF; PIRSF036578; RFC1; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00292; BRCT; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
DR PROSITE; PS50172; BRCT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR036578};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|PIRNR:PIRNR036578};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR036578}; Nucleus {ECO:0000256|PIRNR:PIRNR036578};
KW Reference proteome {ECO:0000313|Proteomes:UP000075714}.
FT DOMAIN 371..452
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..217
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..473
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1187 AA; 120965 MW; B6D5D656D624FE73 CRC64;
MGKTEPSPAK PPPAKDIRSF FKKQDTKPGT SSKAPAEAAK VEKPVTVAAP PAAAAAPPAA
ASPAAPKPAV PQPKAAATKP AEPKPASRKR AAVIDDDDDD DDVIVLDGAG AKGAAAGQVA
AGAGVGKVSK KSPGKAAPGC SGSGGKGAAA GARRGGGGGK APAAKKRRVI QDDDDDDDQD
VVLQESSEDD DDEYMEDVES ESDDDGGEVE DEEDGDDFVK GAAGKRQPKK AKAPAAAAKP
ASQKTPAKAA ASPKAPAAKA PAATGSGGKK AAKAGAGPAP AADGAAAGEG SGGKGSRKSA
AGTAAAKKKS GPASFAMDPN AAAAIAAVNE AAAKLPAEEQ LEFSLMAEGA DAAGNDAAQP
PNYGNKDVPR GHPDCLTGRT FVMSGVLDSL MRSDADALIR RHGGKVTQSV SGRTAFLLVG
HNCGRSKYRG AKQHGTKIID EDGLFALIRA SEPFAPKDQP PPAAAPASQP PAGSQPSQPS
SQAASRAGPA AISATGFFGS GAGAGTGAGP SGSRAAPPPA SLGGAAGGSG GQLNQLWVDK
YKPKNSVELV GNNTLVANLK QWLESWEGVH LRGAAPPTAK GGGSKPKDLT KKAALLSGPP
GIGKTSAAHI MAREAGFEVV EMNASDTRNK SGKVSDGIAG KQSNVIKEMV SNTTLPLGMM
GTMGAGGKAA AAAAGPRRQL LIMDEVDGMS GGDRGGIQDL IDTIKRSKIP IICICNDKYN
QKLKSLRNHC LELEFRKPTV QQISKRMSEI CQREGLQVNQ ATMDALVTGA GGDLRLILGQ
LQMVRLRSRA LSFDEVRGKL GTSKDADMSP FECGRKLLEP ACALLSMGDR MELVFADMDL
VPLLVQENYL NHRPTIAPDP AGRLRAIAKA ADSISSGDVV NNTLRRSQNW GLMPFAAVMS
CLLPAAYMRG SREIFGLFPT EQNFPRFTAW LGNNSSCGKQ RRLLGELATT MAASGRVSSG
RSAVRLEYAS ALRHLLVEPL AAREEEAVPE VVELMHEYCI DREQLDYIVD VTSFKSQAAW
AKDRFKEVPA KVKSAFTRNL NSTTPAARCT AQVEEVKLGR GAAKGKAKGR KAAATAEEED
EEGGEAEEGE EAKPVVKTEP GEGGEGGAAD DEDDVDPGTL ARRLAKSGVE IKLQDDGKAA
AKGKKGGGGG GRGGGAAAAG GAKGARGGGG GGGRGGGRGG GKGGAKK
//
