ID A0A445HMW9_GLYSO Unreviewed; 876 AA.
AC A0A445HMW9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401};
DE Flags: Fragment;
GN ORFNames=D0Y65_033843 {ECO:0000313|EMBL:RZB75127.1};
OS Glycine soja (Wild soybean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:RZB75127.1, ECO:0000313|Proteomes:UP000289340};
RN [1] {ECO:0000313|EMBL:RZB75127.1, ECO:0000313|Proteomes:UP000289340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZB75127.1};
RA Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT "A high-quality reference genome of wild soybean provides a powerful tool
RT to mine soybean genomes.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Heterotetramer of subunits RFC2, RFC3, RFC4 and RFC5 that can
CC form a complex with RFC1. {ECO:0000256|ARBA:ARBA00011480}.
CC -!- SIMILARITY: Belongs to the activator 1 large subunit family.
CC {ECO:0000256|ARBA:ARBA00006116}.
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:RZB75127.1}.
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DR EMBL; QZWG01000012; RZB75127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A445HMW9; -.
DR Proteomes; UP000289340; Chromosome 12.
DR GO; GO:0005663; C:DNA replication factor C complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
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:InterPro.
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 Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; 2.
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};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000289340}.
FT DOMAIN 299..377
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 116..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RZB75127.1"
SQ SEQUENCE 876 AA; 96251 MW; 3007EEBFE1A7D6DA CRC64;
KAGTSEILAI LPGYPDNVRV NEEGGHQHAA VIRYSPEGRL LQILEDSEGK VVKAVSEVEE
KDGKLWMGSV LMPFVARGSQ HNTLVQLVGA KFSLFSRLNL NAQMSDIRKW FMKTHDKGNN
AASSKPSNQP KPSSDKPHSE KTVAGGQESS GRRITSKYFN SNKQKGKDKK EMQELPAKRK
NMKDSEEIPE PKKIHEDDGD DSVLPTNKKK LADTTPTKKL KSGSGRGLPQ KSAVLEESDE
DDDKDAVSAA KSAGRGDGGR GAPGRSTSGR GRGGGRGGFM NFGERKDPPH KGEKEVPEGA
PDCLAGLTFV ISGTLDSLER EEAEDLIKRH GGRVTGSVSK KTNYLLCDED IGGRKSEKAK
QLGTSFLTED GLFDMIRGSK PAKAPSQEDK KPVNKAVAVA SQSKVSPKSQ VKVPLSSRSP
SKQAKPKTAT TVQSSLMWTE KYRPKDPKDI IGNQSLVLQL RNWLKAWNEH FLDTGNKKQG
KKQNDSGLKK AVLLSGTPGI GKTTSATLVC QELGFQAIEV NASDSRGKAD SKIEKGISGS
KTNSVKELVT NEAIGINMGR SKHYKSVLIM DEVDGMSAGD RGGVADLIAS IKISKIPIIC
ICNDRYSQKL KSLVNYCLLL SFRKPTKQQM AKRLMDVAKA ERLQVNEIAL EELAERVNGD
MRMALNQLQY MSLSMSIINY DDIRQRFLTN AKDEDISPFT AVDKLFGFNA GKLKMDERIN
LSMSDPDLVP LIIQENYINY RPSMAGKDDS GVKRMNLIAR AAESIADGDI VNVQIRRYRQ
WQLSQTSSVA TSIIPASLLH GQREILEQGE RNFNRFGGWL GKNSTMGKNL RLLDDLHVHI
LASRESSSGR DTIRMEYLTL LLKQMTETLR TLPKVG
//
