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Database: UniProt
Entry: A0A1S3QMK4_SALSA
LinkDB: A0A1S3QMK4_SALSA
Original site: A0A1S3QMK4_SALSA 
ID   A0A1S3QMK4_SALSA        Unreviewed;      1154 AA.
AC   A0A1S3QMK4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, 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   Name=rfc1 {ECO:0000313|RefSeq:XP_014041288.1};
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014041288.1};
RN   [1] {ECO:0000313|RefSeq:XP_014041288.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_014041288.1; XM_014185813.1.
DR   AlphaFoldDB; A0A1S3QMK4; -.
DR   KEGG; sasa:106594440; -.
DR   OrthoDB; 6297at2759; -.
DR   Proteomes; UP000087266; Unplaced.
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:SF36; 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:UP000087266}.
FT   DOMAIN          410..488
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..579
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1083..1154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..59
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..89
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..118
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..260
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..371
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        514..533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..579
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1102..1117
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1118..1147
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1154 AA;  126160 MW;  F213D7E21C20F11F CRC64;
     MDIRRFFVSS KPAAQKPSQD GNLNTESPKK KSVSTDEEVK KKQTATKVVK KKKKDSDKKT
     KKRAVIESDS EEEVVEHKQK VRKQHPPLPP AKKDPVQYVS ETDSDSDNFL SLKKSAKPQD
     NGVTKPGKAR TGTKEIYRSP SKPTPAPAKG KGVIKKSPPA PVTPKSAPQH TKRTPTSVLD
     YFGSGSVQRS GKKLVASTKR KADHDESLTD EVIAQQLQMD EDMELERLVH EDEEFARTLA
     MLDQEPHAKK ARKDSGKDLG SDTSANKSIA NSSHSSTTSQ SQSNGRDHNQ DVIGPSPKKV
     PPLVKTSSKL AVMKRREVEE EGGGKTNLTI KMPVSPKKEF LTTSSTDRKS KPKTGSVTMV
     TTRTTLKTSP KKESTSPEDS EKKRGNSSAF RSFLNRDGPR ALGSKPIPTG AENCLEGCVF
     VISGVLESME REDAKSLIER YGGKVTGNVS KRTTYLVMGR DGGAAKTDKA EGFGTKILDE
     DGLLELIRCS PGKKSKYLIA AEAENKGFKS RTPDTEALSR TPKQSSKPSP SKPGSASGRG
     VRVGDSVTPP ARGTGSGVKR GLDLGGKSQS SSSSATPSLP SFAGEDFSLL WVDKYRPQNL
     KAVIGQQGDQ SQANKLLRWL KNWHTHHAVG GAKPAGRGFG KFSSTKDNGS SFKAALLSGP
     PGVGKTTTAA LVCQELGYSY VEMNASCTRS KNSLNLIAES LNNSSINNYY TGSSQTVSSK
     HVLIMDEIDG MAGNEDRGGI QEMIGLIKQS RIPIICMCND RNHQKIRSLA NYCFDLRFQR
     PRLEQIKGAM MSIAFKEGLK VPPPALNEMI LASNQDIRQV LHNLSMWSAK DKVMTYDRVK
     EDANNARKDM KLGPFDVCRK VFSKGEESGH MTLIDKSDLF FHDYALAPLF IQENYIHVRP
     AAAGGDLKSH LVLLSKTADC ICDGDLVDRQ IRSKQAWSLL PTQAIYSSVL PGELMRGYMN
     SFPSFPSWLG KFSSCNKHSR IIQELASHMS LKTLSSRQAV SLDYLPYLRM SLLCPLQRRG
     AEGAGQAVQL LDDYHLVRED VDSLMEISLW GGQPDPYAQL DPKVKSAFTR AYNRETHLTP
     YSLQPIKKGR RGGGVEAELG GEEQAEQPEE EEEEEGVAAD AMIKKKAKPS KEPKKEKTTA
     GDSGKGKGKG KGRK
//
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