ID A0A384CXR3_URSMA Unreviewed; 1153 AA.
AC A0A384CXR3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 03-AUG-2022, sequence version 2.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN Name=RFC1 {ECO:0000313|RefSeq:XP_008699632.2};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008699632.2};
RN [1] {ECO:0000313|RefSeq:XP_008699632.2}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008699632.2};
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_008699632.2; XM_008701410.2.
DR AlphaFoldDB; A0A384CXR3; -.
DR STRING; 29073.ENSUMAP00000000784; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000261680; 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:UP000261680}.
FT DOMAIN 401..479
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 46..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1085..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1153 AA; 128748 MW; 1D4EEF00DE32FD98 CRC64;
MDIRKFFGVI PSGKKPVTET IKKSEKTKSA EETLKAKKGI KEIKVNSSCK EDDSKQKQPN
KKKRIIYDSD SESEETVQVK NAKKQPEKLP LSSKPGKILR QDPVTYISET DEEDDFMCKK
AASKSKENGG STNSYLGASN MKKNEENTKT KNKPLSPIKL TPTSVLDYFG TGSVQRSDKK
MVASKRKQPS QNADDSRLND EAIAKQLQLD EDAELERQLH EDEEFARTLA MLDEEPKTKK
ARKDPGEREA FSSVQANLSK AEKHTSPHKV KTEQFSDDRK NCSPKKQTKC ESLIGSQQHL
KSSPHKIGET SPKASSKVAL LKKKGESSYK ETEPMASKRK ENAVELKGQT KTPKKPKSSP
AKKESVSPED SEKRRTNYQA YRSYLNREGP KALGSKEIPK GAENCLEGLT FVITGVLESI
ERDEAKSLIE RYGGKVTGNV SKKTNYLVMG RDSGQSKSDK AAALGTNIID EDGLLNLIRT
MPGKKSKYEI AVEAEMKKEK SKLERTPQKK DQGKRKISPT KKESGSKKSR LTPKKDSSTK
PVKKETSVLW RCLDFEEQVA EETNGDSRAR SLADDSPENK VEDLLWVDKY KPTSLKTIIG
QQGDQSCANK LLRWLRNWHK GPSEDQKRAK FGKFAGKDDG SSFKAALLSG PPGVGKTTTA
SLVCQELGYS YVELNASDTR SKNSLKEIVA ESLNNTSITG FYSTSQHGSG GAAHSVSMKH
ALIMDEVDGM AGNEDRGGIQ ELIGLIKHTK IPIICMCNDR NHPKIRSLVH YCFDLRFQRP
RVEQIKGAMM SIAFKEGLKI PPPAMNEIIL GANQDIRQVL HNLRMWCARS KALTYDQAKA
DSHRAKKDIK LGPFDVARKV FAAGEETAHM SLVDKSDLFF HDYSIAPLFV QENYIHVKPI
AAGGDMKKHL MLLSRAADSI CDGDLVDRQI RSRQNWSLLP TQAIYASVLP GELMRGYMTQ
FPTFPSWLGK HSSTGKHDRI VQDLALHMSL RTYSSKRTVN MDYLSHIRDA LVQPLTSQGV
EGVQDVIALM DTYYLMKEDF ENIMEISSWG GKPSPFSKLD PKVKAAFTRT YNKEVHLTPY
SLQAVKTPRH STGPALDSEY SEDLNEDDSQ SEEKDQDSVE TDAMIKKKTK SSKPSKSEKD
KESRKGKGKS SKK
//
