ID A0A3Q2ZBV4_KRYMA Unreviewed; 1180 AA.
AC A0A3Q2ZBV4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000000045.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000000045.1}
RP IDENTIFICATION.
RG Ensembl;
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_017263914.1; XM_017408425.1.
DR AlphaFoldDB; A0A3Q2ZBV4; -.
DR STRING; 37003.ENSKMAP00000000045; -.
DR Ensembl; ENSKMAT00000000069.1; ENSKMAP00000000045.1; ENSKMAG00000000061.1.
DR GeneID; 108231386; -.
DR KEGG; kmr:108231386; -.
DR CTD; 5981; -.
DR GeneTree; ENSGT00730000111066; -.
DR OMA; LICNERN; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000264800; 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:UP000264800}.
FT DOMAIN 426..506
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..192
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1180 AA; 127970 MW; E8AC75A645CAA4C6 CRC64;
MDIRRFFGPV SGKPAVQKAA PSENLKSKDK KKKVSLSSDE DGKKKGSTKV KSSKTEEQHK
CGETKRRKRA VIESDSEEEE EEEPVMKSKK PSKEKGRTSK AGLPPKKDPV QYVSETDSDS
DNFLSLGKVS KLKQNGAAKT KKPGPESSHS GSKGPVKSPI APSSSQPRAG PKSPPAPATP
KSAPPPPPKQ TPTSVLDYFG TGTIHRSDKK LVASTKRKAP TQDSGDLISD EEMARQLQME
EEKELEKQVH NDEEFARTLA MLDAEPQTKK ARKTSEDQPG PSTTPRKSST AAAAVSGTSS
PPKARGRISV DGIGPSPRNS PIKSSSKLAM MKKKDEAKDQ GPKTKTPTKN KISPKKEPPS
SSVSGMKFVP KTQTTPTAAK ASPKKPETTS ISPDDAEKKK MNSSAYRSYL NREGPRALGS
KEIPTGAENC LEGCVFVLTG VLESMERDDA KTLIERYGGK VTGNISKKTT YLVQGRDSGA
SKLEKAESLG TKILDEDGLL DLIRTKPGKK SKYEIAAEAE ITASKSRTPP SHTSKSTPKA
QKISPSKGNS RSPHTPSPSK TGQARGHGSR AGDGSATPGR GSGRTARREL GLPSPSAPGP
SPPSPTGESL LWVDKYRPRS LKAVIGQQGE QSCANKLLRW LQSWNKHHSS SSSSSKPAAA
RFGKFGGKDD GSGYKAALLS GPPGVGKTTT AALVCEELGF SYVEMNASCT RSKNSLKEVV
AESLNNTSIE NFYKGMSQTV SSKHVMIMDE VDGMAGNEDR GGMQELIGLI KNTKIPIICM
CNDRNHPKIR SLANYCFDLR FQRPRVEQIK GAMMSVAYKE GIKIPPPALN EIILASNQDV
RQVIHNLSMW SAKNKVMTYD QCKSDAASAR KDMKLGPFDV CRKVFASGEE SAHMSLIDKS
DLFFHDYSLA PLFVQENYVH VRPSAAQGDV KSHLVLLSKT ADSISDGDLV DRQIRSRQNW
SLLPTQAIFA SVIPGELMRG YMAQFPVFPS WLGKNSSTNK HARIIQELAS HMSLKTLSTR
QAVNLDYLHY LRLMLLHPLQ KDGVEGAGRA VQLLDDYQLI REDVDSIMES SVWGGQPDPY
SKLDSKVKAA FTRAYNKEVH LTPYSLQAVK KGRRGGGDVE LGGESMDLDG PGSEDEGEEL
QTDAMIKQKK TKTTKESKKE KKEDSGKGKG KGKGKGKAKK
//
