ID A0A493TA27_ANAPP Unreviewed; 1105 AA.
AC A0A493TA27;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN Name=RFC1 {ECO:0000313|Ensembl:ENSAPLP00000022548.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000022548.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000022548.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000022548.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A493TA27; -.
DR Ensembl; ENSAPLT00000023981.1; ENSAPLP00000022548.1; ENSAPLG00000010594.2.
DR GeneTree; ENSGT00730000111066; -.
DR OMA; LICNERN; -.
DR Proteomes; UP000016666; Chromosome 4.
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:UP000016666}.
FT DOMAIN 357..435
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1067
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1098
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1105 AA; 123333 MW; 43E18CD1D4CE4474 CRC64;
MDIRKFFGVV PPGKRQECEN VKKSDKIKNG EGDSSGKKRG KETKVKNSPS EDVPKQKQTN
KKKRIIYDSD DDDDFVNKRI SLKPKENGAS AISCPGSTTV KKEDVKPRAK PKPLSPVKLT
PTSALDYFGT SSVQRSEKKL VASKRKEPSQ SRDSTVDDEA IARQLQLEED SELERQLHED
EEFAKTLAML DETPQKKKAR RDSEEQTVLS IKSSPNVTEG YKQSQRVKAT NSAGEAKQTK
SENSKGSHLP PQSTDSKLAE KSTDKTLPLK PTSKLVALKR KEEIAEKERG TQSSVSKEKP
QGKEEKKTPK KEKISPKKAE SVSPEDSEKK RNNYQAYRSF LNREGPKALG SKEIPQGAEN
CLEGLTFVIT GVLESIERDE AKSLIERYGG KVTGNVSKKT NYLVMGRDCG QSKCEKASAL
GTKIIDEDGL FDLVRTMPGK KSKYELAAES EAKKTESRHK KTPQKTEASR KSFSPLKREA
DIKKRNSTPE KGATFKSVKK ETAAVRKLTD FKQQAVEKKE VPEPKGNLVS ESNENGTERL
LWVDKYKPTS LKAIIGQQGE QSCANKLLRW LRNWHKNTSE DGQAKASKLG GKDDGISSKA
ALLSGPPGVG KTTTAALVCK ELGYSYVELN ASDTRSKNSL KEVVAESLNN TSIKDFCSGT
SSSVSGKHVL IMDEVDGMAG NEDRGGIQEL ISLIKHTKIP IICMCNDRNH PKIRSLVHYC
FDLRFQRPRL EQIKGAMMSI AFKEGLKIPP PAMHEIILAA NQDIRQVLHN LNMWCAKDKS
LTYDEAKTDA SRAKKDIKLG PFDVVRKVFA AGEEASRMSL IDKSDLFFHD YSLAPLFVQE
NYVHVKPAAA GGDLKKHLML LSRAADSICD GDLVDRQIRS KQNWNLLPTQ AIYSSVLPGE
LMRGYMSQFP VFPSWLGKFS STGKHERIVQ ELAMHMSLRT QMCKRTVNME YLSYLRDALV
QPLKDFGADG VQQAITFMDS YCLMKEDVEN IMEISMWGGK PSPFSKLDSK VKAAFTRAYN
KEAHLTPYSL NSVKTSKRQS ASMATSELSE DLNVDETQSD EDEQDSVESD AMIKQKKAKS
SKLPKREKND EPTKKEGKRK EKTRH
//
