ID A0A2K6C0J5_MACNE Unreviewed; 1134 AA.
AC A0A2K6C0J5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
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|Ensembl:ENSMNEP00000017187.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000017187.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000017187.1}
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; A0A2K6C0J5; -.
DR Ensembl; ENSMNET00000041412.1; ENSMNEP00000017187.1; ENSMNEG00000032597.1.
DR GeneTree; ENSGT00730000111066; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000032597; Expressed in pituitary gland and 12 other cell types or tissues.
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:UP000233120}.
FT DOMAIN 402..480
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 47..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1082..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1109
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1134 AA; 127066 MW; 301C06A45E80EEAE CRC64;
MDIRKFFGVI PSGKKLVTET VKKNEKTKSD EETLKAKKGI KEIKVNSSRK EDDFKQKQPS
KKKRIIYDSD SESEETLQVK NAKKQPEKPP VSSKPGKISR QDPVTYISET DEEDDFMCKK
AASKSKENGR STNSHLGTSN MKKNEENTKT KNKPLSPIKL TPTSVLDYFG TGSVQRSNKK
MVASKRKELS QNTNESGLND EAIAKQLQLD EDAELERQLH EDEEFARTLA MLDEEPKTKK
ARKDTEEGET FSSVQANLNK AEKRKYPHKV KTEQFSDERK SYSPRKQTKY ESSKEPQQHS
KSSADKIGEV SSPKASSKLA IMKRKEESAY KETESVASKR KENAVELKGE TKTPKKTKSS
PAKKESISPE DSEKKRTNYQ AYRSYLNREG PKALGSKEIP KGAENCLEGL IFVITGVLES
IERDEAKSLI ERYGGKVTGN VSKKTNYLVM GRDSGQSKSD KAAALGTKII DEDGLLNLIR
TMPGKKSKYE IAVETEMKKE SKLERTPQKN VQGKRKISPS KKESESKKSK PTSKRDSLAK
TIKKETDVFW RGLDFKEQVA EETSGDSKAR NLADDSSENK VENLLWVDKY KPTSLKTIIG
QQGDQSCANK LLRWLRNWHK SSSEDKKHAK FGKFSGKDDG SSFKAALLSG PPGVGKTTTA
SLVCQELGYS YVELNASDTR SKSSLKAIVA ESLSNTSIKG FYSNGAASSV STKHALIMDE
VDGMAGNEDR GGIQELIGLI KHTKIPIICM CNDRNHPKIR SLVHYCFDLR FQRPRVEQIK
GAMMSIAFKE GLKIPPPAMN EIILGANQDI RQVLHNLSMW CARSKALTYD QAKADSHRAK
KDIKMGPFDV ARKVFAAGEE TAHMSLMDKS DLFFHDYSIA PLFVQENYIH VKPVAAGGDM
KKHLMLLSRA ADSICDGDLV DSQIRSKQNW SLLPTQAIYA SVLPGELMRG FMTQFPTFPS
WLGKHSSTGK HDRIVQDLAL HMSLRTYSSK RTVNMDYLSH LRDALVQPLT LQGVDGVQDV
VALMDTYYLM KEDFENIMEI SSWGGKPSPF SKLDPKVKAA FTRAYNKEAH LTPYSLQAIK
ASRHSTSPSL DSEYNEELNE DDSQSDEKDQ DAIETDAMIK NVEQETFKLE ISSL
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