ID G1PP22_MYOLU Unreviewed; 1140 AA.
AC G1PP22;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN Name=RFC1 {ECO:0000313|Ensembl:ENSMLUP00000012729.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000012729.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000012729.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000012729.2}
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 EMBL; AAPE02017279; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02017280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PP22; -.
DR STRING; 59463.ENSMLUP00000012729; -.
DR Ensembl; ENSMLUT00000013989.2; ENSMLUP00000012729.2; ENSMLUG00000013981.2.
DR eggNOG; KOG1968; Eukaryota.
DR GeneTree; ENSGT00730000111066; -.
DR HOGENOM; CLU_003574_0_0_1; -.
DR InParanoid; G1PP22; -.
DR OMA; LICNERN; -.
DR TreeFam; TF105722; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005663; C:DNA replication factor C complex; IEA:Ensembl.
DR GO; GO:0031391; C:Elg1 RFC-like complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0061860; F:DNA clamp unloader activity; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:Ensembl.
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:UP000001074}.
FT DOMAIN 402..480
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1069..1140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..377
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..542
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1102
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1140 AA; 127426 MW; 835355462DE830F4 CRC64;
DIRKFFGVIP SGKKSASETI KKNEKTKSAE ETSKAKKGIK EIKVNSSCKD DDSKQKQPNR
KKRIIYDSGT DSESEETVQV KNAKKQPEKL PLSKPGKILR QDPVTYISET DEEDDFMCKK
AASKSKENGR STNSYLGASN MKKNEENAKT KNKPLSPIKL THTSVLDYFG TASVQRSDKK
MVASKRKEPS KSANDSRLND EAIAKQLQLD EDAELERQLH EDEEFARTLA MLDEEPKNKK
ALKDPEERET FSSVHANLNK AEKHKCPYKV KTDQFLDERK NCSPKKQIKC ESSKESQQHS
KSSAHKRGET SSPTASSKLT LLKKKEESSS KETEPMSLKR KEYPIELKGE AKSPKKIKSS
PAKKESVSPE DSEKRRTNYQ AYRSYLNREG PKALGSKEIP KGAENCLEGL IFVITGVLES
IERDEAKSLI ERYGGKVTGN VSKKTNYLVM GRDSGQSKSD KAAALGTKII DEDGLLDLIR
TMPGKKSKYE IAVEAEMNKE KSKLQRTPQK NYQGKRKISP NKKESESKKS QRTPKKDSSM
TSIKKETSVV QRGLDFKEQV AEETSGDSSE NKVANLLWVD KYKPTSLKTI IGQQGDQSCA
NKLLRWLQNW HKSPSEDRKH AAKFGKFAGK DDGSSFKAAL LSGPPGVGKT TTASLVCQEL
GYSYVELNAS DTRSKNSLKD IVAESLNNTS IKGFYSSGAA PSVSMKHALI MDEVDGMAGN
EDRGGIQELI GLIKHTKIPI ICMCNDRNHP KIRSLVHYCF DLRFQRPRVE QIKGAMMSIA
FKEGLKIPPP AMNEIILGSN QDIRQVLHNL SMWCARSKAL TYDQAKADSQ RAKKDIKLGP
FDVARKVFAA GEETAHMSLV DKSDLFFHDY SIAPLFVQEN YIHVKPVAAG GDIKKHLMLL
SRAADSICDG DLVDRQIRSK QNWSLLPTQA IYASVLPGEL MRGYMTQFPT FPSWLGKHSS
TGRHDRLVQD LALHMSLRTY SSKRTINMDY LSHIRDALVQ PLTSQGVEGV QDVVALMDAY
YLMKEDFENI MEISSWGGKP SPFSKLDPKV KAAFTRAYNK EAHLTPYSLQ AVKAPRHSTG
PALDPEHSEE LQEDDSQSDE KEQDAVETDA MIKKKTKSSK PSKSEKDKES RKGKGKGSKK
//
