ID A0A0T6B3N2_9SCAR Unreviewed; 997 AA.
AC A0A0T6B3N2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, 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};
GN ORFNames=AMK59_6013 {ECO:0000313|EMBL:KRT81463.1};
OS Oryctes borbonicus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Scarabaeiformia;
OC Scarabaeidae; Dynastinae; Oryctes.
OX NCBI_TaxID=1629725 {ECO:0000313|EMBL:KRT81463.1, ECO:0000313|Proteomes:UP000051574};
RN [1] {ECO:0000313|EMBL:KRT81463.1, ECO:0000313|Proteomes:UP000051574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OB123 {ECO:0000313|EMBL:KRT81463.1};
RC TISSUE=Whole animal {ECO:0000313|EMBL:KRT81463.1};
RA Meyer J.M., Markov G.V., Baskaran P., Herrmann M., Sommer R.J.,
RA Roedelsperger C.;
RT "Draft genome of the scarab beetle Oryctes borbonicus.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRT81463.1}.
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DR EMBL; LJIG01016151; KRT81463.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6B3N2; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000051574; Unassembled WGS sequence.
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; 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:SF6; 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 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:UP000051574}.
FT DOMAIN 241..318
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 58..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..953
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 997 AA; 111881 MW; 77F14347324C8426 CRC64;
MSQDIRSFFS VIAGKPNRNT VVSTKRRAIT IDSSDDEIIA ASPVDVKQKV TIKTKKRKII
DSDSDDESKK TKANKESTKP ERNKLQKVNA ADIFGSTPIK QTKVEKKETH HDKSSEKTPL
VKHKTKSKAK TPLKLETELG IHDDPEFEQV LLDLDNDILL NNVNALDKTV EEALNNPTNS
MSTHKRNTTT PKRKSKVDEE SDELDKDQER YEKRRHSALL YQKYLNRSGP AHHGAKEYPK
GKPNCLNGLC FLRTGVLDSL EGGEFDQLVK DHGGRTVHAV SKKVDYVVEG VEPGPAKLEK
ARKYGIPSIG EDTFLDLILT KSGMKPKYAK GASTGDSAND SNIEECHADT KTSSPKVAEK
SQKDTGRTNA SPKKLADRKI EDKEATKPII TKLSSDNNDI PKVTIINEYF YGKRTPEVIV
NEKEIVNISV IQENLSWADK YKPTDIKSII GQQGDRSCMR KLLYWLSKWH ENHSGKGRPK
IPKPSPWSKT DDGAYFKCAL LSGPPGIGKT TTATLVAKEL EFDVVEFNAS DTRSKRLLHE
QVAQLLSTNS IAGFVKEGTA PTKKHVLLMD EVDGMAGNED RGGMQELIQL IKNTSIPIIC
MCNDRNHAKV RSLANYCFDL RFSKPRLEQI KGAMMSVCFK EDLKIKPETL TQIISGTGMD
VRQTLNHLSM WTVNNKSLSV EEAQKEANAA QKDTILGPWE VLRKVFSQDE HKTMSVADRF
RLFYYDYSIG PLFVQENYLQ VQPNCPRSET LQRVSWTADS ISKSDLVDKK MRSSNNWSLL
EVQAIYSSVL PGQYMEGNVR GQINFPTWLG KNSKKGKFKR LVSELQAHMR ISTSGSRKSV
NLDYIYHLRN CIIKPLRERG TNGIEKAMEV MHSYNLLRED LDGIMEVSHW SRQKDPMAMV
DSKVKAAFTR AYNKDNAKLP YSASSAAIKK KAHTAVDDNP YEEEEEGNSA AEDDDDITKD
AMIKAKKKPV KGKDDKTEAS TSKKGSSSTR GKGTRKK
//
