ID A0A4V3S7K3_9HYME Unreviewed; 970 AA.
AC A0A4V3S7K3;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=DBV15_02952 {ECO:0000313|EMBL:TGZ37704.1};
OS Temnothorax longispinosus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Temnothorax.
OX NCBI_TaxID=300112 {ECO:0000313|EMBL:TGZ37704.1, ECO:0000313|Proteomes:UP000310200};
RN [1] {ECO:0000313|EMBL:TGZ37704.1, ECO:0000313|Proteomes:UP000310200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:TGZ37704.1};
RX PubMed=30967075;
RA Kaur R., Stoldt M., Jongepier E., Feldmeyer B., Menzel F.,
RA Bornberg-Bauer E., Foitzik S.;
RT "Ant behaviour and brain gene expression of defending hosts depend on the
RT ecological success of the intruding social parasite.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 374:20180192-20180192(2019).
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:TGZ37704.1}.
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DR EMBL; QBLH01003519; TGZ37704.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4V3S7K3; -.
DR STRING; 300112.A0A4V3S7K3; -.
DR Proteomes; UP000310200; 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 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:UP000310200}.
FT DOMAIN 269..349
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 896..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..46
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..913
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 108418 MW; CF60BC7F05824C7A CRC64;
MPRDIRSYFA RVGSSQKNSE PVVSKPQKRR VISSDEDEEP KSSAKRTKVV RKTKKVSVLS
DSEDDTTIVE IVTKNSQSKS KKNESQKPCT EVSLSEVFGK KPITRVEETK VSRKLQKVES
EFHDDEDFEA VLKQLDTAED IVMHDKKKDK NSAKNADTPK KSEAAEVKMS PGKSNEHSKV
VTCSPPRQKE KKRNINGNLN ISDKQLNNST STSVSEEDQD TGKSQSRKKP KMDLFDERVE
KKKQRAIMYE KYLQRGGARN PGSKEIPTGA ENCLAGVSFV ITGVLDSLER NEAEDLIRKY
GGRTVNTVSS KVTYIIVGDE AGPTKLTKAN SLGIKQISED DLLEMIRTRP EGKAKAIKPT
KAKLNMKKIP NKSENDKSPS PSKIIALDSP KKIKTPPLDS LEKIKTSPVS NQEVTTSVGS
ELLVEKYKPK TLKQIIGQQG DKSCAHNLYV WLRDWHKNRQ DPKYKDGTGK QTHGQSFKAA
LLSGPPGVGK TTTVQIVCKE LGYDLVEFNA SDTRNKTLLK EAVSGLLSNT TMKDYVIGTK
QKITNKHVLL MDEVDGMAGN EDRGGLQELV SLIKCTEVPI ICICNDRFNT KVKTISTHSY
ELKYQKLRVE QIRSSMKSLC FKENIKISTE DLDRLIESTN YDIRQVINHL EFLGSQMSHV
EKTDKKHSNK NVKLGIFDVT KIAFNAEQQK SMSLNDKIGL YFHDYNGAAL FIQENYSGVR
ICQASPRQRL ERIAHAADSI SQGDLVDKVI RGNMMWSLLP MHACFSFVIP ANEMSGNLDG
LIRFPSWFGR NSKATRFNRL MQELTTHTRL ATGANKDALN MDYLAHLRNA IVKPLIENGV
DGIEAAINVM GKYHLTREDL DSVIEISAWP GLRDPTTNLD SKVKAAFTRA YQKNPPMLPY
AINSTATAKK RSTQDSNDFM EEEDDDEETD NVDSDKMIKA KKPSTSKAAT STKKGGEPAK
KRGRGRGKAK
//
