ID A0A0L0DLD2_THETB Unreviewed; 906 AA.
AC A0A0L0DLD2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=AMSG_09220 {ECO:0000313|EMBL:KNC53144.1};
OS Thecamonas trahens ATCC 50062.
OC Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC53144.1, ECO:0000313|Proteomes:UP000054408};
RN [1] {ECO:0000313|EMBL:KNC53144.1, ECO:0000313|Proteomes:UP000054408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC53144.1,
RC ECO:0000313|Proteomes:UP000054408};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL Submitted (MAY-2010) 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}.
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DR EMBL; GL349479; KNC53144.1; -; Genomic_DNA.
DR RefSeq; XP_013754618.1; XM_013899164.1.
DR AlphaFoldDB; A0A0L0DLD2; -.
DR STRING; 461836.A0A0L0DLD2; -.
DR EnsemblProtists; KNC53144; KNC53144; AMSG_09220.
DR GeneID; 25567725; -.
DR eggNOG; KOG1968; Eukaryota.
DR OMA; LICNERN; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000054408; 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 PRINTS; PR01217; PRICHEXTENSN.
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:UP000054408}.
FT DOMAIN 253..319
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 873..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 876..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 906 AA; 96299 MW; 0A649D8024046F99 CRC64;
MGGGGSKPKP KPQSKPKPKP KPTATPNTAI ATATATATAT PTTASRRPIV LDSSSDDDFM
APPPKVVATA PMAKSANKQK RKAVPISIVP VGPRSAPIIP GSSRPPSTGK ARPPVRIAPK
ASSASPSPLP SSAKPAPKPA AAKPQTSKPA AAKPQTAKPA ATKPQTAKPA ATKPQTAKPT
AAKHQAFKPP TAKPPAPKTT QSAPPNLLPP PKSTIDVVAA GAPKFSDVGV TASFDETVVL
DKAGVPKGKP YCMQGLHICV TGQLRALERN AFHDLVLRYG GKPAKSVTKK LHYLVIGEAP
GEAKLKKAKA QNVTILSEDD FFAWYPTLPE QAYAPSKTTK AKTSKAAQAL ASRASAPTSA
ARPTSLPATA KAAVDPSSQL WTVKYAPQTV GDLVGNTTKI ENLSLWLANW HTAFRSGVAV
KIKNSSGKPV PLKSRAVLLS GQPGIGKTSA ALLVARAAGF HPIEFNASDT RSKTSLRAHV
KSLTENKTMH QFFGGASTAR ETKKHVLIMD EVDGMSSGDR GGLAELAAII KTTKVPIICM
CNDAASPKMR TFKNHTYLLP FQRPTAAQIK HRVVSIAAAE GLALEPAAVD SLVAQTGADI
RQILNLMQMW AVDAQIVNYE TVQKTLATGG KNIDRGPFQL MEDFLKGDNF RALGAMGCLN
AYFGDPSLVP LLVQENYLST RPFQAQPGNP IRTCDMMKRS ADAIAYADIL ETRARSVQSW
KYMPIHAVLS CAVPGFYMHG HMHRPAFSAW LGKYSKATRL SRLNRELTIH MRLRISASPD
AVVCDYLPTL ASLLALPLAH ETGVDAMIER MAYYYLTRDD WSNIMELAAR SPKLKATTSS
ISGKTKAAFT RAYKKRAASL ALPYTTAATT KAVYKGGKSD GKKAPKPVLP LSDDDDDDDA
NSSVRL
//