ID A0A168GNP6_CORDF Unreviewed; 1024 AA.
AC A0A168GNP6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=LEL_06403 {ECO:0000313|EMBL:OAA76719.1};
OS Akanthomyces lecanii RCEF 1005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Akanthomyces;
OC Cordyceps confragosa.
OX NCBI_TaxID=1081108 {ECO:0000313|EMBL:OAA76719.1, ECO:0000313|Proteomes:UP000076881};
RN [1] {ECO:0000313|EMBL:OAA76719.1, ECO:0000313|Proteomes:UP000076881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 1005 {ECO:0000313|EMBL:OAA76719.1,
RC ECO:0000313|Proteomes:UP000076881};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA76719.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AZHF01000004; OAA76719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168GNP6; -.
DR STRING; 1081108.A0A168GNP6; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000076881; 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:0006271; P:DNA strand elongation involved in DNA replication; IEA:UniProt.
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: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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000076881}.
FT DOMAIN 299..378
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 389..430
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 25..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..974
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1016
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 111971 MW; 69A85007EEB34AFE CRC64;
MPDIRSFFTP KGGAAVAAVK AEPASQKPDN KRRKVGRKVI EDSDDDEVVE KKPAAKSTPK
ASKKKAEDDG LEISTNDYFA SNKAQTSTQA TPKKPTTAAS KADVPVRSSP RSKTTVAKTA
ALSSDKPAPK RTSRSSHQRK QDDDDAHMED ADEDGDDIFA ADIKGRGKGD DDYAEDSDED
MLPQPSGAAA KEKQTQDTKP SRAAAASKKR KTPEQDSDEE EEEELPRKKP TASKPRAPRA
KKADVPEDAA IQDILDSVAT VRPPTPPPKD PNTKFDWRKA AGGGNATVQP VGSADIPEGE
EECLSGLSFV FTGVLSTIGR DEGQALVKRY GGKVTGQPSS KTSFVVLGDD AGPSKLAKIK
SFGIRTIDEN GLFDLIRKLP AHGGTGKGAQ KAQEKKKADE EKIKQQIAEM EAEEKAKRVA
EAKAAKLAAS VPGAARPPPP SNVPTQLLTS KYAPTQLNHI CGNKGQVEKI QAWLRNWPKA
KKYNFQKRGA DGLGGERAII ISGPPGIGKT TAAHLAARLE GYDVLESNAS DARSKRLVEA
GVSDVMNNTS LLGFFAGDGK SVDTTKKKMV LIMDEVDGMS GGDRGGVGAM AKFCKKTEVP
LILICNERRL PKMKPFDHVA FDIRFNRPTV DQVRSRIMTI CHREGLKLPP PVVDALIEGS
NKDIRQIINM ISTAKLDQTS LNYDQGKAMT KAWEKHVVLK PWDICQKMLG GGLFAPASKA
TLNDKIELYF NDHEFSFLMI QENYLRCKPM ALNGKGYNKR EEKLKALELF DQAAQSISDG
DLVDRMIHGP QQQWSLMPTH AIFSTVRPAS FIAGQLMGSN FTSYLGNLSK TGKLGRFIRE
IHSHMRLKSS GDHNEIRQQY MPVLWKQLID KLQVEGPESV SEVIDLMDAY YLTREDFDAI
QELGVGPMDE SNVKIESKAK AAFTRTYNAM SHPVPFMKAS TNVVAPKKSA QDVPDLEEAI
EEEDDAEVVE APAQDDDEID FKKDKYIKKP KAKKATKKSK AKADDEDEDE KPKPKSKAKA
KAKK
//
