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Database: UniProt
Entry: G3Y2T2_ASPNA
LinkDB: G3Y2T2_ASPNA
Original site: G3Y2T2_ASPNA 
ID   G3Y2T2_ASPNA            Unreviewed;      1035 AA.
AC   G3Y2T2;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN   ORFNames=ASPNIDRAFT_52205 {ECO:0000313|EMBL:EHA22854.1};
OS   Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS   NCTC 3858a / NRRL 328 / USDA 3528.7).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA22854.1, ECO:0000313|Proteomes:UP000009038};
RN   [1] {ECO:0000313|EMBL:EHA22854.1, ECO:0000313|Proteomes:UP000009038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC   NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX   PubMed=21543515; DOI=10.1101/gr.112169.110;
RA   Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA   Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA   Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA   van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA   Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA   Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA   Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA   Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA   Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT   "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT   versus enzyme-producing CBS 513.88.";
RL   Genome Res. 21:885-897(2011).
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:EHA22854.1}.
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DR   EMBL; ACJE01000010; EHA22854.1; -; Genomic_DNA.
DR   AlphaFoldDB; G3Y2T2; -.
DR   STRING; 380704.G3Y2T2; -.
DR   HOGENOM; CLU_003574_1_1_1; -.
DR   Proteomes; UP000009038; 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   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}.
FT   DOMAIN          299..378
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          959..1035
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..31
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..447
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        959..977
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        978..993
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1006..1027
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1035 AA;  114441 MW;  62AA87ED4070F4F1 CRC64;
     MPADIRSFFG GKSRTRKVVD DSDEEEVVAT KSVSPKVKAP SKPQPEVSKG EPTTSSDYFA
     SSKKRGRPAK ETKTSQPAVT DEPEAKPSPK PKKSTSTEKP APRPQRGTRK ATTVVDDDEL
     GGDDIHATEY KKTGKGDDDY VEEEDKESDS DFEELAVKPA SAASGRQGRK KAATAESDED
     VVMEDLPKRP SSAAKSAATQ PARKRKSEVL EKDEDYDSKT SPKKAAQTKA APRTPKKPRA
     STKTDRPESK EIQDIFDSIP TIRPPSPPRE TGEKAKFNYA AHAQRSRSPV AGGADIPEGA
     ENCLAGLSFV FTGVLDTLGR DEGQNLVKKY GGKVTGAPSS KTSYVVLGAD AGPKKLATIK
     QHNLKTINEE GLFELIRRLP ANGGDGKAAE QHEAKKKAEE EKIRAMAAEI DREEKRKAAA
     TRNTAPSGPQ PPSSSQSTTQ STKTDDRLWT TKYAPTSMNM ICGNKGVVEK LQNWLRDWHK
     NAKAGFNKPG KDGSGMYRSV MIHGPPGIGK TTAAHLVAKL EGYDVVETNA SDTRSKKLVE
     NGLLGVLDTT SLQGYFSGVG KKVESAKKNL VLIMDEVDGM SAGDRGGVGA LASIAKKTHI
     PLILICNERR LPKMKPFDHV TYELPFRRPT AEQIRARLST ICFREGLRIP PQVLDSLIEG
     TNADIRQVIN MLSTVKLDQT NLDFEKGKQM SKAWEKHIVL KPWDIVGKIL SAQMFSPSSK
     ATLNDKIELY FNDHEFSPLM LQENYLKTRP ALAGAYHGRE QKLKQLELMD NAASSISDGD
     LVDRMIHGTQ QQWSLMPTHA VFSFVRPASF TYGNMMERPG FTSWLGQNSK QGKLWRYIKE
     IQGHMRLRAS GDRDEIRQQY MPLLWDRLVR RLMVEGKDSV DDVIDFMDSY FLTREDWDAL
     VELGLGPMDE SNVKLQTQTK AAFTRIYNQR SHPLPFIKAS SIAAPKKMPK EKPDIEDAIE
     ESDEEEVLED DSKDNDESEE LDLKKDKYVR VPKKAAKGGA AKGRKSKKAA AGDDDFIDDE
     EEKPKKARGR KPKAK
//
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