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Database: UniProt
Entry: A0A1J9QY50_9PEZI
LinkDB: A0A1J9QY50_9PEZI
Original site: A0A1J9QY50_9PEZI 
ID   A0A1J9QY50_9PEZI        Unreviewed;      1088 AA.
AC   A0A1J9QY50;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN   ORFNames=BKCO1_3100029 {ECO:0000313|EMBL:OJD33297.1};
OS   Diplodia corticola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC   Diplodia.
OX   NCBI_TaxID=236234 {ECO:0000313|EMBL:OJD33297.1, ECO:0000313|Proteomes:UP000183809};
RN   [1] {ECO:0000313|EMBL:OJD33297.1, ECO:0000313|Proteomes:UP000183809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 112549 {ECO:0000313|EMBL:OJD33297.1,
RC   ECO:0000313|Proteomes:UP000183809};
RA   Fernandes I., De Jonge R., Van De Peer Y., Devreese B., Alves A.,
RA   Esteves A.C.;
RT   "Proteomics and genomics reveal pathogen-plant mechanisms compatible with a
RT   hemibiotrophic lifestyle of Diplodia corticola.";
RL   Submitted (OCT-2016) 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:OJD33297.1}.
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DR   EMBL; MNUE01000031; OJD33297.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9QY50; -.
DR   STRING; 236234.A0A1J9QY50; -.
DR   OrthoDB; 6297at2759; -.
DR   Proteomes; UP000183809; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183809}.
FT   DOMAIN          348..427
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..345
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1003..1088
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..167
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        168..185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..277
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1015..1035
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1061..1080
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1088 AA;  119461 MW;  9FEF16FB54685487 CRC64;
     MPADIRSFFG GKPAAQPAKE ESTSEEAMQA EIYSPRSQAK PAAKKRGRPA RKVVEDSDDE
     EEPPKKATPK KPAPKKQAKR EATPEGEATT ASAFFGDKKP ARSAPSKASK AAAKTETPKS
     TPKKAKASDK TAVTPTRTSA RKKKPATYSE VKDEDEDFLD DDEDGDDIFT AAFKKKGKHA
     DDYEESSEDE PVALPQRQAS GRGQKKLKDE GDFEPEADVD MKDAKPEDDF VVPDDDEEIV
     DNKSAKKAKP AAKAGRKRKS AETDDELEAE PPKKARGKKT SPAKKKAKKD EPENAAMKEL
     LDSIPTVRPP SPPPKDGDAP KKFNPFKAGA HANSGPAPQS GALDIPEGKP NCLAGMTFVF
     TGLLEYLDRE AGQQLVKRYG GKVTSGPSSK TSYVVLGSDA GPSKLQKIKQ FKLKTINEEG
     LFALIKKLPA NGGDSKAAAA YEQKQAAEEK KIKEMAEEME REERRKGGAG GAGGGSATAA
     ARSAASSQAP GSQTSGSQSA QDNRLWTVKY APTQLTQICG NKTQVEKLQR WLRNFPKSQK
     KGFKLGGPDG SGLFRAVMIH GPPGIGKTTA AHLVAKIEGY DVVERNASDA RSKKLVQDGL
     QGVLETTSLL GYFAGDGKKV EESKKKLVLI MDEVDGMSAG DRGGVGALAA VCKKSEIPMI
     LICNDRRLPK MKPFDYVTYD LGFRRPTTDQ IRSRIMTIIF REGLKMPKNV IDALIEGTSA
     DIRQVVNMVS TAKLDETAMD YDKSKEMSKA WEKHIILKPW DIVGKILQGH MFSPTSKHTL
     NDKTELYFND HELSYLMLQE NYLGTNPMRV GNHQGKERNL KLLELVDNAA ESISDGDLVD
     SMIHGSQQQW SLMPTHAMFS FVRPASFVAG TMAGFKTNFP QWLGRNSSQG KLTRMIKEIQ
     GHMRLRTSGD RHEIRQQYVP ILWNELVKKL EVEGKEAVPE VIDLMDSYFL TKEDFDAIME
     LGVGPMDQEK IKIETQAKAT FTRLYNQQSH PIPFMKASSI VAPKQAVKEK PDLEEAIEES
     DEGEVMDEPD AKKDEDEEGD ITKDKYIKQP KKKAAPKKKA TKKSAAADDD DEEEEKPKKS
     KGKGRAKK
//
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