ID A0A074W9C2_9PEZI Unreviewed; 1040 AA.
AC A0A074W9C2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Replication factor C subunit 1 {ECO:0000256|ARBA:ARBA00020401, ECO:0000256|PIRNR:PIRNR036578};
GN ORFNames=M436DRAFT_55056 {ECO:0000313|EMBL:KEQ69675.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ69675.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ69675.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ69675.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584720; KEQ69675.1; -; Genomic_DNA.
DR RefSeq; XP_013423817.1; XM_013568363.1.
DR AlphaFoldDB; A0A074W9C2; -.
DR STRING; 1043004.A0A074W9C2; -.
DR GeneID; 25412055; -.
DR HOGENOM; CLU_003574_1_1_1; -.
DR OrthoDB; 6297at2759; -.
DR Proteomes; UP000027730; 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; 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; PR00364; DISEASERSIST.
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:UP000027730}.
FT DOMAIN 307..380
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 60..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..200
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..981
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1004
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1040 AA; 113932 MW; 5C41BDBDD9B58CC1 CRC64;
MPADIRSFFG GKPSSATPPA KEEKKAPAKK GRARKVVDDS DDEPEFCKRV CLISLPVPSP
IDMLLRKREP SPQGEETTTA AYFATKNKPK PAAATTKSTA TTKSPAKPAP STKSPAKPVK
SENSPPPSTD DLNPEDFPDD DFDDAFTTEY KRENPPAEQP TDMPPKKRAA ATKAKKVKDE
DYDVEMEDTN ADDDFVIPDE HDDMEIEKPT KAKPKPKAST KRKSKDLDTD EEEKPKPKKP
RAAPKKKEKD PPVEDPAELK AILDDIPLIQ APDPPSDNEG ADKPKWYNRP KDSNPAPGAG
SLDIPDGADN CLAGLTFVFT GQLTYLSRED GQNLVKRYGG KCTTAPSKKT DYVVLGAEAG
PKKLATIKQF GIKTINEEGL CALIAKLPAN GGNSVAGAKF AEQQKKEAGK IRKEAEELER
VEREKAAAGP VAQPKGIAAD GTDNRLWTVK YAPTQLGQIC GNKGQVEKLG TWLRNFHKNA
RKDFKLAGKD GSGTYRAVMI HGPPGIGKTT AAHLVAKLEG FDIVESNASD TRSKKLVENG
LKGVLSTTSL NGYFASGEVD TNKKKMCLIM DEVDGMSAGD RGGVGALAAV CKKTQVPMIL
ICNDRKLPKM KPFDFVTFDL PFRRPTNDMI RARIATIAHR EGLKMPPNVM NALIEGTGAD
IRQVVNMIST AKLDQSAMDF NKGKEMSKAW EKHVVLKPWD ITSKILGGGM FQAASKSTLN
DKIELYFNDH EFSPLMLQEN YLGTKPILAA DAPNAKMANL ETLKLSSQAA DSISDGDLVD
RMVHGSQQQW SLMPTHAIMS FVRPASFVAG SQAGSQTRFT TWLGKNSSYG KLSRQVKEIQ
GHMRLRTSGD RHEIRQQYMP TLWQNLVKKL ESEGKEAVPE VIELMDQYFL TKDDFDAILE
LGVGPMKQED VKLESQTKAT FTRMYNAQSH PLPFMKASSV VNPSKKIAKE KPDLEEAMDD
SEDEALLKDA AEDDAEEEED MDISKDKYVA KPKKKKAPAK AAAKGKGKKK ADSGDEDDEE
EEKPKPAARK KAPAKPRAKK
//
