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Database: UniProt
Entry: A0A0J0XJH2_9TREE
LinkDB: A0A0J0XJH2_9TREE
Original site: A0A0J0XJH2_9TREE 
ID   A0A0J0XJH2_9TREE        Unreviewed;       365 AA.
AC   A0A0J0XJH2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Putative DNA replication factor {ECO:0000313|EMBL:KLT41233.1};
GN   ORFNames=CC85DRAFT_286671 {ECO:0000313|EMBL:KLT41233.1};
OS   Cutaneotrichosporon oleaginosum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX   NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT41233.1, ECO:0000313|Proteomes:UP000053611};
RN   [1] {ECO:0000313|EMBL:KLT41233.1, ECO:0000313|Proteomes:UP000053611}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBC0246 {ECO:0000313|EMBL:KLT41233.1,
RC   ECO:0000313|Proteomes:UP000053611};
RG   DOE Joint Genome Institute;
RA   Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA   Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT   "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT   T. oleaginosus allow insights into substrate utilization and the diverse
RT   evolutionary trajectories of mating systems in fungi.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000256|ARBA:ARBA00005378}.
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DR   EMBL; KQ087221; KLT41233.1; -; Genomic_DNA.
DR   RefSeq; XP_018277724.1; XM_018423594.1.
DR   AlphaFoldDB; A0A0J0XJH2; -.
DR   STRING; 879819.A0A0J0XJH2; -.
DR   GeneID; 28984197; -.
DR   OrthoDB; 275853at2759; -.
DR   Proteomes; UP000053611; Unassembled WGS sequence.
DR   GO; GO:0031391; C:Elg1 RFC-like complex; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0090618; P:DNA clamp unloading; IEA:UniProt.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR013748; Rep_factorC_C.
DR   InterPro; IPR047854; RFC_lid.
DR   PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR   PANTHER; PTHR11669:SF20; REPLICATION FACTOR C SUBUNIT 4; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF08542; Rep_fac_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053611}.
FT   DOMAIN          52..191
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   365 AA;  39794 MW;  4FC9BF1B22868E22 CRC64;
     MATTFGARPA ATAEQQQRLQ PWVEKYRPKT IDDVSSQENT VAVLRKALAS TNLPHMLFYG
     PPGTGKTSTI LALARQLFGP DLFRSRVLEL NASDERGISV VREKIKTFAR ETPRNVGISS
     DGKVYPSPPY KLIILDEADS MTQDAQSALR RIMETYSRIT RFCLVCNYVT RIIEPLASRC
     SKFRFRPLAA GSSQARIEMI ASAEGVNAEP GVLELILKLA NGDLRKAITY LQTAQRLHSA
     SNPPTPITTM SVHEISGVVP DGVIDRLVRS MGIEPGEGIS PSAASGFEGV RNAVRSVGRE
     GWSAGQVLEQ IHDAIVPMES IPTMAKANAA IAIAECDKAL CEGGDEELQL FECCLRVKDA
     MEKAY
//
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