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Database: UniProt
Entry: V5GVB2_KALBG
LinkDB: V5GVB2_KALBG
Original site: V5GVB2_KALBG 
ID   V5GVB2_KALBG            Unreviewed;       384 AA.
AC   V5GVB2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Replication factor C, subunit RFC4 {ECO:0000313|EMBL:EST09842.1};
GN   ORFNames=PSEUBRA_SCAF1g00297 {ECO:0000313|EMBL:EST09842.1};
OS   Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX   NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST09842.1, ECO:0000313|Proteomes:UP000019377};
RN   [1] {ECO:0000313|Proteomes:UP000019377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX   PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA   Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA   Goldman G.H.;
RT   "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT   high producer of endo-1,4-xylanase isolated from an insect pest of
RT   sugarcane.";
RL   Genome Announc. 1:E0092013-E0092013(2013).
CC   -!- SIMILARITY: Belongs to the activator 1 small subunits family.
CC       {ECO:0000256|ARBA:ARBA00005378}.
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DR   EMBL; KI545851; EST09842.1; -; Genomic_DNA.
DR   RefSeq; XP_016294831.1; XM_016435859.1.
DR   AlphaFoldDB; V5GVB2; -.
DR   STRING; 1365824.V5GVB2; -.
DR   GeneID; 27418488; -.
DR   eggNOG; KOG0989; Eukaryota.
DR   HOGENOM; CLU_042324_1_0_1; -.
DR   OMA; GCQSGSF; -.
DR   OrthoDB; 275853at2759; -.
DR   Proteomes; UP000019377; 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:UP000019377}.
FT   DOMAIN          61..193
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   384 AA;  42586 MW;  9118745EEEECF623 CRC64;
     MFLQQSSKAH NAGQAAQKEK LAKERAAMRP WVEKYRPKTI DDVAAQEHTV AVLQKTLMSN
     NLPHMLFYGP PGTGKTSTIL ALARQLFGPE LMKTRVLELN ASDERGISVV REKIKNFAKL
     AVTNPKEGFP CPPFKIIILD EADSMTQDAQ SALRRIMEQY SRITRFCLVC NYVTRIIEPL
     ASRCSKFRFR SLDTSSTKTR LEMIASAESV AFRDDAVLDT LISTSDGDLR RAITYLQSAS
     RLHSVAGDEK SAVTSESIVE IAGVVPTRVI ASLAKAVGIE AYNSDDDVEM DSVGGARKKD
     AFERIREEVR TITREGYSIT QLLVQLHDHI IAHPTLLAKI KAKAALLMAQ MDKCLTDGAD
     EELQLLNLCL KLQEVVQTDG KAYV
//
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