ID H2AY04_KAZAF Unreviewed; 501 AA.
AC H2AY04;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 13-SEP-2023, entry version 49.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=KAFR0G02200 {ECO:0000313|EMBL:CCF59254.1};
GN ORFNames=KAFR_0G02200 {ECO:0000313|EMBL:CCF59254.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF59254.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF59254.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
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DR EMBL; HE650827; CCF59254.1; -; Genomic_DNA.
DR RefSeq; XP_003958389.1; XM_003958340.1.
DR AlphaFoldDB; H2AY04; -.
DR STRING; 1071382.H2AY04; -.
DR GeneID; 13887233; -.
DR KEGG; kaf:KAFR_0G02200; -.
DR eggNOG; KOG0745; Eukaryota.
DR HOGENOM; CLU_014218_1_2_1; -.
DR InParanoid; H2AY04; -.
DR OrthoDB; 452393at2759; -.
DR Proteomes; UP000005220; Chromosome 7.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 1.10.8.60; -; 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; IPR019489; Clp_ATPase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48102:SF7; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48102; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPX-LIKE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220}.
FT DOMAIN 124..288
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 360..445
FT /note="Clp ATPase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01086"
FT COILED 99..126
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 501 AA; 55392 MW; 636DEA750933E376 CRC64;
MFSMLSRRTA VFVGRSKLSS TIAIRTLIGS SKVEAIPSPR KIKKQLDEYI IGQETSKKVL
SVAVYNHYLR VNDKLRKNEI KKQKKLLELN KSLSVESSNS EATAGLKSIK RQLDNLEDAD
LELSKSNVLV VGPSGSGKTL LATTLARILD VPIAVTDCTQ LTQAGYIGQD VEVCIERLLV
NANFDVSKAE RGIIVLDEID KLSKPAASIG TKDVSGEGVQ QSLLKIIEGH KVELTVKRPV
KSQKGNENKN QVTTTKEENF VIDTSNILFM IMGAFVGLDK HVVNRINALK DSNKKGKEEG
TKNSEEKKRS KFGNFIEDVE LPNGEKVSAL SLTTPTDLVG FGLIPELVGR VPIITALDPL
QTTDLYNILR EPKNALLDQY EYIFKQFGVR LCVTKKAIKR IAQLALNEGT GARGLRGVME
RLLLNVNFES PDSGISYVLI DESTVNSLQQ TKYSLATHVD AKYYLSSQQG DLIRDASRED
IILAGLLEKE FLRTSVIERK N
//