ID H2AU77_KAZAF Unreviewed; 1147 AA.
AC H2AU77;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=DNA repair protein RAD5 {ECO:0000256|ARBA:ARBA00013412};
GN Name=KAFR0D02790 {ECO:0000313|EMBL:CCF57927.1};
GN ORFNames=KAFR_0D02790 {ECO:0000313|EMBL:CCF57927.1};
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:CCF57927.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF57927.1, 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).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; HE650824; CCF57927.1; -; Genomic_DNA.
DR RefSeq; XP_003957062.1; XM_003957013.1.
DR AlphaFoldDB; H2AU77; -.
DR STRING; 1071382.H2AU77; -.
DR GeneID; 13885885; -.
DR KEGG; kaf:KAFR_0D02790; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_5_1; -.
DR InParanoid; H2AU77; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000005220; Chromosome 4.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014905; HIRAN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 502..709
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 893..940
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 976..1143
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 115..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1147 AA; 132225 MW; 4104AF68C50FD596 CRC64;
MIETEQNDSE KKRFFKDELE SSQETQLIFD KSLENKSSFL FADHSVEDVP KSQAESVIPE
GNVTMQVFCT ELKSIIPEMS DNICEELYNK FRDSQDRLSN AITYYFEHYN NEKKDMFDQT
PSSPAPAASS SSSGTPSSQW LFTQSKRRKT YGERNIERLK PNIRWKRFIG ALQVTAMATR
PTIRPLKYGT ELKLLKTSSS PKIYDTTGRK KSTMANYVRV FDNKESRELG RFSEDIAQTI
YPLLDTDEIS FEVTMVYCGN KRLSIGDNFI LQVDCFLSSL LFDSSKNGYA PDVNHDFHRR
SWENSKKGIV ETEEELQRRS RTTALISLFD KLSLRPILKE AEDTEKINKS FTNDTEVIDL
EDDETLDRIM SQDSEALEAT THNEDSMNLN QLKNFYNITQ SSDSLKILPE TEPSKDVFKL
ELRKYQKQGL TWMLRREHEF EKAAGDDKEI DSNMMNPLWR QFMWPKNMSW TAQKLEDHCE
DLSEDIFFYA NLHTGEFSFE KPILKTMTRG GILSDEMGLG KTISTLALIS TVPYDSEAIG
KKLFKTETAL SDTDETFKRR PYASKTSLVV VPMSLLNQWS DEFQKANASS TMYSEVYYGG
NVTNLKKLLT QVKNPPTIVF TTYGIVQNEW SKLLKEHKDK DMSEPTTGLF SLDFYRIVID
EGHIIRNRSA ATSKAIMNLS SKCRWVLTGT PIINRLDDLY SLVKFLALEP WSQIGYWKAF
VSTPFENKNY KQAFDVVNAI LEPVLLRRTK QMKDTNGKPL VELPPKEIRV EKLKLNKSQE
GVYKLLLDRA ESSVRSGLAR GDLLKKYSTI LVHILRLRQV CCDVRLIGTQ DENDEDLLNS
NSFFSQASDN DIMLKDALSE SYECNFTQED LDAAISRLQE KYTKKEQLKS LECSICTTEP
IKFEKLIFLE CGHPYCEGCL AEYFEYQKQK KLNSKCPNCR LTISSNRLLT VDRNGISDNI
TFIQYNNNPK SAKIAALLRH LQQLQDSSSG EHVVVFSQFS SYLDILEREL SEFLPAKTTK
IYKFDGRLSL KERSTILSDF QVKDFAKQKI LLLSLKAGGV GLNLTCASHA FMMDPWWSPS
MEDQAIDRIH RIGQQNSVNV TRFIIENSIE EKMLRIQERK RTIGEAMDAD EDERRKRRIE
EIKMLFE
//
