ID H2AV82_KAZAF Unreviewed; 175 AA.
AC H2AV82;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 22-FEB-2023, entry version 50.
DE RecName: Full=Bis(5'-adenosyl)-triphosphatase {ECO:0000256|ARBA:ARBA00014605, ECO:0000256|RuleBase:RU366076};
DE EC=3.6.1.29 {ECO:0000256|ARBA:ARBA00012377, ECO:0000256|RuleBase:RU366076};
GN Name=KAFR0E01280 {ECO:0000313|EMBL:CCF58282.1};
GN ORFNames=KAFR_0E01280 {ECO:0000313|EMBL:CCF58282.1};
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:CCF58282.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF58282.1, 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 -!- FUNCTION: Cleaves A-5'-PPP-5'A to yield AMP and ADP. Can cleave all
CC dinucleoside polyphosphates, provided the phosphate chain contains at
CC least 3 phosphates and that 1 of the 2 bases composing the nucleotide
CC is a purine. Is most effective on dinucleoside triphosphates.
CC Negatively regulates intracellular dinucleoside polyphosphate levels,
CC which elevate following heat shock. {ECO:0000256|ARBA:ARBA00025241}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(3)-bis(5'-adenosyl) triphosphate = ADP + AMP + 2
CC H(+); Xref=Rhea:RHEA:13893, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58529, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC EC=3.6.1.29; Evidence={ECO:0000256|ARBA:ARBA00001475,
CC ECO:0000256|RuleBase:RU366076};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936,
CC ECO:0000256|RuleBase:RU366076};
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DR EMBL; HE650825; CCF58282.1; -; Genomic_DNA.
DR RefSeq; XP_003957417.1; XM_003957368.1.
DR AlphaFoldDB; H2AV82; -.
DR STRING; 1071382.H2AV82; -.
DR GeneID; 13882861; -.
DR KEGG; kaf:KAFR_0E01280; -.
DR eggNOG; KOG3379; Eukaryota.
DR HOGENOM; CLU_056776_7_2_1; -.
DR InParanoid; H2AV82; -.
DR OrthoDB; 1365844at2759; -.
DR Proteomes; UP000005220; Chromosome 5.
DR GO; GO:0047710; F:bis(5'-adenosyl)-triphosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR CDD; cd01275; FHIT; 1.
DR Gene3D; 3.30.428.10; HIT-like; 1.
DR InterPro; IPR039383; FHIT.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR PANTHER; PTHR46243; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR PANTHER; PTHR46243:SF1; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR Pfam; PF01230; HIT; 1.
DR SUPFAM; SSF54197; HIT-like; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|RuleBase:RU366076};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU366076};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220}.
FT DOMAIN 3..115
FT /note="HIT"
FT /evidence="ECO:0000259|PROSITE:PS51084"
FT COILED 139..166
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 96..100
FT /note="Histidine triad motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00464"
FT ACT_SITE 98
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-1"
FT BINDING 28
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 91..94
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-2"
FT SITE 115
FT /note="Important for induction of apoptosis"
FT /evidence="ECO:0000256|PIRSR:PIRSR639383-3"
SQ SEQUENCE 175 AA; 20627 MW; 5A7BE248E443A597 CRC64;
MTKPIYFSRF VVSDQVFYRS KYSYALVNLR PIVPGHVLVV PYNTNVITLS QLSRDESIDY
FQTIQLIQSF ITWKYKSDAM NVAIQDGPEA GQSVPHLHTH LIPRFKQNNV GDKIYNMLND
WDARRDEYLK EQIVFKPDDQ RIERSMETMR NEAEELNKSI GEFIKTFPEL TSKWI
//
