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Database: UniProt
Entry: I2GX88_TETBL
LinkDB: I2GX88_TETBL
Original site: I2GX88_TETBL 
ID   I2GX88_TETBL            Unreviewed;      1032 AA.
AC   I2GX88;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN   Name=TBLA0A09560 {ECO:0000313|EMBL:CCH58740.1};
GN   ORFNames=TBLA_0A09560 {ECO:0000313|EMBL:CCH58740.1};
OS   Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS   10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX   NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH58740.1, ECO:0000313|Proteomes:UP000002866};
RN   [1] {ECO:0000313|EMBL:CCH58740.1, ECO:0000313|Proteomes:UP000002866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC   UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
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: Membrane {ECO:0000256|RuleBase:RU362081}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000256|RuleBase:RU362081}.
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DR   EMBL; HE806316; CCH58740.1; -; Genomic_DNA.
DR   RefSeq; XP_004178259.1; XM_004178211.1.
DR   AlphaFoldDB; I2GX88; -.
DR   STRING; 1071380.I2GX88; -.
DR   GeneID; 14493476; -.
DR   KEGG; tbl:TBLA_0A09560; -.
DR   eggNOG; KOG0207; Eukaryota.
DR   HOGENOM; CLU_001771_0_1_1; -.
DR   InParanoid; I2GX88; -.
DR   OMA; GGKFMVC; -.
DR   OrthoDB; 5480493at2759; -.
DR   Proteomes; UP000002866; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd00371; HMA; 2.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 2.
DR   Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR   Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR017969; Heavy-metal-associated_CS.
DR   InterPro; IPR006121; HMA_dom.
DR   InterPro; IPR036163; HMA_dom_sf.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR   PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 2.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR   SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF55008; HMA, heavy metal-associated domain; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 2.
DR   PROSITE; PS50846; HMA_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002866};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM        255..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        297..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        336..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        378..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        532..555
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        575..599
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        920..943
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        949..966
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          2..68
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          77..143
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          1013..1032
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          171..198
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1032 AA;  116165 MW;  3B8F33B543BE5657 CRC64;
     MRELILNIGG LTCSSCIKTV TKALNKEPCV TSCNVSLTTC EAIIIYNENK GKINDIIESI
     KKVGFEALKV TDTNLNRINK FSVEGMTCGG CTSKITTKLM SDDDIYRVDV SLITQECEVE
     FNPQAMDSNK IQELIENCGF NCSIIASGDG EIESRLRGGD PMRRTALRIF NFDYYKDVDL
     LKEQLEKLEQ DILIENVDDE RGVIAVQYDS SKIGIRSIFH KVEELGFQVI LDSPFDNSTQ
     IKLLSKIKET KFWKMNCLIS GIFGIILLML YMWIPFLVSR FLIDETFPYN ESLIKGLFYR
     DIFGFLIATY VQFYIGKYFY IKAFNSIKHC NGTMDTLVCI STSCAYIFSV YSIIKNIIIE
     QEIEVVDRAE IVIRLPNVNF TTSIMLFAFI SFGKYLEQKA KSKTSTALKN LMSLTPSSCF
     ILDEEDNMNL KEIPVDLLQD GDLINVSPGM KVPVDGIITY GESEVDESLM TGESVLVKKT
     INDDVIAGSI NGPGTFIFRA THVGDETKLS FIIKTMKQAQ LIKAPIQRYA DYLASLFVPI
     IILLAFLTFC FWFFVSQYYK GDDLPNIFQD EKYGNFYVCL RISISVIVVA CPCALGLATP
     TAVMVGTGMA AENGVLIKGG DKLEIFNKIK TIIFDKTGTI TTGKMKVIEM RFKHSKVEND
     YYGENEYKQN EEYLIKCLIL LTRSSEHPVS KAIYSYLCER YPVRKSGEIE MIESKYSIGN
     GIKGKFEIKG VSEDLVEIGI GQKTLYNNEE EYDDDKENDY TRSYVFLQNK VVAIIELNDQ
     IKRDSYETIE YLKNRNYNVF MISGDNRRAT MKVSEEIGIP IDHVFSEVLP IEKCNIIKDI
     KKNWPGNEYV AFVGDGINDS PSLATSDLGI SISSGTDVAI DTADIVILSN EESNSNTTIK
     EVCYALDISK ATFATIKRNL FWATIYNILM IPISMGALSH WGITLDPMLA GLAMAMSSVC
     VVLSSLRLKR WKPPVIGEEN ALTSKDDLVV FGTWGNYLRH KLGTSWAHLR RAMGSSHQGR
     PRDPEAQLEL IG
//
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