ID R9XJS3_ASHAC Unreviewed; 1232 AA.
AC R9XJS3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=AaceriAGL041Cp {ECO:0000313|EMBL:AGO13827.1};
GN ORFNames=AACERI_AaceriAGL041C {ECO:0000313|EMBL:AGO13827.1};
OS Ashbya aceri (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=566037 {ECO:0000313|EMBL:AGO13827.1, ECO:0000313|Proteomes:UP000016920};
RN [1] {ECO:0000313|Proteomes:UP000016920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; CP006026; AGO13827.1; -; Genomic_DNA.
DR AlphaFoldDB; R9XJS3; -.
DR HOGENOM; CLU_001771_0_2_1; -.
DR OrthoDB; 5480493at2759; -.
DR Proteomes; UP000016920; Chromosome VII.
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; 1.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 1.
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; 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:SF32; COPPER RESISTANCE P-TYPE ATPASE (EUROFUNG); 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
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; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
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 460..484
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 504..522
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 556..577
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 592..609
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 749..777
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 797..820
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1142..1163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1169..1194
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 273..340
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 1232 AA; 135028 MW; 7BE91A52B819CE00 CRC64;
MESMGNMSEL ILNIMISNIH CEQCEVHLKS VLSNFFYLDG NEDAHKTVSE SGNGWHGHIG
IRGLFLFQKR HKLTVSQWST NTSLGLVTLR VPIKAGNEKD FKSKFESTYY SVLKRELKRA
GFDVYHMKVT CTLSDEEMRN EEGASNLAET NRKISTKLKR AHLAYCNSCL EAAKYSSSSE
STEPTKPELY RATFSLSQPV FNGNIGSSVK AVIRTALKTS SEDEHETEIS DEGKISVLIS
NKLYAQRVVD ALRDNDFQAQ LVDIKPIVNE LKYKITAIIG GITCASCCSS ITKATSKLEF
ISDVAVNAIT KTGVFISDMN DEKAINRLKE VIEECGFEFE LVGSPEQVSH DSVLAERRVV
TIEVEGMYCQ NCPQRVVSSL QNYSKARIQV NQAPTLNKPY LTFSYTPDES NGTTIRALLE
HVRTAISPTD SNYDLNVKIV EGSSLDKRLK AINDKERKSV LRCLIFTIIV AIPTFVFGIV
GMSLLPSEHK FRKWLEEPLW VNNVPRVIWI LLMLSTPVYF SVAEQFHAKA CRELHFLWVR
QKSWTARLCR FGSMNLLISL GTSVAYFASI LLLILSAHKK EATDHKGSAD TYFDSVVFLI
LFLLIGRLLE SISKAKMVET LEGLTSLKQR TGILLQVNGT DGLTKETSVS AEMLELGDYI
LIKPGTTPPV DALIAEGESQ FDESPLTGES TPITHLVGDQ IFAGTVNVGQ CAVIAKVSTA
PGNSLLDHVI SAVRDGQLRR APIERIADVL TGYFVPCIVL LAIITWAIWL ILGYAGALAP
EKLDGSTGGW PFWSLEFAIA VFVIACPCGI GLAAPTALFV GANIAAKYGI LARGGSAAFQ
MGSKVTTVCF DKTGTLTKGC APEVTDYSLY PDTHIHAILG KALHDLGLAS KHPLSRAMKD
FALKIFGGDL ADVSVLNIKE IPGRGMTGII KPSSDQSSSL SDSMIPSEIV VGNERFMAEN
GCQLSPHQQN LLYSWKIEGR SIIIVAMKFP EGTTTVSFMP VLLMAVQDEL RPEAKEVIQI
LHDRGIECWM ISGDNELAAN AVAREIGIKN VIADVLPEGK AEKIQWIREA SHCNGAIAMV
GDGMNDAPAI AAADVGISLA SGSDLAMISC DFVLLSKKNP LAAIVILLQL SKKVFRRVKF
NFVWALIYNI ICIPIAAGVL YPYKETRLSP VWASIAMAAS SVSVVLSSIL LRLYRPSKIA
AQLQGSPQIT SRSHIRRQKW PDGAFLSAEQ QV
//
