ID A0A2T2NMD5_CORCC Unreviewed; 1155 AA.
AC A0A2T2NMD5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Heavy metal translocatin {ECO:0000313|EMBL:PSN66601.1};
GN ORFNames=BS50DRAFT_600319 {ECO:0000313|EMBL:PSN66601.1};
OS Corynespora cassiicola Philippines.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Corynesporascaceae; Corynespora.
OX NCBI_TaxID=1448308 {ECO:0000313|EMBL:PSN66601.1, ECO:0000313|Proteomes:UP000240883};
RN [1] {ECO:0000313|EMBL:PSN66601.1, ECO:0000313|Proteomes:UP000240883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philippines {ECO:0000313|EMBL:PSN66601.1,
RC ECO:0000313|Proteomes:UP000240883};
RX PubMed=29551995; DOI=10.3389/fmicb.2018.00276;
RA Lopez D., Ribeiro S., Label P., Fumanal B., Venisse J.S., Kohler A.,
RA de Oliveira R.R., Labutti K., Lipzen A., Lail K., Bauer D., Ohm R.A.,
RA Barry K.W., Spatafora J., Grigoriev I.V., Martin F.M., Pujade-Renaud V.;
RT "Genome-Wide Analysis of Corynespora cassiicola Leaf Fall Disease Putative
RT Effectors.";
RL Front. Microbiol. 9:276-276(2018).
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; KZ678135; PSN66601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T2NMD5; -.
DR STRING; 1448308.A0A2T2NMD5; -.
DR Proteomes; UP000240883; Unassembled WGS sequence.
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:0005507; F:copper ion binding; IEA:InterPro.
DR CDD; cd00371; HMA; 4.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 4.
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; IPR006122; HMA_Cu_ion-bd.
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 NCBIfam; TIGR00003; copper ion binding protein; 3.
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; 3.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00942; CUATPASEI.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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; 4.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 4.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Ion transport {ECO:0000256|ARBA:ARBA00022796};
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 Reference proteome {ECO:0000313|Proteomes:UP000240883};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT TRANSMEM 363..385
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 397..417
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 438..459
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 648..670
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 690..712
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1039..1062
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1068..1089
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 2..68
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 99..165
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 188..254
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 271..337
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 1155 AA; 122506 MW; D3608BBB1B0F7C64 CRC64;
MATTTLKVEG MTCGACTSAI ESGFQGVNGV GNVSISLVME RAVIQHDPNT ITADQVKEII
EDRGFDAEVL STDLPMVHDV DDHFLSDSDD EDEVAGQTST TTLSVEGMTC GACTSAIEGA
FKDVAGIKSF SISLLSERAV IEHDPSIIPP EKLAETIEDV GFDAAVLDTV VAAPQKKAGK
SRNKSKSMTT TVAVEGMTCG ACTSAIESGF KDVEGVYQFN ISLLANRAVL VHDPSKLTEE
QIVEIIEDRG FDAKVISSVD GSVQQSSSAN NAIHLKVYGL PNSTAASELE ALLRKRPGIT
NATVNFSTSR ATIHREQQIV GLRAIVEAIE AAGYNALVSD SDDNNAQLES LAKTKEIQEW
RHAVKFSACF AVPVFLISMF IPMFLPFLDF GSFRIFPGLY LGDVICLVLT LPVQFGIGKR
FYVSAYKSLS HGAPTMDVLV VLGTSAAFFF SIASMLVSIC MPPHSKPTTL FDTSTMLITF
VSLGRYLENS AKGQTSKALS NLMSLAPSMA TIYADPIAAA KAAEGWDVTE EKAERSSMEG
NAIEERTIAT ELIEVGDVVI LRPGDKIPAD GTVTRGESYV DESMVTGEAM PILKKKGVPL
VAGTVNGAGR LDFAVTRAGR DTQLSQIVRL VQEAQTSRAP IQRLADTVAG YFVPIILTLG
LATFVAWMVL SHVLPYPPKV FLDHASGGKL MVCLKLCIAV IVFACPCALG LATPTAVMVG
TGVGARMGIL VKGGAALETA TKINHIVFDK TGTLTIGKMS VSKADIQGEW AQAGYKKDLW
WTLIGLAEMG SEHPIAKAIV ASAKEHLRVG SDGTLDGSVG DFEAVVGKGI AATVEAALSR
ERQRYRVLIG NAAFLLSEGV NVPDLMEEPL TPSAPRDEPS GGVRSAGITT IHTAIGKTYT
GTLGLSDTIK PSARAAVLAL QRLGISSSIV TGDMASSAMV VASQVGIEPV DVHASATPSD
KKAIVADLQS RGYIVAMVGD GINDSPALAS ADIGIALSTG TDVAMEAASI VLMSSTDLLA
IPASLILSRY IFNRIKMNLA WACMYNFIGL PFAMGFFLPW GLSLHPMAAG AAMASSSVSV
VLSSLHLNFW RRPKWLKVSV LDPSATVPEN ERGAEELDER GVIGTFIDWI KETIAARRRN
REEAGYVPLR DMGDA
//
