ID A0A2T2P8I2_CORCC Unreviewed; 1115 AA.
AC A0A2T2P8I2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN ORFNames=BS50DRAFT_193050 {ECO:0000313|EMBL:PSN73678.1};
OS Corynespora cassiicola Philippines.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Corynesporascaceae; Corynespora.
OX NCBI_TaxID=1448308 {ECO:0000313|EMBL:PSN73678.1, ECO:0000313|Proteomes:UP000240883};
RN [1] {ECO:0000313|EMBL:PSN73678.1, ECO:0000313|Proteomes:UP000240883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philippines {ECO:0000313|EMBL:PSN73678.1,
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; KZ678129; PSN73678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T2P8I2; -.
DR STRING; 1448308.A0A2T2P8I2; -.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 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; 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; PTHR46594; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR46594:SF4; P-TYPE CATION-TRANSPORTING ATPASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000240883};
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 427..448
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 455..474
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 494..513
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 682..704
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 724..752
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1049..1072
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1078..1099
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 217..278
FT /note="HMA"
FT /evidence="ECO:0000259|Pfam:PF00403"
FT REGION 137..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1115 AA; 121863 MW; 39C5B68054C398FD CRC64;
MDRPGCCSSD GHIQKAHRQE LNTELEEYRS HCTWEGPGQT FLLPTTHTIN STESHITGQT
QGRGFIGNFP GAITALSIPK SSEDSTQVST VPCTEISSNS CNYEEDPALC CDRTHRTQSP
SMSSLIDSTS LLTGIYKHPN QHTHEGSHAH EGQHVHGPSD DVALLEGEPR PPSRFSSTCC
AHTQKVCGSR LNDTGLSPLS PSVYNAVDPP EGCERIVLTI SGLKCGCCET GISRAVSLTP
AVLSYQVNVV LARVEIDLDT NRSSVAELIK KLNGSTGYTF EQYIQPQGQT LELLVADSTE
IQNAGMPYGV THIETGKRKT WRLTSWRGRQ KVVPMEKIAR NTAQSIRSPP TDSKKRKVEK
SAQDAEEKDT GSLILQHTVR IHYDALKIGA RDVFEYFVQL APGQVLKLAS PAAEPSIANG
VKATKRALAV FLVSVVLTIP VLVLTWCPGI DHGKLIYAHP SLALATLVQF IAIKEFVPGA
LRSLIHSFLF EMDFLIAIST TIAYVFSVIC YVFRIKGKPL ETGSFFETST LLVTLILLGR
LIGEYARLSA ARSVSFRSLQ ADEAHILLSA DNSGPLRRTR KIDARLLQYG DRFLVQRHSR
IVTDGEVIYG GSEVDESMIT GESLKVVKGL GQKVYAGTDN GDGMLVVKLT KLPHENSISR
IATLVENAEL TKPKTQALAD RIAGWFVPVV ALIGVSVFLI WLAVERFHNL REPRSSIVRA
MTYAISTLIV SCPCAIGLAV PMVVLIAGGV AARYGIIFRD PRKIEIARSI TDVVFDKTGT
LTTGVLEVVE GQFHTSDQVN ASASKGMLLG LLKENDHPVA EAVRIWLERE AKKDKSIRPW
EIVDRRTIPG CGIVGICKAS DLEIRAGNPQ WLNVAALESG HTLFCMTIEL PSEIVRQSIV
GNSSVSLPGK PSVIAATIRL QDQAQNTAST VVNLLKQRNI NVHMISGDGE GSVNELAHTL
GIPKQMTRFR HRPGQKQKYV KELQNNGGVV MFVGDGLNDA VALRQADVGV HINKGHEIAK
SASDVILMTT RLQDILILLD ISHAAYRRII LNFGWSALYN VLAILMAAGV FIKFRILPAF
AGLGELVSVL PVVLIAFTMR FYDYGRDYRE VTETS
//