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Database: UniProt
Entry: A0A2T2P8I2_CORCC
LinkDB: A0A2T2P8I2_CORCC
Original site: A0A2T2P8I2_CORCC 
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
//
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