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Entry: A0A4D9EBF6_9SAUR
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ID   A0A4D9EBF6_9SAUR        Unreviewed;      1541 AA.
AC   A0A4D9EBF6;
DT   03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   03-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE            EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
GN   ORFNames=DR999_PMT09585 {ECO:0000313|EMBL:TFK07537.1};
OS   Platysternon megacephalum (big-headed turtle).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Testudinoidea; Platysternidae; Platysternon.
OX   NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK07537.1, ECO:0000313|Proteomes:UP000297703};
RN   [1] {ECO:0000313|EMBL:TFK07537.1, ECO:0000313|Proteomes:UP000297703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DO16091913 {ECO:0000313|EMBL:TFK07537.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TFK07537.1};
RA   Gong S.;
RT   "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:TFK07537.1, ECO:0000313|Proteomes:UP000297703}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DO16091913 {ECO:0000313|EMBL:TFK07537.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:TFK07537.1};
RA   Gong S.;
RT   "The genome sequence of big-headed turtle.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC       {ECO:0000256|ARBA:ARBA00004166}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004166}. Membrane
CC       {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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TFK07537.1}.
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DR   EMBL; QXTE01000082; TFK07537.1; -; Genomic_DNA.
DR   STRING; 55544.A0A4D9EBF6; -.
DR   Proteomes; UP000297703; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005802; C:trans-Golgi network; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00371; HMA; 6.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 6.
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; 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; 4.
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; 6.
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; 6.
DR   SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 5.
DR   PROSITE; PS50846; HMA_2; 6.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, 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   Kinase {ECO:0000313|EMBL:TFK07537.1};
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|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000297703};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000313|EMBL:TFK07537.1};
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        722..741
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        761..783
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        795..821
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        827..848
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        991..1015
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        1035..1058
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        1404..1426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          124..190
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          209..275
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          320..386
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          423..489
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          556..622
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          632..698
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          45..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1509..1541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1517..1531
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1541 AA;  165907 MW;  78FE40209904DF52 CRC64;
     MKRESDSDLK RDQSTLATLN NKNVTLVTFH KRQSSNAVPA LLIVSEPSKS GSPGKAGDCS
     QKEEKVSQSY SVGASEVNSM HALSKSSSPA SCVREPIMKQ NFAFDNIGYE GSAENMPSLL
     PQTSTVTVNI LGMTCQSCVQ SIEGRISKVK GIVSIKISLE QSNAVIKYIQ SEIGPQEICQ
     EIGEMGFDAS IAEGRTTASP VRSTSLGEAL MKLRVEGMTC QSCVNTIEGK IGKLHGVLRI
     KVSLSNQEAV IAYQPYIIHP EDIKNHIDNM GYESTIKSKL APLKLGMIDL ERLQTTSTKK
     TPASLNNSNV EPVVGKMNST TMTLGVEGMH CKSCVKNIEG NISGLPGIHS IKVSLEHKNA
     VVQFNPNVIT PVSLQQAIEA LPPGNFKVSL PNGVEANNGE LLSKAAFSSP QFRSTSSGDQ
     LTSTSVLSID GMTCGSCVQS IEGTMSQRKG VQHISVSLAE RTGTIHYNSA VTNSEELRGA
     IEDMGFDASI LTDTTTWKYM DQPLFRDAVI QPNAWESASQ RTENVSESSH QGYYSDVQPK
     NSYLGSPKPP SLATTEKCFM QITGMTCASC VSNIERNLQK EDGIVSVLVA LMAGKAEIKY
     KPESIQPLEI VQLIQNLGFN ATVIEDHTAT DGNVELIITG MTCASCVHNI ESKLTRTNGI
     FYASVALATS KAHIQFDPEI IGPRDIIQII EGIGFHASLA KRDPNAHNLD HKKEIKQWRK
     SFLCSLVFGI PVLILMIYML IPDGQQHSTM VLEQNLIPGL SILNLLFFVL CTLVQFLGGW
     YFYVQAYKSL KHKTANMDVL IVLATTIAYI YSCVILVVAI AEKAEESPVT FFDTPPMLFV
     FISLGRWLEH IAKSKTSEAL AKLMSLQATE ATIVTLGPDH SVIREVQLAV ELVQRGDIVK
     VVPGGKFPVD GKVIEGSSMA DESLITGEAM PVTKKPGSTV IAGSINAHGS VLVNATHVGS
     DTTLAQIVKL VEEAQMSKAP IQQLADKFSG YFVPFIIIIS TVTLLVWITI GFINFDVVQK
     YFPHQNKHLS KAEVILRFAF QTSITVLCIA CPCSLGLATP TAVMVGTGVA AQNGILIKGG
     KPLEMAHKIK TVMFDKTGTI TCGVPKVIRM LLLGDMAKLS LKKVLAIVGT AEASSEHPLG
     MAVTKYCKEE LGTESLGYCT DFQAVPGCGI SCKVRSVEAV LGQSEQSVNE QNAYLSSVSM
     ISLGHSSSIM VSESDGAAAP LTYSVLIGNR EWMRRNGLLI SSDVNDAMTG HEMKGQTAIL
     VAIDGALCGM IAIADTVKQE AALAVHTLQN MGIDVVLITG DNRKTAKAIA TQVGIKKVFA
     EVLPSHKVAK VQELQNEGKK VAMVGDGVND SPALAGADIG IAIGTGTDVA IEAADVVLIR
     NDLLDVVASI HLSKRTVRRI RINLVLALIY NLLGIPIAAG VFMPIGIVLQ PWMGSAAMAA
     SSVSVVLSSL QLKCYKKPGT ERYEAKAQGH MKPLTPSQIS VHIGMDDRRR DSPRPTAWDQ
     ISQVSLSSLT SNKLPGHGGF REEEGGKWSL LTNNRDEEQY I
//
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