ID A0A0V0VFK7_9BILA Unreviewed; 1347 AA.
AC A0A0V0VFK7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=P-type Cu(+) transporter {ECO:0000256|ARBA:ARBA00012517};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
DE Flags: Fragment;
GN ORFNames=T09_9686 {ECO:0000313|EMBL:KRX62215.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX62215.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX62215.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX62215.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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:KRX62215.1}.
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DR EMBL; JYDN01000040; KRX62215.1; -; Genomic_DNA.
DR Proteomes; UP000054681; 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:0140581; F:P-type monovalent copper transporter activity; IEA:UniProtKB-EC.
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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 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; 2.
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; PR00943; CUATPASE.
DR PRINTS; PR00942; CUATPASEI.
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; 4.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 3.
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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
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 504..525
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 545..564
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 576..601
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 769..794
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1203..1225
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1237..1258
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 92..158
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 173..239
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 316..382
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 414..480
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX62215.1"
SQ SEQUENCE 1347 AA; 147770 MW; 7339E025C0A9D55E CRC64;
LLGIHIKYNV IMLNVKKHCL LLSIFCFDEL VELSSSSSLN NILMSTEGIV FVEWTSDRVC
EVLHLSDTLC VKDLMSILTK FCSSVVLEDS YLAVKLVISG MTCQSCASAV KRTLLALQGV
YKVKVVVEEK CAYVAYNINH IDVLQMVQSI EEAGFSIVKT NISNLEHLSP SVKECNLNVV
GMTCKSCEMN LSKALLSRLP LLKATFSAVT NSGIVLYDAQ RCTAHQIIDA INDMGYEASI
STEESSTRKG AREENSFEVD YLGIGSSRKS LNVKKNKFEN NIISKRKLSS STAVHIDMQK
LQARMFVGDG QQQEFERCTL AIEGMTCASC VANIERNLMN VDGISKVLVS LIAGKADVTY
DATVIFPSQI VNFVEDMGFA CKLMEESTAT KRKLELMVEF VYYLNRIDKF EYYNLCLKQI
VGMTCTSCVH RIERNVKNLR GVVDAEVTLT NSSGVFIYEP NQCTPRSIMK CIEDLGYSCS
LLSKENRSAA LSHNHDISRW KKSFLISLLF GLPVMAVMVY YHWILHTMDK PENQWHVIPG
LSFDNLLLFL LCTPIQFLGG RYFYVKSYKA FKHCTANMDV LIVLATTISY IYSVIVLIAA
VLSKWSISPM TFFDVPPMLL MFISLGRWLE SIAKAKTSEV LSKLMTLQAK DATIVQLGNN
NEILSEASID LELVQIGDYL KVVPGAKIPV DGKVIFGSSS ADESYITGEP LPVTKAPGST
VIGGSVNLNG NLIIEATHAI QDSTLAQIVK LVEEAQTSKA PIQHLADKIA SYFVPGVILI
ASLTWIVWLI IGFIDVDIIR NSFGGHCMFL EPVHQNHSVH SSDAHADHIQ NLELIFKFAF
DCAITVLAIA CPCSLGLATP TAVMVGTGVG AKNGILIKGG EPLELAHKIT TIIFDKTGTV
TQGKPKLTKI CLFVNEIDIS LHYLLAIIGT AESNSEHPIA EAITAHVKQF LKTERFGVCK
LFQTSPGHGV RCIVSDVEMM MQKSEKLAEK GNVSFLNDVE VVNYNFGLPP SSCNEQILEE
GSNREWEVLI GNRKWLDKHG IQITNEVDGV MSSEEQMGRI AVLVAINGKV VSVFSVADCV
KAESALAVYS LQKMGLKTIL LTGDNCRTAA ATAKQIGISV VFAEVLPNHK KIKVEQLQRR
NEVVAMVGDG INDSPALAAA DVGIAIAAGA DVAIESASIV LIKNNLLDVV AAIDLSQKTT
RRIWINFLFA SIYNLLSIPV AAGAFRTIGF GLQPWMAAAA MALSSVSVVT SSLMLKLYNK
PTVESLTTAD FANHISRLRS AHYGSIEVHR GLEEFKPRKK RSPSASIQSK ILSLIRSVDQ
NNTSHTCEPT LQQGLLSSDS MDDDMQI
//
