ID A0A195E2A2_9HYME Unreviewed; 1244 AA.
AC A0A195E2A2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=ALC57_08383 {ECO:0000313|EMBL:KYN19206.1};
OS Trachymyrmex cornetzi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN19206.1, ECO:0000313|Proteomes:UP000078492};
RN [1] {ECO:0000313|EMBL:KYN19206.1, ECO:0000313|Proteomes:UP000078492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN19206.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYN19206.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex cornetzi WGS genome.";
RL Submitted (SEP-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}.
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DR EMBL; KQ979763; KYN19206.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A195E2A2; -.
DR STRING; 471704.A0A195E2A2; -.
DR Proteomes; UP000078492; 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; 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; 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; 4.
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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
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:UP000078492};
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 387..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 431..453
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 465..488
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 657..681
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 702..725
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1097..1122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 1128..1148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 12..78
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 97..162
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 213..279
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 296..362
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KYN19206.1"
SQ SEQUENCE 1244 AA; 135684 MW; DC3290688454163B CRC64;
IPEARQLVEE TNTVKINIKG MTCQSCVTNI ERIIGKRPDV VNLRVILEEK AGYIKYKANE
TTPQILAEAI EEMGFTATPS DESTEYEEKI SSVLSTSICF IHIEGMTCTS CVKNITGALS
KKPSIKNVNI SLKNKEAKIY YSTDLTPNQI AIYIQELGFN AYVKESDDTE RSQSDLVLNK
KKKKKEVEKK KVEKEVVLQA NGAGDIKELS KEQKCFLHVT GMTCGSCVAA IEKHCKKLYG
VNSILVALMA AKAEVTYDPS KIRAGDIASS ISELGFPTTL IEECGSGEGD VELKISLCPF
NIMGMTCASC VNKIESSVKR LPGIRSAMVA LATQRGKFKY DVEKTGIRDI VECINKLGFT
AQLFSNRDKE SRDYLDQKEE ISKWRTAFLV SLIFGVPCMA TMTYFMIVMS YGNKTHEEMC
CIVPGLSWEN LLLLVFSTPV QFFGGWHFYV QAYKALKHCT TNMDVLISMT TTISYLYSIA
VLTAAIIMKE NVSPQTFFDT PPMLLVFISL GRWLEHVAKG KTSEALSKLL SLKATDAVLV
SLGSNNEILS ERLISIDLVQ RGDVLKVVQG AKVPVDGRVL SGQSACDESL ITGESMPVPK
KKGSLVIGGS INQNGPLLVT ATHTGEHTTL AQIVRLVEEA QTNKAPIQHL ADKIAGYFIP
LVIAVSIVTL VIWIIIGYIN VEQLPISHND QINKHGMNRE EIIFQYAFRS ALAVLAIACP
CALGLATPTA VMVGTGVGAL NGILIKGAEP LENAHKVKCV LFDKTGTLTH GTPTVTKIAL
FVEERICSLG KMLLVVGTAE INSEHPIASA IVRFVKETLG LTTTGQYSNF QAVAGCGLKC
KVTHLDGALF EVLKSEQIVN YMNHAYDSPV GTYILNNVPI EAMPIAEITQ EKQNIDLQLL
LSPGMRGDPG DLDDMYEVCI GNREWMRRNA INIPEEVERQ MVNEEDLGHT AVLVSINNML
VAMISVADTV KPEAHLAVYT LKKMGLQVIL LTGDNRKTAA SIAKQVGISK VFAEVLPSHK
VAKIQRLQDQ GLRVAMVGDG VNDSPALAQS DVGIAIASGT DVAVEAADVV LMRNDLLDVI
ACLDLSRKTV CRIRLNFLLA SVYNLLGIPI AAGVFSSFGF FLQPWMSSAA MALSSVSVVG
SSLLLKLYRK PTKATLETSE YTAAMQAHST ARTIELDTIS LHRGLDDSVV PINRSTSTLS
RIFGKSKVEV EGHLLGEETD EIDLAVDFSN YRKNVKNSAD ITSV
//
