ID A0A0L7QQK9_9HYME Unreviewed; 1167 AA.
AC A0A0L7QQK9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative cation-transporting ATPase 13A1 {ECO:0000313|EMBL:KOC60801.1};
GN ORFNames=WH47_05579 {ECO:0000313|EMBL:KOC60801.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC60801.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC60801.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC60801.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000}.
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DR EMBL; KQ414786; KOC60801.1; -; Genomic_DNA.
DR RefSeq; XP_017794879.1; XM_017939390.1.
DR AlphaFoldDB; A0A0L7QQK9; -.
DR STRING; 597456.A0A0L7QQK9; -.
DR EnsemblMetazoa; XM_017939390.1; XP_017794879.1; LOC108576401.
DR GeneID; 108576401; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000053825; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR CDD; cd07543; P-type_ATPase_cation; 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; IPR006544; P-type_TPase_V.
DR InterPro; IPR047820; P5A-type_ATPase.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR NCBIfam; TIGR01657; P-ATPase-V; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR PANTHER; PTHR45630:SF7; ENDOPLASMIC RETICULUM TRANSMEMBRANE HELIX TRANSLOCASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
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; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053825};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..233
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 954..975
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 996..1017
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1062..1085
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1097..1118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1138..1159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 1167 AA; 130656 MW; F5F21947C47BDFEC CRC64;
MATIASSRVD ELVQTVTLHN PRKLLFTGYI LPFVILHAIW IYSWIFVYGI DEYYDAGLVG
IAAIGVLQIL ICLCCQWSVH IHTFLNCSSE INPYKAKIAK VVPTPNNGSS ELIKLHHSEQ
QEPWFIFQKT KYHWNPDKKS FEGLQFPINH SVKHYCEWNG YLDEKDITAA EDKYGKNKLD
MVVPEFRELF KERAIAPFFV FQVFYVALWC LDKYWYYSIS TLIMLIMFEY TLVQQQLKNM
AEIRKMGNKP YMIMVYRNRR WRSMFTDQLV PGDIVSITRS QNDNLVPCDM LLLRGPCVID
ESMLTGESVP QMKEPIEDVD GHKQLDIEGD GKLHVLFGGT KVVQHSPPSK SMPGLKATDN
GCVAYVLRTG FSTSQGKLLR TILFGVKRVT ANNLEAFGFI LFLLVFAIAA ASYVWIKASE
DPTRNRYKLF LECTLILTSV IPPELPIELS LAVNTSLLAL SKLGVFCTEP FRIPFAGKVE
ICCFDKTGTL TSDNLVVEGI AGIQGKPDVI QISDAPIESI QVLATCHSLV QLDDGIVGDP
LEKATLRAIK WNLTKADSMI PRKGQSPVLK IVQRHHFSSA LKRMAVVAGY TTPGSSEINY
MTTVKGAPEV IKTMLSSVPE NYDSTYLSLS RRGARVLALG YRKISGSLTS QDLRELTRDD
LEKNLIFAGF VIISCPLKPD SEAVIKEIVH SSHSVVMITG DNPLTACHVG RELHFTKKPV
TLILTCYDGE WLWESVDRKI NLPLEMKNVS VRRNEIWREY ALCVTGEGLT YLKDNARELL
RKLLPHVVIF ARCEPKQKEF IIVTLQDLGY TTLMCGDGTN DVGALKHAQV GVAILSSLSD
RISTEKQDNA KHESLISNSA VVNGPRSNPR VPANARAKIQ KILKELEEQS VIVKLGDASI
AAPFTSKMSS IQCICHVIKQ GRCTLVTTLQ MFKILALNAL GLAYSQSVLY LDGIHFSDAQ
ATLQGILLAI CFLFISRSKP LTTLSKQRPL PNIFNLYTIA TVLLQFAVHF VSLVYLVREA
TFLSPKSDKL AAILTPSSNA TNTTMVSIPN LNDEDEPFEP NLLNSTVFII VMAIQISTFA
INYRGQPYME SLLQNKSLLY CLMGSSIVIL GLACGFLPEL ATLFEIVDFP SDFRRLLVQV
LIADFALAYV VDRVCSWLFG EGRYQKL
//
