ID T1G799_HELRO Unreviewed; 968 AA.
AC T1G799;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN Name=20216946 {ECO:0000313|EnsemblMetazoa:HelroP89193};
GN ORFNames=HELRODRAFT_89193 {ECO:0000313|EMBL:ESN93246.1};
OS Helobdella robusta (Californian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Rhynchobdellida; Glossiphoniidae; Helobdella.
OX NCBI_TaxID=6412 {ECO:0000313|EnsemblMetazoa:HelroP89193, ECO:0000313|Proteomes:UP000015101};
RN [1] {ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RA Hellsten U., Grimwood J., Chapman J.A., Shapiro H., Aerts A., Otillar R.P.,
RA Terry A.Y., Boore J.L., Simakov O., Marletaz F., Cho S.-J.,
RA Edsinger-Gonzales E., Havlak P., Kuo D.-H., Larsson T., Lv J., Arendt D.,
RA Savage R., Osoegawa K., de Jong P., Lindberg D.R., Seaver E.C.,
RA Weisblat D.A., Putnam N.H., Grigoriev I.V., Rokhsar D.S.;
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ESN93246.1, ECO:0000313|Proteomes:UP000015101}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
RN [3] {ECO:0000313|EnsemblMetazoa:HelroP89193}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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; AMQM01007498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KB097628; ESN93246.1; -; Genomic_DNA.
DR RefSeq; XP_009028643.1; XM_009030395.1.
DR AlphaFoldDB; T1G799; -.
DR STRING; 6412.T1G799; -.
DR EnsemblMetazoa; HelroT89193; HelroP89193; HelroG89193.
DR GeneID; 20216946; -.
DR KEGG; hro:HELRODRAFT_89193; -.
DR CTD; 20216946; -.
DR eggNOG; KOG0208; Eukaryota.
DR HOGENOM; CLU_001828_0_0_1; -.
DR InParanoid; T1G799; -.
DR OMA; FSCFQYM; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000015101; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015203; F:polyamine transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:1902047; P:polyamine transmembrane transport; IBA:GO_Central.
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; 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:SF8; CATION-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR45630; CATION-TRANSPORTING ATPASE-RELATED; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000015101};
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 71..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 297..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 760..781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 787..808
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 820..845
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 872..891
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 903..928
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 940..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 968 AA; 109277 MW; C74F60AD8D9F8284 CRC64;
MINHKYFLHK KIKYIWNDEL QMFQKLRGLD GERFCSQFHL SKGHSQEEES RWRNIYGFNN
IIAHVTPVYK LFLTEALNPF YVFQLFSIIL WYADDYEFYA SCIVITCIIS LGVSVRQTRS
MQRALKHTLS PSEVVSVYRK DIQDFESVTS DILVPGDLIE IPPSGCVMQC DAVLITGNCI
VNESMLTGES VPLTKTPLPG EGVFNSNDHS KHILFCGTHV MQTRYYDNKK VKAVVMRTGF
YTAKGELVRS IMFPKPLDFK FTKDAFKFVG VLALVACIGM IYTIVLMVKK GESLSLIIIR
SLDLVTIVIP PALPAAMTVG IVFAQKRLKQ SQIFCINPSA INLCGAINAF CFDKTGTLTE
EGLDFMCVVP VINGNKFAKE EQQLFKLDKK DPLLVAMATC HSLTIIDGHI VGDPLDLKMF
QATNWDLEES GSDESKYDVM TPTIVHPKNP DIVLPYQVGI LRMFTFSSKM QRMSVVVREL
GCDPVHCFVK GSPEIIVTFC EPSSVPCNFQ EVLMFYTKQG FRVIGFAYKT LYKLSYVKIQ
RMEREAVESN LIFLGLLVLE NRLKPESTSV IRKLKDAHIR TIMVTGDNIL TALSVARDCE
MIEKNDKAVL VSARAPTPSN PVDVEFNLCE DLKHKKVMLD VEQFGMNHLI VDGKSWLNIK
KFYPDILDKL AVRGTVFARF LPEQKQQLIE LLQENGYFVG MCGDGANDCG ALKTAHAGIS
LSEAEASVAS PFTSKQANIS CVLNVMREGR AALVTSFGTF KFMAGYSLTQ FLSVCLLYWI
GANFTDFAFL YIDLVLLTSL GLTFSYTASH WNLGKKPPSV TLIAAPPILS VIFQLVVNLS
FQFLLWRFAS NQPWSVVPFV DHNDRNYRCH EVTLIFAISS FQYITMSIVF TKGSPHRRNI
FSNYVFLVDI IVCFVLSAYL TLCPFPWLQK VLELSLSPSF IFRVLIVATA ILNFMISFIV
EVIFHFLH
//