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Database: UniProt
Entry: A0A3B3TD30_9TELE
LinkDB: A0A3B3TD30_9TELE
Original site: A0A3B3TD30_9TELE 
ID   A0A3B3TD30_9TELE        Unreviewed;      1265 AA.
AC   A0A3B3TD30;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Probable cation-transporting ATPase 13A3 {ECO:0000313|Ensembl:ENSPKIP00000040211.1};
OS   Paramormyrops kingsleyae.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC   Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX   NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000040211.1, ECO:0000313|Proteomes:UP000261540};
RN   [1] {ECO:0000313|Ensembl:ENSPKIP00000040211.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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   AlphaFoldDB; A0A3B3TD30; -.
DR   STRING; 1676925.ENSPKIP00000040211; -.
DR   Ensembl; ENSPKIT00000021229.1; ENSPKIP00000040211.1; ENSPKIG00000017263.1.
DR   GeneTree; ENSGT00940000155941; -.
DR   Proteomes; UP000261540; Unplaced.
DR   GO; GO:0016020; C: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:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015662; F:P-type ion transporter activity; IEA:InterPro.
DR   CDD; cd07542; 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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR047819; P5A-ATPase_N.
DR   InterPro; IPR047821; P5B-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:SF12; POLYAMINE-TRANSPORTING ATPASE 13A3; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF12409; P5-ATPase; 1.
DR   PRINTS; PR00119; CATATPASE.
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; 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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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        34..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        245..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        423..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        462..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        939..964
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        976..996
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1008..1027
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1081..1099
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1111..1131
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1151..1171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..161
FT                   /note="P5B-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12409"
FT   DOMAIN          187..237
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00690"
FT   REGION          1051..1071
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1232..1265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1265 AA;  140942 MW;  4DE3EADB5AD06354 CRC64;
     MEKERWREME KVGFQLVNRG EEEEMEVCGF VPSPWRICLL VLGCVLSGGL LALLLLWVPQ
     WSVRWACVPA PLPQASVLLL RTTDEFGRYF RVRIKTLQIP HMDPPGMGVA SEGAGGVARD
     GAGGVAREQA ITEDCGKGPQ EHALYWEVRC FHLQSVTYMW NSEARSYQPL DTLDHGIPIA
     NFYSLHSRGL SASRQENRRL FYGINQIEVK VPSVPNLLVK EVLNPFYIFQ VFSVILWSLD
     DYYYYASAIF LMSLLSVCTS LYTVRKHYIL LHDMVSAHNV IRCSVYRGDQ EVEEILSTDL
     VPGDVIIIPS NGMMMPCDAA LIGGTCIVNE SMLTGESVPV TKTQLPLPPS GGDDDRLQEP
     AYDPEEHRRH TLFCGTQVIQ TRYYSGESVK AVVVRTGFST VKGQLVRSIL YPKPSNFQLY
     RDAVRFLLGL VCVAAVGVAY SIYTSASQGE SVGRIVLEAL DIITITVPPA LPAAMTAGIV
     YAQHRLRRTG IFCTSPHRIN TCGQVNLVCF DKTGTLTEDG LDLWGIQRVE DSRFTPPEQE
     MAEDVQAPSH FLVAMASCHS LTRIEGRLAG DPLDIKMFEA TGWDLEEPSP DETSNHDLIM
     PTVVRPAKPP PGRSPPCQEI DQDIRELMGR YEVGVLAQFP FSSTLQRMSV VTRVLGERRL
     QAYLKGAPET VVSLCQPDTV PPDFWEVLDS YTRQGLRVIA LAHRQLEPKF TWHRLHITNR
     EAIECEMKFL GLLMLQNKLK PQTVPVLAEL HQAHIRTIMV TGDSMLTAVS VARECGLIPP
     HTQVIITEAQ PSHEGQPATV SWSYSQDSPY PMLPPGETQV SLGTQQNPPR TSYHFAMSGR
     TFAIILEHFS ELLPKLLLCG TVYARMAPDQ KTQLVEELQK VDYYVAMCGD GANDCGALKR
     AHAGISLSEL EASVASPFTS RTPDISCVPH LIREGRAALV TSFCVFKFMA LYSIIQYLCV
     LLLYSILSNM GDSQYLFIDI AIIMSLAFTM SLSPAWKQLV AQHPPSTLLA PPLLLSVVGQ
     ILLALSFQTA TFLLADIYAQ NETQPSDWLV GNTTGMTTNG SRPVSDKDEK DSDNIENLQN
     TSLFFVSGCQ YLTVALVFNR GPPFRQPLYT NYLFMLCIVF CYGFLIVNLL HPVPALQDFF
     QLVFIPMEWR VTLLGLIIAN LILAFTLESF ITDFKDLWNR SFARQKLDEP HPDSLCPQME
     VDGIPSPSRA CCCHSSEPPR ARYQRLAQQL LLDPDWPPPP STKAKPPTRV DSGAVQGLVP
     QTTPL
//
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