ID V5EXE9_KALBG Unreviewed; 1242 AA.
AC V5EXE9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=PSEUBRA_SCAF21g03360 {ECO:0000313|EMBL:EST07114.1};
OS Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST07114.1, ECO:0000313|Proteomes:UP000019377};
RN [1] {ECO:0000313|Proteomes:UP000019377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA Goldman G.H.;
RT "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT high producer of endo-1,4-xylanase isolated from an insect pest of
RT sugarcane.";
RL Genome Announc. 1:E0092013-E0092013(2013).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|RuleBase:RU362082};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU362082}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362082}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type V subfamily. {ECO:0000256|ARBA:ARBA00006000,
CC ECO:0000256|RuleBase:RU362082}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362082}.
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DR EMBL; KI545864; EST07114.1; -; Genomic_DNA.
DR RefSeq; XP_016292103.1; XM_016436404.1.
DR AlphaFoldDB; V5EXE9; -.
DR STRING; 1365824.V5EXE9; -.
DR eggNOG; KOG0208; Eukaryota.
DR HOGENOM; CLU_001828_5_0_1; -.
DR OMA; FSCFQYM; -.
DR OrthoDB; 6047at2759; -.
DR Proteomes; UP000019377; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140358; F:P-type transmembrane transporter activity; IEA:InterPro.
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; 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; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
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; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF12409; P5-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, ECO:0000256|RuleBase:RU362082};
KW Magnesium {ECO:0000256|RuleBase:RU362082};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362082};
KW Metal-binding {ECO:0000256|RuleBase:RU362082};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362082};
KW Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU362082};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362082};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362082}.
FT TRANSMEM 295..312
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 434..453
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 640..660
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 672..700
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1192..1214
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 278..362
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT DOMAIN 400..454
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00690"
FT REGION 1..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..176
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1242 AA; 137742 MW; 8794591B76D4D617 CRC64;
MTEPDRSRRG GQSSSKSKQH FEVAADEYQA PFQLPAKKSE AISASSERSV SPDSVAGRRK
PASQRSGSTY HFGRRKRVPE DADLTGTSQP KGMLGSILAS IRGDRGDDDN DDARSRRSFS
RPLLSRRRSS QSNISSRAGR SDAGDEDEDE DYDNTRGWSD DDYGFDDEDD DDSYRSSDDD
ASNRNGILPS AFGTLSGAVD PVFGDTRFST DHPPEDELDA ELAGRDLETG EPSGFGRSEG
DVNARGRTSG QSVEAARTEL SYLDKSSKSR QQVYLMEEDT LIRFTGYKTL VGKQVIYTIV
CCLTLGIVYL IGRWLPRFRL KYVCKETEFE KAEFIMIENQ WGDLHKEKID TIPFARPLAT
TEQLMELTFF DFRYTRYALH PPTGRFRMIK DWRDPLWTSL AAINNGISFD AEKDRSTIFG
KNAIEIQAKS TWQLLVDEVL HPFYMFQIVS IILWSFDNYY YYAFCIAVIS LVSIFTTLLE
TRQTVNRMRE MSRFSCDVRV LREGNWQVLD SNDLVPGDVY DVAEPGLLLF PADSVLLSGD
AIVNESMLTG ESVPVSKIPL TTPSMVGLHA AGTEVTADLA KHFLFSGTRI IRIRGSGSTD
KNEAGAKAMV VRTGFNTTKG ALVRSMLFPK PMGFKFYRDS FRFIGFLAMI AGIGFLFAAV
NFVKMGIAWH TIVIRALDLI TVVVPPALPA TMSIGISFAI NRLRKVGIFC ISPNRVIIGG
KVDVFCFDKT GTLTAEGLDV LGTRTIDLKA GRFSELHESV DEMPVGAGTK SDADARKMPL
LYALATCHSL KVVDGEVIGD PLDVKMFEHT GWTLDEGKDR SAKATTKTGT AKNGKSKLTE
RPPALVQTVV RPPGGQAFEV EDAIKSGRHA HFLELGVLRT FEFVSSLRRM SVIVKRLKSQ
SMEVFVKGAP EVMADICDKD TFPADYDDLL SYYTKHGYRV IACAGKSMAG MSWIKAQRMR
REQAESGLRF LGLIIFENKL KEGSAPAIEV LKNANIVTKM VTGDNPRTAI SVARECGMVG
QSAHVFMPTF VEGDQRSPRA VIDWSSVDDD RIKLDPYNLQ PREVDPHVLD LEEFDFQDYQ
LALTGDVFRW MIDFAPIETV RRMLIKGTIF ARMSPDEKHE LVERLQAMSY TCGFCGDGAN
DCGALKAADI GISLSEAEAS VAAPFTSNRG DISCVLDTIA EGRAALVTSF NCFSYICLTS
LIQFSSVLLM YSIGSSLGDW EFMYLDFACL FLSVFSARTG PP
//
