ID A0A1M8A4N6_MALS4 Unreviewed; 1537 AA.
AC A0A1M8A4N6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Cation-transporting ATPase {ECO:0000256|RuleBase:RU362082};
DE EC=7.2.2.- {ECO:0000256|RuleBase:RU362082};
GN ORFNames=MSYG_1700 {ECO:0000313|EMBL:SHO77359.1};
OS Malassezia sympodialis (strain ATCC 42132) (Atopic eczema-associated
OS yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=1230383 {ECO:0000313|EMBL:SHO77359.1, ECO:0000313|Proteomes:UP000186303};
RN [1] {ECO:0000313|Proteomes:UP000186303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42132 {ECO:0000313|Proteomes:UP000186303};
RX PubMed=28100699; DOI=10.1093/nar/gkx006;
RA Zhu Y., Engstroem P.G., Tellgren-Roth C., Baudo C.D., Kennell J.C., Sun S.,
RA Billmyre R.B., Schroeder M.S., Andersson A., Holm T., Sigurgeirsson B.,
RA Wu G., Sankaranarayanan S.R., Siddharthan R., Sanyal K., Lundeberg J.,
RA Nystedt B., Boekhout T., Dawson T.L. Jr., Heitman J., Scheynius A.,
RA Lehtioe J.;
RT "Proteogenomics produces comprehensive and highly accurate protein-coding
RT gene annotation in a complete genome assembly of Malassezia sympodialis.";
RL Nucleic Acids Res. 45:2629-2643(2017).
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}.
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DR EMBL; LT671822; SHO77359.1; -; Genomic_DNA.
DR STRING; 1230383.A0A1M8A4N6; -.
DR VEuPathDB; FungiDB:MSYG_1700; -.
DR OMA; FSCFQYM; -.
DR Proteomes; UP000186303; Chromosome 2.
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: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; 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; 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; 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|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|RuleBase:RU362082};
KW Reference proteome {ECO:0000313|Proteomes:UP000186303};
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 381..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 553..572
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 760..780
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 792..821
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1293..1311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1317..1336
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1357..1378
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1404..1423
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1435..1453
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT TRANSMEM 1473..1493
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362082"
FT DOMAIN 365..499
FT /note="P5B-type ATPase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12409"
FT REGION 28..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1537 AA; 170513 MW; EB3DFBEA2B543C0F CRC64;
MGAPVGRSRE RPMELAEEQY QAPFTDRLSR TNSDAQVSVT SSSVSSSFFD EHERRDAEAY
LHEAAQEGDV DNAPVRTRRR RDSQVGSYDD TNTIFDGPSA EFVPSSVSSM HHYMARPSFP
SYSRSKRRQS LSRTSRSRLP GSSVHSYGRS SRNPSPSSAH THESGRSPPS SVISYRKRTY
PRAMVRPHDQ AGQDGHPASS SLIGSLFSGF RGEAGDEADE PLRLSNGDDD RHSWTEDASD
LLDESAVDDD MEDALLDDAS DRSSRSSVPR GSPTHHFVPN FFDVDPFPEE RVDGQEESTA
PPFDDPAMPP KPVHLRDYPG LTESLLEDNA DTPRGLLGAA EEPPRYSVWL DKTCRSKQQI
YLIDEDTLIR VSGYKTRPGR YIAFIVACVL TLGLVGLLSL WFPRWRMRYI WEASDFADAE
FVMVENQYGD LSQESFISVP FARPLSSVFP PSSCDPPCTH AQAQAMMHGE VSNEPAAQEA
ETLVDLILFE YRYQRFLLHP PSGRFRTIQD WRDTAWTSTH TMRQGIMSDL ERERQVFFGP
NVIEIAGKST AELLVGEVLH PFYMFQLVSI VLWSLDDYFY YAFCIAAMSV GSILSTLVET
KKTIARMREM NRFVCAVRVL RDGAWVWADS SELVPGDVYD ASDAGLSVLP ADSVLLSGDA
IVNESMLTGE SVPISKQPLD DRVVQTLKTT HSDLATHLAK HFLFAGTKVV RIRPVLGGNG
TDEAVAKAMV VRTGFNTTKG SLVRGMLFPK PMGFKFYRDS FRFIGFLGCI ALVGLCFNTV
KFVQLGIAWS TLIIRVLDLV TVVVPPALPA TMSIGTAFAI ARLRQRGVFC ISPTRVNMGG
KVNVVCFDKT GTLTEDGLDV LGARTVDPTT GQFSELHQTV DEIPTTEQGP LPLLHALTTC
HNLKVVDGEV IGDPLDVKMF EYTHWHIDEG EGLDAVHALH GRERPPALVQ TVVRPPGGPA
FDAAQAYDEA PHFLELGVIR TFEFVSALRR MSVIVKQLHS SSMEIFVKGA PEALVDICDR
SSLPADFDDL LSYYTQHGYR VIACAGKSLT GLGWVEAQRM TRAEAESDLQ FLGLIVFENK
LKAGSAPAIS TLRHAHIGCK MVTGDNPRTA VSVARECGIL GPSTTVFLPT FAHGSPEQPN
DVVLDWTSTD DEGIKLHPDT LKPLDRDPMQ VDLLDYELAV TGDVFRWMTD YAPIELVRRM
LIKGTIFARM SPDEKHDLVN RLQELGYTVG MCGDGANDCG ALKAADMGIS LSEAEASVAA
PFTSTRPDIS CVIEVIKEGR AALVTSFSCF KYMALYSLIQ FTSITILYNL ASSLGDFQFL
YIDLFMILPV AVAMARTRPY PTLHTKRPTA NLVSKKVLLS MLGQVIICSL FQALTFWLTR
RQPWYEPPSV NPDELNVVSA ENSALFLVSS FQYLTVAAVF SVGPPFRQPM YTNPMLVGSL
TVLSLFSLFF LFVRSGFFFE LMGLVHFPAI FHWQLLALVV LNTAACFLFE SYLTSPTLQL
IKWLQRIHRG KRHDKLRKPH QKTYKAVLLS MNDPAVA
//