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Database: UniProt
Entry: A0A1M8A4N6_MALS4
LinkDB: A0A1M8A4N6_MALS4
Original site: A0A1M8A4N6_MALS4 
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
//
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