GenomeNet

Database: UniProt
Entry: M9M0I4_PSEA3
LinkDB: M9M0I4_PSEA3
Original site: M9M0I4_PSEA3 
ID   M9M0I4_PSEA3            Unreviewed;      1620 AA.
AC   M9M0I4;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=MaoC-like domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PANT_9d00080 {ECO:0000313|EMBL:GAC73385.1};
OS   Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX   NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC73385.1, ECO:0000313|Proteomes:UP000011976};
RN   [1] {ECO:0000313|Proteomes:UP000011976}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX   PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA   Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA   Machida M., Kitamoto D.;
RT   "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT   producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL   Genome Announc. 1:E0006413-E0006413(2013).
CC   -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC       {ECO:0000256|ARBA:ARBA00005005}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Peroxisome
CC       {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {ECO:0000256|ARBA:ARBA00006484}.
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DR   EMBL; DF196775; GAC73385.1; -; Genomic_DNA.
DR   STRING; 1151754.M9M0I4; -.
DR   OrthoDB; 2140828at2759; -.
DR   UniPathway; UPA00659; -.
DR   Proteomes; UP000011976; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008324; F:monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0098771; P:inorganic ion homeostasis; IEA:UniProt.
DR   GO; GO:0030003; P:intracellular monoatomic cation homeostasis; IEA:UniProt.
DR   CDD; cd03448; HDE_HSD; 1.
DR   CDD; cd05353; hydroxyacyl-CoA-like_DH_SDR_c-like; 2.
DR   Gene3D; 1.10.287.4290; -; 2.
DR   Gene3D; 1.20.1510.10; Cation efflux protein transmembrane domain; 1.
DR   Gene3D; 3.30.70.1350; Cation efflux protein, cytoplasmic domain; 1.
DR   Gene3D; 3.10.129.10; Hotdog Thioesterase; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR   InterPro; IPR002524; Cation_efflux.
DR   InterPro; IPR027470; Cation_efflux_CTD.
DR   InterPro; IPR036837; Cation_efflux_CTD_sf.
DR   InterPro; IPR027469; Cation_efflux_TMD_sf.
DR   InterPro; IPR029069; HotDog_dom_sf.
DR   InterPro; IPR002539; MaoC-like_dom.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR   InterPro; IPR002347; SDR_fam.
DR   NCBIfam; TIGR01297; CDF; 1.
DR   PANTHER; PTHR45024; DEHYDROGENASES, SHORT CHAIN; 1.
DR   PANTHER; PTHR45024:SF2; SCP2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00106; adh_short; 2.
DR   Pfam; PF01545; Cation_efflux; 1.
DR   Pfam; PF01575; MaoC_dehydratas; 1.
DR   Pfam; PF16916; ZT_dimer; 1.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SMART; SM00822; PKS_KR; 1.
DR   SUPFAM; SSF160240; Cation efflux protein cytoplasmic domain-like; 1.
DR   SUPFAM; SSF161111; Cation efflux protein transmembrane domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
DR   PROSITE; PS00061; ADH_SHORT; 2.
PE   3: Inferred from homology;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011976};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          806..915
FT                   /note="MaoC-like"
FT                   /evidence="ECO:0000259|Pfam:PF01575"
FT   DOMAIN          1544..1611
FT                   /note="Cation efflux protein cytoplasmic"
FT                   /evidence="ECO:0000259|Pfam:PF16916"
FT   REGION          621..644
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          790..814
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          955..992
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1091..1114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1177..1276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        621..638
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1188..1229
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1620 AA;  172580 MW;  84C36EBD8D075CB8 CRC64;
     MSDFPSTENG KISFKNRVVV VTGAGNGLGR AYALFFASRG AKVLINDLGP SAKDKNKKAA
     DVVVEEIQQA GGEAIANYDS NTDGEKVIQQ AIDKWGRIDI LINNAGILRD KSYFTDDRFF
     AFRTNSFKAM SDKEWDQITA VHITGSYACA KAAWPHMRKQ KFGRIINTSS AAGIYGNFGQ
     ANYAAAKHAM IGFGKTLAIE GAKYNILSNV LAPVAASQLT ATVMPPEMLE NLTPDYVVPI
     VAYLVSAENK EVSGHVFECG AGFFAQVRRE RSRGVVFKTD DSFTPAAVRA KIDEILDFDE
     KPEYPFRITD ANHMEFLERA KEAKSNDQGE GPVRFDGKTV LVTGAGAGLG RAYAHMFGKL
     GANVVVNDFL EKNAAAVVDE IKKAGGKAAP AVGSVEDGEK IVKAAVDAFG SIHVIINNAG
     ILRDKSFAAM SDQEWHAVLN THLRGTYSVC HAAWPIFQQQ KYGRIVNTTS AVGIYGNFGQ
     ANYSTAKAGI IGFTNTLGIE GKKYNILANT IAPNAGTAMT ATIWPQEMVD AFKPDYVAPM
     VGYLASEANE DLTSSLFEVS GGWVAAVRWQ RAGGHSFSHG KPPSPEKIVK KWSKITDYET
     NPSWPTSPSD SLGDIVSNFG QEEEDEDDDD EGGAGGDYSD PEDPEIVQKA KKEPIEDSEF
     SYGERDVILY NLGVGATEKD LDLVFEQDDD FRAVPTFGVI PQFMASGGIP LDWLPNFSPM
     MLLHGEQYLA IKKPIPTSAT LVNKPKLMEV LDKGKAAAVT SVVHTFDKGS GDLVFESQST
     VFIRGSGGFG GKKSGKDRGA ASAANKPPSR KADKVVTEKT TDAQAALYRL SGDYNPLHID
     PSFAQVGGFD KPILHGLCSF GISGKHIFRE YGAYKDIKVR FTGHVFPGET LETSMWKEGN
     KVIFTTRVVE RDTQALGAAA VTLADDTGTR LRWHHSSTHL EALFGSWTCA SDAPPGHHTS
     VTKGPSEDVA HGPTAHPKPS SARVPPPSRC RSPPPIGLLL LLPMRLSSRS RSFLTTTTAG
     KPLRSTPLAL ASIETRASTT RQPRKVVASS TARPQPPVVY ARFKSTHHPA HPTAVPTSPV
     LPKPSHIAST LATEEARPPV AHPQPPPHQG PPRLVRYEAD SHAHPQHPLA LYPSSYSHAS
     YPDPASYRAH LSNRRAPASL FGLFPSTSIT AASVKASSDP HAYPGAGPTI QTSITTPTQA
     TSRPVAIDST APSDAMTASA SSIVDATKSG QAELHQRKKG AAAPASATAA AVATSKHSHS
     HGHHGHHHGH DHGSPEEADK LLAALKGKGD RGSNITLAGL VSNVGLCGAK GVAGVYLNSA
     ALLADAAHSL SDMFADLVTL FCWKMSQKPP SASHPLGYGK YETMGSLGVS LVLVAGAVGI
     GFHSYGLLLE AIQPTLQHAP AAIQALSHFT GSIASAGGLL HDHHDHGAVA HGEGGVLDPN
     AMWFALLSIA VKEWLYHATL KIAREENSSV LEANALHHRS DSLSSAVTFL AIGGSWLGFP
     VLDPLGGLLV AGLIGKQGAD LLIGALGELS DRGVEPEILQ TLDQAIVEVQ KQNPLLLGWK
     DLRAVKSGVS TFADVTLQLP NDATLHTASH IEAQVRAKIT AAVKGVKEVR VRLVTVDATN
//
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