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CHO2_BLAGS
ID   CHO2_BLAGS              Reviewed;         977 AA.
AC   C5JCV0; A0A179UAC4;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Phosphatidylethanolamine N-methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217};
DE            Short=PE methyltransferase {ECO:0000255|HAMAP-Rule:MF_03217};
DE            Short=PEAMT {ECO:0000255|HAMAP-Rule:MF_03217};
DE            Short=PEMT {ECO:0000255|HAMAP-Rule:MF_03217};
DE            EC=2.1.1.17 {ECO:0000255|HAMAP-Rule:MF_03217};
GN   Name=CHO2; ORFNames=BDBG_00845;
OS   Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=559298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SLH14081;
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
CC   -!- FUNCTION: Catalyzes the first step of the methylation pathway of
CC       phosphatidylcholine biosynthesis, the SAM-dependent methylation of
CC       phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine
CC       (PMME). {ECO:0000255|HAMAP-Rule:MF_03217}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-
CC         methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine +
CC         H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03217};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_03217}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03217}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03217}.
CC   -!- SIMILARITY: Belongs to the class VI-like SAM-binding methyltransferase
CC       superfamily. CHO2 family. {ECO:0000255|HAMAP-Rule:MF_03217}.
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DR   EMBL; GG657448; OAT04249.1; -; Genomic_DNA.
DR   RefSeq; XP_002629599.1; XM_002629553.1.
DR   AlphaFoldDB; C5JCV0; -.
DR   SMR; C5JCV0; -.
DR   STRING; 559298.C5JCV0; -.
DR   EnsemblFungi; OAT04249; OAT04249; BDBG_00845.
DR   GeneID; 8508161; -.
DR   KEGG; bgh:BDBG_00845; -.
DR   VEuPathDB; FungiDB:BDBG_00845; -.
DR   HOGENOM; CLU_005987_0_0_1; -.
DR   UniPathway; UPA00753; -.
DR   Proteomes; UP000002038; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004608; F:phosphatidylethanolamine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_03217; PEMT; 1.
DR   InterPro; IPR007318; Phopholipid_MeTrfase.
DR   InterPro; IPR016219; Phosphatid-EA_MeTrfase_fun.
DR   Pfam; PF04191; PEMT; 2.
DR   PIRSF; PIRSF000383; PEAMT; 1.
DR   PROSITE; PS51598; SAM_CHO2; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Methyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..977
FT                   /note="Phosphatidylethanolamine N-methyltransferase"
FT                   /id="PRO_0000405870"
FT   TOPO_DOM        1..88
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        89..109
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        110..112
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        134..198
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        220..226
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        227..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        248..280
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        302..303
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        325..397
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        398..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        419
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        441..471
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        472..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        489..498
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        499..519
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        520..562
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        563..583
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        584..977
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          703..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        710..724
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   977 AA;  110820 MW;  291D18F0D86BD1CC CRC64;
     MSEQATSSGL ESRSNGLRER NLQASKSAAD RDVASQSLED KLQVEEGEAD TEKKTFGRTP
     DGTVFTVPPT RDMVSQLLSP SEPKNISDIF VLAILGCHIL LLWFLPSSFR VAAFAVIFLF
     WRASYNIGIG WLLHMQSNGR TLVCWAKKSN IFVNPSTGQN PHPTLYKLLK WELETKISEQ
     YSFEEAPTEY NTWLVFRRVV DLILMCDFTS YCLFAIACGG RPTGESFIML ALRWITGMSL
     VLFNLWVKLD AHRVVKDFAW YWGDFFYLID QDLTFDGVFE MAPHPMYSVG YAGYYGISLM
     AASYKILFIS ILAHAAQFAF LVLVENPHIE KTYNAPPPRK RVADTDTKPQ EDENSHEGSV
     VSDTLSSAPV IPPLQPSSMH SLLGLHNIDL YRSTDQSVLL AQVLFFALTT LTPSTPVYQF
     CFVLNAALWR IWYSVGIGYI LNRQSNCKMW TRHFVKYGES NHEAWRQWKG TYHLSMTMTY
     ASFIAAAWKM YSFPQDWRYG LVLLRHILGA SLIALQIWTS TSIYESLGEF GWFFGDFFFD
     EFPKLTYSGI YRFLNNPERV LGLAGVWGAV LITSTKSVVF LALLSHTLTL AFIQLVERPH
     MQKLYGQSLR RDAGLVRSLK RSLPPSLKQI HGSVDKILDD SFEFIEEFIE AARPKLAAGV
     QTFVKDTSAL FQKYPARVTI SRLEPDLAGY DLKDYSITLE GTQPSRPAQF ERASDKEGER
     ARSMPYRRGE QENLMFEYGA PIKVKWTAPL NHSKKDWVGL YMVTDNTSRE VTRVSSQGRW
     IATNQASFDS ETCEQGLISS DIVLKSSRDD GEPRDVASGE MVFSGDKLWW TQGVFEFRYH
     HNGKHNVMAV SRPFEICIGR FDEDDIEVDN YGLVRAAVEA ALLPVVQNCF DRDPEIAPQT
     VEEHYGCLVD RDGKYSKRVV FAVHHMFGIE FAPEVVRADG NIRNLAWRIC NAKKVLAPYS
     MSRSNGASTP TAAHEED
 
 
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