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CHO2_PARBA
ID   CHO2_PARBA              Reviewed;         979 AA.
AC   C1GZK1;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 2.
DT   25-MAY-2022, entry version 59.
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=PAAG_03945;
OS   Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides
OS   brasiliensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-826 / Pb01;
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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; KN294000; EEH42024.2; -; Genomic_DNA.
DR   RefSeq; XP_002794352.2; XM_002794306.2.
DR   AlphaFoldDB; C1GZK1; -.
DR   SMR; C1GZK1; -.
DR   STRING; 502779.C1GZK1; -.
DR   EnsemblFungi; EEH42024; EEH42024; PAAG_03945.
DR   GeneID; 9097550; -.
DR   KEGG; pbl:PAAG_03945; -.
DR   VEuPathDB; FungiDB:PAAG_03945; -.
DR   eggNOG; ENOG502QRGH; Eukaryota.
DR   HOGENOM; CLU_005987_0_0_1; -.
DR   OMA; DWVGLYM; -.
DR   OrthoDB; 170424at2759; -.
DR   UniPathway; UPA00753; -.
DR   Proteomes; UP000002059; Partially assembled 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..979
FT                   /note="Phosphatidylethanolamine N-methyltransferase"
FT                   /id="PRO_0000405901"
FT   TOPO_DOM        1..89
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        111..113
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        135..199
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        221..227
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        228..248
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        249..281
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        282..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        303..304
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        326..398
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        399..418
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        419..422
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        423..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        446..474
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        475..494
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        495..499
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        500..520
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        521..565
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TRANSMEM        566..586
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   TOPO_DOM        587..979
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03217"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          704..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        713..729
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   979 AA;  110825 MW;  06E5437C136FF2E4 CRC64;
     MSGPASSTGF HIHAEGLHER NVQPSKPTSD GGVAPKALDD KSRVEEDERT DSEKKTFGRT
     PGGTIFTVPP TRDMVSQLLS PSEPKNLSDI FVLAIISCHI FLLRFLPSSF RVAAFAIIFL
     FWRAAYNIGI GWLLHMQSNG RTLVCWAKKS NIFVNPSTGR NPHPVLYNLL KWELETKIPE
     QYSFEDAPTE YNTWLVFRRV VDLILMCDFT SYCLFAIACG GRPAGEGFIM LALRWITGMS
     LVLFNLWVKL DAHRVVKDFA WYWGDFFYLI DQDLTFDGVF EMAPHPMYSV GYAGYYGISL
     MAASYKLLFI SILAHAAQFA FLVLVENPHI EKTYNAPPPR KRVAVDTDNV KPQDDDVSQD
     SSVINDNEYS GKAVATLEPS SMHNLLGPHN FDLYRITDSS VLLIQILFSA LAILTPSTPV
     YQFFFVLNAA LWRVWYSVGI GYILNRQSHC KMWTRHFVKY GESNQEAWQQ WKGTYHLSMT
     MTYASFIAAT WKMYSFPQDW GYGLVLLRHI LGASLIALQI WTSASIYESL GEFGWFFGDF
     FFDQSPKLTY SGIYRYLNNP ERVLGLAGVW GAVLITSTKS VISLALLSHT LTIAFIQLVE
     RPHMQKLYGQ SLRRDAGLVR SLKRSLPPSL KQFHGSVDKI LDDSIEFIEE FIEAARPKLA
     AGVKTFVKDT SALFQKYPAR ITISRLEPDL AGYDQKDYSI SLEGTQSSEP AQFERASDKE
     GEKARSMPDR RGEQVNLMFE YGAPIKVKWT APLNHSKKDW IGLYMVTDNT SREITRISSQ
     GRWIGTNKAS FDSLTCEQGL ISSDIVINKF REDGEPKDVA SGEMVFSGDK LWWTQGVFEF
     RYHHNGKHNV MAVSRPFEIR IGRFDDDAIY GDRYGLVRAA IESALLPVVQ NCFDRDPDIA
     PQTVEEQYGS LVDRNGKYSR RVVFAVHQMF GIEFAPEVVR ADGNVRNLAW RICNAKKVLA
     PYSMSRTNGA TTPTAEHES
 
 
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