ID C5PA94_COCP7 Unreviewed; 477 AA.
AC C5PA94;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Mannosyltransferase {ECO:0000256|RuleBase:RU363075};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU363075};
GN ORFNames=CPC735_008290 {ECO:0000313|EMBL:EER26656.1};
OS Coccidioides posadasii (strain C735) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=222929 {ECO:0000313|EMBL:EER26656.1, ECO:0000313|Proteomes:UP000009084};
RN [1] {ECO:0000313|EMBL:EER26656.1, ECO:0000313|Proteomes:UP000009084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-
CC (1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = a
CC dolichyl phosphate + alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-
CC Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + H(+);
CC Xref=Rhea:RHEA:29539, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:12630, Rhea:RHEA-COMP:12631, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:132519,
CC ChEBI:CHEBI:132520; EC=2.4.1.261;
CC Evidence={ECO:0000256|ARBA:ARBA00034020};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + alpha-D-Man-(1->2)-
CC alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-
CC Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-
CC diphosphodolichol = a dolichyl phosphate + alpha-D-Man-(1->2)-alpha-
CC D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-
CC (1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC alpha-D-GlcNAc-diphosphodolichol + H(+); Xref=Rhea:RHEA:29531,
CC Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527, Rhea:RHEA-COMP:12628,
CC Rhea:RHEA-COMP:12629, ChEBI:CHEBI:15378, ChEBI:CHEBI:57683,
CC ChEBI:CHEBI:58211, ChEBI:CHEBI:132516, ChEBI:CHEBI:132517;
CC EC=2.4.1.259; Evidence={ECO:0000256|ARBA:ARBA00033991};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363075}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477,
CC ECO:0000256|RuleBase:RU363075}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 22 family.
CC {ECO:0000256|ARBA:ARBA00007063, ECO:0000256|RuleBase:RU363075}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EER26656.1}.
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DR EMBL; ACFW01000030; EER26656.1; -; Genomic_DNA.
DR RefSeq; XP_003068801.1; XM_003068755.1.
DR AlphaFoldDB; C5PA94; -.
DR GeneID; 9694284; -.
DR KEGG; cpw:CPC735_008290; -.
DR VEuPathDB; FungiDB:CPC735_008290; -.
DR HOGENOM; CLU_018152_0_0_1; -.
DR OrthoDB; 162888at2759; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000009084; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052926; F:dol-P-Man:Man(6)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052918; F:dol-P-Man:Man(8)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR InterPro; IPR005599; GPI_mannosylTrfase.
DR PANTHER; PTHR22760:SF2; ALPHA-1,2-MANNOSYLTRANSFERASE ALG9; 1.
DR PANTHER; PTHR22760; GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF03901; Glyco_transf_22; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU363075};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU363075,
KW ECO:0000313|EMBL:EER26656.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363075};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EER26656.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU363075};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU363075}.
FT TRANSMEM 22..41
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 47..65
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 77..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 115..132
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 144..163
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 244..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU363075"
SQ SEQUENCE 477 AA; 53744 MW; FDB4CA209F2D0B9F CRC64;
MALAFTCTMC ETRLYSVISR TLNPRIGVLF LMIMLFSPGM FHASTALLPS SFAMYTSMLG
LSAFLDSRRG LQTARGIMWF GIGALIGWPF AGALVVPFVL EELVLGIIFQ EAQPVFSRIF
SGIARCLGVL LLEVAVDSFF YRKLVVVPWN IVAYNVFGGA GKGPDIFGTE PWTFYARNLL
LNFNIWFVLA LSSGPLLALQ ALFRPHKTSK ETLLRSITYL FPFYLWLGIF TFQPHKEERF
MYPAYPFLAL NAAIGLHILL AYLGSNNRQE LVGRIPVKLK FAVIISAALF GLNLGLLRIV
GMTTAYNAPL KVFGDLEQPN ITSTGDFVCV GKEWYRFPSS FFLPDNLRAK FVRSEFKGLL
PGEFVESKKS GPFTGTWMVP SGMNDMNQED VSKYTDISQC DFLVDSYFLG DRESDLQPHY
ILDDKMWEKV SCKPFLDSGR TGALGRILWV PDLPFIPKNM QRKYGQYCLL KRRAVNV
//
