ID W9XVV8_9EURO Unreviewed; 747 AA.
AC W9XVV8;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Alpha-1,3-mannosyltransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O3_05382 {ECO:0000313|EMBL:EXJ84712.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ84712.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ84712.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ84712.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the MNN1/MNT family.
CC {ECO:0000256|ARBA:ARBA00009105}.
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:EXJ84712.1}.
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DR EMBL; AMGY01000004; EXJ84712.1; -; Genomic_DNA.
DR RefSeq; XP_007733697.1; XM_007735507.1.
DR AlphaFoldDB; W9XVV8; -.
DR STRING; 1182542.W9XVV8; -.
DR GeneID; 19169497; -.
DR eggNOG; ENOG502RZ48; Eukaryota.
DR HOGENOM; CLU_021103_0_0_1; -.
DR OrthoDB; 1385692at2759; -.
DR Proteomes; UP000019478; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR GO; GO:0043934; P:sporulation; IEA:UniProt.
DR InterPro; IPR022751; Alpha_mannosyltransferase.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR31392; ALPHA-1,3-MANNOSYLTRANSFERASE MNN1-RELATED; 1.
DR PANTHER; PTHR31392:SF1; ALPHA-1,3-MANNOSYLTRANSFERASE MNN1-RELATED; 1.
DR Pfam; PF11051; Mannosyl_trans3; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000019478};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 54..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 747 AA; 84941 MW; 773E69CF1B763010 CRC64;
MFTPRHAPLK EGRSFPGLPY AGPSRRALRS RQGALLLLVL ICVPLIYFLS SSPSTSTSDA
LLQSPAPDSI RPPSSEPREP GRDDPEVALK PNPNEHQQAP SIDPVGADLI DVHSPAGGRP
PFEAPPVEAP VQRPKAPAPA AGEVEDQDQE RFSPNDHDRS DPAKSRYQQS PSWGKPASDE
SFSFSERRRF ERALTRVINL LPGEMEGRDL LRQVEGTGKE KLREMGLRVR EYKKFFEAWE
DLHLTSDEEG GTYVRDDVIQ YLRHHVHQPS SDELSETGFA QTVHSYEAYR YFLVKFGQLL
FPWTAPYFPD HMTLHSHFKR GGRGIVLTAG DDQAPFLLTT IPTFRKLGCD LPIEVMYLGD
SDLSEDYRAD LEALDGVITR DIAQMVNDEG WKLAGWAAKP FAILFSSFRE CIFIDADSLF
FRNPEILFDD PGYQQTGALF FRDRLIMPEN KKRWLQQILP KPISRQVKQS RFWTGDSGHM
QESGVVVVDK WRHFMALLLV TRMNGPDRDG NKDEGRVGVY DMVYGDKETF WIGWELVGDM
DYSFHQGDAG AMGVVQEAPV KEEDKKKKEE EKKGPKEEEK KEKPPRRKKK EPKPVVINEN
GEVVEGDAFG DGQEGHEQGH EQHEDGTEEF EEFEQQEEPP EEKKPEPSSY TMCAPQLLHL
DLDGKPLWFN GWLLDNKFAD KKQKKFAKFE HYLIEPRDVR EPGAWQLEES NMCCLTTDAP
LKRDFTLEEK AVLDMMIKSA RDAGITG
//
