ID M7TVE0_BOTF1 Unreviewed; 428 AA.
AC M7TVE0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 03-MAY-2023, entry version 27.
DE SubName: Full=Putative initiation-specific alpha mannosyltransferase protein {ECO:0000313|EMBL:EMR85235.1};
GN ORFNames=BcDW1_6230 {ECO:0000313|EMBL:EMR85235.1};
OS Botryotinia fuckeliana (strain BcDW1) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=1290391 {ECO:0000313|EMBL:EMR85235.1, ECO:0000313|Proteomes:UP000012045};
RN [1] {ECO:0000313|Proteomes:UP000012045}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BcDW1 {ECO:0000313|Proteomes:UP000012045};
RX PubMed=23704180; DOI=10.1128/genomea.00252-13;
RA Blanco-Ulate B., Allen G., Powell A.L., Cantu D.;
RT "Draft genome sequence of Botrytis cinerea BcDW1, inoculum for noble rot of
RT grape berries.";
RL Genome Announc. 1:E0025213-E0025213(2013).
CC -!- SIMILARITY: Belongs to the glycosyltransferase 32 family.
CC {ECO:0000256|ARBA:ARBA00009003}.
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DR EMBL; KB707917; EMR85235.1; -; Genomic_DNA.
DR AlphaFoldDB; M7TVE0; -.
DR STRING; 1290391.M7TVE0; -.
DR HOGENOM; CLU_022381_0_0_1; -.
DR Proteomes; UP000012045; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000009; F:alpha-1,6-mannosyltransferase activity; IEA:InterPro.
DR GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:UniProt.
DR Gene3D; 3.90.550.20; -; 1.
DR InterPro; IPR007577; GlycoTrfase_DXD_sugar-bd_CS.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR039367; Och1-like.
DR PANTHER; PTHR31834; INITIATION-SPECIFIC ALPHA-1,6-MANNOSYLTRANSFERASE; 1.
DR PANTHER; PTHR31834:SF8; TRANSFERASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G14040)-RELATED; 1.
DR Pfam; PF04488; Gly_transf_sug; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000313|EMBL:EMR85235.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transferase {ECO:0000313|EMBL:EMR85235.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 317..428
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 428 AA; 49546 MW; 0403E3025BBA0494 CRC64;
MYRQISCQYQ TFFLSFITIF LLIIVAIQHE EISSKRKLTI STKSSNSSVV ISAPLATYSS
EAPGFPRKLW YKVGPQGVSD EAKRFRHHCL DINPGYKYEV LTDAFADEYV WKWFSHRPDI
LNTYFSLNIP ILKADLLRYL ILYADGGVWF DLDVSCEDTP IDNWVLAEHR AANLVVGLEF
DYDYQEDTAM YSQFASWTIM AKPRSPHLMQ VINDILDELN EIARRNDVSI EGIELSMISD
VVDITGPKRM TWGIIKSLKE ILGRELDDRD VGELRSARLI HDVLILPGNA FAGTQNGFKK
EKGKVFVNHH YAGTWKNKFG GEAEKGSEKE KEIEEEKRIE QEMEEKKTEE ERIEQERMEQ
EQKDTEQEHE TEEGNGNEQS KNVEDEKEGK ESKQQETSEH GKKIKENNDT EDKEAKEKED
PEQEKENL
//