ID A0A2K1R017_9PEZI Unreviewed; 763 AA.
AC A0A2K1R017;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Alpha-1,3-mannosyltransferase MNN14 {ECO:0008006|Google:ProtNLM};
GN ORFNames=CAC42_364 {ECO:0000313|EMBL:PNS20637.1};
OS Sphaceloma murrayae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS20637.1, ECO:0000313|Proteomes:UP000243797};
RN [1] {ECO:0000313|EMBL:PNS20637.1, ECO:0000313|Proteomes:UP000243797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS20637.1,
RC ECO:0000313|Proteomes:UP000243797};
RA Cheng Q.;
RT "Draft genome sequence of a variant of Elsinoe murrayae.";
RL Submitted (JUN-2017) 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:PNS20637.1}.
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DR EMBL; NKHZ01000022; PNS20637.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1R017; -.
DR STRING; 2082308.A0A2K1R017; -.
DR InParanoid; A0A2K1R017; -.
DR OrthoDB; 1385692at2759; -.
DR Proteomes; UP000243797; 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:0006486; P:protein glycosylation; IEA:InterPro.
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:UP000243797};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 55..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 85601 MW; DE9A1B110DB7AEDB CRC64;
MSRSDPSSPS SIPFKEDMYR LYAKRRRQPR WVRVFLAALV VTFIYLVVIN TGSHPTSWST
GRVAIPKTDP RPPAVEEQGL NTRGTVKADQ VPLADHPRSD RSPKSEEVEQ SGDQDIPSGR
EPRSKPHRTK ESGSEVKDDS TRKLESDLKH VFAIMPDELH LRELLRPIQN SGKERLREIG
LRARAFRTFL EAWEEVHFVH GKNTITIRDD IVNYLSKAKD LSAVSTSRTR ADIIRSYENF
RYFLTKMSDL LFPWTAPYFA DHMTLHASLR YGGRGIVLSG GDGQLSYLLT SVKAIRKLGC
NLPIEVMYLG DDDLGDDSRS ELEALPGVIT RDMEQMVRDE GWQLKGWAGK PFAILLSSFR
EVIFIDADAQ FFLTPEVLFE DEAYEENGAL FFRDRLMFPE SKRKWLQQIL PKPMSRNVRS
SRFWTGESGH MQESGVVVVD KWRHFMALLM VTRMNGPDRD GDKDKGIVGT YDMVYGDKET
FWLGWELVGD SDYAFHPGNA GNMGVAHESI KEAMKNVGKG DDEEETAPEE SPDLYAKEDP
PATEDSKAGQ KDSLAAEAKP APSDKTKDGE KEPPTEKKAA DGTTSPEKPT KADQDSPLAD
GPLGDKLTPE TSDSPAADEA ASVPKVRRKR ATIPGRDEEG AKTNRPLADD VEMGALPVPG
RNYTICAPQL LHLGRDGRPL WFNGWILDNK FDQDHAKVSK FEVFMSELKA GADSADWKLE
QNNMCCLESD KINTFTKQEK QVLKDIVRLA GESGGLGKKH RAR
//
