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Database: UniProt
Entry: A0A168IWP4_MUCCL
LinkDB: A0A168IWP4_MUCCL
Original site: A0A168IWP4_MUCCL 
ID   A0A168IWP4_MUCCL        Unreviewed;       844 AA.
AC   A0A168IWP4;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAD00454.1};
GN   ORFNames=MUCCIDRAFT_147376 {ECO:0000313|EMBL:OAD00454.1};
OS   Mucor lusitanicus CBS 277.49.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=747725 {ECO:0000313|EMBL:OAD00454.1, ECO:0000313|Proteomes:UP000077051};
RN   [1] {ECO:0000313|EMBL:OAD00454.1, ECO:0000313|Proteomes:UP000077051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 277.49 {ECO:0000313|EMBL:OAD00454.1,
RC   ECO:0000313|Proteomes:UP000077051};
RG   DOE Joint Genome Institute;
RA   Corrochano L.M., Kuo A., Marcet-Houben M., Polaino S., Salamov A.,
RA   Villalobos J.M., Alvarez M.I., Avalos J., Benito E.P., Benoit I.,
RA   Burger G., Camino L.P., Canovas D., Cerda-Olmedo E., Cheng J.-F.,
RA   Dominguez A., Elias M., Eslava A.P., Glaser F., Grimwood J., Gutierrez G.,
RA   Heitman J., Henrissat B., Iturriaga E.A., Lang B.F., Lavin J.L., Lee S.,
RA   Li W., Lindquist E., Lopez-Garcia S., Luque E.M., Marcos A.T., Martin J.,
RA   Mccluskey K., Medina H.R., Miralles-Duran A., Miyazaki A., Munoz-Torres E.,
RA   Oguiza J.A., Ohm R., Olmedo M., Orejas M., Ortiz-Castellanos L.,
RA   Pisabarro A.G., Rodriguez-Romero J., Ruiz-Herrera J., Ruiz-Vazquez R.,
RA   Sanz C., Schackwitz W., Schmutz J., Shahriari M., Shelest E.,
RA   Silva-Franco F., Soanes D., Syed K., Tagua V.G., Talbot N.J., Thon M.,
RA   De Vries R.P., Wiebenga A., Yadav J.S., Braun E.L., Baker S., Garre V.,
RA   Horwitz B., Torres-Martinez S., Idnurm A., Herrera-Estrella A.,
RA   Gabaldon T., Grigoriev I.V.;
RT   "Expansion of signal transduction pathways in fungi by whole-genome
RT   duplication.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00037882}.
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:OAD00454.1}.
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DR   EMBL; AMYB01000007; OAD00454.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168IWP4; -.
DR   STRING; 747725.A0A168IWP4; -.
DR   VEuPathDB; FungiDB:QYA_147376; -.
DR   OrthoDB; 1416at2759; -.
DR   Proteomes; UP000077051; Unassembled WGS sequence.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1580.10; paralog of FGE (formylglycine-generating enzyme); 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR024775; DinB-like.
DR   InterPro; IPR019257; MeTrfase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR017805; SAM_MeTrfase_EasF-type_put.
DR   InterPro; IPR005532; SUMF_dom.
DR   InterPro; IPR042095; SUMF_sf.
DR   NCBIfam; TIGR03439; methyl_EasF; 1.
DR   PANTHER; PTHR43397; ERGOTHIONEINE BIOSYNTHESIS PROTEIN 1; 1.
DR   PANTHER; PTHR43397:SF1; ERGOTHIONEINE BIOSYNTHESIS PROTEIN 1; 1.
DR   Pfam; PF12867; DinB_2; 1.
DR   Pfam; PF03781; FGE-sulfatase; 2.
DR   Pfam; PF10017; Methyltransf_33; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077051};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          57..369
FT                   /note="Histidine-specific methyltransferase SAM-dependent"
FT                   /evidence="ECO:0000259|Pfam:PF10017"
FT   DOMAIN          437..575
FT                   /note="DinB-like"
FT                   /evidence="ECO:0000259|Pfam:PF12867"
FT   DOMAIN          618..736
FT                   /note="Sulfatase-modifying factor enzyme"
FT                   /evidence="ECO:0000259|Pfam:PF03781"
FT   DOMAIN          770..842
FT                   /note="Sulfatase-modifying factor enzyme"
FT                   /evidence="ECO:0000259|Pfam:PF03781"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   844 AA;  97476 MW;  65B91D4AC840031B CRC64;
     MSYRAPSPPS TGYSIIDIRG PLYGGKNDTQ DVTARPPSPQ ASDNSEDAFN GSDLVNTILD
     SLDKPANHKS IPTYILYDKK GLQLFDQITQ LDDEYYLTGA ELDILIRRSE EMVDRLQDGS
     VIFELGAGAL RKTQVILRAI EKKKVHVTYY ALDLDQHELD KSLASLGEFQ YVQLHGLLGT
     YDQGIPWVSK HFTNSNIQKN FLWMGSSIGN QNRLESAMFL RKLQRMCMEP GDLFVIGFDK
     RNDPEKIELA YDDSRGVTRE FILNGLDHVN RIMGKENFMN RRDFAYHSIY QEKQGRHLSH
     YRALKDIVIS YKTPQKAYSI KIQKDELIHV EHSYKYSLDE IESILTAADL NMVNYWTDSK
     QQYRLVLAEN RPFICYHCNE GQFDLTRAIE SDESATFDYA LNKTWPIETL PSLHEWQELW
     KSWDVVTQQM LNHRKMLFER PIALRHPFIF YLGHIPAFLD IQLSRHAVDQ DLGPTDLTEP
     ASYADIFERG IDPDLDDPTV CNPHSPVPAN DHEWPAIDSI LAYQKRIRER LQRLLVYWES
     EAFKTQSSNW VDSRQRQARI VWMCFEHEAM HLETLLYMLI QSPNVLPPKG IALPSWKLFM
     RSNALPSLTP LSESPLMKLP GGTISLGHDD HESLDHKSKG HEFGWDNESP ERQVSIAAFD
     IQTRPVTNGE YFQFLQDTQA DFIPASWLKQ DDQIFVKTVF GPCPLAYAQH WPVQTSYKQA
     DLYAQHKGAR LPSEAEMIHF RDTATTEKWP NIGFENWSPT DVSNERVHSL GDVWEWTSTV
     WDAHEGFEAS QLYPGYSADF FDGKHHVVLG GSWATHPRIA ERRSFRNWYQ AGYPYVFSGF
     RLCH
//
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