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Database: UniProt
Entry: S9XBL7_SCHCR
LinkDB: S9XBL7_SCHCR
Original site: S9XBL7_SCHCR 
ID   S9XBL7_SCHCR            Unreviewed;       507 AA.
AC   S9XBL7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Uroporphyrin methyltransferase {ECO:0000313|EMBL:EPY51201.1};
GN   ORFNames=SPOG_02378 {ECO:0000313|EMBL:EPY51201.1};
OS   Schizosaccharomyces cryophilus (strain OY26 / ATCC MYA-4695 / CBS 11777 /
OS   NBRC 106824 / NRRL Y48691) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=653667 {ECO:0000313|EMBL:EPY51201.1, ECO:0000313|Proteomes:UP000015464};
RN   [1] {ECO:0000313|EMBL:EPY51201.1, ECO:0000313|Proteomes:UP000015464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OY26 / ATCC MYA-4695 / CBS 11777 / NBRC 106824 / NRRL Y48691
RC   {ECO:0000313|Proteomes:UP000015464};
RX   PubMed=21511999; DOI=10.1126/science.1203357;
RA   Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA   Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA   Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA   Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA   French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA   Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA   Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA   Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA   Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA   Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT   "Comparative functional genomics of the fission yeasts.";
RL   Science 332:930-936(2011).
CC   -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC       {ECO:0000256|RuleBase:RU003960}.
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DR   EMBL; KE546991; EPY51201.1; -; Genomic_DNA.
DR   RefSeq; XP_013023774.1; XM_013168320.1.
DR   AlphaFoldDB; S9XBL7; -.
DR   STRING; 653667.S9XBL7; -.
DR   EnsemblFungi; EPY51201; EPY51201; SPOG_02378.
DR   GeneID; 25036702; -.
DR   eggNOG; KOG1527; Eukaryota.
DR   HOGENOM; CLU_011276_11_1_1; -.
DR   OMA; EDLNWSA; -.
DR   OrthoDB; 296644at2759; -.
DR   Proteomes; UP000015464; Unassembled WGS sequence.
DR   GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0019354; P:siroheme biosynthetic process; IEA:InterPro.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:InterPro.
DR   CDD; cd11642; SUMT; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR000878; 4pyrrol_Mease.
DR   InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR   InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR   InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR   InterPro; IPR006366; CobA/CysG_C.
DR   InterPro; IPR012066; Met1_fungi.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR003043; Uropor_MeTrfase_CS.
DR   NCBIfam; TIGR01469; cobA_cysG_Cterm; 1.
DR   PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR   PANTHER; PTHR45790:SF6; UROPORPHYRINOGEN-III C-METHYLTRANSFERASE; 1.
DR   Pfam; PF13241; NAD_binding_7; 1.
DR   Pfam; PF00590; TP_methylase; 1.
DR   PIRSF; PIRSF036555; SUMT_yeast; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF75615; Siroheme synthase middle domains-like; 1.
DR   SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
DR   PROSITE; PS00840; SUMT_2; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU003960};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015464};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT   DOMAIN          265..470
FT                   /note="Tetrapyrrole methylase"
FT                   /evidence="ECO:0000259|Pfam:PF00590"
SQ   SEQUENCE   507 AA;  55477 MW;  E2B35732806C3EE8 CRC64;
     MLISTSLENA AAIVIGSGKS ACKRVDLCLS KGVSKVVWFC GSTSTGGFDL GPFQENKLTI
     DKVHLVPICS FDPSTSLFTL GNALTSYIID IVFITDTKFP LNEKIYDLCK RNRIPVNIVD
     CPSLCSFTLP ACWSEPPLQI ALSTTSNGCR IAQRLLRHVV SSLPPGIGEA VRRFGVARSS
     TKNPQKRQWI NHVSDFWPLE KLIRMSEEDI LSVISDDYML PLTSSEPSFT GSSRTSMSSQ
     EDLTKEKVSL PLDPNEFPTN KKGSIVLVGS GPGDPELLTI AARNAIQKAD YLLADKLVPE
     SVLKLIPRHT PLFIARKFPG NADKAQDELH EIALDALKRG DYVVRLKQGD PYIYGRGGEE
     VLFFHKHGYV PKVIPGISSA LMAPVSAGIP ITQRGVADQF LVCTGTSQKG AMPVIPPFVA
     SQTAVFLMAL HRLDILVDAL LQNGWPKDLP VCIAERVSCP DQRFIFSTLE MVVEVYNTYE
     SLPPGLLITG YSCQALSEVP LVSRFSH
//
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