ID R1FY49_BOTPV Unreviewed; 932 AA.
AC R1FY49;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=precorrin-2 dehydrogenase {ECO:0000256|ARBA:ARBA00012400};
DE EC=1.3.1.76 {ECO:0000256|ARBA:ARBA00012400};
GN ORFNames=UCRNP2_9260 {ECO:0000313|EMBL:EOD44035.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD44035.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family.
CC {ECO:0000256|RuleBase:RU003960}.
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DR EMBL; KB916766; EOD44035.1; -; Genomic_DNA.
DR RefSeq; XP_007588495.1; XM_007588433.1.
DR AlphaFoldDB; R1FY49; -.
DR STRING; 1287680.R1FY49; -.
DR KEGG; npa:UCRNP2_9260; -.
DR eggNOG; KOG1527; Eukaryota.
DR HOGENOM; CLU_313980_0_0_1; -.
DR OrthoDB; 296644at2759; -.
DR Proteomes; UP000013521; 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 GO; GO:0019354; P:siroheme biosynthetic process; IEA:InterPro.
DR CDD; cd11642; SUMT; 1.
DR Gene3D; 1.10.10.2570; -; 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; IPR040666; Atg29_N.
DR InterPro; IPR039362; ATG29_sf.
DR InterPro; IPR006366; CobA/CysG_C.
DR InterPro; IPR028162; Met8_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028281; Sirohaem_synthase_central.
DR InterPro; IPR003043; Uropor_MeTrfase_CS.
DR PANTHER; PTHR45790; SIROHEME SYNTHASE-RELATED; 1.
DR PANTHER; PTHR45790:SF6; UROPORPHYRINOGEN-III C-METHYLTRANSFERASE; 1.
DR Pfam; PF18388; ATG29_N; 1.
DR Pfam; PF13241; NAD_binding_7; 1.
DR Pfam; PF14823; Sirohm_synth_C; 1.
DR Pfam; PF14824; Sirohm_synth_M; 1.
DR Pfam; PF00590; TP_methylase; 1.
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}; NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003960}.
FT DOMAIN 133..159
FT /note="Siroheme synthase central"
FT /evidence="ECO:0000259|Pfam:PF14824"
FT DOMAIN 210..255
FT /note="Siroheme biosynthesis protein Met8 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14823"
FT DOMAIN 273..482
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT DOMAIN 569..628
FT /note="Atg29 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18388"
FT REGION 186..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 101158 MW; 8681F4A73F173BBB CRC64;
MAPALLTAVD SADHVHLIVG SNPLAGARCT RALEVGARPV LIAPEHASVH YGLMKRIDDG
EVSWVKRDFK DDDLTTLGRE EVGHVVDAVF VTLGGKSALS THISTLCRRL RIPVNVADAP
NLCTFTLLST YTDGPLQVGV TTSGKGCKLS ARIRREIAAS LPSDLGQAVD RLGVMRRRIW
EEDHAAELSM DPEAEEDEAG QSATFNKLVT PEDAEAARGR RMRWLAQICE YWPLRRLAGI
TDEDVEAVLR SYSTSDSSGL DPGAVDQRRR RGRIVLAGSG PGNPDLLTRA THKAILSADL
ILADKLVPEP VLALVPRRTT VFIARKFPGN ADKAQEELLQ MGLEGLRAGK TVVRLKQGDP
YIYGRGAEEY DFFRAHGHIP IVLPGITSAL SAPLFAAIPP THRSVADQVL ICTGTGRKGA
APDPPAYVPT RTVVFLMALH RLSALIDSLV LDEAKKWPKE TPCAVLERAS CPDQRVIRTT
LEYVCTAVEE EGSRPPGLLV VGLACEVLWK GGQKWVVEEG FKGFGELGVE ASPTAAHQHT
RTRTLSNANA AAKRTSTVGA PLVEQKVHYT VLVRLPFARG DFVDPAQVEW DSTKDQALWK
ITSRPMSGVA GAGRREIDWQ ELAARFEVPP SFILQQAAWL YERHLQHVRA QMRKESSSTD
DDKNNPIRRS QLFKRPPRFM SRQVKPGLPR LDDVDVEYDD TTDYGDRAGD ERSDGDDDDD
DDEFLPFAVP TRRRTTNNNQ AQRQDPSTAP RRAHTHDERR STGAAATRGG AADAGRPSRP
PLSSVAAGKQ PIRSATMDSS FTSASDARST DGDDGSGRRG SGASPGTPGA FAGRRQKRRA
GTLTAPYSPS GGPASGALSP RHRAELARLS PRTRGKEGSE GTPSMGSSFS DLDDASVTQS
ALEEQLLSHM QHQGGLSKMS TISQALRSRY LP
//
