ID I9AX76_9FIRM Unreviewed; 1269 AA.
AC I9AX76;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Carbamoyltransferase {ECO:0000313|EMBL:EIW17492.1};
GN ORFNames=FB4_4241 {ECO:0000313|EMBL:EIW17492.1};
OS Pelosinus fermentans B4.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Pelosinus.
OX NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW17492.1, ECO:0000313|Proteomes:UP000004324};
RN [1] {ECO:0000313|EMBL:EIW17492.1, ECO:0000313|Proteomes:UP000004324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:EIW17492.1,
RC ECO:0000313|Proteomes:UP000004324};
RX PubMed=22933770; DOI=10.1128/JB.01174-12;
RA Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL J. Bacteriol. 194:5147-5148(2012).
CC -!- SIMILARITY: Belongs to the NodU/CmcH family.
CC {ECO:0000256|ARBA:ARBA00006129}.
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:EIW17492.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKVJ01000030; EIW17492.1; -; Genomic_DNA.
DR RefSeq; WP_007935942.1; NZ_AKVJ01000030.1.
DR AlphaFoldDB; I9AX76; -.
DR PATRIC; fig|1149862.3.peg.3210; -.
DR OrthoDB; 9780777at2; -.
DR Proteomes; UP000004324; Unassembled WGS sequence.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:UniProt.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IEA:UniProt.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:InterPro.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR Gene3D; 3.90.870.20; Carbamoyltransferase, C-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR031730; Carbam_trans_C.
DR InterPro; IPR038152; Carbam_trans_C_sf.
DR InterPro; IPR003696; Carbtransf_dom.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR007848; Small_mtfrase_dom.
DR PANTHER; PTHR34847; NODULATION PROTEIN U; 1.
DR PANTHER; PTHR34847:SF1; NODULATION PROTEIN U; 1.
DR Pfam; PF16861; Carbam_trans_C; 1.
DR Pfam; PF02543; Carbam_trans_N; 1.
DR Pfam; PF05175; MTS; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000313|EMBL:EIW17492.1}.
FT DOMAIN 86..338
FT /note="Carbamoyltransferase"
FT /evidence="ECO:0000259|Pfam:PF02543"
FT DOMAIN 393..563
FT /note="Carbamoyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16861"
FT DOMAIN 895..1040
FT /note="Methyltransferase small"
FT /evidence="ECO:0000259|Pfam:PF05175"
SQ SEQUENCE 1269 AA; 145246 MW; 5D9AD2012770B447 CRC64;
MGTSNEPMYH LGINLGHDRS AAIVRKGKIE VAIQQERLDR TKNSIGFLHQ SLGDCRNIQI
PHEAIQYCLR KYDIKINDLS SITANMPGID YSKDILQRIF PKELSDKIFM IPSHHLSHAY
TAYWPSGFEE AIILVVDASG STDKEGFTES YSLYIAKGTE IKLLHSEKVK AYLASLSTLG
SIYEFITKLA GFSTTIGKNL AIPEAGKLMG LAPYGTYCDQ WHEWLHTKSE SYSIDISAYD
LFLEVEALKK LHDDGKGKAY LRPYIVDLAY KIQSELEKAL LHIVELAIEQ TNCKKLCCAG
GVALNSVVNY KLLTKLNLED IFIFPAAGDA GIAAGNALWA YHSIEKGNLR PKLEKADLGR
EYTENELESA LHKFANEIII EKLSYQEMVA TCASQMSKGN IIARFEGGSE FGPRALGHRS
IIADPTFRKI KDIMNYRVKF REAFRPFAPV IPLEEISTIF EQATACPFML LVSNIKKEYH
DQIPSVTHHD GTGRVQTVTS EHNTFFYDLC YNMVKEREGC PVILNTSFNI AGQPIIETPE
EAISTFLSTD IDFLSLEDYW IRKRHSPVLS YEEHLAQLQE PEYPHGLAEK RIDVTDLMRK
LDEAIFYGNT KNSFWSANEL KKISSQGAIY KETSVLFAKN PLGNHFSAQL GKDLLLLLDP
LGMSEIRDLT DLIPSTYYTY EEIRLIILCY KGTETELEEL RLELNLPEKA FWGKLEWASK
QLKRYKLPYK ILRRENDSIN SKPANITLGQ FTDESFRLYN TLKQFNDNLT LHGYLESNIC
KLLDIETLQS IEPTYIHYYN KHKLGHGKLE DLLRLFLLRD SLSKERIIEI LGEYCFQNLC
NLGIIIPRGN WFASRVDIYC VNDFFIATDH RYMIYEEDMI QENPVMYIGM DSLGLVHTVP
KYPSKNTLDL CTGSGIQAIT ASCYSKKVVG IDINPRAIRF ARFNAQLNGI SNIKFVEGNL
YAPIANEKFD TILANPPFVP SPDNNLDFRD GGKNGEKLLK VIIKNADLHL SNEGRLFIVS
DLVNVHHYEE KLNQWWGKTK ADKLVLTTAD RNDILFSIPH CHYPFKQTIE QYNNELDMWI
QNFNYSNISS VNFGYILIKK GGNSFYSKSI YNPTQGINKK VTEYFEQINM LHSVEWENLS
LYLSDDLHVK ADYSFSTAND KTFYLYSTNQ FYSEYLIDKN LYNILERIAE EEPTLEELAD
KNYVVDLIYK GIVKIKLKKQ YPNYSDCYEC KEVAATLSHS VNSETRKDIH IKEFQTKTTP
TCLTSYIRQ
//
