ID A0A1J4RY39_9BACT Unreviewed; 381 AA.
AC A0A1J4RY39;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 03-MAY-2023, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OIN91839.1};
GN ORFNames=AUJ42_01230 {ECO:0000313|EMBL:OIN91839.1};
OS Candidatus Collierbacteria bacterium CG1_02_44_10.
OC Bacteria; Candidatus Collierbacteria.
OX NCBI_TaxID=1805087 {ECO:0000313|EMBL:OIN91839.1, ECO:0000313|Proteomes:UP000182345};
RN [1] {ECO:0000313|EMBL:OIN91839.1, ECO:0000313|Proteomes:UP000182345}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1_02_44_10 {ECO:0000313|EMBL:OIN91839.1};
RX PubMed=27112493;
RA Probst A.J., Castelle C.J., Singh A., Brown C.T., Anantharaman K.,
RA Sharon I., Hug L.A., Burstein D., Emerson J.B., Thomas B.C., Banfield J.F.;
RT "Genomic resolution of a cold subsurface aquifer community provides
RT metabolic insights for novel microbes adapted to high CO concentrations.";
RL Environ. Microbiol. 0:0-0(2016).
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:OIN91839.1}.
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DR EMBL; MNUK01000033; OIN91839.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4RY39; -.
DR Proteomes; UP000182345; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035596; F:methylthiotransferase activity; IEA:InterPro.
DR GO; GO:0006400; P:tRNA modification; IEA:InterPro.
DR CDD; cd01335; Radical_SAM; 1.
DR Gene3D; 3.30.750.200; -; 1.
DR Gene3D; 3.30.750.210; -; 1.
DR Gene3D; 3.40.50.12160; Methylthiotransferase, N-terminal domain; 1.
DR InterPro; IPR006638; Elp3/MiaA/NifB-like_rSAM.
DR InterPro; IPR005839; Methylthiotransferase.
DR InterPro; IPR020612; Methylthiotransferase_CS.
DR InterPro; IPR013848; Methylthiotransferase_N.
DR InterPro; IPR038135; Methylthiotransferase_N_sf.
DR InterPro; IPR007197; rSAM.
DR PANTHER; PTHR43020; CDK5 REGULATORY SUBUNIT-ASSOCIATED PROTEIN 1; 1.
DR PANTHER; PTHR43020:SF2; MITOCHONDRIAL TRNA METHYLTHIOTRANSFERASE CDK5RAP1; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR Pfam; PF00919; UPF0004; 1.
DR SFLD; SFLDG01082; B12-binding_domain_containing; 1.
DR SFLD; SFLDG01061; methylthiotransferase; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS51449; MTTASE_N; 1.
DR PROSITE; PS01278; MTTASE_RADICAL; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 2..118
FT /note="MTTase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51449"
FT DOMAIN 114..375
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
SQ SEQUENCE 381 AA; 43334 MW; 1538082CCDC1C290 CRC64;
MPSVFINTFG CQANKSDSER ILGDYLSRGY AEADTWKVAD EIVINTCSVR QSAEDRVTGF
LLNVDKFFAR KQRPKIILTG CMLHFNEKEI RVLLPQIDEI LPIGEVGFNQ KAIRKEKDKA
FISISSGCNS FCTFCIVPFS RGRERSRPID DIVREVAGLA GEGYTEITLL GQNVNSWGLE
KVGVALRKMF MDKDTFNSDI FPSNQSQYFK PQDTPPFVTL LREISKINGI QKISFFTSNP
WDFWDELVDE IAKNPKIDRF IHLPVQSGSN RILKLMNRGY TRESFLNLIN QIKVKIPDVV
FGTDIIVGFP GETEDDFRDT LNLVKEVGFK VAFVARYSPR PGTVSAKLFP DDIPASIKKE
RWEILDQITN KDNLRSRPIV P
//
