ID A0A2G9LXM4_9ARCH Unreviewed; 368 AA. AC A0A2G9LXM4; DT 31-JAN-2018, integrated into UniProtKB/TrEMBL. DT 31-JAN-2018, sequence version 1. DT 14-DEC-2022, entry version 16. DE SubName: Full=Putative peptide-modifying radical SAM/SPASM domain-containing protein {ECO:0000313|EMBL:PIN71102.1}; GN ORFNames=COV77_03845 {ECO:0000313|EMBL:PIN71102.1}; OS Candidatus Pacearchaeota archaeon CG11_big_fil_rev_8_21_14_0_20_30_13. OC Archaea; Candidatus Pacearchaeota. OX NCBI_TaxID=1974447 {ECO:0000313|EMBL:PIN71102.1, ECO:0000313|Proteomes:UP000229845}; RN [1] {ECO:0000313|EMBL:PIN71102.1, ECO:0000313|Proteomes:UP000229845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CG11_big_fil_rev_8_21_14_0_20_30_13 RC {ECO:0000313|EMBL:PIN71102.1}; RA Probst A.J., Ladd B., Jarett J.K., Geller-Mcgrath D.E., Sieber C.M., RA Emerson J.B., Anantharaman K., Thomas B.C., Malmstrom R., Stieglmeier M., RA Klingl A., Woyke T., Ryan C.M., Banfield J.F.; RT "Depth-based differentiation of microbial function through sediment-hosted RT aquifers and enrichment of novel symbionts in the deep terrestrial RT subsurface."; RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic CC sulfatase-maturating enzyme family. {ECO:0000256|ARBA:ARBA00023601}. 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:PIN71102.1}. 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; PCVV01000051; PIN71102.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2G9LXM4; -. DR EnsemblBacteria; PIN71102; PIN71102; COV77_03845. DR Proteomes; UP000229845; Unassembled WGS sequence. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR023819; Pep-mod_rSAM_AF0577. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023867; Sulphatase_maturase_rSAM. DR PANTHER; PTHR43273; ANAEROBIC SULFATASE-MATURATING ENZYME HOMOLOG ASLB-RELATED; 1. DR PANTHER; PTHR43273:SF2; RADICAL SAM DOMAIN CONTAINING PROTEIN; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SFLD; SFLDS00029; Radical_SAM; 1. DR SFLD; SFLDG01104; Uncharacterised_Radical_SAM_Su; 1. DR TIGRFAMs; TIGR04084; rSAM_AF0577; 1. PE 3: Inferred from homology; 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}. FT DOMAIN 6..168 FT /note="Radical SAM core" FT /evidence="ECO:0000259|Pfam:PF04055" SQ SEQUENCE 368 AA; 43202 MW; 35378C22461722C5 CRC64; MQYHIILTER CNLKCKYCYE KSMQEFDNGL GEKWDYDEDT PFDSEVSIDK LKKFIKPEDR LIFYGGEPLV MVEKIKEIMD NLDCKFGIQT NGILLKRLPI EYIKRIDKML VSIDGDSERT NFNRGKGVYE IVIKNLKELC SRGYSGEVVV RMTLLFPDLF KQVKHLISLI EEEIINSIHW QIDAGFYKFD FDKEKFSEFV KEYNKNISQL VNWWTNEIRN GKVYLIYPFL GIFNRIIGWD KETKLPCGSG YENFTVTTSG KISSCPIMNS VKKFYCGDIE KGIEKEIHVQ DDECEKCLNF KICGGRCLYW RNAKLWSPEG DKLICETIGY LINSIKEKVP EIENLLKKGI VKKEQFEYEK YFGPEIIP //