ID A0A060HGJ4_9ARCH Unreviewed; 363 AA.
AC A0A060HGJ4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Putative diphthine synthase {ECO:0000313|EMBL:AIC14450.1};
GN ORFNames=NVIE_002640 {ECO:0000313|EMBL:AIC14450.1};
OS Nitrososphaera viennensis EN76.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrososphaerales;
OC Nitrososphaeraceae; Nitrososphaera.
OX NCBI_TaxID=926571 {ECO:0000313|EMBL:AIC14450.1, ECO:0000313|Proteomes:UP000027093};
RN [1] {ECO:0000313|EMBL:AIC14450.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EN76 {ECO:0000313|EMBL:AIC14450.1};
RX PubMed=24907263; DOI=10.1099/ijs.0.063172-0;
RA Stieglmeier M., Klingl A., Alves R.J., Rittmann S.K., Melcher M.,
RA Leisch N., Schleper C.;
RT "Nitrososphaera viennensis gen. nov., sp. nov., an aerobic and mesophilic,
RT ammonia-oxidizing archaeon from soil and a member of the archaeal phylum
RT Thaumarchaeota.";
RL Int. J. Syst. Evol. Microbiol. 64:2738-2752(2014).
RN [2] {ECO:0000313|EMBL:AIC14450.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EN76 {ECO:0000313|EMBL:AIC14450.1};
RA Kerou M.L., Offre P., Spang A.M., Schleper C.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005156}.
CC -!- SIMILARITY: Belongs to the diphthine synthase family.
CC {ECO:0000256|ARBA:ARBA00006729}.
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DR EMBL; CP007536; AIC14450.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060HGJ4; -.
DR STRING; 926571.NVIE_002640; -.
DR KEGG; nvn:NVIE_002640; -.
DR HOGENOM; CLU_066040_0_0_2; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000027093; Chromosome.
DR GO; GO:0004164; F:diphthine synthase activity; IEA:InterPro.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0017183; P:protein histidyl modification to diphthamide; IEA:UniProtKB-UniPathway.
DR CDD; cd11647; DHP5_DphB; 1.
DR Gene3D; 1.20.1270.90; AF1782-like; 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; IPR036809; AF1782-like_sf.
DR InterPro; IPR004551; Dphthn_synthase.
DR InterPro; IPR023140; DUF357.
DR NCBIfam; TIGR00522; dph5; 1.
DR PANTHER; PTHR10882:SF0; DIPHTHINE METHYL ESTER SYNTHASE; 1.
DR PANTHER; PTHR10882; DIPHTHINE SYNTHASE; 1.
DR Pfam; PF04010; DUF357; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR SUPFAM; SSF158372; AF1782-like; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Reference proteome {ECO:0000313|Proteomes:UP000027093};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..231
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT DOMAIN 284..355
FT /note="DUF357"
FT /evidence="ECO:0000259|Pfam:PF04010"
SQ SEQUENCE 363 AA; 40112 MW; 08E72DA6DA7BFC75 CRC64;
MRLSFGYMLW LVGAGISGHR GLSLEAVQVL KKCEIVFVER FTSALADSDL EGINAAIGKS
AKPVQRWFVE DGREMLDAAR EKQVALVTYG DPLLATTHTE LRTRAAKASI KTSVLHAASG
ITSIMGECGL HMYKFGRTVT MMSEPKSAIS VYNTVFDNLL LGSHTLILTE YSHDEKTGEP
FFLDPAVVLK MLLDCERDLR HRVFSEETFV VVASRLGSDD SRIVSGKIKS LAGVGFGTGP
HSVIVPASLH FTEEEALEAL TVCLDSPVDN AASVKRISAQ MIERYAPKAR EAVQHMRDIL
RKEGEKKENK GMHEVLDNAE YYIDDAERFL RQGKHELAVL SIGYAEGLVD ALRFQKGINP
WNP
//
