ID K0BAJ8_9ARCH Unreviewed; 269 AA.
AC K0BAJ8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Diphthine synthase {ECO:0000313|EMBL:AFS83233.1};
GN ORFNames=NSED_07195 {ECO:0000313|EMBL:AFS83233.1};
OS Candidatus Nitrosopumilus sediminis.
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC Nitrosopumilaceae; Nitrosopumilus.
OX NCBI_TaxID=1229909 {ECO:0000313|EMBL:AFS83233.1, ECO:0000313|Proteomes:UP000006100};
RN [1] {ECO:0000313|EMBL:AFS83233.1, ECO:0000313|Proteomes:UP000006100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR2 {ECO:0000313|EMBL:AFS83233.1,
RC ECO:0000313|Proteomes:UP000006100};
RX PubMed=23209211; DOI=10.1128/JB.01869-12;
RA Park S.J., Kim J.G., Jung M.Y., Kim S.J., Cha I.T., Ghai R.,
RA Martin-Cuadrado A.B., Rodriguez-Valera F., Rhee S.K.;
RT "Draft Genome Sequence of an Ammonia-Oxidizing Archaeon, "Candidatus
RT Nitrosopumilus sediminis" AR2, from Svalbard in the Arctic Circle.";
RL J. Bacteriol. 194:6948-6949(2012).
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; CP003843; AFS83233.1; -; Genomic_DNA.
DR AlphaFoldDB; K0BAJ8; -.
DR STRING; 1229909.NSED_07195; -.
DR KEGG; nir:NSED_07195; -.
DR PATRIC; fig|1229909.8.peg.1580; -.
DR eggNOG; arCOG04161; Archaea.
DR HOGENOM; CLU_066040_0_0_2; -.
DR UniPathway; UPA00559; -.
DR Proteomes; UP000006100; 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 InterPro; IPR000878; 4pyrrol_Mease.
DR InterPro; IPR035996; 4pyrrol_Methylase_sf.
DR InterPro; IPR014777; 4pyrrole_Mease_sub1.
DR InterPro; IPR014776; 4pyrrole_Mease_sub2.
DR InterPro; IPR004551; Dphthn_synthase.
DR NCBIfam; TIGR00522; dph5; 1.
DR PANTHER; PTHR10882:SF0; DIPHTHINE METHYL ESTER SYNTHASE; 1.
DR PANTHER; PTHR10882; DIPHTHINE SYNTHASE; 1.
DR Pfam; PF00590; TP_methylase; 1.
DR PIRSF; PIRSF036432; Diphthine_synth; 1.
DR SUPFAM; SSF53790; Tetrapyrrole methylase; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|PIRSR:PIRSR036432-1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..220
FT /note="Tetrapyrrole methylase"
FT /evidence="ECO:0000259|Pfam:PF00590"
FT BINDING 9
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 162
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
FT BINDING 230
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR036432-1"
SQ SEQUENCE 269 AA; 30283 MW; E5C300715A50956B CRC64;
MLWFVGLGIS GFKSIPSEAL DVLSKADIVY LEQFTSPIGK SDLSKIKNAT KGEFKLAKRW
LVEDGNEILK NAKKKKVALL AYGDPYIATT HIELRTRAIE EKIKTQSIHA SSSLTSMIGE
CGLHFYKVGR IATIMSEMKS LTTPYYVIYK NIIEGNHTVL LLEFNQDKDF FLDPKDALNG
LLETEKGQIR NVISPSTYVI IASRIGFKDQ RIISGKISSL KKTDFGKPPH TVIIPGRLHF
TESDALKIFS QCIDEPFDNT EKTKKFQFK
//
