YHMF_METFE
ID YHMF_METFE Reviewed; 285 AA.
AC P19268;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Uncharacterized 32.2 kDa protein in hmfB 3'region;
OS Methanothermus fervidus.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanothermaceae; Methanothermus.
OX NCBI_TaxID=2180;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2377617; DOI=10.1073/pnas.87.15.5788;
RA Sandman K.M., Krzycki J.A., Dobrinski B., Lurz R., Reeve J.N.;
RT "HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon
RT Methanothermus fervidus, is most closely related to histones.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:5788-5791(1990).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742};
CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00742}.
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DR EMBL; M34778; AAA72081.1; -; Genomic_DNA.
DR RefSeq; WP_013414264.1; NC_014658.1.
DR AlphaFoldDB; P19268; -.
DR SMR; P19268; -.
DR PRIDE; P19268; -.
DR GeneID; 9962948; -.
DR OMA; YELTTIM; -.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR InterPro; IPR005925; Agmatinase-rel.
DR InterPro; IPR006035; Ureohydrolase.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR InterPro; IPR020855; Ureohydrolase_Mn_BS.
DR PANTHER; PTHR11358; PTHR11358; 1.
DR Pfam; PF00491; Arginase; 1.
DR PIRSF; PIRSF036979; Arginase; 1.
DR SUPFAM; SSF52768; SSF52768; 1.
DR TIGRFAMs; TIGR01230; agmatinase; 1.
DR PROSITE; PS01053; ARGINASE_1; 1.
DR PROSITE; PS51409; ARGINASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Manganese; Metal-binding.
FT CHAIN 1..285
FT /note="Uncharacterized 32.2 kDa protein in hmfB 3'region"
FT /id="PRO_0000173785"
FT BINDING 110
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 131
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 131
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 133
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 135
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 214
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 214
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
FT BINDING 216
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00742"
SQ SEQUENCE 285 AA; 32227 MW; 79E1934258502CD7 CRC64;
MGLKFAYSKD PSSLKYLSNK KVFGLLGVPF DSTSTYKPGS RFGPLMIRQA SYNFENYSLH
YRKKLDVPII DLGDIEVILG DFKNTCRNIS EKVQEVLKKG MIPIVLGGEH SITYGVVKTF
DLSDVTILHF DAHMDMANTY AGKKFSHATV MRRIYELHPK KIVQIGVRSC TKEEHEFVLN
ENIKYYTSRD IIEKFNMVLN EINKLDGPFY VTVDIDVLDP GYAPGVGNPT PVGITPYHME
KFIEKIARKK IIGIDIVEVA TDRIGDPAAM NAAKILYDFL FAIKI