ID B3T1S9_9ZZZZ Unreviewed; 397 AA.
AC B3T1S9;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Putative peptidase family M20/M25/M40 {ECO:0000313|EMBL:ABZ06538.1};
GN ORFNames=ALOHA_HF4000093M11ctg1g24 {ECO:0000313|EMBL:ABZ06538.1};
OS uncultured marine microorganism HF4000_093M11.
OC unclassified sequences; environmental samples.
OX NCBI_TaxID=455519 {ECO:0000313|EMBL:ABZ06538.1};
RN [1] {ECO:0000313|EMBL:ABZ06538.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=18580971; DOI=10.1038/ismej.2008.62;
RA Konstantinidis K.T., Delong E.F.;
RT "Genomic patterns of recombination, clonal divergence and environment in
RT marine microbial populations.";
RL ISME J. 2:1052-1065(2008).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M20A family. ArgE subfamily.
CC {ECO:0000256|ARBA:ARBA00005691}.
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DR EMBL; EU016578; ABZ06538.1; -; Genomic_DNA.
DR AlphaFoldDB; B3T1S9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd03894; M20_ArgE; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010169; AcOrn-deacetyl.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01892; AcOrn-deacetyl; 1.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 185..295
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 397 AA; 43764 MW; A6CCC55E3B08EAA0 CRC64;
MATQNNIIDQ VFPETLKILS DLIKFKTVSG TSNLKLIEYC EKKLDKLGAI SFKTFHDSKL
QANLFSTINC KKKLNGGGII LSGHTDVVPA SGKKWSSDPF VATEKDNKIY GRGSCDMKGF
IACALALAPF FASQNLKKPI HFSFTYDEET ACQGAPIMLK ELKKRNVKCS ICIVGEPTSM
KAVQAHKGCS EYSTYFTGLA GHGSAPDKGV NAVEYASRYI NKLMELREEL KKRVPKNSVF
TPPYSTIQIG GIKGGLARNV IADQCTVDWE MRPVIPEDGK FVTENIEAYA KNVLLPEMRK
VYPKANIKKE IIGEIIGFTK EEKSDAVNLV CNLTGDNSRD VVSFGTEAGL FQELGISTVV
CGPGSIEQAH KIDEYVSFDQ LKLCLKMLID LKEQLTN
//
