ID A0A2U2ZCJ4_9ACTN Unreviewed; 449 AA.
AC A0A2U2ZCJ4;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:PWI10005.1};
GN ORFNames=DIZ27_13010 {ECO:0000313|EMBL:PWI10005.1};
OS Streptomyces sp. NWU339.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2185284 {ECO:0000313|EMBL:PWI10005.1, ECO:0000313|Proteomes:UP000245372};
RN [1] {ECO:0000313|EMBL:PWI10005.1, ECO:0000313|Proteomes:UP000245372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NWU339 {ECO:0000313|EMBL:PWI10005.1,
RC ECO:0000313|Proteomes:UP000245372};
RA Adegboye M.F., Lobb B., Babalola O., Doxey A.C., Ma K.;
RT "Draft genomes of two novel cellulolytic Streptomyces strains isolated from
RT South African rhizosphere soils.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:PWI10005.1}.
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DR EMBL; QFRK01000009; PWI10005.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2ZCJ4; -.
DR OrthoDB; 9777385at2; -.
DR Proteomes; UP000245372; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017439; Amidohydrolase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01891; amidohydrolases; 1.
DR PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 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.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:PWI10005.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245372}.
FT DOMAIN 217..310
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..26
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 449 AA; 46128 MW; 9F0D2289B9E8FCD5 CRC64;
MTSPSQHAPG PAPAGPGAPP GPGALPPGAE RLLTRVGEVL RPALTHYLDL HAHPEVSGEE
ARTADRFGRR LAAAGCELTH QVGGHGVVGV LRNGDGPRVW LRAELDALPM RERSGLPYAS
RNDAMHACGH DLHLAAAAGA ADLLARLSDR WRGTLLVVGQ PAEETLAGAE AMLRDGLYER
FGRPDVVLAQ HAAPMPSGTV AHATGQAPMA AAGAVLEVVL HGRGGHVATP HLAVDPVVTA
AAVVTRLQNV VARETAPADQ VTLTVGTVRA GTAANVIPDH ALLGIAVRAA GEASLDRALA
AVRRIVRAES AAAGAPREPE VTVASRSAAL LCDPRTTGSV RRAHTGLLGP ARVLPWPGSM
ATEDFPLFGD AGAAIHGERG IPLVYWMLGV ADPDTWLRTT SDGTTSDGPD SAPPPAPNHS
PHFAPHIGSA LRPAIAALTI AALDRFAAV
//