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Database: UniProt
Entry: A0A1H5KAE2_9ACTN
LinkDB: A0A1H5KAE2_9ACTN
Original site: A0A1H5KAE2_9ACTN 
ID   A0A1H5KAE2_9ACTN        Unreviewed;       462 AA.
AC   A0A1H5KAE2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Predicted Zn-dependent peptidase {ECO:0000313|EMBL:SEE61833.1};
GN   ORFNames=SAMN05216489_07421 {ECO:0000313|EMBL:SEE61833.1};
OS   Streptomyces sp. 3213.3.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1855348 {ECO:0000313|EMBL:SEE61833.1, ECO:0000313|Proteomes:UP000198754};
RN   [1] {ECO:0000313|EMBL:SEE61833.1, ECO:0000313|Proteomes:UP000198754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3213 {ECO:0000313|EMBL:SEE61833.1,
RC   ECO:0000313|Proteomes:UP000198754};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FNTK01000001; SEE61833.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H5KAE2; -.
DR   STRING; 1855348.SAMN05216489_07421; -.
DR   Proteomes; UP000198754; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198754}.
FT   DOMAIN          38..169
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          191..374
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   462 AA;  49251 MW;  F615E4A44D0A122C CRC64;
     MTELATMEFH PQPQAGEARP WAFPAPERRT LDNGLTVLRC HRPGQQVVAV EVLLDAPLEA
     EPAGLDGVAT ITARAFSEGT DKHSAEEFAA ELERSGATLD AHADHPGLRL SLEVPASRLA
     KGLGLLSDAL RAPAFADSEV ERLVRNRLDE IPHETANPSR RAAKELSKEL FPASSRMSRP
     RQGTEETVQK IDSGAVRAFY DRHVRPATAT VVVVGDLTGI DLDALLAETL GSWTGSTAQP
     RPVPPVTADD TGRVVIVHRP GAVQTQLLIG RVGADRHDRV WPAQVLGTYC LGGTLTSRLD
     RVLREEKGYT YGVRAFGQVL RSAPDGTGVS MLAISGSVDT PNTGPALDDL WTVLRKLAEG
     GLTDAERDIA VQNLVGVAPL KYETAAAVAS TLADQVEQHL PDDYQATLYR QLAATGTVEA
     TAAVVSAFPV DRLVTILVGD AEQIKEPVEA LGIGEVTVVP AE
//
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