ID   A0A0X3XNJ1_9ACTN        Unreviewed;       725 AA.
AC   A0A0X3XNJ1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Peptidase C14 caspase domain-containing protein {ECO:0000259|Pfam:PF00656};
GN   ORFNames=ADL34_20900 {ECO:0000313|EMBL:KUL73043.1};
OS   Streptomyces sp. NRRL WC-3605.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL73043.1, ECO:0000313|Proteomes:UP000052945};
RN   [1] {ECO:0000313|EMBL:KUL73043.1, ECO:0000313|Proteomes:UP000052945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL73043.1,
RC   ECO:0000313|Proteomes:UP000052945};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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:KUL73043.1}.
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DR   EMBL; LLZN01000064; KUL73043.1; -; Genomic_DNA.
DR   RefSeq; WP_062670962.1; NZ_LLZN01000064.1.
DR   AlphaFoldDB; A0A0X3XNJ1; -.
DR   OrthoDB; 491589at2; -.
DR   Proteomes; UP000052945; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   PANTHER; PTHR22576:SF37; MALT1 PARACASPASE HOMOLOG; 1.
DR   PANTHER; PTHR22576; MUCOSA ASSOCIATED LYMPHOID TISSUE LYMPHOMA TRANSLOCATION PROTEIN 1/PARACASPASE; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   SUPFAM; SSF52129; Caspase-like; 1.
DR   PROSITE; PS00018; EF_HAND_1; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000052945};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        650..674
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        702..720
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..242
FT                   /note="Peptidase C14 caspase"
FT                   /evidence="ECO:0000259|Pfam:PF00656"
FT   REGION          415..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   725 AA;  76733 MW;  9D3B4A9C5855748B CRC64;
     MTDTRHALII ANERYDDRAL KQLKAPGHDA DALAEVLGDP RIGDFDVDVV SNQPSYVLRR
     RIEHFFSDRR RDDTLVVHFS CHGIKSESGE LYFAASDTEP LLLEATAVPA QFVRRCMSRS
     RAGRTVLFLD CCYGGAFSRS SSGVRATGDV NVLDSFATDK PAGGRGWAVI TASSSMEYAV
     EGGDLTEDTA PRPSVFTGAV VRGLDTGEAD LDADGEISLD DLYDYVYDRV RGQNPHQTPG
     KTVEMHGELH LAHSRRGRRV EIAAEPIPES WRAALRSKNH FTRMGAVAEL RYRLASESLP
     VAEGARQALL DVADNDMRQI ADNARAHLRE IRLQPSPSRL DFGRLHRDAP EPHGTVTLGG
     LPLARACVPR PTEPWLRVTE VADGLDVTVD PAAEGRLSAD ILLKGVADEA VIHVEAEREP
     QARSAARSPA TGPERETPLR PASAPAPGTE DAPRHQHARA DGAPDQARRH PAEEPRPTPA
     GVTSAEAGTR DRSADETRLV ATPDAPPPHP AETRPRSDDE TRVAATPQAP PQPPEGTRPG
     PSDDAAGDAR RGRTSPPAGA GASAAGRGNA ETRVVQGGSR PVSAHAADRA SGDGPVRSRW
     APVVAGIALA SAAASAATFV AAVVAGVPAV RDFAGAGTGD SRTLGSFVDG TGTVPLLVAS
     VVTAVVALVL GAVARHEVRA RPERYTRASA TSTAALTTPA RYVAIPALFL AVLAFIAWLA
     TRGLT
//