ID A0A1Q4X5V8_9PSEU Unreviewed; 712 AA.
AC A0A1Q4X5V8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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=A6A25_40325 {ECO:0000313|EMBL:OKI17707.1};
OS Saccharothrix sp. CB00851.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1835005 {ECO:0000313|EMBL:OKI17707.1, ECO:0000313|Proteomes:UP000186828};
RN [1] {ECO:0000313|EMBL:OKI17707.1, ECO:0000313|Proteomes:UP000186828}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB00851 {ECO:0000313|EMBL:OKI17707.1,
RC ECO:0000313|Proteomes:UP000186828};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI17707.1}.
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DR EMBL; LWLC01000048; OKI17707.1; -; Genomic_DNA.
DR RefSeq; WP_073898111.1; NZ_LWLC01000048.1.
DR AlphaFoldDB; A0A1Q4X5V8; -.
DR STRING; 1835005.A6A25_40325; -.
DR Proteomes; UP000186828; 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 Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR011600; Pept_C14_caspase.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
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 Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF52129; Caspase-like; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000186828};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW WD repeat {ECO:0000256|PROSITE-ProRule:PRU00221}.
FT TRANSMEM 686..706
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..239
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REPEAT 484..518
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 299..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..337
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 712 AA; 76432 MW; 0C68E129F464FA91 CRC64;
MRRALLIATD TYRDPTFGAL RAPRLDAAEL DAVLSDPAIG GFDTEVLVNE PVQQVRERVE
TVLGQAGRDD LVLLYLSGHG VKARLGDLHF VTTDTRRTVL ATTSLDAAFV RRQIDDSLAG
QVVVWLDCCY GGAFPSGMLP RATEDVDVVQ QLTEGRGCAV MTASTHIQYA YEPVGEHVDD
RAEPSVFTKA IIDGLRTGDA DLDHDGEISV RDLYGYVYDR VRRTNPDQTP TSSGTLSGDL
RIAYAGTPLP AGLPDELRRL LRSPEDGFRR AGLRILDDRA QAGDPISLAA LRALEERADH
ALSPSPGTSA RPATATTPAP AATMPAPAAP APPDSGPPAT EEAGRLIRML LRRTAPEFHA
SGVVGRGHSR VVFSHDSSML AAGTRVWSTD GWRTIFDLPH DHVGILAFSP DDRLVVVSGS
GRLTLFRTAT WEPLAAIPFT EPVDHVGFDH DGTLLAVTAQ RTTTIFHATG EHWQALDEPR
FRAVRDARFC PDTPRLVVAT DDGRIELWDT RTWTRLGSTT LRGVRVAAVR YGLVLAAASA
DTVAVWRTDT WEMAASARLG DPTHLGPVAF GPELNVLICD GWHGLELRGV DDGKTYQTIA
STVRSPVLSG DRRFLAGLAP QGSRRKGSEV WVWARDHGEA IGLGPGRTPP KASTATRNAV
LRLVGRFSAV GGGVYAALGL LASTEWATAA ALGAGGVLAA GAWWAVDRTW IT
//