ID A0A0N1GFJ8_9ACTN Unreviewed; 1656 AA.
AC A0A0N1GFJ8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Peptidase C14 caspase catalytic subunit p20 {ECO:0000313|EMBL:KPI18792.1};
GN ORFNames=OK006_10206 {ECO:0000313|EMBL:KPI18792.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI18792.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI18792.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI18792.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-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:KPI18792.1}.
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DR EMBL; LJCU01000033; KPI18792.1; -; Genomic_DNA.
DR PATRIC; fig|1592326.3.peg.1926; -.
DR Proteomes; UP000037912; Unassembled WGS sequence.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00200; WD40; 3.
DR Gene3D; 3.40.50.1460; -; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 4.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011600; Pept_C14_caspase.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR22847:SF748; TRANSCRIPTIONAL REPRESSOR TUP11; 1.
DR PANTHER; PTHR22847; WD40 REPEAT PROTEIN; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 17.
DR SUPFAM; SSF52129; Caspase-like; 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 6.
DR PROSITE; PS50082; WD_REPEATS_2; 12.
DR PROSITE; PS50294; WD_REPEATS_REGION; 4.
PE 4: Predicted;
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 52..200
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REPEAT 818..861
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 863..906
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 908..951
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 975..996
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1062..1084
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1086..1129
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1131..1167
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1176..1219
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1310..1345
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1355..1398
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1489..1532
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1577..1619
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1656 AA; 173021 MW; 81384E7416484C4F CRC64;
MWAGDRGGAG VSGLSRDGGA GDNGGPRRFL IATAIAHYSK SPGWNRPSLV EARDQIIELF
TGQLGYQHET DLGLNPAKAQ LTDQLRAFSK SPDRREDDLL AVYISGHGEV LDGDEHVLLT
ADTDPDDVDY TALPTAELAR AILRGTSVRR LLLVLDTCYS GQGGNDTAAT ALKRISAEWG
QATGSGLVIV SSAQPHQQAQ AGLFPRLLSD AVGNRATAGH GPRALPVDMV VKQMNAHPAL
PKHQRISLAM VGLTGEVPEF FANPRYGTWL TDVDLAIQEA AEFDEQARRR DTELTRRLLV
HAMGYPGDAA EGWWFCGRHA VLADLAKWLR TPAADRHDCR VVTAGPGSGK TAVLGLIAAL
AHPERRRTVP VGSLGLAPSL VPDAEAVDVA VYAQNLTDTD VLKALAAAAR VRANTVGELL
KALDARDGER PFTALIDALD EAATPDTLCT QILKPLINYS EGRIRLLLGT RPDLLDSLGI
RPSNDVGSGR IIDLDDSRYA DPEALTAYTV RTLIEAHPNS PYRRRPEALR PVAEAVAAAA
GPSFLVARIT AGTLAAAEDV VADPQNPAWR ASLPCHAGQA MREDLVGRLG DDAQRAADLL
RPLAFAQGQG LPWEDIWALA ASEISGRSYT DDDVVWLRSA AGSYVVEATE SDRSAYRLYH
QALAEHLRDG INAQAVHTAV AEILTARVPY LADGTREWAR AHPYALNHLA THAAAAGCLD
EVLGDTEYLS HAATRSLTPH LQHARSDTAR LTAAVYRTSA GPHSTDTASE RRQVLALDAA
RAGATALRQQ LIDHTPEGHW IPRWATGSGF TPALRDTLSG HTGPVREVAC TNLDGAPVAV
TGDDDGVVRV WDMRTGAPIG QPLTGHAGPV QAVACTNLDG VPVAVTGDDG GVVRVWDLRT
GTPIGQPLTG HTGQVQVVAC TNLDGALVAV TGGHDGRVRV WDLRGGTLLG QPLTGTIGRV
TVVACTEMGE APVAVTGGSD GMMRVWDLRG GTLLGQPLTG AIDGVRSMAC TELDGTPIAV
TGDGPDGVLA WDLRTGTAIG QPQTGDTRVN AVACTELEGT PILVTGDDGV VRVWDLRTGT
PIGRPLTGHA GQVQAVACAK VDGAPVAVTG DDGGVVRVWD LRTGTPIGQP LTGHTGLIRA
VACTEIDGMP VAVTGSRDGT IRAWDLRGSV LLGQPLTDHM GGLRSVACTE VDGAPVAVTG
SDTGMVRVWD LRTGTRLRNL LTGDTDGVRS MACTKVDGVP VAVTGDGPDG RVRVWDLRTG
TPIGQPQGGE FSVTAVACTE VNGVPVTVVG NGGVLRVWDL RSGTPIGRPL TGHTEPVLAV
ACAEVDGGPV AVTGDASGVV RVWDLGGGAF LGQPATGHTN WVEGVACTEV DGVSVAVTGS
RDGTVRVWDL RDGTPIGQPL TGHTNWMRAV TCTEVDGVPI AVICDNTRVR AWDLRDGVPI
GRPLTSNTGG VGAVACTEVD GVPVAVTGWD DGRARMWDLR TGTLIGSAVT GHTGGVGAVA
CTEVDGVPVA VIGSRDGMVR VWDLRGGALL GQPLTGHTGP VRTVACTQVD GTPVAVVGGG
MAQMWDLRSG IIIGQPLTGH IGGVSAVACT EMDGVPVAVS TDNGTVRVWN LRTGKPAGVL
RIPNPSVVAV TFRGDLVVGM GNDVAVFNRR TLQRLR
//
