ID S4MUV8_9ACTN Unreviewed; 1276 AA.
AC S4MUV8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Peptidase C14 caspase domain-containing protein {ECO:0000259|Pfam:PF00656};
GN ORFNames=STAFG_2417 {ECO:0000313|EMBL:EPJ40546.1};
OS Streptomyces afghaniensis 772.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1283301 {ECO:0000313|EMBL:EPJ40546.1, ECO:0000313|Proteomes:UP000015001};
RN [1] {ECO:0000313|EMBL:EPJ40546.1, ECO:0000313|Proteomes:UP000015001}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=772 {ECO:0000313|EMBL:EPJ40546.1,
RC ECO:0000313|Proteomes:UP000015001};
RA Gruening B.A., Praeg A., Erxleben A., Guenther S., Fiedler H.-P.,
RA Goodfellow M., Mueller M.;
RT "Draft Genome Sequence of Streptomyces afghaniensis, Which Produces
RT Compounds of the Julimycin B-Complex.";
RL Submitted (FEB-2013) 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:EPJ40546.1}.
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DR EMBL; AOPY01001369; EPJ40546.1; -; Genomic_DNA.
DR AlphaFoldDB; S4MUV8; -.
DR PATRIC; fig|1283301.3.peg.2391; -.
DR HOGENOM; CLU_263491_0_0_11; -.
DR Proteomes; UP000015001; Unassembled WGS sequence.
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; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR011600; Pept_C14_caspase.
DR Pfam; PF00656; Peptidase_C14; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52129; Caspase-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000015001}.
FT DOMAIN 4..169
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1094..1276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1189..1206
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1264
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 140231 MW; 64B795AFE3AFBAC4 CRC64;
MQALADPTRN EITERVSEVS ASAPPGSTLL LYFTGHGVRI GTTDYLVPAD ARAPADDGDG
DDAAGWELPH VRESLLEADI SRYLANCRAG TVLWLIDACR AADAGRGGVF GSNVVKGPPH
SGFAMMTSCG PGELSGGAKT GSFFTAALAR AFDPLTEATT VEQVYEKAKH GTRALAVEAQ
AGPQQVLIHY GTDLAERTKS LVVAEGRGLL EAWQDAVRTP ALWERVQECD AGTVAHFQDC
LSALATQAAR HVHHAQRRLP DPWTDDEYPV RLLSDRLPLL LPKGAELSAL EVTALIAGVL
LHETAWAERL GQAAGFRPRL VWRDDEADDQ RRHYEQITEH YPQITEKLTD SYRWLGDPAD
DRHAVTLWLV HRWIEERFAT DEEAVPALFA DRFTARLLDV APPAAGERLG GRAEALSQAL
RTVAAGLALG APPEDERLPP DRHVVRRTPW RLRVRPLAAL LRLAGLLAFD TRCLPEVLAE
HLAVSDPVLP REVITVFRDA YWVPDRDGSA ASYLHLDAVC PHPALHAALA AVVEDADDLG
HLLRESARRL PQDEAELLRG LPARLSDHGL RPDRPDGTDA YDVPLARFSL AQTEIRRLLM
GDKLYDGEPE LALRELYQNA MDACRYREMR VRYLRDLGRD PVPWAGRIRI ETGEDSRGRY
VECVDNGVGM TVDQLKNTFT RAGRRFDQSH AFRREQAAWL RHDSSLRLYP NSRFGIGVFS
YFMLADEMTL VTRPVGTDGR PAEKALRVEI PVSGSLFRVR EEDERDGTAL PEGGTRVRLH
LRRAGALPGG SAVSVLRSLV LISEFLLEVR DQDGTEEIWL PGDLKSGEEP GAFSTRFAVE
AVPGTLWWVS DKGAIVCDGI ATDQRPFGYV LNLSGAHAGE LSVNRKKLER YDVLWAQEQF
RQGARAFLGQ ETPGLEWLWS MESRESSIAR VLWEVLRGHG VRASLGHGRR IDLDELGWFR
LDGGVHGGRG HREGEEASRL VRPWRLAALG SEHRDRHTAP PLSLSGHPVP QPGWADIAEK
VEGDWRVAVR MADAQNTTVA EVLRATRGLR IAHPQLAGPA VLGDGDLDWE PGITDWYVTT
GLLGRKRDPL DGFAAPSGEP CGQAAGGRRH SLPAPARGPL RHRPRLRHVP EAARRAGRGV
RPVRAVRGQA AGHRPGPPPG PRLHRRRAEA PLPPGGQVRL AARRPPLGRA GGGRRHGPRH
GRGATAHGRL RLAGPPRTRP GSDRTLGRRT GRAARRPAHL PRPPRRRPPR AALGRHHRSG
RGARSLRVGG RTPPGP
//