ID A0A1H9WYM5_9PSEU Unreviewed; 792 AA.
AC A0A1H9WYM5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Caspase domain-containing protein {ECO:0000313|EMBL:SES39058.1};
GN ORFNames=SAMN04487818_11220 {ECO:0000313|EMBL:SES39058.1};
OS Actinokineospora terrae.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinokineospora.
OX NCBI_TaxID=155974 {ECO:0000313|EMBL:SES39058.1, ECO:0000313|Proteomes:UP000199051};
RN [1] {ECO:0000313|EMBL:SES39058.1, ECO:0000313|Proteomes:UP000199051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44260 {ECO:0000313|EMBL:SES39058.1,
RC ECO:0000313|Proteomes:UP000199051};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOGI01000012; SES39058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9WYM5; -.
DR STRING; 155974.SAMN04487818_11220; -.
DR Proteomes; UP000199051; 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:UP000199051};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 510..529
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 549..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 582..605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..657
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 663..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 695..712
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 762..781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..240
FT /note="Peptidase C14 caspase"
FT /evidence="ECO:0000259|Pfam:PF00656"
FT REGION 313..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..338
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..361
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 83288 MW; 7EB9DA0E0A18B960 CRC64;
MRRALIVASD AYGDLGLREL RAPKHDAAQL AAVLGDPEIG GFSVRTLHNA AVAETNEAIE
DFFADRAPDE LLLLYFSGHG VKDETGDLYF ATAGTKLNRL AATAVAADFV RQRMNRTRAR
RVVLLLDCCY AGAFGRGMVA RAGTAVALEE QFQGRGRAVI TASSAVEYAF EGQEVTDSAT
GGPSVFTSAL VEGLRSGDAD RDQDGLVGLD ELYEYVYDRV RASTSNQTPG KWVFDLQGDL
YIARRGRPVT VPSELPLELR EAISHPNRLV RVGAVDDLTR LLTGGHEGLA LAARLALEAL
SDDDSRSVAA AATSTLAANR PPLPPPVRPE PARPDPVASV PSPAAQSEPD HPQPTRPGAH
PQSTKPEPAQ PRSTQPEPDH PQSTRPGYAR PQSTQSGLTQ PQSAQSGFAR PQSGQPDAAP
PPATQPSAAQ SKSTQPESTQ LESAQPQPAR SELGTPAQPE PDRPGPARSK QGRQRRGLAE
IVRLKLAPPE HASDTPSPIT QSRETPRTLL VWRAVSAVLA IAAAVTLAAT PGDVALQTTY
GSFVRGPVLV PASTSVLVPL VGWLLIAALV GLVVVHRGRR AIALGAAFGA IAIMAAFATR
LAAIGVMGTP VRFYCLGLLG AFLAVVIANA VRRRGWLWEV ITGAGALTVA TVALAFPRYR
DDTGTVVLIG LAVLVGAAVT HLVRTARAGR PVARDITFHA LVIAIACVGL ALDDVDMTIR
LTVAALSLAA QPLFTDRGSL LPARAGLVAT LVVMVPPDVE DITQTLVLTS AAVIAAVVAM
WPEPGKTRAR AV
//