ID A0A0C2QT16_9CYAN Unreviewed; 412 AA.
AC A0A0C2QT16;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:KIJ81460.1};
GN ORFNames=SD80_25860 {ECO:0000313|EMBL:KIJ81460.1};
OS Scytonema tolypothrichoides VB-61278.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=1233231 {ECO:0000313|EMBL:KIJ81460.1};
RN [1] {ECO:0000313|EMBL:KIJ81460.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB-61278 {ECO:0000313|EMBL:KIJ81460.1};
RA Tripathy S., Das A., Panda A., Malar M.C., Adhikary S.P.;
RT "Draft genome sequence of Scytonema tolypothrichoides VB-61278.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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:KIJ81460.1}.
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DR EMBL; JXCA01000014; KIJ81460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2QT16; -.
DR STRING; 1233231.SD80_25860; -.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR048172; HhoA_HhoB_HtrA-like.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR NCBIfam; NF041521; HhoA_HhoB_HtrA; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KIJ81460.1}.
FT DOMAIN 296..395
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 48..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 412 AA; 43599 MW; C03BF3058342BB0F CRC64;
MVPFDPSANN NQTQKRFSWQ KSVTHLSLVL LGSGVTLSGG YLLAGNPLSP QQPNSQEVAV
SNNKTAQSNL PPTTNNNFVT TVVDKIGPAV VRIDASRTVT SRVPEVFNDP FFRDFFGLGS
MQPRRRTERG TGSGFIVSSD GRILTNAHVV DGAQTVRVRL KDGRSFEGKV LGTDPVTDVA
VIQIQASGLP TVRLGNSDQL TPGEWAIAIG NPLGLDNSVT TGIISATGRS SSAVGVPDQR
VKFIQTDAAI NPGNSGGPLL NQQGEVIGMN TAIIQGAQGL GFAIPINTAQ RIANQLVANG
KIEHSFVGIQ MVDVTPELKQ EINSDPNRLM KVDAANGVLV VRVVPNSPAA KAGLRAGDVI
QKLNGKSVTE AQTIQQTVEN SSVGENLRLQ LRRQGTNIDL SVRTGAIPVQ IQ
//
