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Database: UniProt
Entry: A0A0C2PZ59_9CYAN
LinkDB: A0A0C2PZ59_9CYAN
Original site: A0A0C2PZ59_9CYAN 
ID   A0A0C2PZ59_9CYAN        Unreviewed;       401 AA.
AC   A0A0C2PZ59;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Serine protease {ECO:0000313|EMBL:KIJ76844.1};
GN   ORFNames=SD81_14450 {ECO:0000313|EMBL:KIJ76844.1};
OS   Tolypothrix campylonemoides VB511288.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC   Tolypothrix.
OX   NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ76844.1};
RN   [1] {ECO:0000313|EMBL:KIJ76844.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VB511288 {ECO:0000313|EMBL:KIJ76844.1};
RA   Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT   "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT   VB511288.";
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:KIJ76844.1}.
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DR   EMBL; JXCB01000008; KIJ76844.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C2PZ59; -.
DR   OrthoDB; 9807133at2; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KIJ76844.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          284..386
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   401 AA;  42577 MW;  562EDAD824B54922 CRC64;
     MKLSLKQLVI YLSILTIGGG AGLLGSRYLP PQNRLFRELR TVTASSPPEI APANPVGGQV
     AAPSADNMNF IATAVQRTGP AVVRINATRK VANPISDALK NPLLRRFFGE EEQPFPKERI
     ERGTGSGFIL SENGQILTNA HVVADTDTVQ VTLKDGRTFE GRVVGVDSVT DVAVVKISDY
     DLPTVKLGTS QNLIPGQWAI AIGNPLGLDN TVTIGIISAT DRTSAQVGVP DKRVSFIQTD
     AAINPGNSGG PLLNAQGEVI GVNTAIRADA QGLGFAIPIE TAARIANELF TKGRVRHPFL
     GVEMSDLSSS KKQQINQDKN LNIKQDVGIA ITGVLENSPA QRGGLLPGDL IQKVNGKQVK
     TSAQVQKQVE SSTVGDILEI EVNRNGKIQT FKVQSGAYPQ K
//
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