ID A0A0D6L1Q8_9CYAN Unreviewed; 420 AA.
AC A0A0D6L1Q8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Protease Do {ECO:0000313|EMBL:EKF05669.1};
GN ORFNames=FDUTEX481_00524 {ECO:0000313|EMBL:EKF05669.1};
OS Tolypothrix sp. PCC 7601.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1188 {ECO:0000313|EMBL:EKF05669.1, ECO:0000313|Proteomes:UP000032761};
RN [1] {ECO:0000313|EMBL:EKF05669.1, ECO:0000313|Proteomes:UP000032761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7601 / UTEX B 481 {ECO:0000313|Proteomes:UP000032761};
RX PubMed=25953173;
RA Yerrapragada S., Shukla A., Hallsworth-Pepin K., Choi K., Wollam A.,
RA Clifton S., Qin X., Muzny D., Raghuraman S., Ashki H., Uzman A.,
RA Highlander S.K., Fryszczyn B.G., Fox G.E., Tirumalai M.R., Liu Y., Kim S.,
RA Kehoe D.M., Weinstock G.M.;
RT "Extreme Sensory Complexity Encoded in the 10-Megabase Draft Genome
RT Sequence of the Chromatically Acclimating Cyanobacterium Tolypothrix sp.
RT PCC 7601.";
RL Genome Announc. 3:0-0(2015).
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:EKF05669.1}.
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DR EMBL; AGCR01000004; EKF05669.1; -; Genomic_DNA.
DR RefSeq; WP_045867707.1; NZ_JH930357.1.
DR AlphaFoldDB; A0A0D6L1Q8; -.
DR STRING; 1188.FDUTEX481_00524; -.
DR PATRIC; fig|1188.3.peg.520; -.
DR HOGENOM; CLU_020120_1_2_3; -.
DR OrthoDB; 9807133at2; -.
DR Proteomes; UP000032761; Unassembled WGS sequence.
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:EKF05669.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 322..402
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 43791 MW; D6D6BC5C0C9BF70B CRC64;
MQNQPRDGDN FSNSNSSNTS GTKHRNHAPW TKAAASLSLV LLGSGMTLAG GYLAGHPQKL
SQSASNLAVS PVNAAPPITA GTDPNFVTEV VQRVGPAVVR INSSRTVKTQ LPEEFNDPFF
RRFFGSQLPQ GNQVQRGTGS GFIIGKDGRI LTNAHVVDGA DTVTVILKDG RSFQGKVLGK
DELTDVAVVK IQADNLPTVS LGNSDQLQPG QWAIAIGNPL GLDNTVTTGI ISATGRSGNQ
IGASDKRVEF IQTDAAINPG NSGGPLLNSR GEVIGMNTAI IQGAQGLGFS IPINTAQRIS
NQLIATGKAQ HPYLGIQMVG LTPELKQNIN SDPNSGLSVA EDKGVLVVKV VPNSPAAKAG
IRAGDVIQKL NGQTVTDASS IQKAVDNSEI GGDVRLELRR NGQNVSVAVR PGAFPTNLVQ
//
