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Database: UniProt
Entry: A0A367ELN9_9ACTN
LinkDB: A0A367ELN9_9ACTN
Original site: A0A367ELN9_9ACTN 
ID   A0A367ELN9_9ACTN        Unreviewed;       569 AA.
AC   A0A367ELN9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=PDZ domain-containing protein {ECO:0000313|EMBL:RCG18669.1};
GN   ORFNames=DQ384_38900 {ECO:0000313|EMBL:RCG18669.1};
OS   Sphaerisporangium album.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Sphaerisporangium.
OX   NCBI_TaxID=509200 {ECO:0000313|EMBL:RCG18669.1, ECO:0000313|Proteomes:UP000253094};
RN   [1] {ECO:0000313|EMBL:RCG18669.1, ECO:0000313|Proteomes:UP000253094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCTCC AA 208026 {ECO:0000313|EMBL:RCG18669.1,
RC   ECO:0000313|Proteomes:UP000253094};
RA   Li L.;
RT   "Sphaerisporangium craniellae sp. nov., isolated from a marine sponge in
RT   the South China Sea.";
RL   Submitted (JUN-2018) 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:RCG18669.1}.
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DR   EMBL; QOIL01000036; RCG18669.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A367ELN9; -.
DR   OrthoDB; 73775at2; -.
DR   Proteomes; UP000253094; 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:InterPro.
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; 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   PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR   PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253094};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        203..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          472..549
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          1..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        138..185
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   569 AA;  56775 MW;  645218F7EE7A48EB CRC64;
     MRSERQSDVA AADSPGSERS MTDETRTFDA GDVAASSQRS SEGSPPGEPG VMRVRPEFLP
     ASDGRPAGAP VSGPDAFTGP NPFAARGQGY EGGDPFAPGP YAPRDTMTDT LVPFAAESGD
     DTGRRPGGEG ASGWGNPSGP VPPSPRQAPY GSPGGPYPGG PGGPYGPPPP RNPYGMGPGW
     APPPGAPRTE TGAAGSRGPR TGVLAALAVV IALVASTAGS VGTYLLTRSN GDGVDPAYSL
     GTPTGAIVNR APDSVAGVAS KVLPSVVSLD VRGNSEAGTG SGFVIKGGYV VTNNHVVAAA
     AQTGNIKITF NDKKSTAAKI VGRDPSSDIA VVKPDDTFGV PEITLGNSDR VVVGDPVIAI
     GSPLGLTGTV TTGIISSLNR PVTAGGESGS ESSFINAIQT DAAINPGNSG GPLVNGAGEV
     IGVNSAIATL GNSSLGSQSG SIGLGFSIPI NHVRRVAEEL ITTGSAKKSR IGVQLDPDYQ
     GEGVRIATTA EQGQPPVVPG GPADKAGMKP GDVILAIDGN PVSDQAELIV AIRSKAPGDT
     VTLKFRRDGR DMTASVTIDA VPVPTPQPS
//
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