UniProt: A0A654DTK9

Database: UniProt
Entry: A0A654DTK9_9BACT

LinkDB:  A0A654DTK9_9BACT 
Original site:  A0A654DTK9_9BACT

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Ontology (2)   
   GO (2)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (3)   
   SMART (1)   
All databases (19)   

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ID   A0A654DTK9_9BACT        Unreviewed;      1382 AA.
AC   A0A654DTK9;
DT   22-APR-2020, integrated into UniProtKB/TrEMBL.
DT   22-APR-2020, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=PKD domain-containing protein {ECO:0000259|PROSITE:PS50093};
GN   ORFNames=MARINOS108_10368 {ECO:0000313|EMBL:VXD11041.1};
OS   Marinoscillum sp. 108.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Reichenbachiellaceae;
OC   Marinoscillum.
OX   NCBI_TaxID=2653151 {ECO:0000313|EMBL:VXD11041.1, ECO:0000313|Proteomes:UP000437459};
RN   [1] {ECO:0000313|EMBL:VXD11041.1, ECO:0000313|Proteomes:UP000437459}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marinoscillum sp. 108 {ECO:0000313|EMBL:VXD11041.1};
RA   Karimi E.;
RL   Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000256|PROSITE-
CC       ProRule:PRU01240}.
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DR   EMBL; CABWNM010000001; VXD11041.1; -; Genomic_DNA.
DR   Proteomes; UP000437459; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00146; PKD; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   InterPro; IPR026444; Secre_tail.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   PANTHER; PTHR43399; SUBTILISIN-RELATED; 1.
DR   PANTHER; PTHR43399:SF4; TK-SUBTILISIN; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   Pfam; PF18962; Por_Secre_tail; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SMART; SM00089; PKD; 3.
DR   SUPFAM; SSF49299; PKD domain; 2.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS50093; PKD; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000437459};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..1382
FT                   /note="PKD domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5024889243"
FT   DOMAIN          927..980
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   ACT_SITE        157
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        212
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        367
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   1382 AA;  151835 MW;  DA1CFA6C8079D592 CRC64;
     MIKRPTYWLT LLLILISTYG QAQDSHVLPG VLYVKIKSSP STADASTELF QFSEMENLKS
     YTPLRKNANG NRQKASVLDG LFKVVVDPST DIAALCASLH KYANVSYAEP IYAAQLLYVP
     DDPESTTPNQ EYLSVIRAFE AWDVTKGSSD IVIGISDTGL NLTHDDIKSK LYTNTNDPMN
     GLDDDENGYV DDFQGYDFAD NDSLPKCDDS FHGNRVGGLA GAATDNGFGM AGVGFNTMIS
     PLKVYSTALK FINSGYESIL YAADNGYDVI NLSWGGPNSY SQANQDIITY AAVEKNVVIV
     AAAGNTPEDI RFYPASYDHV LSVAASNLND TKASFSTYNY DVDLMAPGNT IYSTDSGNGF
     AKDNGTSYSA PMVAGAAALV KSVFPDLNSL QIMQQLRVTS DPVYTTGTNQ TYEGKLGYGR
     LNVSNAVRED SAKSIRLENL VYDNGNGNYA FYGDTIVLSF EAKNYLFPTD SATLSFTSAS
     SHVEIIRETI YLGAMNTLES DSIQEKIFVI AKDTPPGTDL EIKVSITDGS YIDFQYIELT
     TDPDRLDLNN DQFSITLSGN GDLGFISDGY YNGVGFQWDD QLIAAKMGVA VSLDRSHVSD
     NFPDSIYTNT KASDFVAISP IRFAHHTTPD LHATSVFRDD SAATPLEIVM EQNTLTNRGA
     NFLIQEYRLM NNATESREGL ACSFYLDWEI FNTMQNRSFY DTESKTLITY NLDSSVVVGL
     LTYYDSLPRA QSLDLDVYNG NEQDVQMHYT DSVKYALARE VRFDSAGWQG NGNNVSVMLT
     HDSIALAPSK SRRVAYFMGL SHSFEGLAAV MDSARQVYEE YLNLPVLLER YVSCQGASVS
     IAPASGEVFR FFSDPLGENI IGEGDTLKTG AIVSDTTFYV ANLDSGYEGS IQRIEIALLA
     QIADFQMSTD TLFLDNSVNS VTFTDLSFDP ASWYWDFDNG SQITTQNATV YFRDPGVYTI
     SLTIETNSGC TQTITKELLV ANRPPLPDIE DQQVCADQDF TVSAPNADSI AVYLDGSSPT
     PLQEGPSITL EGISSDTAYY FTNTSGPFES LRKRVYFSIN HANATFEYLP DTLNEATGVL
     FINTSPESAS AQWYVDGLLK SELDTFYMEV RKASYEITLS ITNTTGCANA TTQSVTFATS
     PLPMAENQLI CTGSNLLLEP NNGEWFAFYA NEALSHLIKK GRNLTIAELK KDTTIYVTGL
     DSILPSAAIP VEITVALPQF SIVATPDTLY LSEQSTTSFS TNNDELIGWD WYIDNTPTET
     TSHPILYFDT EGVYDIVLNA TGPMGCTNSD TLKYPVYQSR PEVLLGVDDS QQVIYPNPTT
     GDLFIVVTAP TEVTISDVSG RIMQKIYLEE SALIDLNHLP KDIYLLTLKS QKEISNHRVI
     FK
//

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