ID   H6L739_SAPGL            Unreviewed;      2332 AA.
AC   H6L739;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=PKD domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=SGRA_3915 {ECO:0000313|EMBL:AFC26630.1};
OS   Saprospira grandis (strain Lewin).
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Saprospiraceae;
OC   Saprospira.
OX   NCBI_TaxID=984262 {ECO:0000313|EMBL:AFC26630.1, ECO:0000313|Proteomes:UP000007519};
RN   [1] {ECO:0000313|EMBL:AFC26630.1, ECO:0000313|Proteomes:UP000007519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lewin {ECO:0000313|EMBL:AFC26630.1,
RC   ECO:0000313|Proteomes:UP000007519};
RX   PubMed=22675601; DOI=10.4056/sigs.2445005;
RA   Saw J.H., Yuryev A., Kanbe M., Hou S., Young A.G., Aizawa S., Alam M.;
RT   "Complete genome sequencing and analysis of Saprospira grandis str. Lewin,
RT   a predatory marine bacterium.";
RL   Stand. Genomic Sci. 6:84-93(2012).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002831; AFC26630.1; -; Genomic_DNA.
DR   RefSeq; WP_015694213.1; NC_016940.1.
DR   STRING; 984262.SGRA_3915; -.
DR   KEGG; sgn:SGRA_3915; -.
DR   eggNOG; COG3291; Bacteria.
DR   HOGENOM; CLU_001092_0_0_10; -.
DR   OrthoDB; 9792152at2; -.
DR   Proteomes; UP000007519; Chromosome.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00146; PKD; 1.
DR   Gene3D; 2.60.40.740; -; 10.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   InterPro; IPR026444; Secre_tail.
DR   InterPro; IPR025667; SprB_repeat.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   Pfam; PF00801; PKD; 1.
DR   Pfam; PF18962; Por_Secre_tail; 1.
DR   Pfam; PF13583; Reprolysin_4; 1.
DR   Pfam; PF13573; SprB; 13.
DR   SMART; SM00089; PKD; 5.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50093; PKD; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007519}.
FT   DOMAIN          209..421
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          1032..1097
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
SQ   SEQUENCE   2332 AA;  237541 MW;  F4B5BE8F5A6E01B1 CRC64;
     MQLTYLRSFL LAWLLLLGSQ LWGQTELWSP IVEDQIPKSG TRYIFAEQYQ TVRLNLDEIR
     TILDVAPMER TPIAAMSQTL LSLPMPDGSY EVFDIVESPI METELAEKFP EIQTYAGRSI
     NDPSKSLRFD LTPQGFHAII LTAGKGTIYI DPYQFGGGDI EHYIVYNRRD FRPAAPKQFV
     CGLTGNNIPL SNFKAAGQSA ARFGSCELRT YRMAVAATGE YTQFHGGTVA LALAAQTTTI
     NRVNSVYERE MAIRMNLVAN NNLIIYTNAT TDPYTNGAPG TMITENQANI DSEIGSANYD
     IGHVFGTNSG GLAGLGVVCS NSGKARGVTG SAAPIGDPFD IDYVAHEVGH QFGCNHTQNN
     NCNRNNATAM EPGSASTIMG YAGICAPNVQ NQSDDYFHSI SLEEMGAFIT GAGHNCPATT
     ALANNAPTVN APAANINIPA NTPFSLTASA TDPDGNTLTY SWEQMENATA TMPPVASSTA
     GPNFRSFEPV TDPTRYFPNL VDLAAGGPFT WEVLPSVSRV MDFRVTVRDN AAGGGCSDHA
     DMQVTVDANS GPFVVLYPSA SGISWNGGGT ETVTWDVAGT DGSPVSCANV DILLSTDGGL
     TYPTVLASNV PNDGTEPISV PNVGTTTGRI MVRCANGYFF DISDNDFTIV LATNDYTLST
     TNNSQSVCAA ATPSYSIDVG QIGSYSDPVT LSLSGLPTGV VGSFSTNPVT PAASSTLTLN
     VGGGVTAGSY PFTVNASSTS GNKSLALTLV VNDPTPTAVT LNSPANGATA LALPVNFDWS
     TAAGANSYTI SIATDAAFTN VVDQATGLSS PNYTSNVLGT GTQYFWEVIA INSCGSSPAA
     GASFSSGLQA CDTISNYDVA NDNPALYNAG GPGGYLSGHN GYGDLAKADY FNYGGANTHL
     TGAYFGFGQA VAANASNSFN VQVWDGTGGT PGAIIASIPI AYQDIVTLIA GGNNVAFVPF
     GNIALPASNE VFVGIEYTYG NDTIALITNT DGETSPATAW EQWGDGTWHA YDETGSWGID
     VAHYIVPVLG TLPSANFSPN NSTICLGNSI TFNNSSTDAD SYEWFFPGGS PASSTAMNPS
     VSYNTAGTYD VALVATNDCI SDTLIVLSAI TVSEVVTGIG SSDETCAGND GTATVSATSG
     TAPYTFLWSD GQTTATASGL SAANYFVTVT DANGCTAVSS VAVTLNCSCT LAATTSATDA
     SCNASNDGSA TAIATAGTTP YSFLWSDGQT TATATNLIAG TYIVTVTDAA GCTTTATAVV
     NEPTALVASA SSSDETCAGN DGTATATISG GTAGYTFLWS DGQTTATATN LIAGTYTLTI
     TDANGCQTTA TAVVNNSCTP CTLASTTSAT DASCNASNDG SATAIATAGT TPYSFLWSDG
     QTMATATNLI AGTYIVTVTD AAGCTTTATA VVNEPTALVA SASSSDETCA GNDGTATATI
     SGGTAGYTFL WSDGQTTATA NNLVAGTYTV TITDANGCQT TATAVVNNSC TPCTLAATTS
     ATDASCNASN DGSATAIATA GTTPYSFLWS DGQTTASASN LIAGTYIVTV TDAAGCTTTA
     TAVVNEPTAL VASASSSDET CAGNDGTATA TISGGTAGYT FLWSDGQTTV TANNLVAGTY
     TVSITDANGC QTTATAVVNN SCTPCTLAAS SSATDASCNA SNDGSATAIA TAGTTPYSFL
     WSDGQTTATA SNLIAGTYTV TVTDAAGCTT TATAVVNEPT ALVASASSSD ETCAGNDGTA
     TATISGGTAG YTFLWSDGQT TATATNLIAG TYTLTITDAN GCTTVATAVV NYNCPCNGSL
     QLTPTDVSCA SNCNGSISLQ SSGLQAPISY RWTNGATVAN PINLCGGNYS VTATDANGCV
     AIASTTVAQP TAMTLATGIN NESCAGNDGN LTAIVNGGTT PYTFAWSNGA NTSSLTALAA
     GVYQLTVTDA NACDLTAAYT VALDNSLASN AVASQNASCA GYADGEAQAV GTGTGLPMNY
     SWSNGANTQV ASGLAAGNYT VTISSGVCSA QRSVQVTEPA AMQIQLMSTE QNCVPGTGAL
     ALNVSGGGGA PYSYLWSNGA TTANVSNLAN GNYSVTITSA NGCEEQRSAS FNIPQGPVLS
     SLSSSPNCSN TADGSLDLTV SPAGNYLYSW SNGANTEDLQ GLAGGIYQVS VTDTAQGCTV
     VLSDTVNAPA SLQLAFSVTQ PHTPTSNNGA LAASENGGTA PFSYLWSTGD SVSQLTNVGV
     GSYSVTVTDA NGCTATDSIF VSAVTGINVQ WAEAFSLYPN PSNGQMQLEL VLQQSQQLEL
     AIFDVLGRQL YQQRLSGQQF SLPLSFDWPA GTYFLRLSSP EGQISQKFVI RR
//