ID A4BGZ7_9GAMM Unreviewed; 1679 AA.
AC A4BGZ7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=PKD domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=MED297_03025 {ECO:0000313|EMBL:EAR08643.1};
OS Reinekea blandensis MED297.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Reinekea.
OX NCBI_TaxID=314283 {ECO:0000313|EMBL:EAR08643.1, ECO:0000313|Proteomes:UP000005953};
RN [1] {ECO:0000313|EMBL:EAR08643.1, ECO:0000313|Proteomes:UP000005953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED297 {ECO:0000313|EMBL:EAR08643.1,
RC ECO:0000313|Proteomes:UP000005953};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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:EAR08643.1}.
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DR EMBL; AAOE01000018; EAR08643.1; -; Genomic_DNA.
DR RefSeq; WP_008047268.1; NZ_CH724153.1.
DR STRING; 314283.MED297_03025; -.
DR HOGENOM; CLU_241530_0_0_6; -.
DR OrthoDB; 292013at2; -.
DR Proteomes; UP000005953; Unassembled WGS sequence.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00838; MPP_superfamily; 1.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 2.60.120.200; -; 3.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR015914; Purple_acid_Pase_N.
DR NCBIfam; NF038128; choice_anch_J; 3.
DR PANTHER; PTHR45867:SF3; ACID PHOSPHATASE TYPE 7; 1.
DR PANTHER; PTHR45867; PURPLE ACID PHOSPHATASE; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF18911; PKD_4; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50093; PKD; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000005953};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1679
FT /note="PKD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002666550"
FT DOMAIN 629..720
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1225..1311
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
SQ SEQUENCE 1679 AA; 183702 MW; FD8BF5DFD1756CFF CRC64;
MKLRTSLLAA SIALPSLTMA AADLERVVWT EQPDTEATIA WRQVSGENPR VEFGQGQSPD
SWQTQPVEQV TTLAHPDDGG VTLETHIARL SGLTPDTAVS YRICDSEGCG DASWFMTAPN
TPSEFSYIAG GDSRTNREPR QMGNELVSKL RPLFILFNGD FTDDGNHDQW VEWLEDWQLA
RSDDGRVYPI IATHGNHEND VIDMLSDVFG IPESSYYVAN IGGSMMDIFS LNSELEPGVG
YGAYSDQDAS GWEVQNEQFV ADAQASDADW KIANYHRPMR PHTSGKTEGE GRIAAWAPTF
TDTGFKLIVE SDTHMSKYTF PVVYSQDEGS YQDFKRDDVN GTMIIGEGSW GAPTRPTDDD
KPWTIDSGSF WQFKLIHASP DAMNIHTVRF GSEHETLRGV ETDISGVGTL TQADQNTNPF
AVPANLPLWQ PLAGSAVTMT LDGFKGADID NLQLVGSKAE WAYLDDNSSP EGWNTLEFDD
SGWARGNAQL GYGDGDEVTE LSFGPDADNK FTTTYFRKRF TLDNPADVIK LTLRLLRDDG
AVVYINGQEV VRSNMPEGDI TPSTFAGSGI GGSAESTFYE YALFADALQS GENVIAVEVH
QSDASSSDLS FDMDLTAVVS DTDAPLADAT TELTAKPLSV SEIQLSWSDD ENFNEVGYQL
ERKIGNGPWE ILTWRLDVNE TSYLDKKLIE GATYHYRVRP YNAAGLGALS NELSVATLSN
PTPKLYEETF ESGGWGELTM ISKASNADWE VVERSEAFYA QNNGYGADSA SDDWIITPAF
ALDFYADAQL AFEAAYNYDG PLINVLYSND YDPAVNDDPA SAEWTAIPEC SAVDGAQPCW
NEPSTGSYVF EVSEVDISSI EGDNVRFAFQ YVSTGTGGGD GRYWQLDNIV VRGLYDAPAL
VGDALNDGVP SDWSVVSVAS DKDWAPGTRA EQAGIFANGF GGDTASEDWL IMPTVELSKA
DNAALEFDFY QKYDGPALKV MASTDYSGDA AAATWTDLGL AMPTLDDTWM TIGPIDLVGL
TGDVTLAFLY TTTGTGGGEG AYHGVANAFV KKHLKGVYQE RVVWTEGFED VSTFGTFSTY
SRASNADWVV EERADNLGAV ANGFGADSAS DDWLISPEFY ILDWQNAQFA FDVYTKYGGP
ALELYISNDY TGEGDPLDAN WTQIEFDQSQ EVDEVWNAYQ VDVSAYTGGA HIAFRYLTTG
TGGGEGRRLG VDNPTLISTY GEESLKANFS IASTTVTTIE PVTFEANVKG GEAPYDYAWN
FGDGTVGGNA NMEHTFADAG TYTVTLTVTD ANGNTVEQAR QNYVTVLQST DVGVPSYAGD
VRVATFNAYL NRSSEGQILA DAQSGDDAQI QNVAEIIQRV RPHVVLLQEF DYVADGSAVK
ALQENYLGKG WNGAERIEYP YVYLAESNTG IITPFDFNKD GQSGQYGDDA YGFGMFYGQY
GMVLLSQYPI DYANARTFQK FLWKDMPDAK LPVNPETGES WYTEEELDVF RLSSKSHWDI
PVKVGKHTLH VLASHPTPPV FDGDEDRNGL RNHDETRFWR DYVDPARSSY IYDDNGNIGG
MKGERHHFVI MGDLNASPVE GDATDDPIGL LMASPYVNGD VQPTSQGGVD NDPANENAPA
HTADWKMRAD YVLPGTWGNK VEQSGVYWPG IADVNHRLVG PGVKSSDHRL VWMDLTFTQ
//
