ID A0A1B6YD54_9BACT Unreviewed; 1738 AA.
AC A0A1B6YD54;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=PKD domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A8B79_12870 {ECO:0000313|EMBL:OAN64233.1};
OS Balneola sp. EhC07.
OC Bacteria; Balneolota; Balneolia; Balneolales; Balneolaceae; Balneola.
OX NCBI_TaxID=1849360 {ECO:0000313|EMBL:OAN64233.1, ECO:0000313|Proteomes:UP000078514};
RN [1] {ECO:0000313|EMBL:OAN64233.1, ECO:0000313|Proteomes:UP000078514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhC08 {ECO:0000313|EMBL:OAN64233.1,
RC ECO:0000313|Proteomes:UP000078514};
RA Lavstsen T., Jespersen J.S.;
RL Submitted (MAY-2016) 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:OAN64233.1}.
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DR EMBL; LXYG01000002; OAN64233.1; -; Genomic_DNA.
DR RefSeq; WP_066217069.1; NZ_LXYG01000002.1.
DR STRING; 1849360.A8B79_12870; -.
DR InParanoid; A0A1B6YD54; -.
DR OrthoDB; 9794455at2; -.
DR Proteomes; UP000078514; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 2.60.40.4070; -; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR010895; CHRD.
DR InterPro; IPR011048; Haem_d1_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
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; IPR026444; Secre_tail.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR NCBIfam; NF038117; choice_anch_I; 1.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR46928; MESENCHYME-SPECIFIC CELL SURFACE GLYCOPROTEIN; 1.
DR PANTHER; PTHR46928:SF1; MESENCHYME-SPECIFIC CELL SURFACE GLYCOPROTEIN; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF07452; CHRD; 1.
DR Pfam; PF00932; LTD; 1.
DR Pfam; PF18911; PKD_4; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SMART; SM00754; CHRD; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF51004; C-terminal (heme d1) domain of cytochrome cd1-nitrite reductase; 1.
DR SUPFAM; SSF74853; Lamin A/C globular tail domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS51841; LTD; 1.
DR PROSITE; PS50093; PKD; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000078514};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1738
FT /note="PKD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008591248"
FT DOMAIN 696..877
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT DOMAIN 1584..1646
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 558..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1738 AA; 185887 MW; 47EA18A060FA752B CRC64;
MKKKANFSLL LAVMIFTSTV VFAQEVSFDF LGDYHTGVFD GGAAEISAYD PASKHLFFTN
ADANSVVVLD ISDPNNPTEV TNIDMSVYGG GVNSVAIFNG LVAVAVEAAI KTDAGSVVFF
EASTGAFINS ITAGALPDML IFTPDGSKVI VANEGEPNDD YDVDPEGSIT IIDVSGGAAS
ATTSTADFTA YNSEKTTLLE AGVRIFGPGA TVAQDLEPEY IAIDSTGTTA YVSLQEANAL
AVVDITSATV TEINALGYKN HATAGNELDA SNDDDEINIT NWPVWGMYQP DAISSFTMNG
TTYIVSANEG DSRDYDGFSE EARVKDLRLN PSIFTDPDLQ EDENLGRINI TTTLGVNTDS
TFLYTELDGD QEVAEVDSDA EGEGEFYLSA TEDTLHYLFY IEGLDFGEIA GGDSVTVSSL
DDVTGMHFHF EESGANGNVV FNIGTDADTE FELVDSTAAW ISGFWVQGEG LNGSDLSDFV
SALKSAAFEE EVNLYVNVHT AANPGGEIRG QLYGDPMYDA LYSYGARSFS IWNPSTGELV
WDSGSEFEQI LSVLDPENFN STNSENDSFD NRSDDKGPEP EAVTVVKLAG KVYAFIGLER
IGGVMVYDIT NPTAPEFVTY DNVRNFDEAN FNEDMIESLD DLADHSGIKT ILESTIASGP
ESISFLKQGA SPIGLPLAVL SNEITGSITI HEINFETQAA PLFFSEYAEG SGNNKYIEVY
NPTNEDVSLA NYAFPNMNNG LTGSNQNNVA GEFDFWNTFP EGAVVPAKGT YVIANSSADA
GVLDFADGTG SVFHNGDDAY ALVYGTENNY EILDIIGDLF ADPGSGWEVA GVANGTQDHT
LVRKVEISHG NPAPQGSFGT NTEDSEWIVL AQNDWSSLGI RGIPEPFTLT VLHNNDGESQ
LLNAGAGFEN FGGVARFKTL TDQQKQDAWD AGNEVIMVSS GDNFLAGTEF NASLDLGTFF
DARAIGLIGY DALAMGNHDF DAGPVTYSGF ISDTRGNMPP FLSANLDFSN QPELLELQTK
GRIAKSTTIE LSNGASVGII GATTENLNFI SSPGTVIVNE VLPAVQAEVA ALQAQNIRSI
VLISHLQGIE EDSLLAAQLT GIDIMIAGGG DELLANDDNL LIPGDEALIR SSYPMIVKDA
ENKEVPVVTT KGNYTYLGRL NVDFDINGEV TSFNGGPIRV ADASLEGGVE EDSQVLQEVV
EPVREYVEQL SRIKVATTEV HLIGERNQIR SRETNLGNLI TDGYLAVTLA TAENFGLDLD
PSRLVALANG GGIRDQIPAG IITASQTFDV LPFGNILAVV EDVSPTLLLE IMENAVSSID
PETGMGTGDG TGRFAQIAGF RIEFDPSEQA IVYNNDQGQT IATQGNRIKT ITLADGTAIV
IDGEIAEGAP TVDLVTADFT ARGGDQYPFR GKEFKTIGIT YQQSLQIYLE DFLGEIVFAS
RYPMGGSGRI IDLKNSIENA APDINLPVEM SFLEDEALTF ELGQVITDAN DELSSLTVLI
QGGQISGSAN GNVLSFSAPE NHFGQERVKV TVMDSFGATA SDSVLITVVP VNDAPTADFK
LEKSGFENGD NVVTFIDESN DEKDPNGAII SYSWNFGDGS TSTDKNPVHT YNSVDEYEVV
LTVTDNEGAV SKSTQTVEVS VVTSIETENL PSEFALKQNY PNPFNPSTNI SYDVPKASKV
HIDVYNIMGQ KVATLVNETK AAGTYSVSFD AAQLSSGMYI YRLQAGNFLS TKKMMLIK
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