ID I0XQ95_9LEPT Unreviewed; 931 AA.
AC I0XQ95;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=PKD/Chitinase domain-containing protein {ECO:0000259|SMART:SM00089};
GN ORFNames=LEP1GSC185_3723 {ECO:0000313|EMBL:EIE01053.1};
OS Leptospira licerasiae serovar Varillal str. VAR 010.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049972 {ECO:0000313|EMBL:EIE01053.1, ECO:0000313|Proteomes:UP000004889};
RN [1] {ECO:0000313|EMBL:EIE01053.1, ECO:0000313|Proteomes:UP000004889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VAR 010 {ECO:0000313|EMBL:EIE01053.1};
RX PubMed=23145189; DOI=10.1371/journal.pntd.0001853;
RA Ricaldi J.N., Fouts D.E., Selengut J.D., Harkins D.M., Patra K.P.,
RA Moreno A., Lehmann J.S., Purushe J., Sanka R., Torres M., Webster N.J.,
RA Vinetz J.M., Matthias M.A.;
RT "Whole Genome Analysis of Leptospira licerasiae Provides Insight into
RT Leptospiral Evolution and Pathogenicity.";
RL PLoS Negl. Trop. Dis. 6:E1853-E1853(2012).
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:EIE01053.1}.
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DR EMBL; AHOO02000009; EIE01053.1; -; Genomic_DNA.
DR RefSeq; WP_008588999.1; NZ_AHOO02000009.1.
DR AlphaFoldDB; I0XQ95; -.
DR PATRIC; fig|1049972.3.peg.2389; -.
DR OrthoDB; 9782766at2; -.
DR Proteomes; UP000004889; Unassembled WGS sequence.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.130; Integrin alpha, N-terminal; 4.
DR InterPro; IPR013517; FG-GAP.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013519; Int_alpha_beta-p.
DR InterPro; IPR028994; Integrin_alpha_N.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR36220:SF1; -; 1.
DR PANTHER; PTHR36220; UNNAMED PRODUCT; 1.
DR Pfam; PF14312; FG-GAP_2; 6.
DR Pfam; PF18911; PKD_4; 1.
DR SMART; SM00191; Int_alpha; 6.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF49299; PKD domain; 1.
PE 4: Predicted;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..931
FT /note="PKD/Chitinase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003636867"
FT DOMAIN 146..230
FT /note="PKD/Chitinase"
FT /evidence="ECO:0000259|SMART:SM00089"
FT DOMAIN 248..336
FT /note="PKD/Chitinase"
FT /evidence="ECO:0000259|SMART:SM00089"
FT REGION 622..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 96283 MW; 9C7EEB185BCC76C5 CRC64;
MKTKLMLILL ICLNSFCSGT NSGLSALAAF LGLPQTPSYG NVQFAVNVSS ALTKVTVTVT
GPGISTPIVQ DLVKVGNTWQ GIIGQIPAGS DRTFSGEGFN ASNVLIQQGQ VTGVSITANS
ITNILLVLSE TNPAPPFSNA APIIDSLVAS TNRVAPSSSI NLSSSAHDPN PSDTLTYLWS
ATGGSFSNSN ILNPVWTSPS TPGQYTITLT VSDQLGASST LSFTADVQLG YGTGYGSINV
GSNSSPFVSN VISDPTSIPP GASTNISLTA FDPDGDTISY SWGSSCAGSF DNANAQDPVF
TASPSASLGP CTLSVSLSDG NGGSNLGNFT IQISQTQTVN LAPQILSSFQ TALALDPSGN
MLFRVTATDP ENTPLSFSWN SSSGVVGTPT NTINGNLTTS EMVWTAPTCG SNLQVSVTVT
DGDGNSANLN YLPVNINGAP TCVLGLWSQQ SYIKASNSEA NDNFGRSWAL SGDTMVVGAP
LEDSSQTTII NGSNPGPSDN SAPASGAVYV YVRNGNTWTQ QAILKPSNSE ESDLFGFAIS
ISGDTIVASA IQEDSNQNYI TNGSSASSDN SMTYSGAVYV FVRNGNTWSQ QAYIKPSNPT
ANDAFGTAIA IEGDTLVVGS HNESGSQNTI TNGQPAPDDD SLYHSGAVYV YKRTGTTWVE
EAYIKAPNPD QGDYFGYSVA ISGDTIAVGA QYEASNQNYI TNGSGASSDN NMPGAGAVYI
FSRSGNSWMP EAYIKPSNPD VYDNFGTAVS IYGDTIVVGT PSEDSNQNTI SSGTNASSDN
SSESAGAVYV FARSGGIWSQ QAYLKASNSD PFDYFGAAIS IYGNTIAVGA LESSSQTTIS
YGNTASSDNS AQYAGAVYIF ERNGTSWAQT AYIKAPNANA YDFFGGVCLD GNNLLVSAYL
ESSSENTITN GVYGSADNSA SGAGAAYIFT R
//