ID A0A2P7TMB0_9SPHI Unreviewed; 1662 AA.
AC A0A2P7TMB0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=PKD domain-containing protein {ECO:0000313|EMBL:PSJ75795.1};
GN ORFNames=C7N43_17130 {ECO:0000313|EMBL:PSJ75795.1};
OS Sphingobacteriales bacterium UPWRP_1.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=2116516 {ECO:0000313|EMBL:PSJ75795.1, ECO:0000313|Proteomes:UP000240367};
RN [1] {ECO:0000313|EMBL:PSJ75795.1, ECO:0000313|Proteomes:UP000240367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UPWRP_1 {ECO:0000313|EMBL:PSJ75795.1,
RC ECO:0000313|Proteomes:UP000240367};
RA Tan S.M.;
RT "Obtaining draft genomes of rare unknown microbial groups and defining 1
RT their spatial structures from highly complex communities.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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:PSJ75795.1}.
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DR EMBL; PXYE01000067; PSJ75795.1; -; Genomic_DNA.
DR Proteomes; UP000240367; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd00063; FN3; 3.
DR CDD; cd06548; GH18_chitinase; 1.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 6.
DR InterPro; IPR011635; CARDB.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR045829; PKD_6.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF07705; CARDB; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF18911; PKD_4; 1.
DR Pfam; PF19408; PKD_6; 1.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS50093; PKD; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Reference proteome {ECO:0000313|Proteomes:UP000240367};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1662
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015197354"
FT DOMAIN 29..394
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 536..621
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1152..1237
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1256..1341
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1354..1440
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
SQ SEQUENCE 1662 AA; 176423 MW; 4733B5EDD9087DEE CRC64;
MRIHPQNIFS AAGMLLIFFC TTLFAQPCKE VIGYYPSWQW YDRAQLVRPA TIDYSKYTIL
NYAFFAPDAN GNISGVDPWA DENLLLGQIN WSTTPPSYYP NTSLIDRAHN NNVKVLVSIG
GWTLSNNFPG IAADPVKRQT FAQSCVNQLQ TYGFDGIDLD WEYPGYAEHN GTPADKQNFT
LLLQAVRDAI DAYGALVDKD FLLTAAVSSA PSNAVNVEWA NVTPLLDMIN LMSYDYFGAW
DPVSNHNSPL YQPAVGDPAF NLNAGFHMLT DTYGVPPGKI NIGVAFYGRS FRQCAGLHQP
HTGADTQTFW QDEGSPLYYN ILNNLGLFNQ NWDVLAQVPY LTGSGALQTV VSYDNPASIA
LKAQYAVNNN ALGVIIWEIT GDYLETAPNS GQIAGTPLAD TLNTVLCGAL QPKPDLTIPS
ATANPFNLTS GSNTTVSCTV ANTGNLGAAA CTLSFYLSAN NTFGPGDVLL TASTIAAINA
GSSLPVSVTL TVPAYATAGV WYIILVADSG NALNESNENN NTAAVLLNVS TPPLPPVADF
TASDVTICAG QQVSFTSLAT NTPTSWAWTF TGGTPATANT ANPVVTYNTP GTFTVSLTAA
NNYGSDNETK TGYITVYANP IANAGPDVAI CSGSSTTLGA SGGINYSWSP TAGLSAANIA
NPVATPAITT TYTVTATNSN GCTATDQITV TVTPTTSAIS GSTTVAANAT ATVYSVANTA
GSTYSWTVPA GATITGGQGT NQITVNWGQT GGIIAVTETA ANACTGTPRT LAVSVQANPV
NCPTRPATYY LTPATLKPAG EIRIGEARLY PVWGVSADAE IPNNRLSWAM AIAHAYQIFA
NVTDTGIMPM NTFFATPLKE SFCGCDAGIQ TDAADPFPLT YQPLSVNDGC FQIEPPPSAY
AELNTMYPQR FPTGQHAQLI GGNHFETAAI GKAYYDIFSV RFLEVNKGWD PFGFFENATD
PLAGVKAIAG AYNRGLWSNL VQNIFYTQRT EALATPDLLT IFADEPVAYD HAQKISNYTV
ALNNQAAMLN PPSLGNTNPA TGQPYNYFKN YYETQVAWAD VQQYLSRIFP LYPDVDTAAV
KTSVQTVFNS INGGASISFR YDFGEVLDAI MLALPVDDPT EQIKINYGCA GGNGNSGGGG
NGGSTGTQNC AVPTGINATE IGSVTATLNW DATAGATGYY MLYRAQNGAW NIASPATNTW
QFTGLMPFTT YEVQLASNCN GVYTNYAPTF TFTTNDYQND CNTNIGANGY TGGCPIPTGL
EAYNITFTTA TIEWDSIPAA SGYYMLYRTL TGAWNIVSPT DNNITLTGLQ ANTSYEILLA
TNCNGIYTEY APSFTFTTNN SGGSSSTVPC PCNVPAGITV TNITMETAQV SWNPVPEATQ
YLLRYRQQGT TTWLQTSLTT TAFALGGLYP ATAYEVQIAS VCGATNGIFS ASVLFNTPNA
PSAVINMKLL LEGAYNTANG LMTTALPAGG YMPGEQPYNT APWNYTGTES ATQIPLTATD
WILVEARSAV NPNTVAERHA AIVLNDGRVQ DADGMAGVKF YSLVPGTPYH FVARHRNHLA
VITAAPQTLS NGMTVDFTVP ATVMLGALQM KALPGGAYAL IAGDLNGNGV ISVSDFNLYR
LQSALLNGYY AADVNLDDSV SVSDFNLYYP NASVIGVSFI RY
//
