ID A0A2P8EBZ4_9ACTN Unreviewed; 1844 AA.
AC A0A2P8EBZ4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=PKD domain-containing protein {ECO:0000313|EMBL:PSL06993.1};
GN ORFNames=CLV30_102382 {ECO:0000313|EMBL:PSL06993.1};
OS Haloactinopolyspora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC Haloactinopolyspora.
OX NCBI_TaxID=648780 {ECO:0000313|EMBL:PSL06993.1, ECO:0000313|Proteomes:UP000243528};
RN [1] {ECO:0000313|EMBL:PSL06993.1, ECO:0000313|Proteomes:UP000243528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45211 {ECO:0000313|EMBL:PSL06993.1,
RC ECO:0000313|Proteomes:UP000243528};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PSL06993.1}.
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DR EMBL; PYGE01000002; PSL06993.1; -; Genomic_DNA.
DR Proteomes; UP000243528; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR CDD; cd04084; CBM6_xylanase-like; 1.
DR CDD; cd00146; PKD; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR006584; Cellulose-bd_IV.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR009784; DUF1349.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR041542; GH43_C2.
DR InterPro; IPR012938; Glc/Sorbosone_DH.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR InterPro; IPR011041; Quinoprot_gluc/sorb_DH.
DR InterPro; IPR029010; ThuA-like.
DR PANTHER; PTHR40469:SF2; GALACTOSE-BINDING DOMAIN-LIKE SUPERFAMILY PROTEIN; 1.
DR PANTHER; PTHR40469; SECRETED GLYCOSYL HYDROLASE; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF07081; DUF1349; 1.
DR Pfam; PF17851; GH43_C2; 1.
DR Pfam; PF07995; GSDH; 1.
DR Pfam; PF18911; PKD_4; 2.
DR Pfam; PF06283; ThuA; 1.
DR SMART; SM00606; CBD_IV; 1.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49299; PKD domain; 2.
DR SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR PROSITE; PS51175; CBM6; 1.
DR PROSITE; PS50093; PKD; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000243528}.
FT DOMAIN 697..780
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 891..1026
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 1036..1118
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 440..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1802..1844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1844 AA; 196214 MW; 2768706175AF6E02 CRC64;
MAGSLAAGVA VPVGIAALAP TATAHPGHGG YSVLVFSKTE GFRHGSIPDG VAAIEQLGAE
HDFQVDATED SAAFTDDNLA QYDVVVWLST TGDVLNADQQ AAFERYIADG GGYAGIHSAS
DTEYDWAWYG DLVGAYFAGH PAQQDATVKV EDPAHPSTQH LDPAWDRFDE WYNYQANPRG
DVHVLASLDE SSYDAGGGAM GSDHPISWCQ NFDGGRSWYT GMGHTVDSFS EPEFLEHILG
GIETAAGVTP ANCAASQPGS FEKVTLDDTT SNPMELAVAG DGRVFYIERN GEVRLIRPDG
SATTVGAVDV YTGQEFGLTG IALDPDFATN NWIYLTYAPA GDQAVDRVSR FTLNGETLDP
ASEQVVLEFP TNRDECCHAG GALEFDGNGD LYLATGDNTN PFSSQGYAPI DEQPGRELWD
AQRTSANSNS LSGKVLRIHP EDDGSYTIPE GNLFPESEDT QDKTRPEIYA MGFRNPFRIG
IDPATDKLMV GDYGPDANSA NPDRGPDGRV EWNIVDEPGF YGWPYCVGDN TPYIDYDFAT
GESGEAFDCA GGPVNDSPNN TGITQLPPAV EAEVWYGYSP NPQFPEIGGG GAPMAGGVYR
YDPSVESDRQ WPAYWDGKAV FAEWNQGNLY SFQLDGAGSA VTDINALFPD MQFLRPHAME
WGPDGALYLI EWGSGFGGDN ADSGVYRIDH VQGERAPIAR IDAGPLSGPT PLEVNFDASG
SIDPEATTLT YEWDFDGDGT VDSTEPTVSH TYTEPGDYTV ALTVTDADGQ QDIANVEVTA
GNTAPEITVT APADGGFFEF GDTIAYEVSV TDAEDGEGVC DRIVTQPGLG HNDHSHEYEE
NFGCTGTFEL PGDEGHTGAN IFGTVTVTYT DDGAPGVSPL TSREVLVLQP KRRQAEHFDE
TGRLAGSDAG GDPGVQTEET GDTAGGGQNV GFIEDGDWWS WDPMNLTAID DITLRAATPN
IGATVEVRTG APDGPTVATI QTEPTGDWQV YDEFTASVSG DTATSSGPLY FVKTTGQLNV
NWVDFGGKGV TENQRPDVTV SADPASGTAP LDVGFAAEAS DPEGDTPLTY AWQFGDGGTA
TGATAQHTYT EAGTYDAEVT VTDARGAEVT ESVTVDVQDG GEPPVCLKGR SDAFDGDTLD
RDRWTTVVRE NQDLAVQDGH LVLPATSTDI YGTNNTDTPN IVLQDLPDGE FTATAKLTMQ
AYRAYQQAGL VIYGDDDNYA KMVLQGRDTG ASNPAARIFQ FIREENGEPN EVGDSNTAQL
GADYPDTVWV RYTSDGSNLR AAYSADGETF TEMPQTKSLD GITDPKIGLI ALAGTDQPAG
EARFDHFQIT PDDTAPAAEP NDEFDGTALD GCRWSVLRPD ESGYRVADGA LEIDTSDGDI
YEDGNSGPSN FVLQPAPEGD EWTIETKVDG SAFDEQYQQG GLIVYGDDGN YVKFDYVVDN
AAGDPVSPRL ELRSEVGDAV QTPQPSVTEL DQAIWHLRLT RSGNTYTGSY SADGETWTDM
PEPVTNSAVA ADAKAGLFAL GGAQGASKTA RFDYFHVKEL EVDETPPTVD VTLDPSEPSG
SNGWWTGPVT VTAEAADDGD GPVDVEYRVD GGDWAPYTEP VVVEADGEHV VDVRATDAAG
NTSEPVGTEI AVDATAPELD VSGVEHGVLY GDSQDLELAW DSSDTGSGAG ETVARLDGDP
VEPGALVLHE IPLGLHDLEV EARDRAGNRT TERFTFFVST SFADMRSLVS RFESEQRLDR
PSTKRLENTL GTAARQAVMG RETRAVERLE KVKDIANDKV ADDVVRDVLI RDADAMIGRL
GATPSDAGAG VTANGGQSLD GTGRLAGDPA PKVGGVEMTP NRLE
//