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Database: UniProt
Entry: A0A0C1YAP8_9ACTN
LinkDB: A0A0C1YAP8_9ACTN
Original site: A0A0C1YAP8_9ACTN 
ID   A0A0C1YAP8_9ACTN        Unreviewed;      1227 AA.
AC   A0A0C1YAP8;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Glycosyl hydrolase {ECO:0000313|EMBL:KIF77692.1};
GN   ORFNames=QR77_35385 {ECO:0000313|EMBL:KIF77692.1};
OS   Streptomyces sp. 150FB.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF77692.1, ECO:0000313|Proteomes:UP000031584};
RN   [1] {ECO:0000313|EMBL:KIF77692.1, ECO:0000313|Proteomes:UP000031584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=150FB {ECO:0000313|EMBL:KIF77692.1,
RC   ECO:0000313|Proteomes:UP000031584};
RA   Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT   "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT   150.";
RL   Submitted (NOV-2014) 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:KIF77692.1}.
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DR   EMBL; JTHL01000001; KIF77692.1; -; Genomic_DNA.
DR   RefSeq; WP_040026091.1; NZ_JTHL01000001.1.
DR   AlphaFoldDB; A0A0C1YAP8; -.
DR   STRING; 1576605.QR77_35385; -.
DR   OrthoDB; 6402258at2; -.
DR   Proteomes; UP000031584; Unassembled WGS sequence.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
DR   CDD; cd04084; CBM6_xylanase-like; 1.
DR   CDD; cd00146; PKD; 1.
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; 1.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR010496; 3-keto-disaccharide_hydrolase.
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; IPR008979; Galactose-bd-like_sf.
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; PF06439; 3keto-disac_hyd; 1.
DR   Pfam; PF03422; CBM_6; 1.
DR   Pfam; PF07995; GSDH; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   Pfam; PF06283; ThuA; 1.
DR   SMART; SM00606; CBD_IV; 1.
DR   SMART; SM00089; PKD; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   SUPFAM; SSF50952; Soluble quinoprotein glucose dehydrogenase; 1.
DR   PROSITE; PS51175; CBM6; 1.
DR   PROSITE; PS50093; PKD; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KIF77692.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031584};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           33..1227
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002142954"
FT   DOMAIN          494..573
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
FT   DOMAIN          687..812
FT                   /note="CBM6"
FT                   /evidence="ECO:0000259|PROSITE:PS51175"
FT   REGION          207..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1227 AA;  131223 MW;  93F27799A803DB30 CRC64;
     MHRKRLRARS LIAYLTGALL VGGSLSAVPA LAAADPAPAA ESFQQVTLAK GAAEVGEPMS
     LAVLPDRRVL HTSRDGTLRI TDAAGDTKVA GTLEVYSHDE EGLQGVGVDP DFAENHAIYL
     YYAPKLNTPA GDAPENGSPA DWAPYDGYNR LSRFTLNDDG TLDKASEKKV LDVATSRGTC
     CHVGGDIAFD GDGNLYLSTG DDTNPFASDG YTPIDERPTR NPAFDARRSA GNSNDLRGKV
     LRVKVADDGS YTIPDGNLFA PGTEKTRPEI YAMGFRNPFR ISVDKKTGIV YVGDYGPDAG
     AASPTRGPGG QVEFARITEA GNFGWPYCTG ANDAFVDYDF ATGASGESFD CAAPKNTSPH
     NTGLVDLPPA QPAWIPYDGG SVPEFGSGGS ESPTGGPVYR YDASLDSPVK FPEAYDGDFF
     AGEFGRQWIK RIEQGDDGTV NKINDFPWSG TQVMDMEFGP DGALYVLDYG LSWFGGDDNS
     AVYRIENTTG GRSPIAVAAA DKTSGKAPLK VTFSSAGTED PDGDALTYAW DFGDGSTSTA
     ADPVHSYKKN GTYTATLTVT DATDRTATAS VHVVAGNTAP KVTLEVPAEG TLFNFGDTLP
     FKVTVTDPED GPIDCSKVTV NYVLGHDSHG HPITSATGCE GTITAPADAD HDPNANIFGV
     LDAEYTDGGG GGQAALTSHD QAQLQPRHRQ AEHFNGSSGI KLQDKTSANG GKTVGDINND
     EWISFKPYNL TGSKTLTARI SSAGAGGFLE VRTGSATGNL LGSAPIPVTG SWDTFQDIDV
     PLRAVPKKST ELFLVFKGGD GALYDLDDFT ISDKAPGKTE KRVLVFSKTA GFRHDAIPEG
     ITALKALGKD SNITVDTTEE ARQFTTNNLA RYDAVVFLST TGDVLNAEQQ KAFEYYISTG
     GGYLGVHAAA DTEYDWPFYG GLVGAWFQGH PQIQPATVRV EDATNPATAH LDTAWTRTDE
     WYNYRTDPRA DVRVLATLDE TSYTGGTMKG DHPIAWCQSY EGGRSFYTGM GHTKESYADP
     AFQQHLLGGL RYAAGQVKAD CKPKTGYRPI FNGQSLDGWK QAGPGKFTIA DGELRSEGGL
     GMLWYQPKQL GSYSLKLDWK LAGDDNSGVF VGFPASDDPW SAVDNGYEVQ IDATDAPDRT
     TGSVYTFKAA DIKARDQVLR PPGQWNNYEI RVQGERLQVF LNGVKINDFT NTDPARSLKD
     GYLGIQNHSA DDQVSFRNIQ LKELPAQ
//
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