ID A0A0M8YJ06_9ACTN Unreviewed; 1429 AA.
AC A0A0M8YJ06;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Secreted glycosyl hydrolase {ECO:0000313|EMBL:KOX26294.1};
GN ORFNames=ADL06_16240 {ECO:0000313|EMBL:KOX26294.1};
OS Streptomyces sp. NRRL F-6491.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX26294.1, ECO:0000313|Proteomes:UP000037743};
RN [1] {ECO:0000313|EMBL:KOX26294.1, ECO:0000313|Proteomes:UP000037743}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX26294.1,
RC ECO:0000313|Proteomes:UP000037743};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOX26294.1}.
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DR EMBL; LGEE01000210; KOX26294.1; -; Genomic_DNA.
DR RefSeq; WP_053649025.1; NZ_LGEE01000210.1.
DR PATRIC; fig|1519495.3.peg.3459; -.
DR Proteomes; UP000037743; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd14490; CBM6-CBM35-CBM36_like_1; 1.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 4.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR011635; CARDB.
DR InterPro; IPR033801; CBM6-CBM35-CBM36-like_1.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF07705; CARDB; 2.
DR Pfam; PF00754; F5_F8_type_C; 3.
DR SMART; SM00231; FA58C; 2.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00710; PbH1; 5.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 3.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS50022; FA58C_3; 3.
DR PROSITE; PS50853; FN3; 2.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000313|EMBL:KOX26294.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1429
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005829191"
FT DOMAIN 14..170
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 172..310
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 320..408
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 413..500
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 492..639
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 386..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1429 AA; 148694 MW; 043542EBE4AC7941 CRC64;
MKLHSWRSRG MSAVIATSLL ALGGPLMTAQ AAGGPNIALG DPAAAGSALP EYGAANVTDG
NQGTYWQSSG SSLPQWVQTD LGTSTRVDEV VLKLPAGWES RNQTLSVQGS ADGTSFSTLK
SSATYTFSPG TGNTVTVGFP AAQARFVRVD ITANTGWQAA QLSELEVHAA DGTSANLAAG
RTLTASSHTE VYAAGNANDG NKATYWESRN NELPQWLRAD LGSSVRVDRV VLRLPDGWGA
RSQTLKVQSS ANGTDFTDLT TSKAYEFAPS GQNSVTIPFG ETTARYIRVL VTANTVQPAA
QLSELEVYGP ATGDTQAPTA PANLAFTEPA TGQVRLTWTA ATDNTGVTGY DVYANNTLLT
SVAGNVTTYT DSRPADQTVT YHVRAKDAAG NQSANSNAVT RQGDTGDTQA PTAPANLAFT
EATSGQVRLT WGASSDNTGV TGYDVYANNT LLTSVVGSVT TYTDSRPANQ TVTYHVRAKD
AAGNQSANSN AVTRNGSGST GSNLAVGKPI SASSTVHGFV AANANDNSTS TYWEGAGGSY
PNTLTVKLGS NADLDRLVLK LDPATAWAAR NQTVEVLGRE QSASGFTSLV AAKSYTFDPA
GGNTVTVPVT ARVADVQLRF TANTGSSAGQ LAEFQVVGVP APNPDLEVTG LTTTPAAPVE
SDQITVGATV RNSGPAAAPA SAVALRLGGT KVATAQVGAL AAGAQTTVSA SIGAREAGSY
ELSAVADEAN AVIEQNESNN THTSPTPLVV KPVTSPDVVT TGVTTTPSSP SAGDTVSFRA
TVRNQGNQAT SAGAHGVTLN LLDKQGATVK TLTGSYSGSL AAGASTVVTL GPWTAANGSY
TVRTVLADDA GELPVKRANN TASQPLFVGR GANMPYTTYE AEDGTVGGGA TVAGPNRTVG
DIAGEASGRK AVNLDATGEY VEFTARAATN TLVTRFSVPD APGGGGIDST INVYVDGVFK
KALPLTSKYA WLYGSEIAPG NSPGSGGPRH VYDEAHLLLG ETVQAGSKIR LQKDAANTAA
YYAIDFVDLE QVAPVANPDP ATYTVPAGFT HQDVQNALDR VRMDTTGKLT GVYLPPGDYQ
TSSKFQVYGK AVKVVGAGPW YTKFHAPSTQ DNTDVGFRAE AAAKGSLFKG FAYFGNYTSR
IDGPGKVFDF ANVTDIVIDD IWNEHMVCLY WGANADRITI KNSRIRNMFA DGINMTNGST
DNHVVNNDAR ATGDDSFALF SAIDAGGADM KNNVYENLTS TLTWRAAGLA VYGGYSNTFR
NIHIADTLVY SGVTISSLDF GYAMNGFGTE PTTFENISIV RAGGHFWGNQ TFPGMWLFSA
SKVFQGIRVN SVDIVDPTYS GIMFQTNYVG GQPQFPIKDT VLTDISVTGA RKSGDAWDAK
SGFGLWANEM PESGQGPAVG EVTFNGLRMN GNAVDIRNNT TTFKINVNP
//
