ID A0A1V9KI88_9ACTN Unreviewed; 842 AA.
AC A0A1V9KI88;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=CBM6 domain-containing protein {ECO:0000259|PROSITE:PS51175};
GN ORFNames=B0675_20465 {ECO:0000313|EMBL:OQQ19187.1};
OS Streptomyces sp. M41(2017).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1955065 {ECO:0000313|EMBL:OQQ19187.1, ECO:0000313|Proteomes:UP000192467};
RN [1] {ECO:0000313|EMBL:OQQ19187.1, ECO:0000313|Proteomes:UP000192467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M41 {ECO:0000313|EMBL:OQQ19187.1,
RC ECO:0000313|Proteomes:UP000192467};
RX PubMed=28326787; DOI=10.1021/acs.orglett.7b00545;
RA Wyche T.P., Ruzzini A.C., Beemelmanns C., Kim K.H., Klassen J.L., Cao S.,
RA Poulsen M., Bugni T.S., Currie C.R., Clardy J.;
RT "Linear Peptides Are the Major Products of a Biosynthetic Pathway That
RT Encodes for Cyclic Depsipeptides.";
RL Org. Lett. 19:1772-1775(2017).
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:OQQ19187.1}.
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DR EMBL; MWFK01000001; OQQ19187.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9KI88; -.
DR STRING; 1955065.B0675_20465; -.
DR OrthoDB; 5476529at2; -.
DR Proteomes; UP000192467; Unassembled WGS sequence.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR CDD; cd04083; CBM35_Lmo2446-like; 1.
DR CDD; cd14490; CBM6-CBM35-CBM36_like_1; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 3.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR033801; CBM6-CBM35-CBM36-like_1.
DR InterPro; IPR005084; CMB_fam6.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006626; PbH1.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR PANTHER; PTHR43863; HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G03140)-RELATED; 1.
DR PANTHER; PTHR43863:SF2; MALTASE-GLUCOAMYLASE, INTESTINAL-LIKE; 1.
DR Pfam; PF16990; CBM_35; 1.
DR Pfam; PF03422; CBM_6; 1.
DR Pfam; PF12708; Pectate_lyase_3; 1.
DR SMART; SM00710; PbH1; 8.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51175; CBM6; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000192467};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..842
FT /note="CBM6 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012076849"
FT DOMAIN 38..166
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT DOMAIN 175..298
FT /note="CBM6"
FT /evidence="ECO:0000259|PROSITE:PS51175"
FT REGION 38..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 842 AA; 87148 MW; 2E0B99F9CF18BF54 CRC64;
MSRSPGIRAR ALVPPLLLAL LAALLFVVAA PRAHAASTTL EAESATRTGG AVTETEHPGY
TGTGYVGGYT DSHKGTASTS FTVSSAVAGS GSLKIRYANG TTAVMTLSLY VNGSKVRQIS
LPATANWDTW STTDEALTYQ KGANTVALTF TSSDSGNINL DNVTAITPTA PTGSVTHEAE
KAFASGGPTR ASSVTGYTGS GYLTGFGTTG ARAAFAVNAA EAKSYSFDVR YRTPDATAAT
ITLVANGLTV RRLSLPATSG AWQTLTTDAP LRAGLNNLTL RRESGDNGNL QLDGLNITAA
AANATRGATV PYTTYEAENG STNGSVLGPD RTYLKTASEA SGRKAVVLDQ TGEYVQFTLS
KPANALTLRY SIPDSASGSA YETPLSLYSA GTHLRDITLT DKYSWVYGGY PYNNDPSQGS
GHHFFDEVHV RLASTLPAGT VLKFQKDATD TASSYTLDLV ETETAPAAYA MPAGFVSATT
LGVTADDGSD DTAALNSAVA TAKNQGKGLW LPSGTYDISG HVNLTGIALR GAGEWYTVLR
GKNGKGGLFG QGGTNTVQDL SISGDVTYRD DAGFDTAVEG DFGNGSTVQN VWIEHTKVGL
WIDAPTNGLY ASGLRIRDTF ADGVNLHKGT AGTEISNSSV RNTGDDALAM FSEAQAVTDS
AYRFDTVQVP LLANGAAIYG GSGNRIEDSL ISDTVTASAG IAISTRNFNP APLPFAGTTT
VARNTLTRTG GYEPNWQSRF GALWIYADAS DITAPVNVTD NTILDSTYSA VLISYQKTVS
NLTVSNLTVS NLTIDKTGAY GIEINSAGSG TFSGVTVTGT ASGGLNLAGG FTVNRGSGNS
GW
//
