ID A0A1T3P4Y4_9ACTN Unreviewed; 782 AA.
AC A0A1T3P4Y4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Chitin-binding type-3 domain-containing protein {ECO:0000259|SMART:SM00495};
GN ORFNames=B4N89_26215 {ECO:0000313|EMBL:OPC83960.1};
OS Embleya scabrispora.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Embleya.
OX NCBI_TaxID=159449 {ECO:0000313|EMBL:OPC83960.1, ECO:0000313|Proteomes:UP000190037};
RN [1] {ECO:0000313|EMBL:OPC83960.1, ECO:0000313|Proteomes:UP000190037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF3 {ECO:0000313|EMBL:OPC83960.1,
RC ECO:0000313|Proteomes:UP000190037};
RA Vazquez M., Ceapa C.D., Rodriguez Luna D., Sanchez Esquivel S.;
RT "Draft genome sequence of Streptomyces scabrisporus NF3, endophyte isolated
RT from Amphipterygium adstringens.";
RL Submitted (MAR-2017) 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:OPC83960.1}.
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DR EMBL; MWQN01000001; OPC83960.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T3P4Y4; -.
DR STRING; 159449.B4N89_26215; -.
DR OrthoDB; 345880at2; -.
DR Proteomes; UP000190037; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd12215; ChiC_BD; 1.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.10.450.40; -; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000190037};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..782
FT /note="Chitin-binding type-3 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012843277"
FT DOMAIN 734..779
FT /note="Chitin-binding type-3"
FT /evidence="ECO:0000259|SMART:SM00495"
FT REGION 26..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 80043 MW; 343C493F4922A331 CRC64;
MNRRTTTAGT VLALIAGLAI GAAGSSSAGT DELSTPPPAS SQDKAVSAAD RAVANGLDAL
AKGPDEKFER QLVTPWINDL YSVAYQRTYR GLPVVGGDAV VMADGQGRVR GTQAATSAQI
AVPTRATVAA GTAEATSKAQ LPVVDKVESH RLVVHVLDGN SNLAWETVVA GRTDTAPSRL
HVFVDANTGQ VLDKVDDVKA GTGNSQWNGP NPLTIQTSGS GSSYSLRDTT RPGLSCADNA
TGQVFTKSTD SWGNGQASSK ETGCVDVMWA AQKEWNMLKD WLGRNGHNGS GGSWPVKVGL
NDVNAYWDGS SVSIGHNQSN QWIGSMDVVG HEFGHGIDQF TPGGTSREAG LGEGTGDIFG
ALTEAYTAEP SPYDTPDYTV GETVNLVGQG PIRYMYKPST NGDPDCYSSS IPSTEVHKAA
GPLNHWFYLL AEGTAANGPG KPGSPTCNQT TLSGVGIQQA GKVFYGGMLL KTSGMTYKKY
RTTTLTAAKS LDPTCALFNK TKAAWDAVSL PAQTGDPTCV GNPDDFSLSL NPTSGSVQPG
GDVTTSVATA TTGGNAQQLT LSTGTLPSGV TAVFTPGTVQ SGGSSSLKFT ASSGAAQGTF
PITITATGTA TTHSAQYQLT VGSGPGNPDF SLSLNPTQGT VTPGGDVTTS LTTATISGTP
QQLTLAAGGL PGGVTAVFTP DTIQSGASSS LKLSASSAAT PGTYTVTVTA TGTGTTHSVD
YRLTVGTGPG NCSAPAWDAN TVYVGGNTVS YQGHTYRAKW WTQGETPGTT GQWGVWLDLG
PC
//
