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Database: UniProt
Entry: A0A2I0SU67_9ACTN
LinkDB: A0A2I0SU67_9ACTN
Original site: A0A2I0SU67_9ACTN 
ID   A0A2I0SU67_9ACTN        Unreviewed;      1424 AA.
AC   A0A2I0SU67;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Secreted glycosyl hydrolase {ECO:0000313|EMBL:PKT73433.1};
GN   ORFNames=CW362_08805 {ECO:0000313|EMBL:PKT73433.1};
OS   Streptomyces populi.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2058924 {ECO:0000313|EMBL:PKT73433.1, ECO:0000313|Proteomes:UP000236178};
RN   [1] {ECO:0000313|EMBL:PKT73433.1, ECO:0000313|Proteomes:UP000236178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A249 {ECO:0000313|EMBL:PKT73433.1,
RC   ECO:0000313|Proteomes:UP000236178};
RA   Wang Z.;
RT   "Streptomyces populusis sp. nov., a novel endophytic actinobacterium
RT   isolated from stems of Populus adenopoda Maxim.";
RL   Submitted (DEC-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:PKT73433.1}.
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DR   EMBL; PJOS01000011; PKT73433.1; -; Genomic_DNA.
DR   OrthoDB; 5476529at2; -.
DR   Proteomes; UP000236178; 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   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   PANTHER; PTHR24543; MULTICOPPER OXIDASE-RELATED; 1.
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.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000313|EMBL:PKT73433.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236178};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..1424
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014125240"
FT   DOMAIN          20..150
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          162..312
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          494..640
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          393..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1424 AA;  148685 MW;  0C673153E7559644 CRC64;
     MTPHKPRSWR SRAATAALAS IVMVLGLPAV GAHAAGGPDA AADAATKAGS ARGAHTAANV
     TDGDADTYWQ AGERSAQWVQ TDLGRTERVR EVVLRLPEHW RARKQTLALQ GSADGKSFAT
     LKSSAQYVFG PGNGNTVKVS FPAALARYVR ADFSGNSIAP TAQLAEMQVL TAAAQTPNLA
     QGKPFTESGH ADVYGAANAG DGNRATYWES KNNAFPQWLQ VDLGSSVKVN QVTLRLPAGW
     PSRSQTLKVQ GSTDNQNFTD LTASKAYTFD SGNDQSATIA LDTTTTRYVR ALFTANTGWP
     AGQASELEVY GPATGDTQAP TAPSNLAFTE PATGQIKLTW NAASDDTAVT GYDVYANGQL
     RASVAGNVLT YTDTQPAGTD ITYFVRAKDA AGNVSSDSNS VTRRGSGGDT QAPTAPGNLA
     YTQSGGDVKL TWQASSDNVK VTGYDVYADG RLLKSVAGDV TTYTDTPAAT ATVTYSVKAK
     DAAGNVSAAS NSVTRTGSTG SGSNLAEGKP IEASSSTFTY VATNANDGQI GTYWESGAGA
     YPATLTTRLG ANADLAQVVV KLNPDAAWST RTQNIQVLGR DQDATAFTSL VAAKDYTFNP
     SSGNTVTIPV SGSVADVQLR FTSNSGAPGG QAAEFQVIGT PAANPDLKVT GITNTPTAPV
     ESDAISLTAT VTNSGTKAAK ATDLDLTLGG TKAATADVPA LAAGETKTVT ASIGARDAGS
     YPVGAEVDPA NKVIEQNEGN NTFTRSDALV VKPVSSSDLL AAPVSWSPSS ASAGDEVKFT
     VAIKNQGTVA SASGGHGVTL TVQDSKGATV KTLSGSYDGA IAAGQTTAPV SLGSWTAVNG
     KYTVKTVIAD DTNELPVKRA NNTTTQPLFV GRGADMPYDM YEAEDGTLGG GAKVVGPNRT
     VGDIAGEASG RKAVTLNGTG QYVEWTTRAA TNTLVTRFSI PDGTDTTLNV YVDGQFLKTI
     DLTSKYAWLY GNETAPGNSP GSGAPRHIYD EANLQLGRTV QAGSKIRLQK DAANSSTYAI
     DFVNTEQATA NPNPDPAAYA VPAGFTHQDV QNALDKVRMD TTGKLVGVYL PAGDYETAGK
     FQVYGKAVKV VGAGPWFTRF HAPSSQENTD VGFRADATAN GSTFAGFAYF GNYTSRIDGP
     GKVFDFANVS GITIDNVWAE HMVCLYWGAN TDGMTIKNTR IRDTFADGVN MTNGSTDNHV
     VNNDARATGD DSFALFSAID AGGADEKNNL YENLTSTLTW RAAGIAVYGG YDNTFRNIRV
     ADTLVYSGIT ISSLDFGYPM NGFGTDPTTI ENVSLDRTGG HFWGSQVFPA IWAFSASKVF
     QGIRVNDVDI DDSTYGGVMF QTNYVGGQPQ FPVKDTIFTD ISITDSKKSG DAFDAKSGFG
     IWANELPEPG QGPAVGEATF RNLRMSGNAQ DIRNTTSTFR INIE
//
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