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Database: UniProt
Entry: D2B4J9_STRRD
LinkDB: D2B4J9_STRRD
Original site: D2B4J9_STRRD 
ID   D2B4J9_STRRD            Unreviewed;       468 AA.
AC   D2B4J9;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   SubName: Full=Xylanase/chitin deacetylase-like protein {ECO:0000313|EMBL:ACZ83685.1};
GN   OrderedLocusNames=Sros_0662 {ECO:0000313|EMBL:ACZ83685.1};
OS   Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI
OS   9100).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Streptosporangium.
OX   NCBI_TaxID=479432 {ECO:0000313|EMBL:ACZ83685.1, ECO:0000313|Proteomes:UP000002029};
RN   [1] {ECO:0000313|EMBL:ACZ83685.1, ECO:0000313|Proteomes:UP000002029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100
RC   {ECO:0000313|Proteomes:UP000002029};
RX   PubMed=21304675; DOI=10.4056/sigs.631049;
RA   Nolan M., Sikorski J., Jando M., Lucas S., Lapidus A., Glavina Del Rio T.,
RA   Chen F., Tice H., Pitluck S., Cheng J.F., Chertkov O., Sims D., Meincke L.,
RA   Brettin T., Han C., Detter J.C., Bruce D., Goodwin L., Land M., Hauser L.,
RA   Chang Y.J., Jeffries C.D., Ivanova N., Mavromatis K., Mikhailova N.,
RA   Chen A., Palaniappan K., Chain P., Rohde M., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Streptosporangium roseum type strain (NI
RT   9100).";
RL   Stand. Genomic Sci. 2:29-37(2010).
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DR   EMBL; CP001814; ACZ83685.1; -; Genomic_DNA.
DR   RefSeq; WP_012887431.1; NC_013595.1.
DR   AlphaFoldDB; D2B4J9; -.
DR   STRING; 479432.Sros_0662; -.
DR   KEGG; sro:Sros_0662; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_037608_2_1_11; -.
DR   OrthoDB; 3521160at2; -.
DR   Proteomes; UP000002029; Chromosome.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd10917; CE4_NodB_like_6s_7s; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR10587:SF132; POSSIBLE GLYCOSYL HYDROLASE; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000313|EMBL:ACZ83685.1};
KW   Glycosidase {ECO:0000313|EMBL:ACZ83685.1};
KW   Hydrolase {ECO:0000313|EMBL:ACZ83685.1};
KW   Polysaccharide degradation {ECO:0000313|EMBL:ACZ83685.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002029};
KW   Xylan degradation {ECO:0000313|EMBL:ACZ83685.1}.
FT   DOMAIN          250..426
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          436..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..459
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   468 AA;  50545 MW;  89BC7CE3D4953531 CRC64;
     MINYVDPSRV QGLSVRTMNG GDTGDRRVHV TYPSIDDAPR LSEKIRRTVT ERLDRFIRDT
     SMNTALPHPE FNVDWQLAAA SDQVVGVRLR TGESLGAGWS ESRTTVWYDR VDRRALDSTA
     LLRDGSALAE LARIVRESLN DRGSPVDPRA VRPDAELFDS LSFNPHGELV VEFDDYQVSG
     GPLGRVAVAV PAAEVAPLLS ATGLRAQRAA AGTARTSPPM GSDESIEAAS TVKLPARSSK
     AGSVDCARVK CVALTYDDGP GPDTGRLLDI LAGADARATF FSVGSNAAAR PELLRRMRQE
     GHLVANHTWS HRDLTSLSTS RIADQIDRTQ YTITQTIWQV PTLVRPPYGA SSVQVASVAR
     RLGLSVVRWS VDTEDRRDRD PGAIADRAVS RARPGAIVLM HDVHGATVDA APEILRRLKE
     KGYTFVTVPE LYGSRGMEPG RTYDSAASGG SSGKSGSVTR ALEKQALP
//
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