ID   C7MMQ8_CRYCD            Unreviewed;       573 AA.
AC   C7MMQ8;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Predicted xylanase/chitin deacetylase {ECO:0000313|EMBL:ACU94198.1};
GN   OrderedLocusNames=Ccur_04760 {ECO:0000313|EMBL:ACU94198.1};
OS   Cryptobacterium curtum (strain ATCC 700683 / DSM 15641 / CCUG 43107 /
OS   12-3).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Cryptobacterium.
OX   NCBI_TaxID=469378 {ECO:0000313|EMBL:ACU94198.1, ECO:0000313|Proteomes:UP000000954};
RN   [1] {ECO:0000313|EMBL:ACU94198.1, ECO:0000313|Proteomes:UP000000954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700683 / DSM 15641 / 12-3
RC   {ECO:0000313|Proteomes:UP000000954};
RX   PubMed=21304644; DOI=10.40456/sigs.12260;
RA   Mavrommatis K., Pukall R., Rohde C., Chen F., Sims D., Brettin T.,
RA   Kuske C., Detter J.C., Han C., Lapidus A., Copeland A., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Ovchinnikova G., Pati A., Ivanova N., Chen A., Palaniappan K., Chain P.,
RA   D'haeseleer P., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Rohde M., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Cryptobacterium curtum type strain (12-3).";
RL   Stand. Genomic Sci. 1:93-100(2009).
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DR   EMBL; CP001682; ACU94198.1; -; Genomic_DNA.
DR   RefSeq; WP_012802886.1; NC_013170.1.
DR   AlphaFoldDB; C7MMQ8; -.
DR   STRING; 469378.Ccur_04760; -.
DR   KEGG; ccu:Ccur_04760; -.
DR   eggNOG; COG0726; Bacteria.
DR   HOGENOM; CLU_034359_0_0_11; -.
DR   OrthoDB; 9763050at2; -.
DR   Proteomes; UP000000954; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR   PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 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:ACU94198.1};
KW   Glycosidase {ECO:0000313|EMBL:ACU94198.1};
KW   Hydrolase {ECO:0000313|EMBL:ACU94198.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Polysaccharide degradation {ECO:0000313|EMBL:ACU94198.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000954};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Xylan degradation {ECO:0000313|EMBL:ACU94198.1}.
FT   TRANSMEM        194..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          366..556
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          1..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   573 AA;  61637 MW;  6DB911AD38AEA93B CRC64;
     MEEQSKYENH HRERPVVHKR TKRTEREKHN AEAEGNLPST HDQDTASFPP VTSQPETMPK
     DSYRGQRPHL TSVPDPQVTA HASISSENNL AHETSSATRE PRQHRAPISQ VSSVESASAV
     AQGNNTAAPN AAQGDNVKAP SAMSGSNPAA AVHAQSYQES TEQGSSFVPV GAHIRDYNMA
     AAHSRQHLGI GVKIFFVLIA AGVVAIVCWW MLFSPISITL NGKMTTVDRG SNVSAIVKSQ
     NVNVSPGRLL AVDGSVIDQT GGETFTATLD GQAVNGNAGV KENSTLTITD GADKTEDYTE
     TTKPIPSQWV DDGTRGAFHE VVGEAADGIA ATRTGKTSGI TVDNQVVKEP VNPTLTRYSI
     DTGGEKVIAL TFDDGPWKDQ TAELLDILDQ NNAKATFFVV GNRIGDTPGG GDLVKREYDS
     GHQVSSHTWD HAAGSGKGVN LGYMTEDEQI NEIVKGQQAI TDATGVEANK IVRTPGGNYS
     LETAQIVHPY VDVEVDWNID TEDWRRPGAA KIESAILSAK PGNVILMHDG GGDRSQTVQA
     VADALPKLRE QGYRFVTIEE LWEYHKKAQQ QSN
//