ID A0A3S0YRD0_9BACL Unreviewed; 1241 AA.
AC A0A3S0YRD0;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=DUF2062 domain-containing protein {ECO:0000313|EMBL:RUS47530.1};
GN ORFNames=ELR57_09940 {ECO:0000313|EMBL:RUS47530.1};
OS Cohnella sp. AR92.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=648716 {ECO:0000313|EMBL:RUS47530.1, ECO:0000313|Proteomes:UP000267180};
RN [1] {ECO:0000313|EMBL:RUS47530.1, ECO:0000313|Proteomes:UP000267180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR92 {ECO:0000313|EMBL:RUS47530.1,
RC ECO:0000313|Proteomes:UP000267180};
RX PubMed=29166641; DOI=10.1159/000480541;
RA Pisa J.H., Manfredi A.P., Perotti N.I., Romero H.G., Breccia J.D.,
RA Martinez M.A.;
RT "Agrowastes as Feedstock for the Production of Endo-?-Xylanase from
RT Cohnella sp. Strain AR92.";
RL J. Mol. Microbiol. Biotechnol. 27:277-288(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:RUS47530.1}.
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DR EMBL; RZJR01000005; RUS47530.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0YRD0; -.
DR OrthoDB; 9766299at2; -.
DR Proteomes; UP000267180; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd10962; CE4_GT2-like; 1.
DR CDD; cd06423; CESA_like; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR018639; DUF2062.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR002509; NODB_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR43630; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR PANTHER; PTHR43630:SF1; POLY-BETA-1,6-N-ACETYL-D-GLUCOSAMINE SYNTHASE; 1.
DR Pfam; PF09835; DUF2062; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF13641; Glyco_tranf_2_3; 1.
DR Pfam; PF01522; Polysacc_deac_1; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51677; NODB; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000267180};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..79
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1136..1157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1163..1183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 246..553
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 615..802
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 1241 AA; 139344 MW; 5E67C7803BF31D6C CRC64;
MNRLADRLAL SLFAPFGKLR GATAGSIGLF VGMLPIAGFR FALLLALSIM LRMSLPALVL
GLSVTFLLPY LHLLTFSLGH RLAAHDAYLA AVPDLTIRNA ALWTTGSGSY WAGSVISGLL
LATLAFPFFM LLFNLPRKRR VQSKNYVFKD EFGRRWVLLR RLGVLTIGVA LAIVAVFCAS
LDSVPLLPDL GLKQPHSPHS SMEKQLSENE LIQQLKDEDQ KHPTFQVGYR RHHLDRLSAS
SSPGKQEVYG FYVNWDENSK QSLLQYSREL TTLLPEWLHM NSDLTISDET DPDVLKLADR
RNLAVQPLIS NYTDDHWDEE AVHRLLQSPE KQQELIRSLH ALVTKYGESG INLDFEAVEP
DDQDLLTAFV QSLTQAFHAD GLQVTQDVPA DDDAFDYGAL AQVADRLIVM MYDEHSETGD
PGPIASSNWF EQSLNQLDIP PGKMVVSMGN YGYDWIANSK QPADNLTFGD LMELAEQSKL
PVYWDDEGDN PYIRYQDGED SHIVWFLDAA TFYNQLKIVQ ENGFRGVALW RLGSEDPGIW
SLLGKPSPSA SDLSVLYNPS PVHYSGEGEI LRIASTSNEG KRSVETDEDG YIDNETYESI
PTPFEVERYG KIKSKQVALT FDDGPSGRYT PEILDILNKY KIKASFFVVG ENAEAYPGLI
KRIYKEGHEL GNHTFTHPDV AAISPTRTRL ELNATQRLIQ EITGHSATFF RPPYVADAEP
STPSELLPIL RAQQMGYTMA GELIDPEDWQ RPSTDAIVDR VMSRLHEGNV ILLHDAGGDR
SQTVEALPRI IEQLQRQGYS FTTLSALIGK TRAETMPPVS DADLPLLQYD RAVFQWLKGW
NLGLRDLFYA AIAIGMLRVA MLFWLSLRHK RDRSSGRVNA DYAPPVSVVI AAYNEQKVIC
NTIESILLSD YPNYEVIVVD DGSTDETARA VLERFGERSD VRLITKPNGG KASAVNTGYR
QANGEIVIAF DADTLIASDS ITRLVCRFQD ERVAAVSGNV KIGNTGNLLT IWQHIEYVTG
FNLERRAFDK LNCIAVVPGA IGAWRKSAVE DAGYYSEDTL AEDADLTLSL LRSGYKIHYE
ERALAYTEAP EDVQSFAKQR YRWTYGTLQC LWKHRGAMFN PKHPALGFIG MPNMWLFQYV
YSVLSPLIDL LFVFSLFSGG SRIATAFYLA FFLLDLSVAY YAFRLEKENP KPLLWLFLQR
IVYRQLMTYV ILKSIFAAVR GSPVGWNKMK RRGSARMDQS M
//
