ID A0A1Q2H1W4_9GAMM Unreviewed; 876 AA.
AC A0A1Q2H1W4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Chitinase {ECO:0000313|EMBL:AQQ01356.1};
GN ORFNames=B0W48_17225 {ECO:0000313|EMBL:AQQ01356.1};
OS Pseudoalteromonas aliena.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=247523 {ECO:0000313|EMBL:AQQ01356.1, ECO:0000313|Proteomes:UP000188243};
RN [1] {ECO:0000313|EMBL:AQQ01356.1, ECO:0000313|Proteomes:UP000188243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EH1 {ECO:0000313|EMBL:AQQ01356.1,
RC ECO:0000313|Proteomes:UP000188243};
RA Kim E., Heo E., Kim H., Kim D.;
RT "Complete genome sequence of the cold-active Pseudoalteromonas aliena
RT strain EH1 isolated from Arctic seawater.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP019628; AQQ01356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q2H1W4; -.
DR STRING; 247523.B0W48_17225; -.
DR KEGG; paln:B0W48_17225; -.
DR Proteomes; UP000188243; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd12215; ChiC_BD; 2.
DR CDD; cd02848; E_set_Chitinase_N; 1.
DR CDD; cd06548; GH18_chitinase; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR013540; ChitinaseA_N.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF02839; CBM_5_12; 2.
DR Pfam; PF08329; ChitinaseA_N; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..876
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013111823"
FT DOMAIN 159..585
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 816..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 876 AA; 93349 MW; FBB512EB1A9D20A6 CRC64;
MNIKQLTVAI GAALFASTAV AAPSTPSINW EPQQYSFVEV DLEGNGSYKQ LVTRVEQVSI
NIQWSAWSGD GGDSYKVYFD DMLVNEGTLA AGSKTGTISF LYDKAGRHTL YVELCEGGST
CARSAGKPIV IADTDGSHLA PLPMDVDANN RDIGVKQDLV TGAYFVEWGI YGRDFDVTNI
PAQNLSHILY GFIPICGENA SLTGGPKRAL ETACAGTADY EVVIHDPWAA VQKALPGVDA
NDPIRGTYSQ LMALKQRYPD LKILPSVGGW TLSDPFGGFT DKANRDTFVA SMEEFLRTWK
FYDGVDIDWE FPGGDGPNPD IGDPINDGPA YVALMQELRA MLDQLEAETG RTYELTSAIG
AGYDKIEDVD YQAASQYMDY IFAMTYDFYG AWSGVTGHQA ALYCGEHISA GECNGTGLDE
SGEPRKGPAY TTDNAVQLLL AQNVPSKKIV VGAAMYGRGW EGVFPTGTTI DGNPMTATGS
GPLKGSNAQG VWEDGVIDYK GIKSFMIGTD GMGVNGFEVG YDDQAQGAYV WNRSTGKLIT
YDNAKSVIAK GQYVQQYNLG GLFAWEIDGD NGDILNAMHD GLGGVVQPVN NKPVLNVQNT
VTVNAGESVS VSATATDADN DVLTFSWTAA AQLSISGETT STVAITAPNV SQDSQFAATV
NVSDGKVTVS KAIVVNVLAP TSGGENTAPV INTLADITLE EGATATVSVI ATDAQNDVLT
YSWSVPAGLK RVGDGAKISL EADAVAQNTD FTVSVFVSDG QVSTTQNFTV SVTNNDSTTP
PAADAWDVSK VYVKGDTVVF NTIIYKAKWW TQGNSPDLGG PWDAQSPPTD GEGNRAWQSS
AVYNSGDKVI YQGNQYQAKW WTQGDKPDSA SVWQLL
//
