ID C5P133_COCP7 Unreviewed; 1690 AA.
AC C5P133;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=CPC735_070730 {ECO:0000313|EMBL:EER29391.1};
OS Coccidioides posadasii (strain C735) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=222929 {ECO:0000313|EMBL:EER29391.1, ECO:0000313|Proteomes:UP000009084};
RN [1] {ECO:0000313|EMBL:EER29391.1, ECO:0000313|Proteomes:UP000009084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C735 {ECO:0000313|Proteomes:UP000009084};
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000822};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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:EER29391.1}.
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DR EMBL; ACFW01000009; EER29391.1; -; Genomic_DNA.
DR RefSeq; XP_003071536.1; XM_003071490.1.
DR GeneID; 9697030; -.
DR KEGG; cpw:CPC735_070730; -.
DR VEuPathDB; FungiDB:CPC735_070730; -.
DR HOGENOM; CLU_001837_2_1_1; -.
DR OrthoDB; 50378at2759; -.
DR Proteomes; UP000009084; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00035; ChtBD1; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR47700:SF2; CHITINASE; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00270; ChtBD1; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00261};
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}.
FT DOMAIN 97..146
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 157..512
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 1643..1668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 111..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 116..130
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 140..144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1690 AA; 188417 MW; 171A1F1314F7B358 CRC64;
MRAQILAEIP PRMIFDYSAK SRGDDALPIC PAAQENVKFL LATDFNIAED YSCAPDRPCS
NGACCPKKTL SCNYGEEYCG TNNISPNEVC WSNCDAKAEC GKNADPPGKE CPLNVCCSKW
GFCGMTKEFC EKGTDDEPGC QSNCDQPRPG KKASEQNIII GYYEAWRHDS NCQGMGLKDI
PVNSLTHLFF SFGYITPGDF KIAGMDGLPD KLFSDFTSLK KKNPGLKTVI ALGGWTFNDP
GPTQKVFSNM VSTKENRAKF IDNLFSFMRQ YAFDGVDFDW EYPGADDRGG IPGDGKNFVK
FLKELNDVNK KQPMHYSVSF TAPSSYWYLR HFDLKAVDYV DFVNMMTYDL HGVWDRDNPI
GSHIYGHSNI TEMRLALDLL WRNDVPAHKV NMGLGFYGRS FQLQDPACDK PGCVFKGGAA
KGACSGESGI LTYREIMAMI KTDKLKPFHD KTAGVKYITY SGDQWVSYDD AETFKQKKEL
AKELGLGGYL IWADAYIPDC YVTGCDGNCK AGFIKITEQK CGKDDKKSKL CCPLAGAPNP
DDCTWRGTAP LCNGHCNDDE VLLQLNKWGS GHHCNDGHKA YCCKSPLAQE NKCYWQGIGK
KCNSGDKAMT FSGTFLSDLV DIAQKIFDII GRRTPIGLLF GDELSEVLDA IELDLMKLYC
CPEEDAKKWK NCKWHGEPGS CFDNHCDANS EVQLTDSYYG AGDTCGVKLE RARVFCCQPV
KGEHLFLPVP LENLFKDPPT GDNIDTDFDL NLDDEDDNPS DTAFQFVVLT SPEELQVSID
KRDGSHWEVF GCKDAVTEGE HTIQMVCTDF SETSNCYKIG LGHGVPGTIL QMPKGCGPGK
YAVAKSMEPA KRQMVPRHLA HLGSRGVVYD LTFDYDFSRV PRDLGNTQMR VDFSNQDNYW
DEVVAATPSK KRKRSLEDVG GNHVRWLEEE FRDDYHFGGL DKRELQERWF GSTVLEWLKK
MVKPEIKRDF THDVDETFTA VIVDETWECE RNNVKYDGHI SAKALTNMRV STSFGFTMIV
TSLIAPLDLS KSYLTFYNEG EITATLTLDA VASISYSKEK TILTLPFPGT SFRIPGIATI
GPQIHISGGL DAQLSVAAKF ETKISIAKWE IRQTLPDGGM DEYKPKEIGP GDPDLDRTGD
FSGIQRPEFY AGVAVEGDIT AKLSAAAEFG VRFDDRWKVG GATVGVVGEG SILVKMAAGI
STEATCPFTY GMQVGAKLYA RADASILKWP ETTYDIVGWE KDIIKGGTCP NLGGLPTVQG
SMPLGLPWST EGNMTSKAHL KHSENASHHS LQKRAAVYGP KFHIPVGDLF CPKDEAGPDF
PENRNDCLQI PGIWDNDKYL TDGDDYYSLT SGARASLDTR GELEKRSNTK ESLLCGKLLM
KSTYPTGGEL PKAPIYGFEK IDCDDYSFGT PLASRVKGIQ YDTEHILEFQ LPGKFLAYLN
KTKGLVYDHP DPNWKNGQGK RVKVSFCTYF EALWDIDPIN IGGSKSTPVA HLGDCYPTKT
RYSNELVVLE HRINIPSKGK AWGSDSQIVA SKTLKDGVEK QPDQAVKTLR ELVGSVLYHK
DPTIAAHLKR QKERVGKMFG LIDKELSKHP RVVNNVKYTP WKPQGLEKEW NKYMRRQHIL
AFTKTTKPVI DWTPKLKDLW ASKAARDAAE PDPNDNQMQQ DEKKKKRALI KKIDALDKAR
SAFSQWKNPF
//
