ID A0A093YQ33_9PEZI Unreviewed; 2979 AA.
AC A0A093YQ33;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
DE Flags: Fragment;
GN ORFNames=O988_00447 {ECO:0000313|EMBL:KFY04848.1};
OS Pseudogymnoascus sp. VKM F-3808.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFY04848.1, ECO:0000313|Proteomes:UP000029329};
RN [1] {ECO:0000313|EMBL:KFY04848.1, ECO:0000313|Proteomes:UP000029329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFY04848.1,
RC ECO:0000313|Proteomes:UP000029329};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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: 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:KFY04848.1}.
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; JPJR01000067; KFY04848.1; -; Genomic_DNA.
DR STRING; 1391699.A0A093YQ33; -.
DR HOGENOM; CLU_226186_0_0_1; -.
DR Proteomes; UP000029329; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd02878; GH18_zymocin_alpha; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR029226; Ecp2.
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 InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR47700:SF1; CHITINASE; 1.
DR PANTHER; PTHR47700; V CHITINASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13720)-RELATED; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF14856; Hce2; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF00067; p450; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS51782; LYSM; 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};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000029329};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..2979
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001890519"
FT DOMAIN 301..346
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 505..876
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 2652..2908
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1953..1981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2337..2383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2539..2558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2913..2933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2294..2321
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1959..1981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2337..2377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2979
FT /evidence="ECO:0000313|EMBL:KFY04848.1"
SQ SEQUENCE 2979 AA; 326303 MW; 5384758E7B061874 CRC64;
MIFSPWVKAA LGAAYGLVMI ADGVSAIQGN RFGGSPGYRN LDRCPKRCAD AGTDPTKWTY
YHSQDQFKHC PLTVFQAFSI YDDVDDSSTH HGIYACSSYG PDFGNLPTVK SLASTTTESI
NATFELGWYD DGYRTAAGEI RSAVKQLRQY LEGGYGSTKT PQILYVRTGR ASVGVYIGQG
LQNEAFSATA LKSLEEDLRS FNASSQALAM QFCQPEYTSE HIFGLFATSN SSFAPVQQAL
RSWSNATCLS FPNSKSFSGP AVLTTAIVST TKPNTIANLT SSSAVKQRSS RMKLHARAEC
TTEQVIQNDS CGSLATRCGI SGADITKYNT KSDFCSTLQP GQHVCCSAGD LPDFSPKPND
DGSCFMYYVP MDDNCSKISA ANSLTNDDLE EFNKETWGWS GCDSLPFNIN ICLSKGDPPM
PATLEGTVCG PAVPGTERPT DGTKLAELNP CALNACCDVW GQCGITAEFC TDTSTGNPGT
AKPNTNGCIS NCGTSMVRGD APASFRKIAY YEGYGMGREC LFQDVLQIDS SEYTHIHFAF
GVLTPDYQIG VGDALSAYQF ENFKRLEGPK RILSFGGWDF STMPETYKIF REGVTAANRV
KMATAIADFI KLHNLDGVDI DWEYPSAPDL PDFDPGTKEE GPNYLAFLVI LKNLLPGKSV
SIAAPASYWY LKGFPIKEIS KIVDYIIYMT YDLHGQWDAQ NPNAVDGCAN GNCLRSQVNL
TETVSAMVMI TKAGVPSNKV VVGVTSYGRA FNMAEAGCYG PSCLYTGTRL QSDATKGRCT
GTAGYISNAE IGEIIKDGSR VTNHFVDTGS NSNILVYDDL QWVGYMDDDI RSSRNALYAG
LNMGGTTNWA SDLHSFHDVP QPMTSWAQFK QVVTGGGDPW NDGPRSGNWT SIGCDSQAKS
DIRGLSPKQR WDGMDCDSAW DDAISVWKER DKDHSSFSFS QSVSITFNGP ENGHCETLTE
LSNCEETPLC PGFDDAVYSG SAAWAIWSSF VFIHQMYESY VNALTSASAT VISNSFSDFE
NKFQPIPPEE DNTWLLLLLD LVTVGVSGIA APFFNQFLAK LPYLIKNANA AANLKDITMM
ALGQSTTIAK DLLKTSADDW DEDSQDSFSN YLGQALGAWG DIASDALERL FDGSDESIEN
LYNIISEGKL LSGDGGETTT KPPTTSEKDL EGNIAKAFFG YAIPTAWTFS KHYSFIIDSG
YPCDTIDPLG DYLSADTMHN TYGCYEDKLY YLATPKGESF VCNPDCSDSK FSAPPGIENL
DGKNFGGITI KDLIQGSVRS YIHSGNKNGG EFVDLDPGSS FNDLWAQDVT TPGYIRLPVC
SPEHAYKNWD TAGPGDNPDP SYPCNIAKGQ DFCQISSFVD QTSDASPSVS DCQQIIKNIE
NDADASWDTG IATQRELVHY GSCAFGVESK SGADGNVMYQ VGAQDIIDLI NESITTAAID
NRSALATRSP VGLSSGAECA ITLRTAVPGP EEANRDREDD QHPLSFNHIG NFWSAFQKLV
LPLYEMIPGT KDRITTKLAY TYYQWFFQDE TATQLPPVFL IVSPYGMYLN SRSAEFNAAM
TARKSDFLKP VHLYHVVEVY GKNMLSSEGE EWKRHRRIVG PSFNEKSNAL VFEESVRQAR
GLLHYFSTMD GNSKDILNVK DVAPHMAMLA LHVICGAAFG VPQTWPGEDE SVLGSRTVPG
FNTKKLNANH KLPFKYTVDL FQDCFLWVAV LPMWLIKIFP MKITQEIYAS FLELSDYFIE
LVEYKFKRLE TGETDRHTMD VLKPLVSALN TSPGFNEMSA AEKMGSLSMS EITGNAFVVL
FAGHETSANI LHFCMVFLAM NRASQSLLHA DIDNIVGKSD PSTWTYAETM NRLYNSMVGA
TQNETLRLMP PVVSIPKHTL STEKGGTVQT VIVNGEALRV PPGTFMHIDA IGTGRDPNNY
PHRPSKFTGK THDLNDFMPE RWLLSSDYHK DATDSEEAKS PTYHTPQDGS KASGQPDELE
SVNYDNSSAL FRPAKGAFIP FSEGPRGCPG RRFAQVEITA VLATIFQEYS VELDVRKWAS
DEEVGRMTKE QRRTLYAKAV RKAEETIRKS DIIITLRLLS GTSIPLRYVK RGSERFGDVG
LVFVESWPSA AHAVMSESQR AQELRKFYAP FDDGSTPGSA QGINQSILDD GALGAYAELI
LWRLRGTRAM VSLIDNTTEY FVAGVTRPDN SSNEITTNND WFGCATIETP GGLCENVMAM
DGSKGEFPCF EVSSLHTHPR YEHQPVVNGS IAAYKYYAGT PITTAHGVNI GSLFVFDNES
RPNGLTVRER KCLFETAEKV MKHLQSKREA AERRRVALMS TGVAKFLERT TWLGDADTDS
NPDFPLSSNS IGESEAQRSS MESTNITSQT STSGDTDVDG WPKKKGASEI VLDKIKKALD
HAAHVLRESL ELTAGGVVFL DTAIGPSEPK ASTDYFDPIQ PDLDSVTSGI GGVNFEDELS
PENDLTMTGI DPKTTIPSGQ VRGFYDEYRP VRVPALSCSK HAYRRSRALD GKTLQDFIDM
YPKGNIWYID EKGYFSSLDQ DDTAGSPQRT TPTEGRRSIY NIGPDSTRQA AEAAILSKVF
QGARQIIFLP LWDASGNRWH SGCFVWSNNS FPVFTVDSEL AYISALSNSV MVEISRLDSI
MANNVKSDFI SSISHEFRSP LHGILASAEF LHDSDLDQTQ DQLVASIRTC GSALLDTINH
VLDYSKINSF QKKNSSGSFS NELDLTANVA LLCERVVDGL IATRGYTGVG NQDTAAADPD
SPHDAPYAHP VEIILDFEDR DWMFKIIPGA LRRIIMNIVG NAMKFTNTGF VLIQLRVKQA
DGRQSDPTSR MGQKILAMNV IDSGRGMSKQ YMERKLYTPF AQEDPFIPGV GLGLSITRNI
IAQLGGKINI RSELGKGTDV EVLIPLALAD TDDTNTPSEL SSTHAHRLDA QDREASAAVG
AVRALAPGKS VAIWRSPAHT SDSRDESLAW KTVAGYCKS
//
