ID A0A094KBN6_9PEZI Unreviewed; 1338 AA.
AC A0A094KBN6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 33.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=V501_00860 {ECO:0000313|EMBL:KFZ19018.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ19018.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ19018.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
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 -!- 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:KFZ19018.1}.
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DR EMBL; JPKD01000292; KFZ19018.1; -; Genomic_DNA.
DR STRING; 1420914.A0A094KBN6; -.
DR HOGENOM; CLU_005872_0_0_1; -.
DR Proteomes; UP000029315; 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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11618; ChtBD1_1; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 3.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001002; Chitin-bd_1.
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; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF333; CHITINASE; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00270; ChtBD1; 4.
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; 2.
DR PROSITE; PS50941; CHIT_BIND_I_2; 3.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261}; Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00261};
KW Reference proteome {ECO:0000313|Proteomes:UP000029315}.
FT DOMAIN 385..437
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 452..800
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 803..849
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 855..900
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT REGION 1299..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 401..413
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 406..420
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 822..836
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 875..889
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 894..898
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1338 AA; 147117 MW; C46F7FB30FA46472 CRC64;
MDNKPDEKRT NSGAFEKFRQ ETDQLLVVPG SFVCWTWLFE HKSFKGSRIS KSLLRPENIL
QPSNNENSLN HETIGAVRMR TDAVLCVERL LLCWHSNDHP ASSFSLMDTR LTTPSQPIFC
SPLDEWQFPR REHSATTTTS TPQSVTDIST LDFDQVLDIR TQSSSESDVE REYVDFIEYL
EVGLVKVEQP HKRINKRQKV RHCRRSLMKM TALEMAMLAN ISYGSAKIIL AETVAAGAYG
ASSTPSPRDE RSGRETEIEA DLFLSSALQD CVRRHRIPEM ELTMRRSALF FFLSFLLHLA
SADISGDGGL VKDAFPNPVP DYAFGLNDRS LGSRQRVCPT PGPGARLCDK DTKCADGSCC
SECGIFGYGP TYCGEGNCTS SCEAVAMCGV YGDLTVNNGE CGMGLCCSAY GWCGTTESHC
IGTPDAPCQS DHGPCAIVAP QKCGVASGTT NKRTIAYYQA VGSYGRICNS IKPRNIDTTK
FTHLYYAFAS INPETFEIAV TDKDKEIIPE FTALNKTLKT WIAVGGFDFS EPDTPTHTTW
SDLVSSAANR KTFITSLMDF MDFWGFSGAD LDWEYPVDET RGGKKTDTAN FVLLVKEMRE
RFGTKYGISM AIAPDYWYLR WFDLFSMQQF VDFFGFMTYD LHGFWDGANA NIGTTIRGQA
GIDEIQNNTA PLYFDKLDFS KINFGLAYYG RGYTLANPTT CKELGCTFTG PSNPGKCTKQ
KGVMSLTEIQ QMIQTEGITP TLLGPQMMKS IQWADQWIGY DDDETFAMKK AWADDYCFGG
TMAWSVDFNS GPGNGNTPPT TTDGTCGKDH DYTMCGNGFG NCCSSGGWCG DSDAHCGSGC
QSESGTCTQG GPTTDGTCGV GNNGLECDLF ESGPCCSNSG YCGFGSSWCG VDNCQAGCAY
FQLQEGLGIK EVDRTQGPLI PDASRWDIKG VTDSQGTRLN RDMWKKTNSG GEFDNWYEDN
FDSPQGWLEA LANPLGLGQS HATCKIDTPC ARPNCKDLEN QQEPGTAWKY MTVISAVNMN
QYFHSLWEAV GNANTRFAAN DWRLSKTFWP AMLSLGGGAG AVAGALTGGA IYEAIAEIQM
GGTSQDDGDH VVSFPTGART TFDKANAAIV AGNGSWPGAR QVHDLFQDGD WVDYREIPVV
SGSVSVTDVE NAFFQLTVAN LVNYAWRQQV VYLACYPMSQ ETFDNTEVKA GNNEDKLKIY
YGGIGCYFQS ALPNKTLLNQ ATSNFDPPGW KELESDDYPF STHDIMISSI DSWDRYGMGE
EDRSRDENFW APFGPGNDYK EAFRSSGLFN IAVCIPETSD DPKAGWDNPN SDDTPTPTGI
ETFFESLHGD GSDSAYQK
//
