ID Q7Z8R6_9ASCO Unreviewed; 1568 AA.
AC Q7Z8R6;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=Chitin-binding protein {ECO:0000313|EMBL:CAD91890.1};
OS Babjeviella inositovora.
OG Plasmid pPin1-3 killer plasmid {ECO:0000313|EMBL:CAD91890.1}.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX NCBI_TaxID=45609 {ECO:0000313|EMBL:CAD91890.1};
RN [1] {ECO:0000313|EMBL:CAD91890.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL Y-18709 {ECO:0000313|EMBL:CAD91890.1};
RC PLASMID=pPin1-3 killer plasmid {ECO:0000313|EMBL:CAD91890.1};
RX PubMed=13680368; DOI=10.1007/s00438-003-0920-5;
RA Klassen R., Meinhardt F.;
RT "Structural and functional analysis of the killer element pPin1-3 from
RT Pichia inositovora.";
RL Mol. Genet. Genomics 270:190-199(2003).
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}.
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DR EMBL; AJ564102; CAD91890.1; -; Genomic_DNA.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 CDD; cd02878; GH18_zymocin_alpha; 1.
DR CDD; cd00118; LysM; 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 Gene3D; 3.10.350.10; LysM domain; 2.
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 InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_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 Pfam; PF01476; LysM; 2.
DR SMART; SM00270; ChtBD1; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF54106; LysM 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.
DR PROSITE; PS51782; LYSM; 1.
PE 4: Predicted;
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 Membrane {ECO:0000256|SAM:Phobius}; Plasmid {ECO:0000313|EMBL:CAD91890.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1463..1490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 739..788
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 801..857
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 867..1202
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 174..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 817..829
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 822..836
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 851..855
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 1568 AA; 172320 MW; 8A87A77C21726BF6 CRC64;
MYLILLFFIN TVISNHLYRS VNISLNSTSL SSFADSSSIE LSSIEAFSSS YESSSTDSLS
SVYESSSIDL SSSYEPFSTE LSSSDYESSS IESISSYEPS STELSSSDYE SSSIESISSS
YDPTQMLKLI YSLAHNISFS DYEPSSVELT SSYEASSTES SSFDYELSSI ESTSSSYKTP
STESSLTELS SSDYESSSSY DPTQMLRLIY SLAYNISSSS NKSSSVINLS NNTKMYYNSS
IETKTSSTPI SRTSSLVLEN SSISNINYKR FTSDIVKSTS TSPKPRIMPK LLALATTSKC
TNADEVALTL NMNNIGSNNY ALPNDVISAA QMFQSWLKGN SNRDSLKYQS GNIVGYLWVG
NMVQNSGAAD TIVANFIQNV GSDGIKDTKY VQYSTANDPA KGAGIVINTK GDLALVQKIV
RTWSKGQSYD AGTYNWNNKV LCYLSYANRK LGGNDEEAGD CDYKKVVSGR PIADTCGVTS
DALIQYNPGV DFTKLNVGQP ICCSEGKPQP YTPKCKDSTE LVINYNYGYV RGTKTDDTKN
NAIAALNSFN SWVSSTGTRG SFKYQSGNTA AFMWIGSMVQ NDGFKNNAIK AFTDEINLQG
MPKVGFLEYM AGDPMKGFGI IIDVSGNLTN VQNAVKNWSM GKGYTIQDAN KSINSQSICY
LDYAKRKSIG NDNEAGDCIY KSLANGQTVD VLCGVNAESI QAYNSGLDFS KLPVGQPVCC
SEGKAPDLRP KKNSDGSCYV YTVKSGDTCS AIFAKYSPLS ELDLMKYNQQ NFGWLGCTNL
QKDYKLCLSD GTVPRPTVNP LAECRPQAPG DKYNTTCPLN ACCSEFGFCG LTSEFCNNKP
SLTGSPGTTG CLTNCGYGHL SSLAGTFKNI AYWLDADGPM ASDPFNYDDG SYDAIHYAFV
NINSDFSIDD SKFSNSKFLN SNLKNSSFGG WGFSTSPSTY QIIRKGVQIG NVVKFANNVV
NFLNKYNLDG LDFDWEYPGA PDILGIPADD PKNGNNYLNF LILVKAMLPA GKTLSVALPA
SYWYLKAFPI YQMHNYVDYF IYMTYDIHGT WDLSKDNAVK CHTNKTEIVD ALKMLNKAGL
NLSKVRGGLA NYGRSYKLAN PSCYAVGCPF TGGGEKGPIT NTDGILADSE IINIDASKSK
NQRWTDSTSE CIFMVYDTNN VVGWTANRNN LQNYYQQNGL RGSSLWLTNY FSHDTYNSTD
YESDWSDEED DDVTINYDPY NCKTSILTDL NNYDNINFYC KQEALINYTI YIAKNATNNI
QNILNNYNTY EKNYNAYVTS IQNSIMSEYL DWYYDKPGSQ YYSCQNANDM NACVVKTVGP
QNTCRYVTMS GLYSLSDNIN LAAASLSLYY NMTINTLIRV YQRCNCTSTL DGNGCEYNIK
YNDCKAADLI QDPMANITMQ NVTDIISLLT NAQNALGNQS PIDILDSLTA ALIFTTAADN
IMEINSKGSQ VREIEKEERE KMIVAIVFGI LGFASMFLGP IDGILAAIAL DTVQMLADWS
ISGSINKGDI ISLCADAVFG IISGLKLGES FASIANTFRA LKNDDLESQL NKFERYREVR
EKLIGKTC
//
