CHI1_ARTBC
ID CHI1_ARTBC Reviewed; 745 AA.
AC D4AT07;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 52.
DE RecName: Full=Probable endochitinase ARB_07371 {ECO:0000305};
DE EC=3.2.1.14 {ECO:0000250|UniProtKB:Q873Y0};
DE Flags: Precursor;
GN ORFNames=ARB_07371;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000312|Proteomes:UP000008866};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
CC -!- FUNCTION: GPI-anchored chitinase involved in the degradation of chitin,
CC a component of the cell walls of fungi and exoskeletal elements of some
CC animals (including worms and arthropods). Required to reshape the cell
CC wall at the sites where cell wall remodeling and/or cell wall
CC maturation actively take place such as sites of conidia formation.
CC {ECO:0000250|UniProtKB:A2R2S8, ECO:0000250|UniProtKB:Q873Y0}.
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:0000250|UniProtKB:Q873Y0};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC anchor {ECO:0000255}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:Q873Y0}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000305}.
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DR EMBL; ABSU01000008; EFE33907.1; -; Genomic_DNA.
DR RefSeq; XP_003014810.1; XM_003014764.1.
DR AlphaFoldDB; D4AT07; -.
DR SMR; D4AT07; -.
DR STRING; 663331.D4AT07; -.
DR EnsemblFungi; EFE33907; EFE33907; ARB_07371.
DR GeneID; 9520347; -.
DR KEGG; abe:ARB_07371; -.
DR eggNOG; KOG4701; Eukaryota.
DR HOGENOM; CLU_007818_8_1_1; -.
DR OMA; GTTCFAY; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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; cd02877; GH18_hevamine_XipI_class_III; 1.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell membrane; Cell wall; Chitin degradation;
KW Chitin-binding; Glycoprotein; Glycosidase; GPI-anchor; Hydrolase;
KW Lipoprotein; Membrane; Polysaccharide degradation; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..720
FT /note="Probable endochitinase ARB_07371"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434414"
FT PROPEP 721..745
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:Q873Y0"
FT /id="PRO_0000434415"
FT DOMAIN 30..351
FT /note="GH18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT REGION 351..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..684
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 178
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT LIPID 720
FT /note="GPI-anchor amidated glycine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 745 AA; 79261 MW; 56BAC7C0C2DB19C6 CRC64;
MALPKTIMAF IAFISFLVST TFAVDVFSTT NVVTYWGQGH DQKRLSHYCQ QAEHDIIVIG
FVNVFPDQGK GGWPGTNFGN QCFMGTYITP EGEETELLSS CHKIIEDIPI CKAAGKTIML
SLGGQAVDGS KTYSVKTRQS AVYFADFLWR AFGPVSPEWD GPRPFGDNVI DGFDFDIEAN
GGANYEYMVE RLRSNFATDS SRQYYLSAAP QCVLPDGNLG NVISSSAFDF IFVQFYNTPS
CSAFNWAQNP SKSGFTFDSW VQFIRKGASR NAKLFIGLVG DHTRVSPHGE YTKDDSNYLA
LPDADKLIKA YMNKYRANFG GVMIWDALTS DENKLVTGTY SSNIKRLLLN NDPSRPTTTS
KTMSSTKTSM STTTSKYTVT TSTISSTSKI SSSTWSMPTM TTSTRTTSST ATRSSTIVTP
STSPNPTTST STTSGHQNTT ATTTEIETQT SKTFITTTSI WSSGTGIGTC TGIPTITTTP
RYPNATFTSD TTGSPTMSDT TITLSVTSSM HQISDTTTTI PTFSTTPIQT SDISLSMPSG
TTTSKHQSSG ITIPGPPHMS TTIVPASPTK PGHSTTTAIV TTTFTSVCPT GITTVTTTYT
TIYCPEATPM PTAGNPPPPP GMEWTTIVTT CTKCASTSAI MTVTYPVTVP SEPMTPTQVP
GTLPPPGAPG TGSGIPPPKT PSNEPGSPGT LTGIFPPKPT MSVPPEMGGN GGDRTPVYTG
GAGVVSPSFS VVVIVLGSIV YHIMQ
