ID A0A176WR04_MARPO Unreviewed; 466 AA.
AC A0A176WR04;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 03-MAY-2023, entry version 23.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAE34955.1};
GN ORFNames=AXG93_593s1110 {ECO:0000313|EMBL:OAE34955.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE34955.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE34955.1, ECO:0000313|Proteomes:UP000077202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE34955.1};
RA Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT "Mechanisms controlling the formation of the plant cell surface in tip-
RT growing cells are functionally conserved among land plants.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:OAE34955.1}.
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DR EMBL; LVLJ01000294; OAE34955.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A176WR04; -.
DR OrthoDB; 2783699at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd00035; ChtBD1; 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; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR46476:SF20; CHITIN-BINDING TYPE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46476; CHITINASE 2-LIKE; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR PRINTS; PR00451; CHITINBINDNG.
DR SMART; SM00270; ChtBD1; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 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; PS51910; GH18_2; 1.
PE 4: Predicted;
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}; Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT DOMAIN 141..182
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 192..466
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 27..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 144..159
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 153..165
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 158..172
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 176..180
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 466 AA; 51218 MW; 45B2EAD09FBA37A2 CRC64;
MVDWLVQLET DMFNRWPLQS LIHFPDLNRH NPPGDPKHET QSKASKSRHL RESRGLVVCH
VCRPTRTKSD RGPRDFIIQT SRRLCRSTLF KRWRPHRYEL NSLNLLAMGL TSGFGMRRGH
GGVAVAISLL ISAGILQLTW AQDCGSAAGG ALCANKLCCS QYGYCGNTAA YCGTGCQSQC
SYAAPKGLFP GRMLFDYLGS NGVAITFNDI PITQSDKTWV LGLSFAIDLT STGQKANGIH
SVYWNPTLTK AAAKAWRQAH SNGRIVIAIG GAVYYTPSGT EVSVDWYNPT NPTQWLANAV
SSLTTIIQDY GADGIDIDIE RFPNGNTNFV SLIGQLIQTL KNNGVINIVS VAPGFDQLAL
YTQLHNSYGS YIDLVNYQFY GEGLNTCAKY KARYNVVVQS LPVNKVGLST QVALDPNTIT
GSTFYNCVTQ IKNEGRAISG VYLWNADLSK NLNNNFQTEK DVDAIL
//
