GenomeNet

Database: UniProt
Entry: A0A0B7NPH0_9FUNG
LinkDB: A0A0B7NPH0_9FUNG
Original site: A0A0B7NPH0_9FUNG 
ID   A0A0B7NPH0_9FUNG        Unreviewed;       396 AA.
AC   A0A0B7NPH0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=NodB homology domain-containing protein {ECO:0000259|PROSITE:PS51677};
GN   Name=PARPA_13631.1 scaffold 47020 {ECO:0000313|EMBL:CEP19317.1};
OS   Parasitella parasitica.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX   NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP19317.1, ECO:0000313|Proteomes:UP000054107};
RN   [1] {ECO:0000313|EMBL:CEP19317.1, ECO:0000313|Proteomes:UP000054107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP19317.1,
RC   ECO:0000313|Proteomes:UP000054107};
RA   Ellenberger Sabrina;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; LN734023; CEP19317.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B7NPH0; -.
DR   STRING; 35722.A0A0B7NPH0; -.
DR   OrthoDB; 1343935at2759; -.
DR   Proteomes; UP000054107; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004099; F:chitin deacetylase activity; IEA:UniProt.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0009272; P:fungal-type cell wall biogenesis; IEA:UniProt.
DR   CDD; cd10952; CE4_MrCDA_like; 1.
DR   Gene3D; 3.20.20.370; Glycoside hydrolase/deacetylase; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR002509; NODB_dom.
DR   PANTHER; PTHR10587:SF105; CHITIN DEACETYLASE 1-RELATED; 1.
DR   PANTHER; PTHR10587; GLYCOSYL TRANSFERASE-RELATED; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..396
FT                   /note="NodB homology domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002121595"
FT   TRANSMEM        376..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          121..311
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000259|PROSITE:PS51677"
FT   REGION          24..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..58
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   396 AA;  42103 MW;  9037AC2C42AD27A1 CRC64;
     MKFTSIATIL TLISVIQAQN VTSSSSSSAE PAAPSAATGA STSTTSTTST TGQISSDYPA
     HGTKPVAKPE WLDLIKSANI TNAPVLKANG NNGPSTSGSD DYCDWSKSGC MGDSIGDCPK
     GTWGLTYDDG PSQYSPILYD FLKTTNQKAT LFMIGANVIQ HRDIVKRAYD EGHEIAIHTW
     THSYMTTLTN EEIVAELKWT ELAIKEIIGV SPRLFRPPYG DIDNRVRDIG NALGFTSVIW
     DHDTNDWMLA EKAPGFQAQW IDGNFTEWIA EAATATTGGL SLEHDIQKVT VDAAIKNLPQ
     LQKAYKVVTV GQCAGVPSYK ESDAIPSINS TVISSSAIPS ATSSVLVAPA APSTTQTQAS
     TANNAHASAG MRSRSFVSGS ALVSAAVMFM FTLYLL
//
DBGET integrated database retrieval system