ID A0A098VU99_9MICR Unreviewed; 270 AA.
AC A0A098VU99;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=NodB homology domain-containing protein {ECO:0000259|PROSITE:PS51677};
GN ORFNames=DI09_3p330 {ECO:0000313|EMBL:KGG51271.1};
OS Mitosporidium daphniae.
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Mitosporidium.
OX NCBI_TaxID=1485682 {ECO:0000313|EMBL:KGG51271.1, ECO:0000313|Proteomes:UP000029725};
RN [1] {ECO:0000313|EMBL:KGG51271.1, ECO:0000313|Proteomes:UP000029725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UGP3 {ECO:0000313|EMBL:KGG51271.1,
RC ECO:0000313|Proteomes:UP000029725};
RC TISSUE=Spores {ECO:0000313|EMBL:KGG51271.1};
RA Haag K.L., James T.Y., Larsson R., Schaer T.M., Refardt D., Pombert J.-F.,
RA Ebert D.;
RT "A new species of microsporidia sheds light on the evolution of extreme
RT parasitism.";
RL Submitted (APR-2014) 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:KGG51271.1}.
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DR EMBL; JMKJ01000333; KGG51271.1; -; Genomic_DNA.
DR RefSeq; XP_013237698.1; XM_013382244.1.
DR AlphaFoldDB; A0A098VU99; -.
DR GeneID; 25259832; -.
DR VEuPathDB; MicrosporidiaDB:DI09_3p330; -.
DR HOGENOM; CLU_021264_11_1_1; -.
DR OrthoDB; 1343935at2759; -.
DR Proteomes; UP000029725; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; PTHR46471; CHITIN DEACETYLASE; 1.
DR PANTHER; PTHR46471:SF2; CHITIN DEACETYLASE-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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029725};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..270
FT /note="NodB homology domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001942034"
FT DOMAIN 36..219
FT /note="NodB homology"
FT /evidence="ECO:0000259|PROSITE:PS51677"
SQ SEQUENCE 270 AA; 29522 MW; 6879734E3E9C5945 CRC64;
MKFKALSLIS AFALYQSAVA APLPSRDPVV NLCPSGYFAF TFDQGPSLYT GDILDALRNL
NVKATFHPVV TFLNEAAIVA NLQRAAEEGH LIGLSLEEDF ELNGISDEDL LDEISARADI
IKQVVGYKPV YLRIPKYKDL GIEQLQKIIS KGYIISTYNI DSYDYSKDDI LGVYKQTLDK
MSPNTKGGFI SVQRDYLASS ASATENVIEY VLEKGYKVVT IDQCAKSKVK DAPGPKGLGQ
IKSRESDASH AFVSSFLTGT LLLIAFLAGL
//
