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Database: UniProt
Entry: M0LZV2_9EURY
LinkDB: M0LZV2_9EURY
Original site: M0LZV2_9EURY 
ID   M0LZV2_9EURY            Unreviewed;       307 AA.
AC   M0LZV2;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   SubName: Full=BNR repeat-containing glycosyl hydrolase {ECO:0000313|EMBL:EMA37655.1};
GN   ORFNames=C447_11805 {ECO:0000313|EMBL:EMA37655.1};
OS   Halococcus hamelinensis 100A6.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=1132509 {ECO:0000313|EMBL:EMA37655.1, ECO:0000313|Proteomes:UP000011566};
RN   [1] {ECO:0000313|EMBL:EMA37655.1, ECO:0000313|Proteomes:UP000011566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=100A6 {ECO:0000313|EMBL:EMA37655.1,
RC   ECO:0000313|Proteomes:UP000011566};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC       {ECO:0000256|ARBA:ARBA00037986}.
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:EMA37655.1}.
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DR   EMBL; AOMB01000033; EMA37655.1; -; Genomic_DNA.
DR   RefSeq; WP_007694109.1; NZ_AOMB01000033.1.
DR   AlphaFoldDB; M0LZV2; -.
DR   PATRIC; fig|1132509.6.peg.2689; -.
DR   eggNOG; arCOG08113; Archaea.
DR   OrthoDB; 197823at2157; -.
DR   Proteomes; UP000011566; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR   InterPro; IPR031778; Sortilin_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR   PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR   Pfam; PF15902; Sortilin-Vps10; 1.
DR   SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000313|EMBL:EMA37655.1};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011566};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          48..165
FT                   /note="Sortilin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF15902"
SQ   SEQUENCE   307 AA;  33287 MW;  CD5C095DFC2B5D1E CRC64;
     MSLLIGTQDG VFRSGESLDD AERVVDAGNT LRVRTLDEDA YAATTSGLYR STDGGRTWEN
     LDVPREEVYS VVTSPDGERL YAGTHPAHLY VSTDNGATWE ECEGFQELPS REEWHTPRHR
     NEAHVRSLGT HADAPDRLVA GVEVGGVHVS DDRGETWTER REGVHHDVHH VLVLGGEEYV
     ASTGGGLYRT RDAGTSWIRL DEAVDHGYFR EAFAFEGTLY VAAARDPPPT WGGESGADAA
     LFESRDGGDT LDAVSYPGEP ASFVLAWTAW NGRVVAGTTE GRVLAREPDG WTTVGHVPSG
     VRSLAAV
//
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