ID   A0A168N180_ABSGL        Unreviewed;      1141 AA.
AC   A0A168N180;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Glycoside hydrolase 35 catalytic domain-containing protein {ECO:0000259|Pfam:PF01301};
GN   Name=ABSGL_05251.1 scaffold 6884 {ECO:0000313|EMBL:SAL99606.1};
OS   Absidia glauca (Pin mould).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX   NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL99606.1};
RN   [1] {ECO:0000313|EMBL:SAL99606.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL99606.1};
RA   Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA   Babar A., Rosenke K.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
CC       {ECO:0000256|ARBA:ARBA00009809, ECO:0000256|RuleBase:RU003679}.
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DR   EMBL; LT552933; SAL99606.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A168N180; -.
DR   STRING; 4829.A0A168N180; -.
DR   InParanoid; A0A168N180; -.
DR   OMA; DGPQHDF; -.
DR   OrthoDB; 1032627at2759; -.
DR   Proteomes; UP000078561; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR031330; Gly_Hdrlase_35_cat.
DR   InterPro; IPR001944; Glycoside_Hdrlase_35.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR23421:SF165; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR23421; BETA-GALACTOSIDASE RELATED; 1.
DR   Pfam; PF01301; Glyco_hydro_35; 1.
DR   PRINTS; PR00742; GLHYDRLASE35.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 2.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          59..434
FT                   /note="Glycoside hydrolase 35 catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01301"
FT   REGION          1080..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1141 AA;  130257 MW;  B074A5D4C14EA69F CRC64;
     MGDMTQLYSL FSLVVPAILG FVLYAHHRTH GVLTDITTES VAYNRSKYGP LLDWDKYSLR
     IEGEPTILLS GEFHYWRVPD RERWPRILQQ YRTAGFNTIR IYFHWGYHSP DDNVYVFDGN
     RDVDYLLTLC EQLGLFVLAA PGPYICAETQ GGGYPAWLAA KRDLRIRHNS IMLWRTYDAE
     FARYEIQWLD HILPILARHQ ITENNDQRRR RGCVLALQID NELFENMATI LPVGLRDQMR
     ILSKAARDAN ITVPLFTNDG FEEGGWVPGK KANFWSKYPF GIDLYGFDKY VVFAPSSSPK
     SWLIDGGTAS GEWQDWDPKR MENSMDRLEK TVRGFGGGAK ESPMFIPEMQ GGWFNHYQLE
     HTYDQIYDFY GDQYTKLLFE TSLAQGVTMA SLYMVYGGTN WGTLGDPDVY TSYDYSACIR
     EFGYLSSRGR NLRQTLIFAQ SFEPYFTRTD YTEKPTLQPS VKTIFNRQRV SVGADQDVAF
     TFFRNFDRQK RDNFEITVNH GTDKFKMGIH FAYKTSFIAV GNYHTINGLH LVQSTLPIHA
     RMVNHSTNEE IWIVEPNSVG GLAFEDTSAT TITGTMQVKS TKPINTIALL QFNIAEGSTT
     IKTDTGALHV VGLAAKDIST LYADFEASYW NQGSDHSRYP GLLAWGADDL YYNRTTKQLE
     VGHNIHDKTL SFVSFSKPID TQTTPDQVMP YLYTKPLTDH TLEQEQHPVE LPLSQWQTRS
     VDWTRLSWQP LARNSKKTLV WNALDYHFTS GHILYRNEFK TPAKSDPRVK LSLNVRHRAT
     VLMNGHIVGG HTTYSRQLFS AGAKIGPDPW FLGTQTYDLT PYLIREGREL KNTLVILVDS
     FGLSRQAFIM NDIRNPRGVI KAKLQGVEDS KIVDQSWEIT GVDVRGLSQP YNSTGFPDEQ
     QEDGFAVLDL TAPSSPTLER QQPLQHQQRI ADHLYRIPLD PTQGVVWWQF AFDNPWKKDK
     TYRVPLRLRL DGAFTAKVIL NDLLVGLYYG NGDGPQHDFY LPEELVKPQG NVVRMLVYTW
     SATEAQIAIK GWHVNVPGSG NLILDASVKP TDYILWKDTY DGLAGGYPVE TLERQWDLNG
     RKTEKNENSS TGADRSLPSS TTFAQQHNIT IETATNVAEE RCSRVKKFLH HLAEHNGQII
     E
//