ID S6D1L3_9EURY Unreviewed; 984 AA.
AC S6D1L3;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN ORFNames=HTIA_2124 {ECO:0000313|EMBL:CCQ34238.1};
OS Halorhabdus tiamatea SARL4B.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halorhabdus.
OX NCBI_TaxID=1033806 {ECO:0000313|EMBL:CCQ34238.1, ECO:0000313|Proteomes:UP000015381};
RN [1] {ECO:0000313|EMBL:CCQ34238.1, ECO:0000313|Proteomes:UP000015381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARL4B {ECO:0000313|Proteomes:UP000015381};
RX PubMed=24428220; DOI=10.1111/1462-2920.12393;
RA Werner J., Ferrer M., Michel G., Mann A.J., Huang S., Juarez S.,
RA Ciordia S., Albar J.P., Alcaide M., La Cono V., Yakimov M.M., Antunes A.,
RA Taborda M., Da Costa M.S., Amann R.I., Gloeckner F.O., Golyshina O.V.,
RA Golyshin P.N., Teeling H.;
RT "Halorhabdus tiamatea: proteogenomics and glycosidase activity measurements
RT identify the first cultivated euryarchaeon from a deep-sea anoxic brine
RT lake as potential polysaccharide degrader.";
RL Environ. Microbiol. 16:2525-2537(2014).
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; HF571520; CCQ34238.1; -; Genomic_DNA.
DR RefSeq; WP_020936338.1; NZ_AFNT02000061.1.
DR AlphaFoldDB; S6D1L3; -.
DR GeneID; 23799322; -.
DR KEGG; hti:HTIA_2124; -.
DR PATRIC; fig|1033806.12.peg.2112; -.
DR HOGENOM; CLU_008926_0_2_2; -.
DR OrthoDB; 373626at2157; -.
DR Proteomes; UP000015381; Chromosome.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.60.40.710; Endoglucanase-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR001956; CBM3.
DR InterPro; IPR036966; CBM3_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR001701; Glyco_hydro_9.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR22298; ENDO-1,4-BETA-GLUCANASE; 1.
DR PANTHER; PTHR22298:SF29; ENDOGLUCANASE; 1.
DR Pfam; PF00942; CBM_3; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00759; Glyco_hydro_9; 1.
DR SMART; SM01067; CBM_3; 1.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR PROSITE; PS51172; CBM3; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 4: Predicted;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:CCQ34238.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCQ34238.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326}.
FT DOMAIN 562..723
FT /note="CBM3"
FT /evidence="ECO:0000259|PROSITE:PS51172"
FT DOMAIN 737..825
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 478..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..841
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 984 AA; 106966 MW; 559D5149625645D6 CRC64;
MTHHDANSRG MGRTNTDRDD GLFRRDLLAA MGLGAGSVAL GTDVGTPSVI SRAAGQTSLE
LDYAHALQQS LYFYDANRCG ATTMGERLQW RGECHHSDTE ISLDAATEDG GTNLSASFID
EYSDVLGPDG TGTVDVSGGF HDAGDHMKFG LPQSFSASTL SWALYEFEDA FRDVGVYDHM
VDILRHFADY FLQSTFRSQD GDVVAFCYHV GEGSIDHNYW GPPELQSSEE YPRPAYFATA
EDPASDQCAG AAAALAITSL VLESEDAEYA VECLDTAQAL YDFAVENRGL GYDGGFYDSS
YDEDELSWAA VWLHIATDDD AYLDDILATD DSGNYAGYLG QIIDSTDDDW QNIWVHSWDT
VWSGVFLKLA PITDDPEHWQ IARWNLEYLS GGAVEHGDDN DTNYASTSDA GFTVLNTWGS
ARYNAAAQFQ AMVYRKYRDT EKAVALTDWA ATQMNYIMGA NPFGYSLIVG FTDDHAEHPH
HRAAHGSKTN SMEEPEEHRH TLWGALVGGP DEDDTHVDET SDYVYNEVAI DFNAGLVGAL
AGFNTFYSDT GDPVAAFPPD EEPIDAYYAE GEVLQENADR TQVRVTIHNE SIHPPHREDG
LSARYFIDIS ELREAGQSID AVSVEVQYDQ QATEGDGSTD VSGPIAWDED AGIYYIELDW
SGNQIYGARE IQISMIAEQD DNWESNWDPS NDPSFQDIGE EATVTEAIPV YLDGELVYGQ
LPGESESEPD DTTAPTAPSN LFVVETTASS AEIEWEAASD EGGSGLDHYT ISVAGDFDQQ
VEAETTGTTV EELDAETTYE IGVSAVDAAG NESDTVTVEA TTDEADDGED DSDDEESPTD
ALVVNDYDGD PAWSSNRNDL GQWCGAGSFE NGSGDVEDGA LVLEYDNGGW YQEQINQAVD
DYSSVVLEVS GANGGEESEI RFAMDGVSDL LANLTDDSIG ASAGEVRIDM ESAGIDPAAQ
GLAVRLNFWQ GGNSTLEIKE VRLE
//
