Q59278 (Q59278_CELFI) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Endoxylanase EMBL CAA90745.1
EC=3.2.1.8 EMBL CAA90745.1

Gene names

Name:

xynC EMBL CAA90745.1

Organism

Cellulomonas fimi EMBL CAA90745.1

Taxonomic identifier

1708 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Cellulomonadaceae › Cellulomonas

Protein attributes

Sequence length	1187 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family. RuleBase RU003432

Ontologies

Keywords
Biological process	Xylan degradation EMBL CAA90745.1
Molecular function	Glycosidase RuleBase RU003432 EMBL CAA90745.1 Hydrolase
Gene Ontology (GO)
Biological process	carbohydrate catabolic process Inferred from electronic annotation. Source: InterPro xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro cation binding Inferred from electronic annotation. Source: InterPro endo-1,4-beta-xylanase activity Inferred from electronic annotation. Source: EC hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q59278 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3AF369D3265E3223	FASTA	1,187	125,379
	10 20 30 40 50 60 MYLDGGDTAP YPDLLLDDVV ITGQAPTDPG GVVPGGAVDP TTTPVATARG TGDVSALTFD 70 80 90 100 110 120 DGPNGATTTA LLDFLAERDI RATFCVIGQN IQAPGGADVL RRIVADGHTL CNHTTSYADM 130 140 150 160 170 180 GGWTAEQVRA DLVENLGIIR DALGDPDAKV PYFRAPNGSW GVTPGVAVAL GMQPLAVTNT 190 200 210 220 230 240 IDDWSTQDVP TLTSNLRDAM KAGQVVLAHD GGGDRSGTLA AVQTVVDERL AAGWTFTLPT 250 260 270 280 290 300 GGADGGSSVP TGLSNDFEAG LGVWGPRGDA TVTLSDDAHG GAQAALVAGR TQAWHGIGAT 310 320 330 340 350 360 VTDVFQTGRT YTVDAWVKLA AGATEPADLR ISVQRDNAGE STYDTVTTAT GVTADAWTHV 370 380 390 400 410 420 QAQYTMAAAE SALLYVESSS SLASFLVDDV VVSGSTAPPV QTDIPSLKDE LPWPVGVAID 430 440 450 460 470 480 ERETVGTGEQ LVVKHYDQIT AENAMKPESI QPTEGAFTFE AGDALIDSAV RNGQRVYGHT 490 500 510 520 530 540 LVWHSQTPDW FFTHADGTPL TSSAADQQIL RDRMRTHIET VADHYRQKYG EYGTAGNPIV 550 560 570 580 590 600 AYDVVNEAIA ESESDGLRRS RWFEVLGEQY LDLAFQYASQ AFNGGDTDGP VQLFLNDYNT 610 620 630 640 650 660 ELPAKRRAML DVVNRLLARD VPVDGLGHQF HVNLLQPVSQ MKASIDAFAT TGLLQAVTEL 670 680 690 700 710 720 DAPIDGTVSQ EKLVAQGYYY ADVFDMLRQY PDLFSVTLWG PYDSRSWREG APLPFDDDLQ 730 740 750 760 770 780 AKPAFWGIVD RGELPTLTRL ADAHAGTPTG VDDPTWRLLP ETSFGDATGF QLRWSADGLV 790 800 810 820 830 840 AYVEVADATD DGADDVVDLF AADQHVTVHR SDAGVVATAS RTAWPCARGR GPDAGRDRAV 850 860 870 880 890 900 RRARHDGASG ERRSWNDLSH GQEDGERLGV VTLVEPVGYV AAVQASTAPV IDGVVDEAWA 910 920 930 940 950 960 DAPVLTTDVQ VEGTPGATAE IRVLWHDDAV DVLATVADPV VDETATNAWE QDSVEIFVDP 970 980 990 1000 1010 1020 VNAKAGAYTP QDGQYRISAS NAQSVSGDLA VIGERLTSAT ALVDGGYVVE ASIALGRDVT 1030 1040 1050 1060 1070 1080 VGDLVGLDFQ VNDATAGVRG SVRTWTDPTG RSYQSTARWG VAELVAPAVE PGPVLTLGAG 1090 1100 1110 1120 1130 1140 SVAAGKKLAV DLAGFEPKAK VRLVLDRVGA APTAPSRSGL FGQLVDGLSA WYWKDVELGS 1150 1160 1170 1180 VRTDADGAAS ATVKVPAWVL PGDFEVKAYV AGEVVASAPV RVRPVFS

References

[1]	"A modular xylanase from mesophilic Cellulomonas fimi contains the same cellulose-binding and thermostabilizing domains as xylanases from thermophilic bacteria." Clarke J.H., Davidson K., Gilbert H.J., Fontes C.M., Hazlewood G.P. FEMS Microbiol. Lett. 139:27-35(1996) [PubMed: 8647371] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z50866 Genomic DNA. Translation: CAA90745.1.
PIR	T31351.
3D structure databases
HSSP	HSSP built from PDB template 1HIZ based on UniProtKB P40943.
ProteinModelPortal	Q59278.
ModBase	Search...
Protein family/group databases
CAZy	CBM22. Carbohydrate-Binding Module Family 22. CBM9. Carbohydrate-Binding Module Family 9. GH10. Glycoside Hydrolase Family 10.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR010502. Carb-bd_dom_fam9. IPR008960. Carb-bd_dom_fam9-like. IPR015922. Carb-bd_dom_fam9-like_subgr. IPR003305. CenC_carb-bd. IPR008979. Galactose-bd-like. IPR011330. Glyco_hydro/deAcase_b/a-brl. IPR001000. Glyco_hydro_10. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. IPR002509. Polysac_deacetylase. [Graphical view]
Gene3D	G3DSA:2.60.40.1190. CBD9. 1 hit. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit. G3DSA:3.20.20.370. Polysac_deacetylase. 1 hit.
Pfam	PF02018. CBM_4_9. 1 hit. PF06452. DUF1083. 1 hit. PF00331. Glyco_hydro_10. 1 hit. PF01522. Polysacc_deac_1. 1 hit. [Graphical view]
PRINTS	PR00134. GLHYDRLASE10.
SMART	SM00633. Glyco_10. 1 hit. [Graphical view]
SUPFAM	SSF49344. CBD9-like. 1 hit. SSF49785. Gal_bind_like. 1 hit. SSF88713. Glyco_hydro/deAcase_b/a-brl. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

Q59278_CELFI

Accession

Primary (citable) accession number: Q59278

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	October 19, 2011
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)