Q9L8L8 (Q9L8L8_9BACL) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Beta-1,4-xylanase XynA EMBL AAF61649.1

Gene names

Name:

xynA EMBL AAF61649.1

Organism

Caldibacillus cellulovorans EMBL AAF61649.1

Taxonomic identifier

74586 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Alicyclobacillaceae › Caldibacillus

Protein attributes

Sequence length	921 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 AAF61649.1
Domain	Signal EMBL AAF61649.1
Molecular function	Glycosidase RuleBase RU003432 Hydrolase
Gene Ontology (GO)
Biological process	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 hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 33	33	Potential EMBL AAF61649.1
	Chain	34 – 921	888	beta-1,4-xylanase XynA EMBL AAF61649.1		PRO_5000057343

Sequences

	Sequence		Length	Mass (Da)
	Q9L8L8 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: C5DDD1A7F7567413	FASTA	921	102,380
	10 20 30 40 50 60 MGTGRAGEWI KKMLLVLAIG LLIPIPYPHV ASAENVLILQ SDFEDGTTQG WVGRGGVETL 70 80 90 100 110 120 TVTSAAAYSG AYGLSVSGRT ETWHGPTLDI TSYIQVGKTY QFSAWVKLPS GSSNTRISMT 130 140 150 160 170 180 MQRTMQDTVY YEQIYFDTAL SGNWIQLKAQ YKLYEPAVNL QVYFEAPDHA TQSFYIDDVR 190 200 210 220 230 240 IEQLPDLPKT VEENIPSLKD VFAGRFPIGT AFENFELLDE QDRKLILKHF NSVTPGNVLK 250 260 270 280 290 300 WDSTEPQEGV FNFTESDKAV AFAVQNGMKI RGHTLIWHNQ TPNWVFYDSN GNLVSKEVLY 310 320 330 340 350 360 QRMERHIKTV VSRYKGIIYA WDVVNEVIDP GQPDGLRRSL WYQIAGEEYI EKAFQFAHEA 370 380 390 400 410 420 DPNALLFIND YNTHESGKSQ ALYNLVQRLK SKGIPVHGVG HQTHINITWP SISEIENSLV 430 440 450 460 470 480 KFSNLGVVQE ITELDMSIYN NSSQKYDTLP SDLAQQQATR YRQLFEMFLR RSSLIQNVTF 490 500 510 520 530 540 WGKDDANTWL RKFPVVRNDW PLLFDEQLKA KPAYWAVVGT VPSPTPTPTS TATPTPTPTV 550 560 570 580 590 600 IPTPTPTPTP TSTPTPTPTP SASGTLRVEY RVGDSSATDN QMKPQLRIVN TGSQAVPLTE 610 620 630 640 650 660 LKVRYWYTKN STQAEQYFCD WAQIGCSNIR AQFVSLAQPV SGADSYIELS FTGGSVPAGG 670 680 690 700 710 720 NTGEIQNRIH FTNWMNYNET DDWSYNGTQT TWGPSTRITL YRNGVLVWGT EPGGGSSTPT 730 740 750 760 770 780 PTPTPTPTPT STPTPTPTPT STPTPTPTPT STPTPTATPT PTPTPTPSAG GNLVVQYRAA 790 800 810 820 830 840 DTNAGDNQLK PHFRIVNRGT TSVPLSELTI RYWYTVDGDK PQVFNCDWAW VGCSNLRGSL 850 860 870 880 890 900 VKLTTGRTGA DYYLEITFTS GAGSLAPGAN SGDIQARINK NDWTNYNEAN DYSYDPTKTS 910 920 FADWNRVTLY RNGQLVWGVE P

References

[1]	"A novel thermostable multidomain 1,4-beta-xylanase from 'Caldibacillus cellulovorans' and effect of its xylan-binding domain on enzyme activity." Sunna A., Gibbs M.D., Bergquist P.L. Microbiology 146:2947-2955(2000) [PubMed: 11065373] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF200304 Genomic DNA. Translation: AAF61649.1.
3D structure databases
HSSP	HSSP built from PDB template 1NBC based on UniProtKB Q06851.
ProteinModelPortal	Q9L8L8.
ModBase	Search...
Protein family/group databases
CAZy	CBM22. Carbohydrate-Binding Module Family 22. CBM3. Carbohydrate-Binding Module Family 3. GH10. Glycoside Hydrolase Family 10.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BRENDA	3.2.1.8. 141207.
Family and domain databases
InterPro	IPR008965. Carb-bd_dom. IPR001956. CBD_3. IPR003305. CenC_carb-bd. IPR008979. Galactose-bd-like. IPR001000. Glyco_hydro_10. IPR013781. Glyco_hydro_subgr_catalytic. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Gene3D	G3DSA:2.60.40.710. CBD_3. 2 hits. G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.
Pfam	PF00942. CBM_3. 2 hits. PF02018. CBM_4_9. 1 hit. PF00331. Glyco_hydro_10. 1 hit. [Graphical view]
PRINTS	PR00134. GLHYDRLASE10.
SMART	SM01067. CBM_3. 2 hits. SM00633. Glyco_10. 1 hit. [Graphical view]
SUPFAM	SSF49384. Cellul_bind. 2 hits. SSF49785. Gal_bind_like. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS51172. CBM3. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q9L8L8_9BACL

Accession

Primary (citable) accession number: Q9L8L8

Entry history

Integrated into UniProtKB/TrEMBL:	October 1, 2000
Last sequence update:	October 1, 2000
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)