Unreviewed, UniProtKB/TrEMBL P96988 (P96988_RHOMR)

Names and origin

Protein names	Submitted name:     Xylanase EMBL CAA60868.2
Organism	Rhodothermus marinus (Rhodothermus obamensis) EMBL CAA60868.2
Taxonomic identifier	29549 [NCBI]
Taxonomic lineage	Bacteria › Bacteroidetes › Sphingobacteria › Sphingobacteriales › Rhodothermaceae › Rhodothermus

Protein attributes

Sequence length	412 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

Ontologies

Keywords
Biological process	Xylan degradation EMBL CAA60868.2
Gene Ontology (GO)
Biological process	xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	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
Experimental info
	Non-terminal residue	1	1	EMBL CAA60868.2

Sequences

	Sequence		Length	Mass (Da)
	P96988-1 [UniParc]. Last modified June 1, 2003. Version 2. Checksum: EBA74A6812B43625	FASTA	412	46,982
	10 20 30 40 50 60 AADVDKFLGN IYSPSQVENF EYYWNCVTPE NAGKWGSVEG TRDQMNWSSL DAAYALARDN 70 80 90 100 110 120 GFCFNFHVLL WGAQQPAWIS ELSPEEQLEE IQEWFQAVAE RYSFTASPFD VVQVVNEPLH 130 140 150 160 170 180 QPPDGQEGRA NYIEALGGAG ETGWDWVITA FELARQIFPE GTRLMINDYG ILSSLETAQQ 190 200 210 220 230 240 YLELIQLLKE RNLIDVIGVQ GHAFSTRSGA PIQEVLDLLA TTGLPIQVTE MDIDGNPNQS 250 260 270 280 290 300 PFVTREQSEQ NQLRDMQRIF PTVWYHPAVE GVTFWGWRPG LWRNDYEAYL VYSNGAERPA 310 320 330 340 350 360 MVWLREFMEA YRESYLSANE PEGTLPEELS VVSWPNPSRG QVRFRYALPF EAEVRLQVFD 370 380 390 400 410 VLGREVMTLA SGRHRAGVYE VAFDGRHLPS GLYLYRLEAN GRVRSGRLVL MR

References

[1]	Nordberg Karlsson E.M. Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: DSM 4252 EMBL CAA60868.2.
[2]	"The solution structure of the CBM4-2 carbohydrate binding module from a thermostable Rhodothermus marinus xylanase." Simpson P.J., Jamieson S.J., Abou-Hachem M., Karlsson E.N., Gilbert H.J., Holst O., Williamson M.P. Biochemistry 41:5712-5719(2002) [PubMed: 11980475] [Abstract] Cited for: STRUCTURE BY NMR OF 410-412.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X87417 Genomic DNA. Translation: CAA60868.2.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K42	NMR	-	A	270-272	[»]
1K45	NMR	-	A	270-272	[»]

ModBase

Search...

Protein family/group databases

CAZy

CBM4. Carbohydrate-Binding Module Family 4.
GH10. Glycoside Hydrolase Family 10.

Family and domain databases

InterPro

IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_sg_catalytic.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

Pfam

PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]

SMART

SM00633. Glyco_10. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

P96988_RHOMR

Accession

Primary (citable) accession number: P96988

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 1997
Last sequence update:	June 1, 2003
Last modified:	June 16, 2009
This is version 41 of the entry and version 2 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)