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Protein
Submitted name:

S-layer associated multidomain endoglucanase

Gene

celA

Organism
Caldanaerobius polysaccharolyticus
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi621 – 6211Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi623 – 6231Calcium 1Combined sources
Metal bindingi645 – 6451Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi648 – 6481Calcium 1; via carbonyl oxygenCombined sources
Binding sitei689 – 6891Beta-D-mannoseCombined sources
Binding sitei693 – 6931Beta-D-mannoseCombined sources
Binding sitei705 – 7051Beta-D-mannoseCombined sources
Binding sitei709 – 7091Beta-D-mannoseCombined sources
Binding sitei709 – 7091GlucoseCombined sources
Binding sitei709 – 7091MannoseCombined sources
Binding sitei733 – 7331Beta-D-mannoseCombined sources
Binding sitei737 – 7371Beta-D-mannoseCombined sources
Metal bindingi749 – 7491Calcium 1Combined sources
Metal bindingi764 – 7641Calcium 2; via carbonyl oxygenCombined sources
Metal bindingi766 – 7661Calcium 2Combined sources
Metal bindingi788 – 7881Calcium 2; via carbonyl oxygenCombined sources
Metal bindingi791 – 7911Calcium 2; via carbonyl oxygenCombined sources
Metal bindingi892 – 8921Calcium 2Combined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources

Protein family/group databases

CAZyiCBM16. Carbohydrate-Binding Module Family 16.
GH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Submitted name:
S-layer associated multidomain endoglucanaseImported
Gene namesi
Name:celAImported
OrganismiCaldanaerobius polysaccharolyticusImported
Taxonomic identifieri44256 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteraceaeCaldanaerobius

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence analysisAdd
BLAST
Chaini33 – 10971065Sequence analysisPRO_5004337352Add
BLAST

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZEWX-ray1.40A/B614-756[»]
2ZEXX-ray1.20A/B614-756[»]
2ZEYX-ray2.20A/B614-756[»]
2ZEZX-ray1.90A/B/C/D756-899[»]
3OEAX-ray1.35A/B614-756[»]
3OEBX-ray1.55A614-756[»]
ProteinModelPortaliQ9ZA17.
SMRiQ9ZA17. Positions 614-898.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZA17.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini908 – 97164SLH (S-layer homology)InterPro annotationAdd
BLAST
Domaini972 – 103160SLH (S-layer homology)InterPro annotationAdd
BLAST
Domaini1038 – 109760SLH (S-layer homology)InterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni632 – 6332Beta-D-mannose bindingCombined sources

Keywords - Domaini

SignalSequence analysis

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR001119. SLH_dom.
[Graphical view]
PfamiPF02018. CBM_4_9. 2 hits.
PF00150. Cellulase. 1 hit.
PF00395. SLH. 3 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51272. SLH. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ZA17-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKVLSKLMV FVMVLTVALG NGVFIGDKQA KAAGTSGDGR FHVVGNKIVD
60 70 80 90 100
PDGNDFVIKG VNIQGYRSWE KRSVLQDVHL IADVWKFNTV RLNCFIGQNN
110 120 130 140 150
WGEGTGANND IDAIIKAFTA KKVVVEIDLH DTTGYPPLSN PPPAPGQPSL
160 170 180 190 200
DQAIAWFKEL AAKYKDNPYV WFNTMNEPGS STAPLDPQWK VANEEIIKAI
210 220 230 240 250
RSTGADNIIV VDGWSYANEG IEQNTPTVDE KRSAVLTYGQ DLLNADSAKN
260 270 280 290 300
TIFAFHNYNE GDIQKKVEDY IDRANAKGLY VFMEEYGKDY SDAAKEGVKS
310 320 330 340 350
GLQAVMNKGA GRIYWNWDGY DLYDLTSGTG RGSGWEINKT DGSKPTNLSW
360 370 380 390 400
VGDKIWDDNH GITPTFDDQN PKVDLALERL IANNNGFKAG DKVQFTTFLR
410 420 430 440 450
NSGDLPIGKD SKVVVKFYVD GVQLGDPVEI SGGIAVGQRI PVTSPELTVS
460 470 480 490 500
KTDFTVKAVI DSSSTYADGA EDAVIENNWI EAAFNSTAPS SGYELVVTGI
510 520 530 540 550
KITPDTVKER DYVQAQVTVA NQGPEATPVT NIIGWFYVNG YYYTLDDAAK
560 570 580 590 600
SCAEQDNVTL KPGESITLST KVKYRAAAPC NFSFVLENLY ADDQNQSNNS
610 620 630 640 650
ITVNVPVKMG EGGVNMVSNP GFEDGLDSWQ DWQQDMSAVP EAAHNGALGL
660 670 680 690 700
KIGGGKAAGG GQDIPLKPNT TYILGAWAKF DSKPAGTFDV VVQYHLKDAN
710 720 730 740 750
NTYVQHILNF NETDWTYKQL LFTTPDVFGS TPQLALWKGD TSKANLYVDD
760 770 780 790 800
VYLVEVSNLI VNGTAENGMD GWPDWGYPVS AVPEAAYGGT KGFKLSGGKQ
810 820 830 840 850
AGMGQKVALK PNTTYILGAW GKFTAKPGTY CDVIVQYHLK DANNTYVQNI
860 870 880 890 900
LRFTETDWTY KQVVFTTPDA FGSDPEFVLW KDDASNADFY ADNITLVEVP
910 920 930 940 950
SSMVNKGSIA PKFTDISSSW AKNEIQVLAS KNIISGYPDG TFKPDKRITR
960 970 980 990 1000
AEFVSMLVKA LGIKQSIPDV PTFSDVNKGD WYYGLVEAAK STGIASGYGK
1010 1020 1030 1040 1050
QFKPDMQITR QEMMVMVVNA LRVNKVEKFV SKGDVSVLGK FKDGGKVQNW
1060 1070 1080 1090
AKDAMAIGVS NGLIKGTGDE YLSPDGRATR AQAAAVIYRM LLQLGRI
Length:1,097
Mass (Da):119,763
Last modified:May 1, 1999 - v1
Checksum:iC41C6EB92C0494B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82255 Genomic DNA. Translation: AAD09354.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82255 Genomic DNA. Translation: AAD09354.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZEWX-ray1.40A/B614-756[»]
2ZEXX-ray1.20A/B614-756[»]
2ZEYX-ray2.20A/B614-756[»]
2ZEZX-ray1.90A/B/C/D756-899[»]
3OEAX-ray1.35A/B614-756[»]
3OEBX-ray1.55A614-756[»]
ProteinModelPortaliQ9ZA17.
SMRiQ9ZA17. Positions 614-898.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM16. Carbohydrate-Binding Module Family 16.
GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ZA17.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR001119. SLH_dom.
[Graphical view]
PfamiPF02018. CBM_4_9. 2 hits.
PF00150. Cellulase. 1 hit.
PF00395. SLH. 3 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51272. SLH. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQ9ZA17_9THEO
AccessioniPrimary (citable) accession number: Q9ZA17
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.