Fervidolysin - Fervidobacterium pennivorans

Preferred order of sections

Names and origin

Protein names

Submitted name:
Fervidolysin EMBL AAK61552.1

Gene names

Name:

fls EMBL AAK61552.1

Organism

Fervidobacterium pennivorans EMBL AAK61552.1

Taxonomic identifier

93466 [NCBI]

Taxonomic lineage

Bacteria › Thermotogae › Thermotogales › Thermotogaceae › Fervidobacterium

Protein attributes

Sequence length	699 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the peptidase S8 family. RuleBase RU003355

Ontologies

Keywords
Ligand	Calcium PDB 1R6V Metal-binding PDB 1R6V
Molecular function	Hydrolase Protease Serine protease RuleBase RU004261
Technical term	3D-structure PDB 1R6V
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

157

1

Calcium PDB 1R6V

Metal binding

199

1

Calcium PDB 1R6V

Metal binding

239

1

Calcium; via carbonyl oxygen PDB 1R6V

Metal binding

241

1

Calcium PDB 1R6V

Metal binding

243

1

Calcium; via carbonyl oxygen PDB 1R6V

Metal binding

245

1

Calcium; via carbonyl oxygen PDB 1R6V

Sequences

Sequence

Length

Mass (Da)

Tools

Q93LQ6 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: A3843EDDC3F1A4DA
Show »

FASTA

699

75,057

        10         20         30         40         50         60 
MRKVLLIASI VALILALFSC ANPSFEPRSK AKDLASLPEI KSQGYHILFG ELRDGEYTEG 

        70         80         90        100        110        120 
KILVGYNDRS EVDKIVKAVN GKVVLELPQI KVVSIKLNGM TVKQAYDKIK ALALKGIRYV 

       130        140        150        160        170        180 
EPSYKRELIK PTVVKPNPDM YKIRKPGLNS TARDYGEELS NELWGLEAIG VTQQLWEEAS 

       190        200        210        220        230        240 
GTNIIVAVVD TGVDGTHPDL EGQVIAGYRP AFDEELPAGT DSSYGGSHGT HVAGTIAAKK 

       250        260        270        280        290        300 
DGKGIVGVAP GAKIMPIVIF DDPALVGGNG YVGDDYVAAG IIWATDHGAK VMNHSWGGWG 

       310        320        330        340        350        360 
YSYTMKEAFD YAMEHGVVMV VSAGNNTSDS HHQYPAGYPG VIQVAALDYY GGTFRVAGFS 

       370        380        390        400        410        420 
SRSDGVSVGA PGVTILSTVP GEDSIGYEGH NENVPATNGG TYDYYQGTSM AAPHVTGVVA 

       430        440        450        460        470        480 
VLLQKFPNAK PWQIRKLLEN TAFDFNGNGW DHDTGYGLVK LDAALQGPLP TQGGVEEFQV 

       490        500        510        520        530        540 
VVTDAKGNFG VPTVFVSMMR DNGSCYYAKT GPDGIARFPH IDSGTYDIFV GGPDHWDRAL 

       550        560        570        580        590        600 
APYDGESIPG GYAIALRMAE ERQASFVGFG VSPDATQLNV NFNSTLQVKF STNLSTLKDP 

       610        620        630        640        650        660 
QFVVVDPLLR GVYGRVAYAR NQTYDLSLLS GQISFGIQTL LPAATDITIQ GTVTLNGEDI 

       670        680        690 
PVYGVLKAGT TWTIIDDFGG LNLGTDSQPI YVWWTIFGQ

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References

[1]	"Molecular characterization of fervidolysin, a subtilisin-like serine protease from the thermophilic bacterium Fervidobacterium pennivorans." Kluskens L.D., Voorhorst W.G., Siezen R.J., Schwerdtfeger R.M., Antranikian G., van der Oost J., de Vos W.M. Extremophiles 6:185-194(2002) [PubMed: 12072953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[2]	"Crystal structure of fervidolysin from Fervidobacterium pennivorans, a keratinolytic enzyme related to subtilisin." Kim J.S., Kluskens L.D., de Vos W.M., Huber R., van der Oost J. J. Mol. Biol. 335:787-797(2004) [PubMed: 14687574] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 29-699 IN COMPLEX WITH CALCIUM.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY035311 Genomic DNA. Translation: AAK61552.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1R6V	X-ray	1.70	A	29-699	[»]

ProteinModelPortal

Q93LQ6.

SMR

Q93LQ6. Positions 29-699.

ModBase

Search...

Protein family/group databases

MEROPS

S08.021.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR000209. Peptidase_S8/S53.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR017306. Peptidase_S8A_fervidolysin.
[Graphical view]

Gene3D

G3DSA:3.40.50.200. Pept_S8_S53. 1 hit.

PANTHER

PTHR10795. SubtilSerProt. 1 hit.

Pfam

PF00082. Peptidase_S8. 1 hit.
[Graphical view]

PIRSF

PIRSF037882. Subtilisin_rel_fervidolysin. 1 hit.

PRINTS

PR00723. SUBTILISIN.

SUPFAM

SSF52743. Pept_S8_S53. 1 hit.

PROSITE

PS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

Q93LQ6_FERPE

Accession

Primary (citable) accession number: Q93LQ6

Entry history

Integrated into UniProtKB/TrEMBL:	December 1, 2001
Last sequence update:	December 1, 2001
Last modified:	November 16, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)