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Protein
Submitted name:

ColH protein

Gene

colH

Organism
Clostridium histolyticum
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi421 – 4211ZincCombined sources
Metal bindingi430 – 4301Calcium 1Combined sources
Metal bindingi455 – 4551Zinc; via tele nitrogenCombined sources
Metal bindingi459 – 4591Zinc; via tele nitrogenCombined sources
Metal bindingi463 – 4631Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi467 – 4671Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi469 – 4691Calcium 1; via carbonyl oxygenCombined sources
Metal bindingi487 – 4871ZincCombined sources
Metal bindingi814 – 8141Calcium 2Combined sources
Metal bindingi815 – 8151Calcium 2; via carbonyl oxygenCombined sources
Metal bindingi842 – 8421Calcium 2Combined sources
Metal bindingi844 – 8441Calcium 2Combined sources
Metal bindingi884 – 8841Calcium 2Combined sources
Metal bindingi908 – 9081Calcium 3
Metal bindingi910 – 9101Calcium 3
Metal bindingi910 – 9101Calcium 4
Metal bindingi912 – 9121Calcium 4
Metal bindingi913 – 9131Calcium 4
Metal bindingi931 – 9311Calcium 3; via carbonyl oxygen
Metal bindingi937 – 9371Calcium 3
Metal bindingi937 – 9371Calcium 4
Metal bindingi938 – 9381Calcium 4; via carbonyl oxygen
Metal bindingi939 – 9391Calcium 3
Metal bindingi939 – 9391Calcium 4

GO - Molecular functioni

  1. serine-type endopeptidase activity Source: InterPro
  2. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources, ZincCombined sources

Protein family/group databases

MEROPSiM09.003.

Names & Taxonomyi

Protein namesi
Submitted name:
ColH proteinImported
Submitted name:
CollagenaseImported
Gene namesi
Name:colHImported
OrganismiClostridium histolyticumImported
Taxonomic identifieri1498 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Subcellular locationi

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. extracellular region Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4040 PotentialImportedAdd
BLAST
Chaini41 – 1021981collagenaseImportedPRO_5000139769Add
BLAST

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JQWX-ray2.00A/B/C902-1021[»]
3JQXX-ray2.20A/B/C902-1021[»]
4AR1X-ray2.01A331-721[»]
4ARFX-ray1.77A331-721[»]
4JGUX-ray1.42A/B806-900[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ46085.

Family & Domainsi

Keywords - Domaini

CollagenImported, SignalImported

Family and domain databases

Gene3Di2.60.40.670. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR007280. Peptidase_C_arc/bac.
IPR013661. Peptidase_M9_N_dom.
IPR002169. Peptidase_M9A/M9B.
IPR022409. PKD/Chitinase_dom.
IPR000601. PKD_dom.
[Graphical view]
PfamiPF01752. Peptidase_M9. 1 hit.
PF08453. Peptidase_M9_N. 1 hit.
PF00801. PKD. 2 hits.
PF04151. PPC. 1 hit.
[Graphical view]
PRINTSiPR00931. MICOLLPTASE.
SMARTiSM00089. PKD. 2 hits.
[Graphical view]
SUPFAMiSSF49299. SSF49299. 2 hits.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50093. PKD. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q46085-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRKCLSKRL MLAITMATIF TVNSTLPIYA AVDKNNATAA VQNESKRYTV
60 70 80 90 100
SYLKTLNYYD LVDLLVKTEI ENLPDLFQYS SDAKEFYGNK TRMSFIMDEI
110 120 130 140 150
GRRAPQYTEI DHKGIPTLVE VVRAGFYLGF HNKELNEINK RSFKERVIPS
160 170 180 190 200
ILAIQKNPNF KLGTEVQDKI VSATGLLAGN ETAPPEVVNN FTPILQDCIK
210 220 230 240 250
NIDRYALDDL KSKALFNVLA APTYDITEYL RATKEKPENT PWYGKIDGFI
260 270 280 290 300
NELKKLALYG KINDNNSWII DNGIYHIAPL GKLHSNNKIG IETLTEVMKV
310 320 330 340 350
YPYLSMQHLQ SADQIKRHYD SKDAEGNKIP LDKFKKEGKE KYCPKTYTFD
360 370 380 390 400
DGKVIIKAGA RVEEEKVKRL YWASKEVNSQ FFRVYGIDKP LEEGNPDDIL
410 420 430 440 450
TMVIYNSPEE YKLNSVLYGY DTNNGGMYIE PEGTFFTYER EAQESTYTLE
460 470 480 490 500
ELFRHEYTHY LQGRYAVPGQ WGRTKLYDND RLTWYEEGGA ELFAGSTRTS
510 520 530 540 550
GILPRKSIVS NIHNTTRNNR YKLSDTVHSK YGASFEFYNY ACMFMDYMYN
560 570 580 590 600
KDMGILNKLN DLAKNNDVDG YDNYIRDLSS NYALNDKYQD HMQERIDNYE
610 620 630 640 650
NLTVPFVADD YLVRHAYKNP NEIYSEISEV AKLKDAKSEV KKSQYFSTFT
660 670 680 690 700
LRGSYTGGAS KGKLEDQKAM NKFIDDSLKK LDTYSWSGYK TLTAYFTNYK
710 720 730 740 750
VDSSNRVTYD VVFHGYLPNE GDSKNSLPYG KINGTYKGTE KEKIKFSSEG
760 770 780 790 800
SFDPDGKIVS YEWDFGDGNK SNEENPEHSY DKVGTYTVKL KVTDDKGESS
810 820 830 840 850
VSTTTAEIKD LSENKLPVIY MHVPKSGALN QKVVFYGKGT YDPDGSIAGY
860 870 880 890 900
QWDFGDGSDF SSEQNPSHVY TKKGEYTVTL RVMDSSGQMS EKTMKIKITD
910 920 930 940 950
PVYPIGTEKE PNNSKETASG PIVPGIPVSG TIENTSDQDY FYFDVITPGE
960 970 980 990 1000
VKIDINKLGY GGATWVVYDE NNNAVSYATD DGQNLSGKFK ADKPGRYYIH
1010 1020
LYMFNGSYMP YRINIEGSVG R
Length:1,021
Mass (Da):116,377
Last modified:November 1, 1996 - v1
Checksum:i826F45EFD96F917C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29981 Genomic DNA. Translation: BAA06251.1.
AB014075 Genomic DNA. Translation: BAA34542.1.
PIRiI40805.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D29981 Genomic DNA. Translation: BAA06251.1.
AB014075 Genomic DNA. Translation: BAA34542.1.
PIRiI40805.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JQWX-ray2.00A/B/C902-1021[»]
3JQXX-ray2.20A/B/C902-1021[»]
4AR1X-ray2.01A331-721[»]
4ARFX-ray1.77A331-721[»]
4JGUX-ray1.42A/B806-900[»]
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM09.003.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ46085.

Family and domain databases

Gene3Di2.60.40.670. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR007280. Peptidase_C_arc/bac.
IPR013661. Peptidase_M9_N_dom.
IPR002169. Peptidase_M9A/M9B.
IPR022409. PKD/Chitinase_dom.
IPR000601. PKD_dom.
[Graphical view]
PfamiPF01752. Peptidase_M9. 1 hit.
PF08453. Peptidase_M9_N. 1 hit.
PF00801. PKD. 2 hits.
PF04151. PPC. 1 hit.
[Graphical view]
PRINTSiPR00931. MICOLLPTASE.
SMARTiSM00089. PKD. 2 hits.
[Graphical view]
SUPFAMiSSF49299. SSF49299. 2 hits.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50093. PKD. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning and nucleotide sequence analysis of the colH gene from Clostridium histolyticum encoding a collagenase and a gelatinase."
    Yoshihara K., Matsushita O., Minami J., Okabe A.
    J. Bacteriol. 176:6489-6496(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: JCM 1403Imported.
  2. "Gene duplication and multiplicity of collagenases in Clostridium histolyticum."
    Matsushita O., Jung C.-M., Katayama S., Minami J., Takahashi Y., Okabe A.
    J. Bacteriol. 181:923-933(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: JCM 1403Imported.
  3. "Structural comparison of ColH and ColG collagen-binding domains from Clostridium histolyticum."
    Bauer R., Wilson J.J., Philominathan S.T., Davis D., Matsushita O., Sakon J.
    J. Bacteriol. 195:318-327(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 902-1021 IN COMPLEX WITH CALCIUM.
  4. "Structural basis for activity regulation and substrate preference of clostridial collagenases G, H, and T."
    Eckhard U., Schonauer E., Brandstetter H.
    J. Biol. Chem. 288:20184-20194(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 331-721 IN COMPLEX WITH CALCIUM AND ZINC.
  5. "Crystal structure of Clostridium histolyticum colH collagenase polycystic kidney disease-like domain 2b at 1.4 Angstrom resolution in presence of calcium."
    Bauer R., Matsushita O., Sakon J.
    Submitted (MAR-2013) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 806-900 IN COMPLEX WITH CALCIUM.

Entry informationi

Entry nameiQ46085_CLOHI
AccessioniPrimary (citable) accession number: Q46085
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: March 4, 2015
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

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 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.