Q46085 (Q46085_CLOHI) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
ColH protein EMBL BAA34542.1

Submitted name:
Collagenase EMBL BAA06251.1

Gene names

Name:

colH EMBL BAA06251.1

Organism

Clostridium histolyticum EMBL BAA06251.1

Taxonomic identifier

1498 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	1021 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

Ontologies

Keywords
Domain	Collagen EMBL BAA06251.1 Signal EMBL BAA06251.1
Technical term	3D-structure PDB 3JQX PDB 3JQW
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular_component	collagen Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding 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 – 40	40	Potential EMBL BAA06251.1
	Chain	41 – 1021	981	collagenase EMBL BAA06251.1		PRO_5000139769

Sequences

	Sequence		Length	Mass (Da)
	Q46085 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 826F45EFD96F917C	FASTA	1,021	116,377
	10 20 30 40 50 60 MKRKCLSKRL MLAITMATIF TVNSTLPIYA AVDKNNATAA VQNESKRYTV SYLKTLNYYD 70 80 90 100 110 120 LVDLLVKTEI ENLPDLFQYS SDAKEFYGNK TRMSFIMDEI GRRAPQYTEI DHKGIPTLVE 130 140 150 160 170 180 VVRAGFYLGF HNKELNEINK RSFKERVIPS ILAIQKNPNF KLGTEVQDKI VSATGLLAGN 190 200 210 220 230 240 ETAPPEVVNN FTPILQDCIK NIDRYALDDL KSKALFNVLA APTYDITEYL RATKEKPENT 250 260 270 280 290 300 PWYGKIDGFI NELKKLALYG KINDNNSWII DNGIYHIAPL GKLHSNNKIG IETLTEVMKV 310 320 330 340 350 360 YPYLSMQHLQ SADQIKRHYD SKDAEGNKIP LDKFKKEGKE KYCPKTYTFD DGKVIIKAGA 370 380 390 400 410 420 RVEEEKVKRL YWASKEVNSQ FFRVYGIDKP LEEGNPDDIL TMVIYNSPEE YKLNSVLYGY 430 440 450 460 470 480 DTNNGGMYIE PEGTFFTYER EAQESTYTLE ELFRHEYTHY LQGRYAVPGQ WGRTKLYDND 490 500 510 520 530 540 RLTWYEEGGA ELFAGSTRTS GILPRKSIVS NIHNTTRNNR YKLSDTVHSK YGASFEFYNY 550 560 570 580 590 600 ACMFMDYMYN KDMGILNKLN DLAKNNDVDG YDNYIRDLSS NYALNDKYQD HMQERIDNYE 610 620 630 640 650 660 NLTVPFVADD YLVRHAYKNP NEIYSEISEV AKLKDAKSEV KKSQYFSTFT LRGSYTGGAS 670 680 690 700 710 720 KGKLEDQKAM NKFIDDSLKK LDTYSWSGYK TLTAYFTNYK VDSSNRVTYD VVFHGYLPNE 730 740 750 760 770 780 GDSKNSLPYG KINGTYKGTE KEKIKFSSEG SFDPDGKIVS YEWDFGDGNK SNEENPEHSY 790 800 810 820 830 840 DKVGTYTVKL KVTDDKGESS VSTTTAEIKD LSENKLPVIY MHVPKSGALN QKVVFYGKGT 850 860 870 880 890 900 YDPDGSIAGY QWDFGDGSDF SSEQNPSHVY TKKGEYTVTL RVMDSSGQMS EKTMKIKITD 910 920 930 940 950 960 PVYPIGTEKE PNNSKETASG PIVPGIPVSG TIENTSDQDY FYFDVITPGE VKIDINKLGY 970 980 990 1000 1010 1020 GGATWVVYDE NNNAVSYATD DGQNLSGKFK ADKPGRYYIH LYMFNGSYMP YRINIEGSVG R

References

[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 1403 EMBL BAA06251.1.
[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 1403 EMBL BAA34542.1.
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D29981 Genomic DNA. Translation: BAA06251.1.
AB014075 Genomic DNA. Translation: BAA34542.1.

PIR

I40805.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3JQW	X-ray	2.00	A/B/C	902-1021	[»]
3JQX	X-ray	2.20	A/B/C	902-1021	[»]

ModBase

Search...

Protein family/group databases

MEROPS

M09.003.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

2.60.40.670. 2 hits.

InterPro

IPR007280. Peptidase_C_arc/bac.
IPR013661. Peptidase_M9_N_dom.
IPR002169. Peptidase_M9A/M9B.
IPR022409. PKD/Chitinase_dom.
IPR000601. PKD_dom.
[Graphical view]

Pfam

PF01752. Peptidase_M9. 1 hit.
PF08453. Peptidase_M9_N. 1 hit.
PF00801. PKD. 2 hits.
PF04151. PPC. 1 hit.
[Graphical view]

PRINTS

PR00931. MICOLLPTASE.

SMART

SM00089. PKD. 2 hits.
[Graphical view]

SUPFAM

SSF49299. PKD. 2 hits.

PROSITE

PS50093. PKD. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q46085.

Entry information

Entry name

Q46085_CLOHI

Accession

Primary (citable) accession number: Q46085

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)