P43870 (T2D3_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Type-2 restriction enzyme HindIII
Short name=R.HindIII
EC=3.1.21.4

Alternative name(s):
Endonuclease HindIII
Type II restriction enzyme HindIII

Gene names

Name:	hindIIIR
Ordered Locus Names:	HI_1393

Organism

Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]

Taxonomic identifier

71421 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › Haemophilus influenzae

Protein attributes

Sequence length	300 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Recognizes the double-stranded sequence AAGCTT and cleaves after A-1.
Catalytic activity	Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.

Ontologies

Keywords
Biological process	Restriction system
Molecular function	Endonuclease Hydrolase Nuclease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA restriction-modification system Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Molecular_function	Type II site-specific deoxyribonuclease activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 300

300

Type-2 restriction enzyme HindIII

PRO_0000077321

Secondary structure

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300

Helix Strand Turn

Details...

Helix

5 – 15

11

Turn

16 – 18

3

Helix

21 – 33

13

Helix

37 – 47

11

Helix

59 – 78

20

Beta strand

81 – 85

5

Beta strand

94 – 103

10

Beta strand

105 – 110

6

Helix

122 – 125

4

Helix

127 – 133

7

Turn

134 – 136

3

Beta strand

137 – 144

8

Helix

146 – 148

3

Beta strand

151 – 153

3

Helix

155 – 163

9

Beta strand

165 – 169

5

Helix

170 – 178

9

Helix

190 – 193

4

Helix

195 – 200

6

Helix

205 – 207

3

Helix

213 – 224

12

Helix

228 – 261

34

Helix

265 – 275

11

Helix

278 – 293

16

Helix

295 – 298

4

Sequences

	Sequence		Length	Mass (Da)
	P43870 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 62F62AC4B18E841B	FASTA	300	34,952
	10 20 30 40 50 60 MKKSALEKLL SLIENLTNQE FKQATNSLIS FIYKLNRNEV IELVRSIGIL PEAIKPSSTQ 70 80 90 100 110 120 EKLFSKAGDI VLAKAFQLLN LNSKPLEQRG NAGDVIALSK EFNYGLVADA KSFRLSRTAK 130 140 150 160 170 180 NQKDFKVKAL SEWREDKDYA VLTAPFFQYP TTKSQIFKQS LDENVLLFSW EHLAILLQLD 190 200 210 220 230 240 LEETNIFSFE QLWNFPKKQS KKTSVSDAEN NFMRDFNKYF MDLFKIDKDT LNQLLQKEIN 250 260 270 280 290 300 FIEERSLIEK EYWKKQINII KNFTREEAIE ALLKDINMSS KIETIDSFIK GIKSNDRLYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, analysis and expression of the HindIII R-M-encoding genes." Nwankwo D.O., Moran L.S., Slatko B.E., Waite-Rees P.A., Dorner L.F., Benner J.S., Wilson G.G. Gene 150:75-80(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]	"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L15391 Genomic DNA. Translation: AAA61958.1.
L42023 Genomic DNA. Translation: AAC23040.1.

PIR

H64121.

RefSeq

NP_439547.1. NC_000907.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E52	X-ray	2.00	A/B/C/D	1-300	[»]
3A4K	X-ray	2.17	A/B/C/D	1-300	[»]

ProteinModelPortal

P43870.

SMR

P43870. Positions 2-300.

ModBase

Search...

Protein-protein interaction databases

STRING

71421.HI1393.

Protein family/group databases

REBASE

1151. HindIII.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC23040; AAC23040; HI_1393.

GeneID

950303.

KEGG

hin:HI1393.

PATRIC

20191483. VBIHaeInf48452_1452.

Phylogenomic databases

eggNOG

NOG45031.

KO

K01155.

OMA

LEETNIF.

ProtClustDB

CLSK216771.

Family and domain databases

InterPro

IPR019043. Restrct_endonuc_II_HindIII.
[Graphical view]

Pfam

PF09518. RE_HindIII. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P43870.

ChEMBL

CHEMBL5004.

EvolutionaryTrace

P43870.

Entry information

Entry name

T2D3_HAEIN

Accession

Primary (citable) accession number: P43870

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program