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Protein

Vanadium chloroperoxidase

Gene

CPO

Organism
Curvularia inaequalis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

RH + Cl- + H2O2 = RCl + 2 H2O.

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei4041
Metal bindingi496Vanadium1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Ligandi

Chloride, Metal-binding, Vanadium

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15997.
BRENDAi1.11.1.B2. 1761.
SABIO-RKP49053.

Protein family/group databases

PeroxiBasei5892. CinaVCPo.

Names & Taxonomyi

Protein namesi
Recommended name:
Vanadium chloroperoxidase (EC:1.11.1.10)
Alternative name(s):
Vanadium chloride peroxidase
Short name:
VCPO
Gene namesi
Name:CPO
OrganismiCurvularia inaequalis
Taxonomic identifieri38902 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaeCurvularia

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000970551 – 609Vanadium chloroperoxidaseAdd BLAST609

Post-translational modificationi

The N-terminus is blocked.

Structurei

Secondary structure

1609
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 20Combined sources5
Helixi22 – 40Combined sources19
Helixi47 – 68Combined sources22
Beta strandi72 – 74Combined sources3
Beta strandi77 – 79Combined sources3
Helixi85 – 87Combined sources3
Helixi98 – 114Combined sources17
Turni118 – 125Combined sources8
Helixi131 – 147Combined sources17
Helixi157 – 173Combined sources17
Turni176 – 179Combined sources4
Beta strandi202 – 207Combined sources6
Beta strandi215 – 218Combined sources4
Helixi226 – 229Combined sources4
Helixi248 – 250Combined sources3
Helixi254 – 268Combined sources15
Helixi280 – 288Combined sources9
Turni295 – 297Combined sources3
Helixi300 – 314Combined sources15
Beta strandi317 – 319Combined sources3
Beta strandi321 – 323Combined sources3
Helixi325 – 356Combined sources32
Helixi361 – 366Combined sources6
Turni371 – 373Combined sources3
Beta strandi388 – 390Combined sources3
Helixi403 – 419Combined sources17
Turni420 – 422Combined sources3
Beta strandi436 – 440Combined sources5
Beta strandi444 – 447Combined sources4
Beta strandi449 – 453Combined sources5
Helixi461 – 463Combined sources3
Beta strandi466 – 468Combined sources3
Beta strandi473 – 477Combined sources5
Helixi479 – 492Combined sources14
Helixi498 – 501Combined sources4
Helixi504 – 507Combined sources4
Helixi530 – 532Combined sources3
Beta strandi538 – 541Combined sources4
Beta strandi542 – 544Combined sources3
Helixi552 – 565Combined sources14
Helixi573 – 575Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IDQX-ray2.03A1-609[»]
1IDUX-ray2.24A1-609[»]
1VNCX-ray2.10A1-609[»]
1VNEX-ray2.15A1-609[»]
1VNFX-ray2.35A1-609[»]
1VNGX-ray2.20A1-609[»]
1VNHX-ray2.11A1-609[»]
1VNIX-ray2.15A1-609[»]
1VNSX-ray1.66A1-609[»]
3BB0X-ray1.50A1-609[»]
ProteinModelPortaliP49053.
SMRiP49053.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49053.

Family & Domainsi

Phylogenomic databases

KOiK17990.

Family and domain databases

Gene3Di1.10.606.10. 1 hit.
1.20.144.10. 1 hit.
InterProiIPR016119. Br/Cl_peroxidase_C.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.

Sequencei

Sequence statusi: Complete.

P49053-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSVTPIPLP KIDEPEEYNT NYILFWNHVG LELNRVTHTV GGPLTGPPLS
60 70 80 90 100
ARALGMLHLA IHDAYFSICP PTDFTTFLSP DTENAAYRLP SPNGANDARQ
110 120 130 140 150
AVAGAALKML SSLYMKPVEQ PNPNPGANIS DNAYAQLGLV LDRSVLEAPG
160 170 180 190 200
GVDRESASFM FGEDVADVFF ALLNDPRGAS QEGYHPTPGR YKFDDEPTHP
210 220 230 240 250
VVLIPVDPNN PNGPKMPFRQ YHAPFYGKTT KRFATQSEHF LADPPGLRSN
260 270 280 290 300
ADETAEYDDA VRVAIAMGGA QALNSTKRSP WQTAQGLYWA YDGSNLIGTP
310 320 330 340 350
PRFYNQIVRR IAVTYKKEED LANSEVNNAD FARLFALVDV ACTDAGIFSW
360 370 380 390 400
KEKWEFEFWR PLSGVRDDGR PDHGDPFWLT LGAPATNTND IPFKPPFPAY
410 420 430 440 450
PSGHATFGGA VFQMVRRYYN GRVGTWKDDE PDNIAIDMMI SEELNGVNRD
460 470 480 490 500
LRQPYDPTAP IEDQPGIVRT RIVRHFDSAW ELMFENAISR IFLGVHWRFD
510 520 530 540 550
AAAARDILIP TTTKDVYAVD NNGATVFQNV EDIRYTTRGT REDPEGLFPI
560 570 580 590 600
GGVPLGIEIA DEIFNNGLKP TPPEIQPMPQ ETPVQKPVGQ QPVKGMWEEE

QAPVVKEAP
Length:609
Mass (Da):67,531
Last modified:February 1, 1996 - v1
Checksum:iA7B710DDF937D3E9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti454P → S AA sequence (PubMed:7744081).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85369 mRNA. Translation: CAA59686.1.
PIRiS69334.

Genome annotation databases

KEGGiag:CAA59686.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85369 mRNA. Translation: CAA59686.1.
PIRiS69334.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IDQX-ray2.03A1-609[»]
1IDUX-ray2.24A1-609[»]
1VNCX-ray2.10A1-609[»]
1VNEX-ray2.15A1-609[»]
1VNFX-ray2.35A1-609[»]
1VNGX-ray2.20A1-609[»]
1VNHX-ray2.11A1-609[»]
1VNIX-ray2.15A1-609[»]
1VNSX-ray1.66A1-609[»]
3BB0X-ray1.50A1-609[»]
ProteinModelPortaliP49053.
SMRiP49053.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei5892. CinaVCPo.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:CAA59686.

Phylogenomic databases

KOiK17990.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15997.
BRENDAi1.11.1.B2. 1761.
SABIO-RKP49053.

Miscellaneous databases

EvolutionaryTraceiP49053.

Family and domain databases

Gene3Di1.10.606.10. 1 hit.
1.20.144.10. 1 hit.
InterProiIPR016119. Br/Cl_peroxidase_C.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamiPF01569. PAP2. 1 hit.
[Graphical view]
SUPFAMiSSF48317. SSF48317. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPRXC_CURIN
AccessioniPrimary (citable) accession number: P49053
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 2, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.