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Q28811

- PHR_POTTR

UniProt

Q28811 - PHR_POTTR

Protein

Deoxyribodipyrimidine photo-lyase

Gene

PHR

Organism
Potorous tridactylus (Potoroo)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation.

    Catalytic activityi

    Cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA).

    Cofactori

    FAD.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei322 – 3221DNABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi468 – 4703FADBy similarity

    GO - Molecular functioni

    1. deoxyribodipyrimidine photo-lyase activity Source: UniProtKB-EC
    2. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. DNA repair Source: UniProtKB-KW
    2. protein-chromophore linkage Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    Chromophore, DNA-binding, FAD, Flavoprotein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxyribodipyrimidine photo-lyase (EC:4.1.99.3)
    Alternative name(s):
    DNA photolyase
    Photoreactivating enzyme
    Gene namesi
    Name:PHR
    OrganismiPotorous tridactylus (Potoroo)
    Taxonomic identifieri9310 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaMetatheriaDiprotodontiaPotoroidaePotorous

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 532532Deoxyribodipyrimidine photo-lyasePRO_0000085120Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliQ28811.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini97 – 229133Photolyase/cryptochrome alpha/betaAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni368 – 3769Interaction with DNABy similarity
    Regioni442 – 4432Interaction with DNABy similarity

    Sequence similaritiesi

    Belongs to the DNA photolyase class-2 family.Curated

    Phylogenomic databases

    HOVERGENiHBG008186.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    InterProiIPR008148. DNA_photolyase_2.
    IPR006050. DNA_photolyase_N.
    IPR005101. Photolyase_FAD-bd/Cryptochr_C.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR10211. PTHR10211. 1 hit.
    PfamiPF00875. DNA_photolyase. 1 hit.
    PF03441. FAD_binding_7. 1 hit.
    [Graphical view]
    SUPFAMiSSF48173. SSF48173. 1 hit.
    SSF52425. SSF52425. 1 hit.
    TIGRFAMsiTIGR00591. phr2. 1 hit.
    PROSITEiPS01083. DNA_PHOTOLYASES_2_1. 1 hit.
    PS01084. DNA_PHOTOLYASES_2_2. 1 hit.
    PS51645. PHR_CRY_ALPHA_BETA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q28811-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDSKKRSHST GGEAENMESQ ESKAKRKPLQ KHQFSKSNVV QKEEKDKTEG    50
    EEKGAEGLQE VVRQSRLRTA PSVLEFRFNK QRVRLISQDC HLQDQSQAFV 100
    YWMSRDQRVQ DNWAFLYAQR LALKQKLPLH VCFCLAPCFL GATIRHYDFM 150
    LRGLEEVAEE CEKLCIPFHL LLGLPKDVLP AFVQTHGIGG IVTDFSPLLH 200
    HTQWVKDVQD ALPRQVPFVQ VDAHNIVPCW VASDKQEYGA RTIRHKIHDR 250
    LPHFLTEFPP VICHPYTSNV QAEPVDWNGC RAGLQVDRSV KEVSWAKPGT 300
    ASGLTMLQSF IAERLPYFGS DRNNPNKDAL SNLSPWFHFG QVSVQRAILE 350
    VQKHRSRYPD SVTNFVEEAV VRRELADNFC FYNKNYDKLE GAYDWAQTTL 400
    RLHAKDKRPH LYSLEQLESG KTHDPLWNAA QMQTVKEGKM HGFLRMYWAK 450
    KILEWTRSPE EALEFAIYLN DRFQLDGWDP NGYVGCMWSI CGIHDQGWAE 500
    REIFGKIRYM NYAGCKRKFD VAEFERKISP AD 532
    Length:532
    Mass (Da):61,631
    Last modified:November 1, 1996 - v1
    Checksum:i0865B1BFDE7BB25B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26020 mRNA. Translation: BAA05041.1.
    PIRiS52046.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26020 mRNA. Translation: BAA05041.1 .
    PIRi S52046.

    3D structure databases

    ProteinModelPortali Q28811.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG008186.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    InterProi IPR008148. DNA_photolyase_2.
    IPR006050. DNA_photolyase_N.
    IPR005101. Photolyase_FAD-bd/Cryptochr_C.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    PANTHERi PTHR10211. PTHR10211. 1 hit.
    Pfami PF00875. DNA_photolyase. 1 hit.
    PF03441. FAD_binding_7. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48173. SSF48173. 1 hit.
    SSF52425. SSF52425. 1 hit.
    TIGRFAMsi TIGR00591. phr2. 1 hit.
    PROSITEi PS01083. DNA_PHOTOLYASES_2_1. 1 hit.
    PS01084. DNA_PHOTOLYASES_2_2. 1 hit.
    PS51645. PHR_CRY_ALPHA_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A new class of DNA photolyases present in various organisms including aplacental mammals."
      Yasui A., Eker A.P., Yasuhira S., Yajima H., Kobayashi T., Takao M., Oikawa A.
      EMBO J. 13:6143-6151(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiPHR_POTTR
    AccessioniPrimary (citable) accession number: Q28811
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3