HRQ1/YDR291W Protein Information Help

Standard Name Hrq1p 1
Systematic Name Ydr291wp
ORF Classification Verified
Description 3'-5' DNA helicase that has DNA strand annealing activity; helicase activity is stimulated by fork structure and 3'-tail length of substrates; belongs to the widely conserved RecQ family of proteins which are involved in maintaining genomic integrity; similar to the human RecQ4p implicated in Rothmund-Thomson syndrome (RTS) (1, 2)
Name Description Homologous to RecQ protein 1
Experimental Data
Molecules/cell 259 3
Predicted Sequence Formatted Sequence or sequence in FASTA format
Length (a.a.) 1,077
Molecular Weight (Da) 123,548
Isoelectric Point (pI) 6.65

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Post-translational Modifications PhosphoGRID | PhosphoPep Database
Domains/motifs See the graphical view and list of proteins that share domains/motifs in common with Hrq1p (InterPro)
Physical Interactions There are 2 total physical interactions (BioGRID)
Homologs PDB Homologs | BLASTP | BLASTP v. fungi | Fungal Alignment | Synteny Viewer
External Sequence Databases EBI: UPI0000069D93 | Q05549
MIPS: YDR291W
NCBI: 1230655 | 398366425 | 74676365 | NP_010577.3
GenBank/EMBL/DDBJ: DAA12130.1 | U51031
External Classifications EC: 3.6.1.- [Hydrolases acting on acid anhydrides in phosphorous-containing anhydrides]
Amino Acid Sequence (or in FASTA format)
 
       1  MEEGPIKKKL KSAGQGSGKT DAFRNFEQFF FRLNTLYTFL ICRKHVVPTF
      51  KTLCGPIETA LKRTVTKEDL AMVMALMPRE CVFKYIDENQ IYTETKIFDF
     101  NNGGFQQKEN DIFELKDVDD QNQTQKSTQL LIFEFIDGTM QRSWSASDRF
     151  SQIKIPTYTT EEMKKMISKR EALFKSRLRE FILEKEKANL DPFSELTNLA
     201  QKYIPRERDY EDPIEAMMKA KQESNEMSIP NYSNNSVITT IPQMIEKLKS
     251  TEFYASQIKH CFTIPSRTAK YKGLCFELAP EVYQGMEHEN FYSHQADAIN
     301  SLHQGENVII TTSTSSGKSL IYQLAAIDLL LKDPESTFMY IFPTKALAQD
     351  QKRAFKVILS KIPELKNAVV DTYDGDTEPE ERAYIRKNAR VIFTNPDMIH
     401  TSILPNHANW RHFLYHLKLV VVDELHIYKG LFGSHVALVM RRLLRLCHCF
     451  YENSGLQFIS CSATLKSPVQ HMKDMFGINE VTLIHEDGSP TGAKHLVVWN
     501  PPILPQHERK RENFIRESAK ILVQLILNNV RTIAFCYVRR VCELLMKEVR
     551  NIFIETGRED LVTEVMSYRG GYSASDRRKI EREMFHGNLK AVISTNALEL
     601  GIDIGGLDAV LMCGFPLSMA NFHQQSGRAG RRNNDSLTLV VASDSPVDQH
     651  YVAHPESLLE VNNFESYQDL VLDFNNILIL EGHIQCAAFE LPINFERDKQ
     701  YFTESHLRKI CVERLHHNQD GYHASNRFLP WPSKCVSLRG GEEDQFAVVD
     751  ITNGRNIIIE EIEASRTSFT LYDGGIFIHQ GYPYLVKEFN PDERYAKVQR
     801  VDVDWVTNQR DFTDVDPQEI ELIRSLRNSD VPVYFGKIKT TIIVFGFFKV
     851  DKYKRIIDAI ETHNPPVIIN SKGLWIDMPK YALEICQKKQ LNVAGAIHGA
     901  QHAIMGMLPR FIVAGVDEIQ TECKAPEKEF AERQTKRKRP ARLIFYDSKG
     951  GKYGSGLCVK AFEHIDDIIE SSLRRIEECP CSDGCPDCVA ASFCKENSLV
    1001  LSKPGAQVVL HCILGHSEDS FIDLIKDGPE PNMPEIKVET VIPVSEHVNF
    1051  SDDFKIIDVR RATKDDTHTN EIIKKEI*

external links for Hrq1p
Homologs Interaction Resources Protein databases/Other Localization Resources
BLASTP (NCBI) BioGRID SCOP Superfamily YPL+
Ashbya (AGD) BOND GPMdb (Mass Spec.) YeastGFP
Aspergillus (AspGD) BioPIXIE MIPS YeastRC Public Image Repository
Candida (CGD) CYC2008 (complexes) Pfam domains
Candida (CandidaDB) Complexome YeastRC Structure Prediction (Seattle)
YGOB GeneMANIA

YOGY


References cited on this page View Complete Literature Guide for Hrq1p
1) Barea F, et al.  (2008) In silico analyses of a new group of fungal and plant RecQ4-homologous proteins. Comput Biol Chem 32(5):349-58
2) Kwon SH, et al.  (2012) Saccharomyces cerevisiae Hrq1 requires a long 3'-tailed DNA substrate for helicase activity. Biochem Biophys Res Commun 427(3):623-8
3) Ghaemmaghami S, et al.  (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41