HFM1/YGL251C Protein Information

Standard Name	Hfm1p
Systematic Name	Ygl251cp
Alias	Mer3p 1
ORF Classification	Verified
Description	Meiosis specific DNA helicase involved in the conversion of double-stranded breaks to later recombination intermediates and in crossover control; catalyzes the unwinding of Holliday junctions; has ssDNA and dsDNA stimulated ATPase activity (2, 3, 4, 5)
Name Description	Helicase Family Member

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	1,187
Molecular Weight (Da)	135,071
Isoelectric Point (pI)	7.59

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Hfm1p (InterPro)
Physical Interactions	There are 7 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0000052EDF \| P51979 MIPS: YGL251C NCBI: 114152816 \| 1150588 \| 1322927 \| 17377416 \| 780546 \| 9755332 \| NP_011263.2 \| NM_001181117.1 GenBank/EMBL/DDBJ: DAA07868.1 \| U22156 \| X94357 \| Z72773
External Classifications	EC: 3.6.1.- [Hydrolases acting on acid anhydrides in phosphorous-containing anhydrides] EC: 3.6.4.12 [DNA helicase]

Amino Acid Sequence (or in FASTA format)
1 MKTKFDRLGT GKRSRPSPNN IDFNDQSATF KRNKKNSRQP SFKVGLSYNS 51 LLDDCDDENE TEEIFEGRGL QFFDKDDNFS ITADDTQVTS KLFDHDLEQT 101 PDEEAKKPKK VTIRKSAKKC LSTTILPDSF RGVFKFTEFN KMQSEAFPSI 151 YESNENCIIS SPTGSGKTVL FELAILRLIK ETNSDTNNTK IIYIAPTKSL 201 CYEMYKNWFP SFVNLSVGML TSDTSFLETE KAKKCNIIIT TPEKWDLLTR 251 RWSDYSRLFE LVKLVLVDEI HTIKEKRGAS LEVILTRMNT MCQNIRFVAL 301 SATVPNIEDL ALWLKTNNEL PANILSFDES YRQVQLTKFV YGYSFNCKND 351 FQKDAIYNSK LIEIIEKHAD NRPVLIFCPT RASTISTAKF LLNNHIFSKS 401 KKRCNHNPSD KILNECMQQG IAFHHAGISL EDRTAVEKEF LAGSINILCS 451 TSTLAVGVNL PAYLVIIKGT KSWNSSEIQE YSDLDVLQMI GRAGRPQFET 501 HGCAVIMTDS KMKQTYENLI HGTDVLESSL HLNLIEHLAA ETSLETVYSI 551 ETAVNWLRNT FFYVRFGKNP AAYQEVNRYV SFHSVEDSQI NQFCQYLLDT 601 LVKVKIIDIS NGEYKSTAYG NAMTRHYISF ESMKQFINAK KFLSLQGILN 651 LLATSEEFSV MRVRHNEKKL FKEINLSPLL KYPFLTEKKQ SQIIDRVSQK 701 VSLLIQYELG GLEFPSYEGA SKLHQTLVQD KFLVFRHCFR LLKCMVDTFI 751 EKSDGTSLKN TLFLLRSLNG HCWENTPMVL RQLKTIGLVS VRRLIRHGIT 801 NLEEMGHLSD TQIEYYLNLK IGNGIKIKND ISLLPCLNIR TKLENCKIEN 851 EELWLTFKVE ISATFKSSIW HGQHLSLDIE TEKSSGELID FRRLQVNKLQ 901 SPRGFRISAK ISPKLEKIEF SIHCQEIAGL GKTIVYSTDH LASQFSAKTP 951 NIRKDLNSLE KCLFYESSSD GEVGKTSRVS HKDGLEESLS SDDSILDYLN 1001 ERKKSSKAVE SAAVIHPEAH SSSHFSNGRQ VRSNGNYECF HSCKDKTQCR 1051 HLCCKEGIPV KYIKEKGPSS IKPVSKPDQI RQPLLAKNIN TTPHLEKRLN 1101 SKPKQWQEEN TDIATVHTLP SKIYNLSQQM SSMEAGEQVL KSGPENCPEI 1151 IPIDLESSDS YSSNTAASSI SDPNGDLDFL GSDIEFE*

Amino Acid Sequence (or in FASTA format)

       1  MKTKFDRLGT GKRSRPSPNN IDFNDQSATF KRNKKNSRQP SFKVGLSYNS
      51  LLDDCDDENE TEEIFEGRGL QFFDKDDNFS ITADDTQVTS KLFDHDLEQT
     101  PDEEAKKPKK VTIRKSAKKC LSTTILPDSF RGVFKFTEFN KMQSEAFPSI
     151  YESNENCIIS SPTGSGKTVL FELAILRLIK ETNSDTNNTK IIYIAPTKSL
     201  CYEMYKNWFP SFVNLSVGML TSDTSFLETE KAKKCNIIIT TPEKWDLLTR
     251  RWSDYSRLFE LVKLVLVDEI HTIKEKRGAS LEVILTRMNT MCQNIRFVAL
     301  SATVPNIEDL ALWLKTNNEL PANILSFDES YRQVQLTKFV YGYSFNCKND
     351  FQKDAIYNSK LIEIIEKHAD NRPVLIFCPT RASTISTAKF LLNNHIFSKS
     401  KKRCNHNPSD KILNECMQQG IAFHHAGISL EDRTAVEKEF LAGSINILCS
     451  TSTLAVGVNL PAYLVIIKGT KSWNSSEIQE YSDLDVLQMI GRAGRPQFET
     501  HGCAVIMTDS KMKQTYENLI HGTDVLESSL HLNLIEHLAA ETSLETVYSI
     551  ETAVNWLRNT FFYVRFGKNP AAYQEVNRYV SFHSVEDSQI NQFCQYLLDT
     601  LVKVKIIDIS NGEYKSTAYG NAMTRHYISF ESMKQFINAK KFLSLQGILN
     651  LLATSEEFSV MRVRHNEKKL FKEINLSPLL KYPFLTEKKQ SQIIDRVSQK
     701  VSLLIQYELG GLEFPSYEGA SKLHQTLVQD KFLVFRHCFR LLKCMVDTFI
     751  EKSDGTSLKN TLFLLRSLNG HCWENTPMVL RQLKTIGLVS VRRLIRHGIT
     801  NLEEMGHLSD TQIEYYLNLK IGNGIKIKND ISLLPCLNIR TKLENCKIEN
     851  EELWLTFKVE ISATFKSSIW HGQHLSLDIE TEKSSGELID FRRLQVNKLQ
     901  SPRGFRISAK ISPKLEKIEF SIHCQEIAGL GKTIVYSTDH LASQFSAKTP
     951  NIRKDLNSLE KCLFYESSSD GEVGKTSRVS HKDGLEESLS SDDSILDYLN
    1001  ERKKSSKAVE SAAVIHPEAH SSSHFSNGRQ VRSNGNYECF HSCKDKTQCR
    1051  HLCCKEGIPV KYIKEKGPSS IKPVSKPDQI RQPLLAKNIN TTPHLEKRLN
    1101  SKPKQWQEEN TDIATVHTLP SKIYNLSQQM SSMEAGEQVL KSGPENCPEI
    1151  IPIDLESSDS YSSNTAASSI SDPNGDLDFL GSDIEFE*

external links for Hfm1p

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
Candida (CGD)	CYC2008 (complexes)	Pfam domains
Candida (CandidaDB)	Complexome	YeastRC Structure Prediction (Seattle)
YGOB	DIP
YOGY	GeneMANIA

References cited on this page View Complete Literature Guide for Hfm1p

1)	Nakagawa T and Ogawa H (1999) The Saccharomyces cerevisiae MER3 gene, encoding a novel helicase-like protein, is required for crossover control in meiosis. EMBO J 18(20):5714-23
2)	Coissac E, et al. (1996) Sequence of a 39,411 bp DNA fragment covering the left end of chromosome VII of Saccharomyces cerevisiae. Yeast 12(15):1555-62
3)	Nakagawa T, et al. (2001) The MER3 helicase involved in meiotic crossing over is stimulated by single-stranded DNA-binding proteins and unwinds DNA in the 3' to 5' direction. J Biol Chem 276(34):31487-93
4)	Nakagawa T and Kolodner RD (2002) Saccharomyces cerevisiae Mer3 is a DNA helicase involved in meiotic crossing over. Mol Cell Biol 22(10):3281-91
5)	Nakagawa T and Kolodner RD (2002) The MER3 DNA helicase catalyzes the unwinding of holliday junctions. J Biol Chem 277(31):28019-24