Species | Mailhella sp900553065 | |||||||||||
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Lineage | Bacteria; Desulfobacterota; Desulfovibrionia; Desulfovibrionales; Desulfovibrionaceae; Mailhella; Mailhella sp900553065 | |||||||||||
CAZyme ID | MGYG000000551_00315 | |||||||||||
CAZy Family | GH23 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 35598; End: 41558 Strand: - |
MQRIRPAGEP AGDVGLGNFG KLRGGDEPEN YRISPEDQLG VGGAKKKYAD NLAAIRLLKQ | 60 |
LQANGAKLAT PEEKSTLVRF VGWGGLPQVF DPKNDKWAAE YRELQGVLSP DEYAAARRST | 120 |
QDAHYTSETV IRGIYQGLSR LGVETGKELH VLEPSAGIGN FIGLCPESFQ ARFLAVELEP | 180 |
TTAAIAAYLY PKARHINNGF QNIPLNTPSF DLAVGNPPFG NQSLYDPEFP ELKKFSIHNY | 240 |
FLAKSMRLLR EGGIAAFVVS RYFMDAVDSS AREHIAGYAD FLGAVRLPET AFRQNALTDV | 300 |
TTDIVFFQKH NGENKRSLEW LHTSSMEVDD LKHGGRRTAV VNSYFASRPE QIIGRMAYSG | 360 |
GMFEDSLNCV SDASQTDLGE EIARCLDALP AVQFSPLPSA EVRKAESVLN HDFLASDYFQ | 420 |
SLKMGALCVE PQSRKIVFKT SGEFGDGGYE PVTVKNETAR LRLSSMIQLR DTLRELLNEE | 480 |
KGEGSESRMA NLRQRLNTQY DAFVKKYGHL NSQTNRSLMR EDPEHALLES LEADYDKGIS | 540 |
PDVARKTGRQ ARPASARKAA VFRQRVLKPA TLAQQAESPK DALVIALRES GKVDFARMEQ | 600 |
LLGRSTDVIQ RDLQEQGLIF LNPATELWEI RDKYLTGNVR AKLRQARDAA SSDPRFLPNV | 660 |
EALTEALPPD IEAVDIGVKF GSAWLPPSVI SDFIEHLHGG KGSQQVDYLP TLGRWSVRVY | 720 |
LYDAALNTNV WGIPEYPAEK IIEALLMNKP IKVEKETGQR DEQGRPITVL DQELTAAAMQ | 780 |
KADEIKQAFT DWIWTDDDRR ASLSRLYNDR FNTNVPPRYD GSHLELVGAS SEVKLRPHQK | 840 |
DAVWRAIQEG TALFDHVVGA GKTMACIATI MESKRMGFVS KPMVVVPNHL LHQWRDEFYK | 900 |
LYPNAHILVA DKTDFTKQNR ERLFSRIATG DWDAVIVAHS SFRKIDMPHD IQREILKEQI | 960 |
DAVLEAIEAV KEAEGGRATV KQLEKQRENM EARYELLLAG TGKKDTSVDF ADLGVDALFV | 1020 |
DESHEFKNLA YQTTMNVSGL GNITGSAKAL DLFIKCRYLQ RKNEGRGVYF LTGTPISNTI | 1080 |
AEVYTLQRYM QYEELQAKGI DHFDSWASTF GQVTSGWELD ATGVNYKLKS RFAKFQNIPE | 1140 |
LLAMYRTFAD VVTKNDLDEQ AKQAWLRPLT PPVTDGKPYN DVAERSGEQA AYMEKIINRM | 1200 |
ENLPPDPRRD NPLKITNDAR KAGLDYRLIE PHADDFAGSK VNAAVERIYH IWSDTAADRG | 1260 |
TQLVFCDLST PKGGRTPTSA PANRNDLELE TLLDVDGTLL PEQKDEESHG TTQAEKDDSG | 1320 |
EDTSVASDMD AVIALSSKFS VYDDIRSKLV ARGVPPEEIA FIHEANTDIR KAKLFSDMNA | 1380 |
GHVRILLGST SKMGAGMNVQ KRLVAAHHLD APWRPSDLEQ RNGRIIRQGN LFYERDPEHF | 1440 |
SVGIYNYATK QTYDARMWQT IEYKAAAIEQ FRKGDLLQRV IDDVQSEAAN AAEMKAAASG | 1500 |
NPLILMQVQL AADLRKLEAL YSQHQRGQHR LRDRLKWLNG TDERLAKAES AYAANIRHRD | 1560 |
SHTHIVKEKD KEKIRIELFA GDKMLTDRDG EKIKDILLGC VKEITRNAGA RVLFGSYRGF | 1620 |
AMHLERYAQS FGGKEGFRIV VTGTDGQEFK PDNLVYLFDD KLSLSGLFQR MDNFLAKGFD | 1680 |
EAMEKFRKTC RHEKAELETT REALGREFPQ KEELTLAREN HSAIIRELQR MQDDASYVSH | 1740 |
WTPKTSDAGA DTTPAEETWQ EIPDAPFSMA DAAPKDHRVC TLTFGEQGDQ TEYAVTHSPV | 1800 |
GYLLNRSHVR ETTRWPIHCL YDDNLWHSLV KGPPGVRFKQ FESREDALNF ARQDAALLGF | 1860 |
ADAMTHPEKD LSAASATESD SYRQAMEKAG FRPSGMDFYG KQEHELKVET GDGGIFELRI | 1920 |
FQTEEGKVGL RVQYEKDHII NGARTVHASF DTLKETLDYA SSYKNMAETQ NITAPPVQET | 1980 |
FSMRMR | 1986 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG4646 | COG4646 | 5.63e-70 | 341 | 891 | 1 | 542 | Adenine-specific DNA methylase, N12 class [Replication, recombination and repair]. |
pfam04851 | ResIII | 5.10e-10 | 832 | 945 | 1 | 144 | Type III restriction enzyme, res subunit. |
cd17919 | DEXHc_Snf | 6.31e-10 | 835 | 1086 | 1 | 170 | DEXH/Q-box helicase domain of DEAD-like helicase Snf family proteins. Sucrose Non-Fermenting (SNF) proteins DEAD-like helicases superfamily. A diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. |
cd18007 | DEXHc_ATRX-like | 1.01e-09 | 835 | 1087 | 1 | 198 | DEXH-box helicase domain of ATRX-like proteins. This family includes ATRX-like members such as transcriptional regulator ATRX (also called alpha thalassemia/mental retardation syndrome X-linked and X-linked nuclear protein or XNP) which is involved in transcriptional regulation and chromatin remodeling, and ARIP4 (also called androgen receptor-interacting protein 4, RAD54 like 2 or RAD54L2) which modulates androgen receptor (AR)-dependent transactivation in a promoter-dependent manner. They are members of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. |
cd18011 | DEXDc_RapA | 1.67e-09 | 835 | 939 | 1 | 130 | DEXH-box helicase domain of RapA. In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QIW86704.1 | 0.0 | 26 | 1729 | 1610 | 3259 |
QIW86628.1 | 0.0 | 26 | 1729 | 1610 | 3259 |
ASV45029.1 | 0.0 | 26 | 1770 | 1542 | 3217 |
AEY69616.1 | 0.0 | 31 | 1736 | 1689 | 3342 |
AXF51455.1 | 0.0 | 31 | 1736 | 1782 | 3435 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q71TF8 | 1.32e-37 | 51 | 1510 | 51 | 1590 | Defense against restriction protein B OS=Escherichia phage P1 OX=2886926 GN=darB PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000083 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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