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Conserved domains on  [gi|1409590592|gb|RAR06181|]
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P-loop containing nucleoside triphosphate hydrolase protein [Stemphylium lycopersici]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
1373-2153 0e+00

ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];


:

Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 773.24  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1373 PIPDILNEMKTLEWYTGQIVpdGHRVFDPQEPVYGDLNFAMSQNLVNALyNTRNITQLYAHQAEAINNLYDGHNVIVSTS 1452
Cdd:COG1205      3 RLEELLERLRASPRYGDQIV--HVRTIPAREARYAPWPDWLPPELRAAL-KKRGIERLYSHQAEAIEAARAGKNVVIATP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1453 TSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQRKSMKELLRFMPgfEDILVETFDGDTPMSDRNYIRDEARIIF 1532
Cdd:COG1205     80 TASGKSLAYLLPVLEALLEDPGATALYLYPTKALARDQLRRLRELAEALG--LGVRVATYDGDTPPEERRWIREHPDIVL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1533 TNPDMLHITILPQEDAWRTYLQNLRFVVVDELHVYNGLFGAHMAFIMRRLRRICAAVGNRHVkFISCSATVANPEEHMKT 1612
Cdd:COG1205    158 TNPDMLHYGLLPHHTRWARFFRNLRYVVIDEAHTYRGVFGSHVANVLRRLRRICRHYGSDPQ-FILASATIGNPAEHAER 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1613 IFGvEEVRLTDFDGSPSGRKEFLCWNTPFKDPGdptsGRGDCMAETAKLFCQLMLRGVRAIAFCRVRKQCEALLAAVKTE 1692
Cdd:COG1205    237 LTG-RPVTVVDEDGSPRGERTFVLWNPPLVDDG----IRRSALAEAARLLADLVREGLRTLVFTRSRRGAELLARYARRA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1693 LtnlERPEVIPRVMSYRGGYTPQDRREIEREMFDGKLCGIVATSALELGVDIGSLDAVVTVGFPYTIANLRQQSGRAGRR 1772
Cdd:COG1205    312 L---REPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRR 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1773 NKDSLSVLVGDCFPTDQYYMSNPDEIFTKPNCALQVDLENMLVVEGHVQCAAHEMPInVEADTVYFGPLLPKIARE---- 1848
Cdd:COG1205    389 GQDSLVVLVAGDDPLDQYYVRHPEELFERPPEAAVIDPDNPYVLAPHLLCAAAELPL-TEGDLELFGPEARELLDAlvee 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1849 -RMRRDEKGFYHVNSRFlpqPSRTVSIRDTEEDHFAIIDVTNGKntVLEELEASRAFFTLYDGGIFLHQGNTYLVKEFSQ 1927
Cdd:COG1205    468 gLLRRRGDGWYWTGDDR---PARDVSLRGAGGENVVIVDATTGR--VIGTVDLPRALRELHPGAIYLHQGETYRVEELDL 542
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1928 ERMLAKVEYVKVDWTTQQRDYTDIDPVETEAIRRIPGSRskAFYGPIKIQQVVYGFFKIDKK-RRILDAVQVDNPPIILF 2006
Cdd:COG1205    543 EERKAYVRPVDVDYYTRALSETDIRILEVLEERELGGVT--VHFGEVEVTEQVTGYKKRRLYtGEVLGEVPLDLPPRTLR 620
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 2007 SKGMWLDVPKSAMDILRSRRLNIAAGIHAAEHAVLSLMPNFV---------ISMPGDVRTEckvpekeflqkestrkRPA 2077
Cdd:COG1205    621 TKAVWLTIPPDLLEAAGLDPEDFPGALHAAEHALIGLLPLFAlcdrwdiggVSTPLHPDTG----------------APT 684
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1409590592 2078 rLTFYDAKGGasGSGISTKAFEFIDTLLNQACQRLTSCHCLEGCNECCNDDACKQSNQVMSKAGAMVIIMCLLGKE 2153
Cdd:COG1205    685 -IFIYDGYPG--GVGLAERGYERFEELLEATRDLIASCPCEDGCPSCVQSPKCGNGNEPLDKAAALRLLEALLGGA 757
Fungal_trans pfam04082
Fungal specific transcription factor domain; This domain is found in a number of fungal ...
546-840 1.42e-67

Fungal specific transcription factor domain; This domain is found in a number of fungal transcription factors including transcriptional activator xlnR, yeast regulatory protein GAL4, and nicotinate catabolism cluster-specific transcription factor HxnR.


:

Pssm-ID: 397964  Cd Length: 262  Bit Score: 229.68  E-value: 1.42e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  546 ISSYWVHFHPQLPILHKPTFNAST----------CPELLLLAIMCLGASCLEKNYGQETTQACAELANFLAWHLRWELFM 615
Cdd:pfam04082    1 LDLFFKNFHPQFPILHRPSFLRDYfelfsspsnyASPLLLLAILALGALFSESPTARSSSSLTDEAADGIHFFLRALILI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  616 DADFRPPAK-LWIFQGLLLLESFEKMYSTRPLHERahiHHATTLTlMRRGSSLIGRSAMDSPPsvkdgksnglggantpd 694
Cdd:pfam04082   81 HEDFSSPSSsLWILQALLLLELYELGTGDRKLHWR---YHGLAIR-LARSLGLHRDPSYVSPS----------------- 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  695 ewWNHWI-TNEATRRAAFGAFVMDSIHATMFGHSAVMVAHEMRLPLPCDEA-LWSATSSSEVGRVEQTLTSNGIKPMSFL 772
Cdd:pfam04082  140 --WKLWIeEAELRRRLFWACFYLDRLISLILGRPPLLSDSDIDLPLPCDDDdLWESDSADEVTLPLISLESKSIKPPLFL 217
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1409590592  773 DGLKKTLNGqtvrtnsfgrtiLMAGLLSVSWHMNQRDLQVSslgvttalggrDKWRGSLTRAFDFWKQ 840
Cdd:pfam04082  218 IKLSKILSK------------ILGSLLSIRSTLDQRDLQLK-----------LSWVRELERALDNWRK 262
PTZ00184 super family cl33172
calmodulin; Provisional
2264-2401 5.41e-28

calmodulin; Provisional


The actual alignment was detected with superfamily member PTZ00184:

Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 111.39  E-value: 5.41e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 2264 YREAFQLFDKRGNGRVDRSALGDLLRACGQNPTLAEIADLERGVGADSANkparAVDFDTFSKILNRPggFREPFDIEEY 2343
Cdd:PTZ00184    13 FKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNG----TIDFPEFLTLMARK--MKDTDSEEEI 86
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1409590592 2344 IRGFQVFDKERSGFVGKGQIKYILTNLGEKMSEEEVDELFKSTIDASNNEVDYREFVK 2401
Cdd:PTZ00184    87 KEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVK 144
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
86-110 1.07e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


:

Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.44  E-value: 1.07e-03
                           10        20
                   ....*....|....*....|....*
gi 1409590592   86 FECPHegCGKSYSRAEHLYRHQLNH 110
Cdd:pfam00096    1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
1373-2153 0e+00

ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 773.24  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1373 PIPDILNEMKTLEWYTGQIVpdGHRVFDPQEPVYGDLNFAMSQNLVNALyNTRNITQLYAHQAEAINNLYDGHNVIVSTS 1452
Cdd:COG1205      3 RLEELLERLRASPRYGDQIV--HVRTIPAREARYAPWPDWLPPELRAAL-KKRGIERLYSHQAEAIEAARAGKNVVIATP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1453 TSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQRKSMKELLRFMPgfEDILVETFDGDTPMSDRNYIRDEARIIF 1532
Cdd:COG1205     80 TASGKSLAYLLPVLEALLEDPGATALYLYPTKALARDQLRRLRELAEALG--LGVRVATYDGDTPPEERRWIREHPDIVL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1533 TNPDMLHITILPQEDAWRTYLQNLRFVVVDELHVYNGLFGAHMAFIMRRLRRICAAVGNRHVkFISCSATVANPEEHMKT 1612
Cdd:COG1205    158 TNPDMLHYGLLPHHTRWARFFRNLRYVVIDEAHTYRGVFGSHVANVLRRLRRICRHYGSDPQ-FILASATIGNPAEHAER 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1613 IFGvEEVRLTDFDGSPSGRKEFLCWNTPFKDPGdptsGRGDCMAETAKLFCQLMLRGVRAIAFCRVRKQCEALLAAVKTE 1692
Cdd:COG1205    237 LTG-RPVTVVDEDGSPRGERTFVLWNPPLVDDG----IRRSALAEAARLLADLVREGLRTLVFTRSRRGAELLARYARRA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1693 LtnlERPEVIPRVMSYRGGYTPQDRREIEREMFDGKLCGIVATSALELGVDIGSLDAVVTVGFPYTIANLRQQSGRAGRR 1772
Cdd:COG1205    312 L---REPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRR 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1773 NKDSLSVLVGDCFPTDQYYMSNPDEIFTKPNCALQVDLENMLVVEGHVQCAAHEMPInVEADTVYFGPLLPKIARE---- 1848
Cdd:COG1205    389 GQDSLVVLVAGDDPLDQYYVRHPEELFERPPEAAVIDPDNPYVLAPHLLCAAAELPL-TEGDLELFGPEARELLDAlvee 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1849 -RMRRDEKGFYHVNSRFlpqPSRTVSIRDTEEDHFAIIDVTNGKntVLEELEASRAFFTLYDGGIFLHQGNTYLVKEFSQ 1927
Cdd:COG1205    468 gLLRRRGDGWYWTGDDR---PARDVSLRGAGGENVVIVDATTGR--VIGTVDLPRALRELHPGAIYLHQGETYRVEELDL 542
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1928 ERMLAKVEYVKVDWTTQQRDYTDIDPVETEAIRRIPGSRskAFYGPIKIQQVVYGFFKIDKK-RRILDAVQVDNPPIILF 2006
Cdd:COG1205    543 EERKAYVRPVDVDYYTRALSETDIRILEVLEERELGGVT--VHFGEVEVTEQVTGYKKRRLYtGEVLGEVPLDLPPRTLR 620
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 2007 SKGMWLDVPKSAMDILRSRRLNIAAGIHAAEHAVLSLMPNFV---------ISMPGDVRTEckvpekeflqkestrkRPA 2077
Cdd:COG1205    621 TKAVWLTIPPDLLEAAGLDPEDFPGALHAAEHALIGLLPLFAlcdrwdiggVSTPLHPDTG----------------APT 684
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1409590592 2078 rLTFYDAKGGasGSGISTKAFEFIDTLLNQACQRLTSCHCLEGCNECCNDDACKQSNQVMSKAGAMVIIMCLLGKE 2153
Cdd:COG1205    685 -IFIYDGYPG--GVGLAERGYERFEELLEATRDLIASCPCEDGCPSCVQSPKCGNGNEPLDKAAALRLLEALLGGA 757
DECH_helic TIGR03817
helicase/secretion neighborhood putative DEAH-box helicase; A conserved gene neighborhood ...
1418-2151 1.60e-171

helicase/secretion neighborhood putative DEAH-box helicase; A conserved gene neighborhood widely spread in the Actinobacteria contains this uncharacterized DEAH-box family helicase encoded convergently towards an operon of genes for protein homologous to type II secretion and pilus formation proteins. The context suggests that this helicase may play a role in conjugal transfer of DNA.


Pssm-ID: 274800 [Multi-domain]  Cd Length: 742  Bit Score: 546.25  E-value: 1.60e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1418 VNALYNTRNITQLYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQRKSMKEL 1497
Cdd:TIGR03817   25 VVAALEAAGIHRPWQHQARAAELAHAGRHVVVATGTASGKSLAYQLPVLSALADDPRATALYLAPTKALAADQLRAVREL 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1498 lrfmpGFEDILVETFDGDTPMSDRNYIRDEARIIFTNPDMLHITILPQEDAWRTYLQNLRFVVVDELHVYNGLFGAHMAF 1577
Cdd:TIGR03817  105 -----TLRGVRPATYDGDTPTEERRWAREHARYVLTNPDMLHRGILPSHARWARFLRRLRYVVIDECHSYRGVFGSHVAL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1578 IMRRLRRICAAVGNRHVkFISCSATVANPEEHMKTIFGVEEVRLTDfDGSPSGRKEFLCWNTPFKdPGDPTSG---RGDC 1654
Cdd:TIGR03817  180 VLRRLRRLCARYGASPV-FVLASATTADPAAAASRLIGAPVVAVTE-DGSPRGARTVALWEPPLT-ELTGENGapvRRSA 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1655 MAETAKLFCQLMLRGVRAIAFCRVRKQCEALLAAVKTELTNLErPEVIPRVMSYRGGYTPQDRREIEREMFDGKLCGIVA 1734
Cdd:TIGR03817  257 SAEAADLLADLVAEGARTLTFVRSRRGAELVAAIARRLLGEVD-PDLAERVAAYRAGYLPEDRRELERALRDGELLGVAT 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1735 TSALELGVDIGSLDAVVTVGFPYTIANLRQQSGRAGRRNKDSLSVLVGDCFPTDQYYMSNPDEIFTKPNCALQVDLENML 1814
Cdd:TIGR03817  336 TNALELGVDISGLDAVVIAGFPGTRASLWQQAGRAGRRGQGALVVLVARDDPLDTYLVHHPEALFDRPVEATVFDPDNPY 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1815 VVEGHVQCAAHEMPINvEADTVYFGP----LLPKIARE-RMRRDEKGfYHVNSRflPQPSRTVSIRDTEEDHFAIIDVTN 1889
Cdd:TIGR03817  416 VLGPHLCCAAAELPLT-EADLELFGPaaaeVLDQLVEQgLLRRRPAG-WFWTRR--ERAHDAVDIRGGGGAPVAIVEAET 491
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1890 GKntVLEELEASRAFFTLYDGGIFLHQGNTYLVKEFSQERMLAKVEYVKVDWTTQQRDYTDIDPVETEAIRRIPGSRSka 1969
Cdd:TIGR03817  492 GR--LLGTVDAGAAHSTVHPGAVYLHQGESYVVDELDLEDGVALVHAEDPDYTTFARETTDISVVEERRRRAWGDVRV-- 567
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1970 FYGPIKIQQVVYGFFkidkKRR-----ILDAVQVDNPPIILFSKGMWLDVPKSAMDILRSRRLNIAAGIHAAEHAVLSLM 2044
Cdd:TIGR03817  568 ALGEVEVTSQVVGYL----RRRlitgeVLDEVPLDLPPRTLRTRAVWYTVTPELLDDAGIDAADVPGALHAAEHAAIGLL 643
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 2045 PNFVISMPGDVrteckvpekeflQKESTRKRP--ARLTFYDAKGGASGSGISTKAFEFIDTLLNQACQRLTSCHCLEGCN 2122
Cdd:TIGR03817  644 PLVATCDRWDI------------GGVSTAVHPdtGLPTVFVYDGHPGGAGFAERGFAKAREWLAATRDAIASCECESGCP 711
                          730       740
                   ....*....|....*....|....*....
gi 1409590592 2123 ECCNDDACKQSNQVMSKAGAMVIIMCLLG 2151
Cdd:TIGR03817  712 SCVQSPKCGNGNDPLDKAGAARLLAAVLG 740
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
1430-1613 7.69e-94

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 301.43  E-value: 7.69e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1430 LYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQRKSMKELLRfmPGFEDILV 1509
Cdd:cd17923      1 LYSHQAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAQDQLRSLRELLE--QLGLGIRV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1510 ETFDGDTPMSDRNYI-RDEARIIFTNPDMLHITILPQEDAWRTYLQNLRFVVVDELHVYNGLFGAHMAFIMRRLRRICaA 1588
Cdd:cd17923     79 ATYDGDTPREERRAIiRNPPRILLTNPDMLHYALLPHHDRWARFLRNLRYVVLDEAHTYRGVFGSHVALLLRRLRRLC-R 157
                          170       180
                   ....*....|....*....|....*
gi 1409590592 1589 VGNRHVKFISCSATVANPEEHMKTI 1613
Cdd:cd17923    158 RYGADPQFILTSATIGNPAEHARTL 182
Fungal_trans pfam04082
Fungal specific transcription factor domain; This domain is found in a number of fungal ...
546-840 1.42e-67

Fungal specific transcription factor domain; This domain is found in a number of fungal transcription factors including transcriptional activator xlnR, yeast regulatory protein GAL4, and nicotinate catabolism cluster-specific transcription factor HxnR.


Pssm-ID: 397964  Cd Length: 262  Bit Score: 229.68  E-value: 1.42e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  546 ISSYWVHFHPQLPILHKPTFNAST----------CPELLLLAIMCLGASCLEKNYGQETTQACAELANFLAWHLRWELFM 615
Cdd:pfam04082    1 LDLFFKNFHPQFPILHRPSFLRDYfelfsspsnyASPLLLLAILALGALFSESPTARSSSSLTDEAADGIHFFLRALILI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  616 DADFRPPAK-LWIFQGLLLLESFEKMYSTRPLHERahiHHATTLTlMRRGSSLIGRSAMDSPPsvkdgksnglggantpd 694
Cdd:pfam04082   81 HEDFSSPSSsLWILQALLLLELYELGTGDRKLHWR---YHGLAIR-LARSLGLHRDPSYVSPS----------------- 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  695 ewWNHWI-TNEATRRAAFGAFVMDSIHATMFGHSAVMVAHEMRLPLPCDEA-LWSATSSSEVGRVEQTLTSNGIKPMSFL 772
Cdd:pfam04082  140 --WKLWIeEAELRRRLFWACFYLDRLISLILGRPPLLSDSDIDLPLPCDDDdLWESDSADEVTLPLISLESKSIKPPLFL 217
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1409590592  773 DGLKKTLNGqtvrtnsfgrtiLMAGLLSVSWHMNQRDLQVSslgvttalggrDKWRGSLTRAFDFWKQ 840
Cdd:pfam04082  218 IKLSKILSK------------ILGSLLSIRSTLDQRDLQLK-----------LSWVRELERALDNWRK 262
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
1431-1608 1.01e-34

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 131.60  E-value: 1.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1431 YAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEPN-TRAMYIFPTKALAQDQrksMKELLRFMPGFEDILV 1509
Cdd:pfam00270    1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNgPQALVLAPTRELAEQI---YEELKKLGKGLGLKVA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1510 ETFDGDTPMSDRNYIRdEARIIFTNPDMLHITILpqedaWRTYLQNLRFVVVDELHVYNGL-FGAHMAFIMRRLRricaa 1588
Cdd:pfam00270   78 SLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQ-----ERKLLKNLKLLVLDEAHRLLDMgFGPDLEEILRRLP----- 146
                          170       180
                   ....*....|....*....|.
gi 1409590592 1589 vgnRHVKFISCSATVA-NPEE 1608
Cdd:pfam00270  147 ---KKRQILLLSATLPrNLED 164
DEXDc smart00487
DEAD-like helicases superfamily;
1425-1634 1.88e-28

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 114.90  E-value: 1.88e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  1425 RNITQLYAHQAEAINNLYDG-HNVIVSTSTSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQrksMKELLRFMPG 1503
Cdd:smart00487    4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQW---AEELKKLGPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  1504 FEDILVETFDGDTPMSD-RNYIRDEARIIFTNPDMLHITIlpqeDAWRTYLQNLRFVVVDELHVY-NGLFGAHMAFIMRR 1581
Cdd:smart00487   81 LGLKVVGLYGGDSKREQlRKLESGKTDILVTTPGRLLDLL----ENDKLSLSNVDLVILDEAHRLlDGGFGDQLEKLLKL 156
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1409590592  1582 LRricaavgnRHVKFISCSATVANPEEHMKTIFGVEEVRLTDFDGSPSGRKEF 1634
Cdd:smart00487  157 LP--------KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPIEQF 201
PTZ00184 PTZ00184
calmodulin; Provisional
2264-2401 5.41e-28

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 111.39  E-value: 5.41e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 2264 YREAFQLFDKRGNGRVDRSALGDLLRACGQNPTLAEIADLERGVGADSANkparAVDFDTFSKILNRPggFREPFDIEEY 2343
Cdd:PTZ00184    13 FKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNG----TIDFPEFLTLMARK--MKDTDSEEEI 86
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1409590592 2344 IRGFQVFDKERSGFVGKGQIKYILTNLGEKMSEEEVDELFKSTIDASNNEVDYREFVK 2401
Cdd:PTZ00184    87 KEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVK 144
PRK13767 PRK13767
ATP-dependent helicase; Provisional
1434-1772 6.56e-19

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 94.18  E-value: 6.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQL-------EQEPNTRAMYIFPTKALAQDQRKSMKELLRFM----- 1501
Cdd:PRK13767    37 QRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELfrlgregELEDKVYCLYVSPLRALNNDIHRNLEEPLTEIreiak 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1502 ---PGFEDILVETFDGDTPMSDRN-YIRDEARIIFTNPDMLHItIL--PQedaWRTYLQNLRFVVVDELH-VYNGLFGAH 1574
Cdd:PRK13767   117 ergEELPEIRVAIRTGDTSSYEKQkMLKKPPHILITTPESLAI-LLnsPK---FREKLRTVKWVIVDEIHsLAENKRGVH 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1575 MAFIMRRLRRIcaaVGNRHVKfISCSATVANPEEHMKTIFGVEEvrltdfDGSP--------SGRKEF----LCwntPFK 1642
Cdd:PRK13767   193 LSLSLERLEEL---AGGEFVR-IGLSATIEPLEEVAKFLVGYED------DGEPrdceivdaRFVKPFdikvIS---PVD 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1643 DPGDPTSGrgdcmaETAKLFCQLMLRGVR----AIAFCRVRKQCEALLAAVKTEltnLERPEVIPRVMSYRGGYTPQDRR 1718
Cdd:PRK13767   260 DLIHTPAE------EISEALYETLHELIKehrtTLIFTNTRSGAERVLYNLRKR---FPEEYDEDNIGAHHSSLSREVRL 330
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1409590592 1719 EIEREMFDGKLCGIVATSALELGVDIGSLDAVVTVGFPYTIANLRQQSGRAGRR 1772
Cdd:PRK13767   331 EVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAGHR 384
fungal_TF_MHR cd12148
fungal transcription factor regulatory middle homology region; This domain is present in the ...
537-763 4.96e-14

fungal transcription factor regulatory middle homology region; This domain is present in the large family of fungal zinc cluster transcription factors that contain an N-terminal GAL4-like C6 zinc binuclear cluster DNA-binding domain. Examples of members of this large fungal group are the following Saccharomyces cerevisiae transcription factors, GAL4, STB5, DAL81, CAT8, RDR1, HAL9, PUT3, PPR1, ASG1, RSF2, PIP2, as well as the C-terminal domain of the Cep3, a subunit of the yeast centromere-binding factor 3. It has been suggested that this region plays a regulatory role.


Pssm-ID: 213391  Cd Length: 410  Bit Score: 76.71  E-value: 4.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  537 LSLHMMQTYISSYWVHFHPQLPILHKPTF------------NASTCPELLLLAIMCLGASCLEKNYGQETTQacAELANF 604
Cdd:cd12148      1 PPREVADRLLDLYFENVHPLFPILHRPTFlrdleslysdpsSLSPASLALLLAVLALAALSLPDSELRGESR--RSLAER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  605 LAWHLRwELFMDADFRPPaKLWIFQGLLLLESFekmYSTRPLHERAHIHHATTLtlmrrgssligRSAMDsppsvkdgks 684
Cdd:cd12148     79 YYEAAR-QLLDLALFLPP-SLETLQALLLLALY---LLGTGDPSSAWLLLGLAI-----------RLAQS---------- 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  685 ngLGGANTPDEWWNH-WITNEATRRAAFGAFVMDSIHATMFGHSAVMVAHEMRLPLPCDEALWSATSSSEVGRVEQTLTS 763
Cdd:cd12148    133 --LGLHRDPSSLPGLsPFERELRRRLWWSLYILDRLLSLSLGRPPSISDEDIDVPLPSNEDDELSPSSSPPPPPSEEPTS 210
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
2347-2404 9.86e-09

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 53.71  E-value: 9.86e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1409590592 2347 FQVFDKERSGFVGKGQIKYILTNLGEKMSEEEVDELFKStIDASNN-EVDYREFVKTIA 2404
Cdd:cd00051      6 FRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIRE-VDKDGDgKIDFEEFLELMA 63
EF-hand_7 pfam13499
EF-hand domain pair;
2347-2401 2.41e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.86  E-value: 2.41e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1409590592 2347 FQVFDKERSGFVGKGQIKYILTNL--GEKMSEEEVDELFKsTIDASNN-EVDYREFVK 2401
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFK-EFDLDKDgRISFEEFLE 64
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
2258-2405 4.21e-06

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 48.25  E-value: 4.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 2258 TMASTNYREAFQLFDKRGNGRVDRSALGDLLRACGQnpTLAEIADlergvgADSANKparaVDFDTFSKILNRPggfREP 2337
Cdd:COG5126      1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWA--TLFSEAD------TDGDGR----ISREEFVAGMESL---FEA 65
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1409590592 2338 FDIEEYIRGFQVFDKERSGFVGKGQIKYILTNLGekMSEEEVDELFKStIDASNN-EVDYREFVKTIAE 2405
Cdd:COG5126     66 TVEPFARAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFAR-LDTDGDgKISFEEFVAAVRD 131
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
86-110 1.07e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.44  E-value: 1.07e-03
                           10        20
                   ....*....|....*....|....*
gi 1409590592   86 FECPHegCGKSYSRAEHLYRHQLNH 110
Cdd:pfam00096    1 YKCPD--CGKSFSRKSNLKRHLRTH 23
 
Name Accession Description Interval E-value
YprA COG1205
ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, ...
1373-2153 0e+00

ATP-dependent helicase YprA, contains C-terminal metal-binding DUF1998 domain [Replication, recombination and repair];


Pssm-ID: 440818 [Multi-domain]  Cd Length: 758  Bit Score: 773.24  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1373 PIPDILNEMKTLEWYTGQIVpdGHRVFDPQEPVYGDLNFAMSQNLVNALyNTRNITQLYAHQAEAINNLYDGHNVIVSTS 1452
Cdd:COG1205      3 RLEELLERLRASPRYGDQIV--HVRTIPAREARYAPWPDWLPPELRAAL-KKRGIERLYSHQAEAIEAARAGKNVVIATP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1453 TSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQRKSMKELLRFMPgfEDILVETFDGDTPMSDRNYIRDEARIIF 1532
Cdd:COG1205     80 TASGKSLAYLLPVLEALLEDPGATALYLYPTKALARDQLRRLRELAEALG--LGVRVATYDGDTPPEERRWIREHPDIVL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1533 TNPDMLHITILPQEDAWRTYLQNLRFVVVDELHVYNGLFGAHMAFIMRRLRRICAAVGNRHVkFISCSATVANPEEHMKT 1612
Cdd:COG1205    158 TNPDMLHYGLLPHHTRWARFFRNLRYVVIDEAHTYRGVFGSHVANVLRRLRRICRHYGSDPQ-FILASATIGNPAEHAER 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1613 IFGvEEVRLTDFDGSPSGRKEFLCWNTPFKDPGdptsGRGDCMAETAKLFCQLMLRGVRAIAFCRVRKQCEALLAAVKTE 1692
Cdd:COG1205    237 LTG-RPVTVVDEDGSPRGERTFVLWNPPLVDDG----IRRSALAEAARLLADLVREGLRTLVFTRSRRGAELLARYARRA 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1693 LtnlERPEVIPRVMSYRGGYTPQDRREIEREMFDGKLCGIVATSALELGVDIGSLDAVVTVGFPYTIANLRQQSGRAGRR 1772
Cdd:COG1205    312 L---REPDLADRVAAYRAGYLPEERREIERGLRSGELLGVVSTNALELGIDIGGLDAVVLAGYPGTRASFWQQAGRAGRR 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1773 NKDSLSVLVGDCFPTDQYYMSNPDEIFTKPNCALQVDLENMLVVEGHVQCAAHEMPInVEADTVYFGPLLPKIARE---- 1848
Cdd:COG1205    389 GQDSLVVLVAGDDPLDQYYVRHPEELFERPPEAAVIDPDNPYVLAPHLLCAAAELPL-TEGDLELFGPEARELLDAlvee 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1849 -RMRRDEKGFYHVNSRFlpqPSRTVSIRDTEEDHFAIIDVTNGKntVLEELEASRAFFTLYDGGIFLHQGNTYLVKEFSQ 1927
Cdd:COG1205    468 gLLRRRGDGWYWTGDDR---PARDVSLRGAGGENVVIVDATTGR--VIGTVDLPRALRELHPGAIYLHQGETYRVEELDL 542
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1928 ERMLAKVEYVKVDWTTQQRDYTDIDPVETEAIRRIPGSRskAFYGPIKIQQVVYGFFKIDKK-RRILDAVQVDNPPIILF 2006
Cdd:COG1205    543 EERKAYVRPVDVDYYTRALSETDIRILEVLEERELGGVT--VHFGEVEVTEQVTGYKKRRLYtGEVLGEVPLDLPPRTLR 620
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 2007 SKGMWLDVPKSAMDILRSRRLNIAAGIHAAEHAVLSLMPNFV---------ISMPGDVRTEckvpekeflqkestrkRPA 2077
Cdd:COG1205    621 TKAVWLTIPPDLLEAAGLDPEDFPGALHAAEHALIGLLPLFAlcdrwdiggVSTPLHPDTG----------------APT 684
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1409590592 2078 rLTFYDAKGGasGSGISTKAFEFIDTLLNQACQRLTSCHCLEGCNECCNDDACKQSNQVMSKAGAMVIIMCLLGKE 2153
Cdd:COG1205    685 -IFIYDGYPG--GVGLAERGYERFEELLEATRDLIASCPCEDGCPSCVQSPKCGNGNEPLDKAAALRLLEALLGGA 757
DECH_helic TIGR03817
helicase/secretion neighborhood putative DEAH-box helicase; A conserved gene neighborhood ...
1418-2151 1.60e-171

helicase/secretion neighborhood putative DEAH-box helicase; A conserved gene neighborhood widely spread in the Actinobacteria contains this uncharacterized DEAH-box family helicase encoded convergently towards an operon of genes for protein homologous to type II secretion and pilus formation proteins. The context suggests that this helicase may play a role in conjugal transfer of DNA.


Pssm-ID: 274800 [Multi-domain]  Cd Length: 742  Bit Score: 546.25  E-value: 1.60e-171
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1418 VNALYNTRNITQLYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQRKSMKEL 1497
Cdd:TIGR03817   25 VVAALEAAGIHRPWQHQARAAELAHAGRHVVVATGTASGKSLAYQLPVLSALADDPRATALYLAPTKALAADQLRAVREL 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1498 lrfmpGFEDILVETFDGDTPMSDRNYIRDEARIIFTNPDMLHITILPQEDAWRTYLQNLRFVVVDELHVYNGLFGAHMAF 1577
Cdd:TIGR03817  105 -----TLRGVRPATYDGDTPTEERRWAREHARYVLTNPDMLHRGILPSHARWARFLRRLRYVVIDECHSYRGVFGSHVAL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1578 IMRRLRRICAAVGNRHVkFISCSATVANPEEHMKTIFGVEEVRLTDfDGSPSGRKEFLCWNTPFKdPGDPTSG---RGDC 1654
Cdd:TIGR03817  180 VLRRLRRLCARYGASPV-FVLASATTADPAAAASRLIGAPVVAVTE-DGSPRGARTVALWEPPLT-ELTGENGapvRRSA 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1655 MAETAKLFCQLMLRGVRAIAFCRVRKQCEALLAAVKTELTNLErPEVIPRVMSYRGGYTPQDRREIEREMFDGKLCGIVA 1734
Cdd:TIGR03817  257 SAEAADLLADLVAEGARTLTFVRSRRGAELVAAIARRLLGEVD-PDLAERVAAYRAGYLPEDRRELERALRDGELLGVAT 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1735 TSALELGVDIGSLDAVVTVGFPYTIANLRQQSGRAGRRNKDSLSVLVGDCFPTDQYYMSNPDEIFTKPNCALQVDLENML 1814
Cdd:TIGR03817  336 TNALELGVDISGLDAVVIAGFPGTRASLWQQAGRAGRRGQGALVVLVARDDPLDTYLVHHPEALFDRPVEATVFDPDNPY 415
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1815 VVEGHVQCAAHEMPINvEADTVYFGP----LLPKIARE-RMRRDEKGfYHVNSRflPQPSRTVSIRDTEEDHFAIIDVTN 1889
Cdd:TIGR03817  416 VLGPHLCCAAAELPLT-EADLELFGPaaaeVLDQLVEQgLLRRRPAG-WFWTRR--ERAHDAVDIRGGGGAPVAIVEAET 491
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1890 GKntVLEELEASRAFFTLYDGGIFLHQGNTYLVKEFSQERMLAKVEYVKVDWTTQQRDYTDIDPVETEAIRRIPGSRSka 1969
Cdd:TIGR03817  492 GR--LLGTVDAGAAHSTVHPGAVYLHQGESYVVDELDLEDGVALVHAEDPDYTTFARETTDISVVEERRRRAWGDVRV-- 567
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1970 FYGPIKIQQVVYGFFkidkKRR-----ILDAVQVDNPPIILFSKGMWLDVPKSAMDILRSRRLNIAAGIHAAEHAVLSLM 2044
Cdd:TIGR03817  568 ALGEVEVTSQVVGYL----RRRlitgeVLDEVPLDLPPRTLRTRAVWYTVTPELLDDAGIDAADVPGALHAAEHAAIGLL 643
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 2045 PNFVISMPGDVrteckvpekeflQKESTRKRP--ARLTFYDAKGGASGSGISTKAFEFIDTLLNQACQRLTSCHCLEGCN 2122
Cdd:TIGR03817  644 PLVATCDRWDI------------GGVSTAVHPdtGLPTVFVYDGHPGGAGFAERGFAKAREWLAATRDAIASCECESGCP 711
                          730       740
                   ....*....|....*....|....*....
gi 1409590592 2123 ECCNDDACKQSNQVMSKAGAMVIIMCLLG 2151
Cdd:TIGR03817  712 SCVQSPKCGNGNDPLDKAGAARLLAAVLG 740
DEXHc_Hrq1-like cd17923
DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a ...
1430-1613 7.69e-94

DEAH-box helicase domain of Hrq1 and similar proteins; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. Hrq1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350681 [Multi-domain]  Cd Length: 182  Bit Score: 301.43  E-value: 7.69e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1430 LYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQRKSMKELLRfmPGFEDILV 1509
Cdd:cd17923      1 LYSHQAEAIEAARAGRSVVVTTGTASGKSLCYQLPILEALLRDPGSRALYLYPTKALAQDQLRSLRELLE--QLGLGIRV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1510 ETFDGDTPMSDRNYI-RDEARIIFTNPDMLHITILPQEDAWRTYLQNLRFVVVDELHVYNGLFGAHMAFIMRRLRRICaA 1588
Cdd:cd17923     79 ATYDGDTPREERRAIiRNPPRILLTNPDMLHYALLPHHDRWARFLRNLRYVVLDEAHTYRGVFGSHVALLLRRLRRLC-R 157
                          170       180
                   ....*....|....*....|....*
gi 1409590592 1589 VGNRHVKFISCSATVANPEEHMKTI 1613
Cdd:cd17923    158 RYGADPQFILTSATIGNPAEHARTL 182
Fungal_trans pfam04082
Fungal specific transcription factor domain; This domain is found in a number of fungal ...
546-840 1.42e-67

Fungal specific transcription factor domain; This domain is found in a number of fungal transcription factors including transcriptional activator xlnR, yeast regulatory protein GAL4, and nicotinate catabolism cluster-specific transcription factor HxnR.


Pssm-ID: 397964  Cd Length: 262  Bit Score: 229.68  E-value: 1.42e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  546 ISSYWVHFHPQLPILHKPTFNAST----------CPELLLLAIMCLGASCLEKNYGQETTQACAELANFLAWHLRWELFM 615
Cdd:pfam04082    1 LDLFFKNFHPQFPILHRPSFLRDYfelfsspsnyASPLLLLAILALGALFSESPTARSSSSLTDEAADGIHFFLRALILI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  616 DADFRPPAK-LWIFQGLLLLESFEKMYSTRPLHERahiHHATTLTlMRRGSSLIGRSAMDSPPsvkdgksnglggantpd 694
Cdd:pfam04082   81 HEDFSSPSSsLWILQALLLLELYELGTGDRKLHWR---YHGLAIR-LARSLGLHRDPSYVSPS----------------- 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  695 ewWNHWI-TNEATRRAAFGAFVMDSIHATMFGHSAVMVAHEMRLPLPCDEA-LWSATSSSEVGRVEQTLTSNGIKPMSFL 772
Cdd:pfam04082  140 --WKLWIeEAELRRRLFWACFYLDRLISLILGRPPLLSDSDIDLPLPCDDDdLWESDSADEVTLPLISLESKSIKPPLFL 217
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1409590592  773 DGLKKTLNGqtvrtnsfgrtiLMAGLLSVSWHMNQRDLQVSslgvttalggrDKWRGSLTRAFDFWKQ 840
Cdd:pfam04082  218 IKLSKILSK------------ILGSLLSIRSTLDQRDLQLK-----------LSWVRELERALDNWRK 262
SF2_C_Hrq cd18797
C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role ...
1633-1782 1.74e-67

C-terminal helicase domain of HrQ family helicases; Yeast Hrq1, similar to RecQ4, plays a role in DNA inter-strand crosslink (ICL) repair and in telomere maintenance. Hrq1 lacks the Sld2-like domain found in RecQ4. HrQ family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350184 [Multi-domain]  Cd Length: 146  Bit Score: 224.44  E-value: 1.74e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1633 EFLCWNTPFKDPGDPTSGRGdcMAETAKLFCQLMLRGVRAIAFCRVRKQCEALLAAVKTELTnlERPEVIPRVMSYRGGY 1712
Cdd:cd18797      1 HFVLWNPPLLDRKDGERGSA--RREAARLFADLVRAGVKTIVFCRSRKLAELLLRYLKARLV--EEGPLASKVASYRAGY 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1713 TPQDRREIEREMFDGKLCGIVATSALELGVDIGSLDAVVTVGFPYTIANLRQQSGRAGRRNKDSLSVLVG 1782
Cdd:cd18797     77 LAEDRREIEAELFNGELLGVVATNALELGIDIGGLDAVVLAGYPGSLASLWQQAGRAGRRGKDSLVILVA 146
DEAD pfam00270
DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. ...
1431-1608 1.01e-34

DEAD/DEAH box helicase; Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.


Pssm-ID: 425570 [Multi-domain]  Cd Length: 165  Bit Score: 131.60  E-value: 1.01e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1431 YAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEPN-TRAMYIFPTKALAQDQrksMKELLRFMPGFEDILV 1509
Cdd:pfam00270    1 TPIQAEAIPAILEGRDVLVQAPTGSGKTLAFLLPALEALDKLDNgPQALVLAPTRELAEQI---YEELKKLGKGLGLKVA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1510 ETFDGDTPMSDRNYIRdEARIIFTNPDMLHITILpqedaWRTYLQNLRFVVVDELHVYNGL-FGAHMAFIMRRLRricaa 1588
Cdd:pfam00270   78 SLLGGDSRKEQLEKLK-GPDILVGTPGRLLDLLQ-----ERKLLKNLKLLVLDEAHRLLDMgFGPDLEEILRRLP----- 146
                          170       180
                   ....*....|....*....|.
gi 1409590592 1589 vgnRHVKFISCSATVA-NPEE 1608
Cdd:pfam00270  147 ---KKRQILLLSATLPrNLED 164
Lhr COG1201
Lhr-like helicase [Replication, recombination and repair];
1424-1788 6.35e-34

Lhr-like helicase [Replication, recombination and repair];


Pssm-ID: 440814 [Multi-domain]  Cd Length: 850  Bit Score: 142.55  E-value: 6.35e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1424 TRNITQLYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEPN-------TRAMYIFPTKALAQDQRKSMKE 1496
Cdd:COG1201     19 AARFGAPTPPQREAWPAIAAGESTLLIAPTGSGKTLAAFLPALDELARRPRpgelpdgLRVLYISPLKALANDIERNLRA 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1497 LL-----RFMPGFEDILVETFDGDTPMSDRnyirdeARIIFTNPDMLhIT-------ILPQEDAwRTYLQNLRFVVVDEL 1564
Cdd:COG1201     99 PLeeigeAAGLPLPEIRVGVRTGDTPASER------QRQRRRPPHIL-ITtpeslalLLTSPDA-RELLRGVRTVIVDEI 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1565 H-VYNGLFGAHMAFIMRRLRRICAavgnRHVKFISCSATVANPEEHMKTIFGVEEVRLTDFDGSPSGRK---EFLCwntP 1640
Cdd:COG1201    171 HaLAGSKRGVHLALSLERLRALAP----RPLQRIGLSATVGPLEEVARFLVGYEDPRPVTIVDAGAGKKpdlEVLV---P 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1641 FKDPGDPTSGRGDCMAETAKLFCQLMLRGVRAIAFCRVRKQCEALLAAVkteltNLERPEVIPRVMSYRGGYTPQDRREI 1720
Cdd:COG1201    244 VEDLIERFPWAGHLWPHLYPRVLDLIEAHRTTLVFTNTRSQAERLFQRL-----NELNPEDALPIAAHHGSLSREQRLEV 318
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1409590592 1721 EREMFDGKLCGIVATSALELGVDIGSLDAVVTVGFPYTIANLRQQSGRAG-RRNKDSlsvlVGDCFPTD 1788
Cdd:COG1201    319 EEALKAGELRAVVATSSLELGIDIGDVDLVIQVGSPKSVARLLQRIGRAGhRVGEVS----KGRLVPTH 383
DEXDc smart00487
DEAD-like helicases superfamily;
1425-1634 1.88e-28

DEAD-like helicases superfamily;


Pssm-ID: 214692 [Multi-domain]  Cd Length: 201  Bit Score: 114.90  E-value: 1.88e-28
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  1425 RNITQLYAHQAEAINNLYDG-HNVIVSTSTSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQrksMKELLRFMPG 1503
Cdd:smart00487    4 FGFEPLRPYQKEAIEALLSGlRDVILAAPTGSGKTLAALLPALEALKRGKGGRVLVLVPTRELAEQW---AEELKKLGPS 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  1504 FEDILVETFDGDTPMSD-RNYIRDEARIIFTNPDMLHITIlpqeDAWRTYLQNLRFVVVDELHVY-NGLFGAHMAFIMRR 1581
Cdd:smart00487   81 LGLKVVGLYGGDSKREQlRKLESGKTDILVTTPGRLLDLL----ENDKLSLSNVDLVILDEAHRLlDGGFGDQLEKLLKL 156
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|...
gi 1409590592  1582 LRricaavgnRHVKFISCSATVANPEEHMKTIFGVEEVRLTDFDGSPSGRKEF 1634
Cdd:smart00487  157 LP--------KNVQLLLLSATPPEEIENLLELFLNDPVFIDVGFTPLEPIEQF 201
PTZ00184 PTZ00184
calmodulin; Provisional
2264-2401 5.41e-28

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 111.39  E-value: 5.41e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 2264 YREAFQLFDKRGNGRVDRSALGDLLRACGQNPTLAEIADLERGVGADSANkparAVDFDTFSKILNRPggFREPFDIEEY 2343
Cdd:PTZ00184    13 FKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNG----TIDFPEFLTLMARK--MKDTDSEEEI 86
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1409590592 2344 IRGFQVFDKERSGFVGKGQIKYILTNLGEKMSEEEVDELFKSTIDASNNEVDYREFVK 2401
Cdd:PTZ00184    87 KEAFKVFDRDGNGFISAAELRHVMTNLGEKLTDEEVDEMIREADVDGDGQINYEEFVK 144
SF2-N cd00046
N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily ...
1444-1602 4.73e-25

N-terminal DEAD/H-box helicase domain of superfamily 2 helicases; The DEAD/H-like superfamily 2 helicases comprise a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This N-terminal domain contains the ATP-binding region.


Pssm-ID: 350668 [Multi-domain]  Cd Length: 146  Bit Score: 102.87  E-value: 4.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1444 GHNVIVSTSTSSGKSLIYQIPVLHQLEqEPNTRAMYIFPTKALAQDQRKSMKELLRfmpgfEDILVETFDGDTPMSDR-N 1522
Cdd:cd00046      1 GENVLITAPTGSGKTLAALLAALLLLL-KKGKKVLVLVPTKALALQTAERLRELFG-----PGIRVAVLVGGSSAEEReK 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1523 YIRDEARIIFTNPDMLHITILPqedAWRTYLQNLRFVVVDELHvynglfgaHMAFIMRRLRRICAAVGNRH---VKFISC 1599
Cdd:cd00046     75 NKLGDADIIIATPDMLLNLLLR---EDRLFLKDLKLIIVDEAH--------ALLIDSRGALILDLAVRKAGlknAQVILL 143

                   ...
gi 1409590592 1600 SAT 1602
Cdd:cd00046    144 SAT 146
DEXHc_LHR-like cd17922
DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA ...
1444-1608 8.16e-25

DEXH-box helicase domain of LHR; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases from 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.


Pssm-ID: 350680 [Multi-domain]  Cd Length: 166  Bit Score: 103.05  E-value: 8.16e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1444 GHNVIVSTSTSSGKSLIYQIPVLHQLEQEPN--TRAMYIFPTKALAQDQRKSMKELLRFMPgfEDILVETFDGDTPMSDR 1521
Cdd:cd17922      1 GRNVLIAAPTGSGKTEAAFLPALSSLADEPEkgVQVLYISPLKALINDQERRLEEPLDEID--LEIPVAVRHGDTSQSEK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1522 NYIRDEAR-IIFTNPDMLHItILPQEDAWRTyLQNLRFVVVDELH-VYNGLFGAHMAFIMRRLRRIcaavGNRHVKFISC 1599
Cdd:cd17922     79 AKQLKNPPgILITTPESLEL-LLVNKKLREL-FAGLRYVVVDEIHaLLGSKRGVQLELLLERLRKL----TGRPLRRIGL 152

                   ....*....
gi 1409590592 1600 SATVANPEE 1608
Cdd:cd17922    153 SATLGNLEE 161
MZB pfam09369
MrfA Zn-binding domain; This is the C-terminal MrfA Zn+2-binding domain (MZB, also referred to ...
2036-2125 7.97e-23

MrfA Zn-binding domain; This is the C-terminal MrfA Zn+2-binding domain (MZB, also referred to as DUF1998) which contains a conserved four-cysteine signature motif. These four Cys reside in a short coil between two alpha-helices and form a metal ion-binding site. This domain is frequently found at the C-terminal of ndNTPases, however, it is also found encoded in a standalone gene, downstream of putative helicase domain-encoding genes associated with bacterial anti-phage defense system DISARM. MrfA (Mitomycin repair factor A, also known as YprA in Bacillus subtilis) is a DNA helicase that supports repair of mitomycin C-induced DNA damage. MrfA homologs are widely distributed in bacteria and are also present in archaea, fungi and plants. The MrfA-homolog in yeast, Hrq1, also reduces mitomycin C sensitivity. Hrq1 has high similarity to human RecQ4 and was therefore assigned to the RecQ-like helicase family. MrfA homologs appear to be missing in Enterobacteria, however, certain pathogenic Escherichia coli and Salmonella strains harbour Z5898-like helicases with this domain.


Pssm-ID: 462776 [Multi-domain]  Cd Length: 78  Bit Score: 94.18  E-value: 7.97e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 2036 AEHAVLSLMPNFVISMPGDVRTECKVPEKeflqkestrkRPARLTFYDAKGGasGSGISTKAFEFIDTLLNQACQRLTSC 2115
Cdd:pfam09369    1 LEHALISALPLFLGCDRSDIGGESYPPDT----------GRPRILIYDAYPG--GAGLAEKAFELLGELLEAALERLESC 68
                           90
                   ....*....|
gi 1409590592 2116 HCLEGCNECC 2125
Cdd:pfam09369   69 DCEAGCPSCL 78
BRR2 COG1204
Replicative superfamily II helicase [Replication, recombination and repair];
1421-1801 2.27e-22

Replicative superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440817 [Multi-domain]  Cd Length: 529  Bit Score: 103.82  E-value: 2.27e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1421 LYNTRNITQLYAHQAEAINN-LYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQepNTRAMYIFPTKALAQDQRKSMKELlr 1499
Cdd:COG1204     14 FLKERGIEELYPPQAEALEAgLLEGKNLVVSAPTASGKTLIAELAILKALLN--GGKALYIVPLRALASEKYREFKRD-- 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1500 fmpgFEDILVET------FDGDTPMSDRNYIrdearIIFTnPDMLHiTILPQEDAWrtyLQNLRFVVVDELHvyngLF-- 1571
Cdd:COG1204     90 ----FEELGIKVgvstgdYDSDDEWLGRYDI-----LVAT-PEKLD-SLLRNGPSW---LRDVDLVVVDEAH----LIdd 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1572 ---GAHMAFIMRRLRRICAAVgnrhvKFISCSATVANPEEhmktIFGVEEVRLTDFDGSPSGRKE--FLCWNTPFKDpGD 1646
Cdd:COG1204    152 esrGPTLEVLLARLRRLNPEA-----QIVALSATIGNAEE----IAEWLDAELVKSDWRPVPLNEgvLYDGVLRFDD-GS 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1647 PTSGRgdcmaETAKLFCQLMLRGVRAIAFCRVRKQCEALLAAVKTELTNL----------ERPEVIPRVMSYR------- 1709
Cdd:COG1204    222 RRSKD-----PTLALALDLLEEGGQVLVFVSSRRDAESLAKKLADELKRRltpeereeleELAEELLEVSEEThtnekla 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1710 -----------GGYTPQDRREIEREMFDGKLCGIVATSALELGV----------DIGSLDAVvtvgfPYTIANLRQQSGR 1768
Cdd:COG1204    297 dclekgvafhhAGLPSELRRLVEDAFREGLIKVLVATPTLAAGVnlparrviirDTKRGGMV-----PIPVLEFKQMAGR 371
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1409590592 1769 AGRRNKDS--LSVLVGDCFPT-----DQYYMSNPDEIFTK 1801
Cdd:COG1204    372 AGRPGYDPygEAILVAKSSDEadelfERYILGEPEPIRSK 411
DEXHc_Ski2 cd17921
DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases ...
1430-1608 8.60e-21

DEXH-box helicase domain of DEAD-like helicase Ski2 family proteins; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350679 [Multi-domain]  Cd Length: 181  Bit Score: 91.94  E-value: 8.60e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1430 LYAHQAEAINNLYD-GHNVIVSTSTSSGKSLIYQIPVLHQLEQEPNtRAMYIFPTKALAQDQRKSMKELLRfmpgFEDIL 1508
Cdd:cd17921      2 LNPIQREALRALYLsGDSVLVSAPTSSGKTLIAELAILRALATSGG-KAVYIAPTRALVNQKEADLRERFG----PLGKN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1509 VETFDGDTpmSDRNYIRDEARIIFTNPDMLHITILpqeDAWRTYLQNLRFVVVDELH-VYNGLFGAHMAFIMRRLRRICa 1587
Cdd:cd17921     77 VGLLTGDP--SVNKLLLAEADILVATPEKLDLLLR---NGGERLIQDVRLVVVDEAHlIGDGERGVVLELLLSRLLRIN- 150
                          170       180
                   ....*....|....*....|.
gi 1409590592 1588 avgnRHVKFISCSATVANPEE 1608
Cdd:cd17921    151 ----KNARFVGLSATLPNAED 167
PRK13767 PRK13767
ATP-dependent helicase; Provisional
1434-1772 6.56e-19

ATP-dependent helicase; Provisional


Pssm-ID: 237497 [Multi-domain]  Cd Length: 876  Bit Score: 94.18  E-value: 6.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQL-------EQEPNTRAMYIFPTKALAQDQRKSMKELLRFM----- 1501
Cdd:PRK13767    37 QRYAIPLIHEGKNVLISSPTGSGKTLAAFLAIIDELfrlgregELEDKVYCLYVSPLRALNNDIHRNLEEPLTEIreiak 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1502 ---PGFEDILVETFDGDTPMSDRN-YIRDEARIIFTNPDMLHItIL--PQedaWRTYLQNLRFVVVDELH-VYNGLFGAH 1574
Cdd:PRK13767   117 ergEELPEIRVAIRTGDTSSYEKQkMLKKPPHILITTPESLAI-LLnsPK---FREKLRTVKWVIVDEIHsLAENKRGVH 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1575 MAFIMRRLRRIcaaVGNRHVKfISCSATVANPEEHMKTIFGVEEvrltdfDGSP--------SGRKEF----LCwntPFK 1642
Cdd:PRK13767   193 LSLSLERLEEL---AGGEFVR-IGLSATIEPLEEVAKFLVGYED------DGEPrdceivdaRFVKPFdikvIS---PVD 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1643 DPGDPTSGrgdcmaETAKLFCQLMLRGVR----AIAFCRVRKQCEALLAAVKTEltnLERPEVIPRVMSYRGGYTPQDRR 1718
Cdd:PRK13767   260 DLIHTPAE------EISEALYETLHELIKehrtTLIFTNTRSGAERVLYNLRKR---FPEEYDEDNIGAHHSSLSREVRL 330
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1409590592 1719 EIEREMFDGKLCGIVATSALELGVDIGSLDAVVTVGFPYTIANLRQQSGRAGRR 1772
Cdd:PRK13767   331 EVEEKLKRGELKVVVSSTSLELGIDIGYIDLVVLLGSPKSVSRLLQRIGRAGHR 384
SF2_C_LHR cd18796
C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a ...
1679-1772 1.66e-17

C-terminal helicase domain of LHR family helicases; Large helicase-related protein (LHR) is a DNA damage-inducible helicase that uses ATP hydrolysis to drive unidirectional 3'-to-5' translocation along single-stranded DNA (ssDNA) and to unwind RNA:DNA duplexes. This group also includes related bacterial and archaeal helicases. LHR family helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350183 [Multi-domain]  Cd Length: 150  Bit Score: 81.54  E-value: 1.66e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1679 RKQCEALLAAVKTELTNLERPEvipRVMSYRGGYTPQDRREIEREMFDGKLCGIVATSALELGVDIGSLDAVVTVGFPYT 1758
Cdd:cd18796     48 RSQAERLAQRLRELCPDRVPPD---FIALHHGSLSRELREEVEAALKRGDLKVVVATSSLELGIDIGDVDLVIQIGSPKS 124
                           90
                   ....*....|....
gi 1409590592 1759 IANLRQQSGRAGRR 1772
Cdd:cd18796    125 VARLLQRLGRSGHR 138
PRK09751 PRK09751
putative ATP-dependent helicase Lhr; Provisional
1453-1770 3.13e-17

putative ATP-dependent helicase Lhr; Provisional


Pssm-ID: 137505 [Multi-domain]  Cd Length: 1490  Bit Score: 89.21  E-value: 3.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1453 TSSGKSLIYQIPVLHQL--EQEPNT---------RAMYIFPTKALAQDQRKS--------MKELLRFMPGFEDILVETFD 1513
Cdd:PRK09751     5 TGSGKTLAAFLYALDRLfrEGGEDTreahkrktsRILYISPIKALGTDVQRNlqiplkgiADERRRRGETEVNLRVGIRT 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1514 GDTPMSDR-NYIRDEARIIFTNPDMLHITILPQEdawRTYLQNLRFVVVDELHVYNGL-FGAHMAFIMRRLRRICAAVGN 1591
Cdd:PRK09751    85 GDTPAQERsKLTRNPPDILITTPESLYLMLTSRA---RETLRGVETVIIDEVHAVAGSkRGAHLALSLERLDALLHTSAQ 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1592 RhvkfISCSATVaNPEEHMKTIFGVEevRLTDFDGSPSGRKEFLCWNTPFKD----------PG-DPTSGRGDCM---AE 1657
Cdd:PRK09751   162 R----IGLSATV-RSASDVAAFLGGD--RPVTVVNPPAMRHPQIRIVVPVANmddvssvasgTGeDSHAGREGSIwpyIE 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1658 TAKLfcQLMLRGVRAIAFCRVRKQCEALLA--------------------------AVKTELTNLERPEVIPRvmSYRGG 1711
Cdd:PRK09751   235 TGIL--DEVLRHRSTIVFTNSRGLAEKLTArlnelyaarlqrspsiavdaahfestSGATSNRVQSSDVFIAR--SHHGS 310
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1409590592 1712 YTPQDRREIEREMFDGKLCGIVATSALELGVDIGSLDAVVTVGFPYTIANLRQQSGRAG 1770
Cdd:PRK09751   311 VSKEQRAITEQALKSGELRCVVATSSLELGIDMGAVDLVIQVATPLSVASGLQRIGRAG 369
DEXHc_HFM1 cd18023
DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box ...
1434-1608 4.76e-16

DEXH-box helicase domain of ATP-dependent DNA helicase HFM1; HFM1 is a type II DEAD box helicase, required for crossover formation and complete synapsis of homologous chromosomes during meiosis. HFM1 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350781 [Multi-domain]  Cd Length: 206  Bit Score: 78.94  E-value: 4.76e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGH-NVIVSTSTSSGKSLIYQIPVLHQLEQEP-----NTRAMYIFPTKALAQDQRKSMKEllRFMPgfEDI 1507
Cdd:cd18023      6 QSEVFPDLLYSDkNFVVSAPTGSGKTVLFELAILRLLKERNplpwgNRKVVYIAPIKALCSEKYDDWKE--KFGP--LGL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1508 LVETFDGDTPMSDRNYIRDeARIIFTNPDMLH-ITILpqedaWRTY---LQNLRFVVVDELHVYNGLFGAHMAFIMRRLR 1583
Cdd:cd18023     82 SCAELTGDTEMDDTFEIQD-ADIILTTPEKWDsMTRR-----WRDNgnlVQLVALVLIDEVHIIKENRGATLEVVVSRMK 155
                          170       180       190
                   ....*....|....*....|....*....|
gi 1409590592 1584 RICAAVGNRH-----VKFISCSATVANPEE 1608
Cdd:cd18023    156 TLSSSSELRGstvrpMRFVAVSATIPNIED 185
DEXHc_archSki2 cd18028
DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play ...
1429-1608 9.98e-15

DEXH-box helicase domain of archaeal Ski2-type helicase; Archaeal Ski2-type RNA helicases play an important role in RNA degradation, processing and splicing pathways. They belong to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350786 [Multi-domain]  Cd Length: 177  Bit Score: 74.29  E-value: 9.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1429 QLYAHQAEAINN-LYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQepNTRAMYIFPTKALAQDQRKSMKELLRfmPGFEdI 1507
Cdd:cd18028      1 ELYPPQAEAVRAgLLKGENLLISIPTASGKTLIAEMAMVNTLLE--GGKALYLVPLRALASEKYEEFKKLEE--IGLK-V 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1508 LVETfdGDTPMSDRNYirDEARIIFTNPDMLHiTILPQEDAWrtyLQNLRFVVVDELHVYNGLF-GAHMAFIMRRLRRIc 1586
Cdd:cd18028     76 GIST--GDYDEDDEWL--GDYDIIVATYEKFD-SLLRHSPSW---LRDVGVVVVDEIHLISDEErGPTLESIVARLRRL- 146
                          170       180
                   ....*....|....*....|..
gi 1409590592 1587 aavgNRHVKFISCSATVANPEE 1608
Cdd:cd18028    147 ----NPNTQIIGLSATIGNPDE 164
HELICc smart00490
helicase superfamily c-terminal domain;
1704-1773 4.66e-14

helicase superfamily c-terminal domain;


Pssm-ID: 197757 [Multi-domain]  Cd Length: 82  Bit Score: 69.16  E-value: 4.66e-14
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  1704 RVMSYRGGYTPQDRREIEREMFDGKLCGIVATSALELGVDIGSLDAVVTVGFPYTIANLRQQSGRAGRRN 1773
Cdd:smart00490   13 KVARLHGGLSQEEREEILDKFNNGKIKVLVATDVAERGLDLPGVDLVIIYDLPWSPASYIQRIGRAGRAG 82
fungal_TF_MHR cd12148
fungal transcription factor regulatory middle homology region; This domain is present in the ...
537-763 4.96e-14

fungal transcription factor regulatory middle homology region; This domain is present in the large family of fungal zinc cluster transcription factors that contain an N-terminal GAL4-like C6 zinc binuclear cluster DNA-binding domain. Examples of members of this large fungal group are the following Saccharomyces cerevisiae transcription factors, GAL4, STB5, DAL81, CAT8, RDR1, HAL9, PUT3, PPR1, ASG1, RSF2, PIP2, as well as the C-terminal domain of the Cep3, a subunit of the yeast centromere-binding factor 3. It has been suggested that this region plays a regulatory role.


Pssm-ID: 213391  Cd Length: 410  Bit Score: 76.71  E-value: 4.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  537 LSLHMMQTYISSYWVHFHPQLPILHKPTF------------NASTCPELLLLAIMCLGASCLEKNYGQETTQacAELANF 604
Cdd:cd12148      1 PPREVADRLLDLYFENVHPLFPILHRPTFlrdleslysdpsSLSPASLALLLAVLALAALSLPDSELRGESR--RSLAER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  605 LAWHLRwELFMDADFRPPaKLWIFQGLLLLESFekmYSTRPLHERAHIHHATTLtlmrrgssligRSAMDsppsvkdgks 684
Cdd:cd12148     79 YYEAAR-QLLDLALFLPP-SLETLQALLLLALY---LLGTGDPSSAWLLLGLAI-----------RLAQS---------- 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592  685 ngLGGANTPDEWWNH-WITNEATRRAAFGAFVMDSIHATMFGHSAVMVAHEMRLPLPCDEALWSATSSSEVGRVEQTLTS 763
Cdd:cd12148    133 --LGLHRDPSSLPGLsPFERELRRRLWWSLYILDRLLSLSLGRPPSISDEDIDVPLPSNEDDELSPSSSPPPPPSEEPTS 210
DEXHc_ASCC3_2 cd18022
C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
1446-1625 2.24e-13

C-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350780 [Multi-domain]  Cd Length: 189  Bit Score: 70.87  E-value: 2.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1446 NVIVSTSTSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQRKSMKEllRFMPGFEDILVEtFDGD-TPmsDRNYI 1524
Cdd:cd18022     19 NVLLGAPTGSGKTIAAELAMFRAFNKYPGSKVVYIAPLKALVRERVDDWKK--RFEEKLGKKVVE-LTGDvTP--DMKAL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1525 RDeARIIFTNPDMLH-ITilpqeDAW--RTYLQNLRFVVVDELHVYNGLFGAHMAFIMRRLRRIcAAVGNRHVKFISCSA 1601
Cdd:cd18022     94 AD-ADIIITTPEKWDgIS-----RSWqtREYVQQVSLIIIDEIHLLGSDRGPVLEVIVSRMNYI-SSQTEKPVRLVGLST 166
                          170       180
                   ....*....|....*....|....
gi 1409590592 1602 TVANPEEhMKTIFGVEEVRLTDFD 1625
Cdd:cd18022    167 ALANAGD-LANWLGIKKMGLFNFR 189
Helicase_C pfam00271
Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, ...
1668-1773 9.73e-13

Helicase conserved C-terminal domain; The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.


Pssm-ID: 459740 [Multi-domain]  Cd Length: 109  Bit Score: 66.47  E-value: 9.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1668 RGVRAIAFCRVRKQCEAllaavktelTNLERPEVIpRVMSYRGGYTPQDRREIEREMFDGKLCGIVATSALELGVDIGSL 1747
Cdd:pfam00271   14 RGGKVLIFSQTKKTLEA---------ELLLEKEGI-KVARLHGDLSQEEREEILEDFRKGKIDVLVATDVAERGLDLPDV 83
                           90       100
                   ....*....|....*....|....*.
gi 1409590592 1748 DAVVTVGFPYTIANLRQQSGRAGRRN 1773
Cdd:pfam00271   84 DLVINYDLPWNPASYIQRIGRAGRAG 109
PRK01172 PRK01172
ATP-dependent DNA helicase;
1429-1779 3.41e-12

ATP-dependent DNA helicase;


Pssm-ID: 100801 [Multi-domain]  Cd Length: 674  Bit Score: 71.84  E-value: 3.41e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1429 QLYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQepNTRAMYIFPTKALAQDQrksMKELLRFMPGFEDIL 1508
Cdd:PRK01172    22 ELYDHQRMAIEQLRKGENVIVSVPTAAGKTLIAYSAIYETFLA--GLKSIYIVPLRSLAMEK---YEELSRLRSLGMRVK 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1509 VETFDGDTPMSdrnYIRDEARIIFTNP---DMLHitilpqEDAWrtYLQNLRFVVVDELHVYNGLF-GAHMAFIMRRLRR 1584
Cdd:PRK01172    97 ISIGDYDDPPD---FIKRYDVVILTSEkadSLIH------HDPY--IINDVGLIVADEIHIIGDEDrGPTLETVLSSARY 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1585 IcaavgNRHVKFISCSATVANPEEhMKTIFGVEEVRlTDFDGSPSgRKEFLCWNTPFKDpGDPTSGrgdcmAETAKLFCQ 1664
Cdd:PRK01172   166 V-----NPDARILALSATVSNANE-LAQWLNASLIK-SNFRPVPL-KLGILYRKRLILD-GYERSQ-----VDINSLIKE 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1665 LMLRGVRAIAFCRVRKQCEAL---LAAVKTELTNLERP------------EVIPRVMSY-RGGYTPQDRREIEREMFDGK 1728
Cdd:PRK01172   232 TVNDGGQVLVFVSSRKNAEDYaemLIQHFPEFNDFKVSsennnvyddslnEMLPHGVAFhHAGLSNEQRRFIEEMFRNRY 311
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1729 LCGIVATSALELGVDIGSLDAVV-------TVGFPYtIANL--RQQSGRAGRRNKDSLSV 1779
Cdd:PRK01172   312 IKVIVATPTLAAGVNLPARLVIVrditrygNGGIRY-LSNMeiKQMIGRAGRPGYDQYGI 370
DEXHc_Brr2_2 cd18021
C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type ...
1434-1605 4.87e-12

C-terminal D[D/E]X[H/Q]-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350779 [Multi-domain]  Cd Length: 191  Bit Score: 66.90  E-value: 4.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGH-NVIVSTSTSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQRKSMKEllRFMPGFEDILVEtF 1512
Cdd:cd18021      8 QTQVFNSLYNTDdNVFVGAPTGSGKTVCAELALLRHWRQNPKGRAVYIAPMQELVDARYKDWRA--KFGPLLGKKVVK-L 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1513 DGDTPMSDRnyIRDEARIIFTNPDmlhitilpQEDA----W--RTYLQNLRFVVVDELHVYNGLFGAHMAFIMRRLRRIC 1586
Cdd:cd18021     85 TGETSTDLK--LLAKSDVILATPE--------QWDVlsrrWkqRKNVQSVELFIADELHLIGGENGPVYEVVVSRMRYIS 154
                          170
                   ....*....|....*....
gi 1409590592 1587 AAVGNRhVKFISCSATVAN 1605
Cdd:cd18021    155 SQLEKP-IRIVGLSSSLAN 172
Dob10 COG4581
Superfamily II RNA helicase [Replication, recombination and repair];
1429-1775 1.23e-11

Superfamily II RNA helicase [Replication, recombination and repair];


Pssm-ID: 443638 [Multi-domain]  Cd Length: 751  Bit Score: 70.35  E-value: 1.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1429 QLYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQepNTRAMYIFPTKALAqdqrkSMKellrfmpgFEDiL 1508
Cdd:COG4581     25 ELDPFQEEAILALEAGRSVLVAAPTGSGKTLVAEFAIFLALAR--GRRSFYTAPIKALS-----NQK--------FFD-L 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1509 VETFDGD-----TpmSDRNyIRDEARI------IFTNpdMLHitilpqedAWRTYLQNLRFVVVDELHVYNGLF-GA--- 1573
Cdd:COG4581     89 VERFGAEnvgllT--GDAS-VNPDAPIvvmtteILRN--MLY--------REGADLEDVGVVVMDEFHYLADPDrGWvwe 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1574 ----HMAfimrrlrricaavgnRHVKFISCSATVANPEE---HMKTIFG-VEEVRLTDfdgspsgRK---EFLCWNTPFK 1642
Cdd:COG4581    156 epiiHLP---------------ARVQLVLLSATVGNAEEfaeWLTRVRGeTAVVVSEE-------RPvplEFHYLVTPRL 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1643 DPG---DPTSGRGDCMAETAKlfcQLMLRG-VRAIAFCRVRKQCEALLAA-VKTELTNLERPEVI----------PRVMS 1707
Cdd:COG4581    214 FPLfrvNPELLRPPSRHEVIE---ELDRGGlLPAIVFIFSRRGCDEAAQQlLSARLTTKEERAEIreaidefaedFSVLF 290
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1708 YR--------------GGYTPQDRREIEREMFDGKLCGIVATSALELGVD-------IGSLD-------AVVTVG-Fpyt 1758
Cdd:COG4581    291 GKtlsrllrrgiavhhAGMLPKYRRLVEELFQAGLLKVVFATDTLAVGINmpartvvFTKLSkfdgerhRPLTAReF--- 367
                          410
                   ....*....|....*..
gi 1409590592 1759 ianlRQQSGRAGRRNKD 1775
Cdd:COG4581    368 ----HQIAGRAGRRGID 380
PTZ00183 PTZ00183
centrin; Provisional
2265-2401 1.33e-11

centrin; Provisional


Pssm-ID: 185503 [Multi-domain]  Cd Length: 158  Bit Score: 64.71  E-value: 1.33e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 2265 REAFQLFDKRGNGRVDRSALGDLLRACGQNPTLAE----IADLER-GVGAdsankparaVDFDTFSKILNRPGGFREPFd 2339
Cdd:PTZ00183    20 REAFDLFDTDGSGTIDPKELKVAMRSLGFEPKKEEikqmIADVDKdGSGK---------IDFEEFLDIMTKKLGERDPR- 89
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1409590592 2340 iEEYIRGFQVFDKERSGFVGKGQIKYILTNLGEKMSEEEVDELFKSTIDASNNEVDYREFVK 2401
Cdd:PTZ00183    90 -EEILKAFRLFDDDKTGKISLKNLKRVAKELGETITDEELQEMIDEADRNGDGEISEEEFYR 150
PRK00254 PRK00254
ski2-like helicase; Provisional
1425-1608 2.97e-11

ski2-like helicase; Provisional


Pssm-ID: 234702 [Multi-domain]  Cd Length: 720  Bit Score: 69.08  E-value: 2.97e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1425 RNITQLYAHQAEAINN-LYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEpNTRAMYIFPTKALAQDQRKSMKELLRFmpg 1503
Cdd:PRK00254    19 RGIEELYPPQAEALKSgVLEGKNLVLAIPTASGKTLVAEIVMVNKLLRE-GGKAVYLVPLKALAEEKYREFKDWEKL--- 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1504 feDILVETFDGDTPMSDRNYIRDEarIIFTNPDMLHiTILPQEDAWrtyLQNLRFVVVDELHVYNGL-FGAHMAFIMRRL 1582
Cdd:PRK00254    95 --GLRVAMTTGDYDSTDEWLGKYD--IIIATAEKFD-SLLRHGSSW---IKDVKLVVADEIHLIGSYdRGATLEMILTHM 166
                          170       180
                   ....*....|....*....|....*.
gi 1409590592 1583 RricaavgNRhVKFISCSATVANPEE 1608
Cdd:PRK00254   167 L-------GR-AQILGLSATVGNAEE 184
DEXHc_RecQ cd17920
DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box ...
1434-1566 5.66e-11

DEXH-box helicase domain of RecQ family proteins; The RecQ family of the type II DEAD box helicase superfamily is a family of highly conserved DNA repair helicases. This domain contains the ATP-binding region.


Pssm-ID: 350678 [Multi-domain]  Cd Length: 200  Bit Score: 64.09  E-value: 5.66e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHqleQEPNTraMYIFPTKALAQDQRKSMKELlrfmpgfeDILVETFD 1513
Cdd:cd17920     17 QLEAINAVLAGRDVLVVMPTGGGKSLCYQLPALL---LDGVT--LVVSPLISLMQDQVDRLQQL--------GIRAAALN 83
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1409590592 1514 GDTPMSDRNYI-----RDEARIIFTNPDMLhitilpQEDAWRTYLQNLR------FVVVDELHV 1566
Cdd:cd17920     84 STLSPEEKREVllrikNGQYKLLYVTPERL------LSPDFLELLQRLPerkrlaLIVVDEAHC 141
PRK02362 PRK02362
ATP-dependent DNA helicase;
1422-1771 9.27e-11

ATP-dependent DNA helicase;


Pssm-ID: 235032 [Multi-domain]  Cd Length: 737  Bit Score: 67.29  E-value: 9.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1422 YNTRNITQLYAHQAEAIN-NLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQepNTRAMYIFPTKALAQDQRKSMKELLRF 1500
Cdd:PRK02362    16 YEAEGIEELYPPQAEAVEaGLLDGKNLLAAIPTASGKTLIAELAMLKAIAR--GGKALYIVPLRALASEKFEEFERFEEL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1501 mpGFeDILVETFDGDtpmSDRNYIRDEARIIFTNP--DMLhitiLPQEDAWrtyLQNLRFVVVDELH-VYNGLFGAHMAF 1577
Cdd:PRK02362    94 --GV-RVGISTGDYD---SRDEWLGDNDIIVATSEkvDSL----LRNGAPW---LDDITCVVVDEVHlIDSANRGPTLEV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1578 IMRRLRRIcaavgNRHVKFISCSATVANPEEhmktIFGVEEVRLTDFDGSPSGRKE--FLCWNTPFKDPGDPTSGRGDcm 1655
Cdd:PRK02362   161 TLAKLRRL-----NPDLQVVALSATIGNADE----LADWLDAELVDSEWRPIDLREgvFYGGAIHFDDSQREVEVPSK-- 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1656 AETAKLFCQLMLRGVRAIAFCRVRKQCEA----LLAAVKTELTNLERP---EVIPRVMS--------------------Y 1708
Cdd:PRK02362   230 DDTLNLVLDTLEEGGQCLVFVSSRRNAEGfakrAASALKKTLTAAERAelaELAEEIREvsdtetskdladcvakgaafH 309
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1409590592 1709 RGGYTPQDRREIEREMFDGKLCGIVATSALELGVDIGSLDAVV------TVGF---PYTIANLRQQSGRAGR 1771
Cdd:PRK02362   310 HAGLSREHRELVEDAFRDRLIKVISSTPTLAAGLNLPARRVIIrdyrryDGGAgmqPIPVLEYHQMAGRAGR 381
DEXHc_POLQ-like cd18026
DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in ...
1418-1608 3.01e-09

DEXH-box helicase domain of DNA polymerase theta; DNA polymerase theta (POLQ) is important in the repair of genomic double-strand breaks (DSBs). POLQ contains an N-terminal type II DEAD box helicase domain which contains the ATP-binding region.


Pssm-ID: 350784 [Multi-domain]  Cd Length: 202  Bit Score: 59.15  E-value: 3.01e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1418 VNALYNTRNITQLYAHQAEAINN--LYDGHNVIVSTSTSSGKSLIYQIPVLHQ-LEQEPNtrAMYIFPTKALAQDQRKSM 1494
Cdd:cd18026      5 VREAYAKKGIKKLYDWQKECLSLpgLLEGRNLVYSLPTSGGKTLVAEILMLKRlLERRKK--ALFVLPYVSIVQEKVDAL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1495 KELLRFMpgfeDILVETFDGDT---PMSDRNyirdeariiftNPDMLHITI---------LPQEDAwrtyLQNLRFVVVD 1562
Cdd:cd18026     83 SPLFEEL----GFRVEGYAGNKgrsPPKRRK-----------SLSVAVCTIekanslvnsLIEEGR----LDELGLVVVD 143
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1409590592 1563 ELH-VYNGLFGAHMAFIMRRLrrICAAVGNrhVKFISCSATVANPEE 1608
Cdd:cd18026    144 ELHmLGDGHRGALLELLLTKL--LYAAQKN--IQIVGMSATLPNLEE 186
SF2_C_RecQ cd18794
C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an ...
1671-1771 4.70e-09

C-terminal helicase domain of the RecQ family helicases; The RecQ helicase family is an evolutionarily conserved class of enzymes, dedicated to preserving genomic integrity by operating in telomere maintenance, DNA repair, and replication. They are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350181 [Multi-domain]  Cd Length: 134  Bit Score: 56.83  E-value: 4.70e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1671 RAIAFCRVRKQCEALLAAVKTELTNLERpeviprvmsYRGGYTPQDRREIEREMFDGKLCGIVATSALELGVDIGSLDAV 1750
Cdd:cd18794     32 SGIIYCLSRKECEQVAARLQSKGISAAA---------YHAGLEPSDRRDVQRKWLRDKIQVIVATVAFGMGIDKPDVRFV 102
                           90       100
                   ....*....|....*....|.
gi 1409590592 1751 VTVGFPYTIANLRQQSGRAGR 1771
Cdd:cd18794    103 IHYSLPKSMESYYQESGRAGR 123
RecQ COG0514
Superfamily II DNA helicase RecQ [Replication, recombination and repair];
1434-1780 4.72e-09

Superfamily II DNA helicase RecQ [Replication, recombination and repair];


Pssm-ID: 440280 [Multi-domain]  Cd Length: 489  Bit Score: 61.31  E-value: 4.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQleqePNTrAMYIFPTKALAQDQRKSMKELlrfmpgfeDILVETFD 1513
Cdd:COG0514     22 QEEIIEAVLAGRDALVVMPTGGGKSLCYQLPALLL----PGL-TLVVSPLIALMKDQVDALRAA--------GIRAAFLN 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1514 GDTPMSDRNYI-----RDEARIIFTNPDMLhitilpQEDAWRTYLQNLR--FVVVDELH-V----------Ynglfgahm 1575
Cdd:COG0514     89 SSLSAEERREVlralrAGELKLLYVAPERL------LNPRFLELLRRLKisLFAIDEAHcIsqwghdfrpdY-------- 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1576 afimRRLRRICAAVGNRHVkfISCSATvANPE--EHMKTIFGVEEVR--LTDFDgspsgRKEfLCWNTPFKDPGDPTSgr 1651
Cdd:COG0514    155 ----RRLGELRERLPNVPV--LALTAT-ATPRvrADIAEQLGLEDPRvfVGSFD-----RPN-LRLEVVPKPPDDKLA-- 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1652 gdcmaetaklfcQLM-----LRGVRAIAFCRVRKQCEALlAAvktELTNLERpevipRVMSYRGGYTPQDRREIEREMFD 1726
Cdd:COG0514    220 ------------QLLdflkeHPGGSGIVYCLSRKKVEEL-AE---WLREAGI-----RAAAYHAGLDAEEREANQDRFLR 278
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1409590592 1727 GKLCGIVATSALELGVDIGSLDAVVTVGFPYTIANLRQQSGRAGRRNKDSLSVL 1780
Cdd:COG0514    279 DEVDVIVATIAFGMGIDKPDVRFVIHYDLPKSIEAYYQEIGRAGRDGLPAEALL 332
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
2347-2404 9.86e-09

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 53.71  E-value: 9.86e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1409590592 2347 FQVFDKERSGFVGKGQIKYILTNLGEKMSEEEVDELFKStIDASNN-EVDYREFVKTIA 2404
Cdd:cd00051      6 FRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIRE-VDKDGDgKIDFEEFLELMA 63
Cas3_I cd09639
CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short ...
1447-1775 5.62e-08

CRISPR/Cas system-associated protein Cas3; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; DEAD/DEAH box helicase DNA helicase cas3'; Often but not always is fused to HD nuclease domain; signature gene for Type I


Pssm-ID: 187770 [Multi-domain]  Cd Length: 353  Bit Score: 57.44  E-value: 5.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1447 VIVSTSTSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQRKSMKELlrFMPGFEDILVETFDGDTPMSD------ 1520
Cdd:cd09639      2 LVIEAPTGYGKTEAALLWALHSLKSQKADRVIIALPTRATINAMYRRAKEA--FGETGLYHSSILSSRIKEMGDseefeh 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1521 --RNYIRDEARIIF-----TNPDMLHITILPQEDAWRTYLQNLRF--VVVDELHVYNGLFGAHMAFIMRRLRRIcaavgn 1591
Cdd:cd09639     80 lfPLYIHSNDTLFLdpitvCTIDQVLKSVFGEFGHYEFTLASIANslLIFDEVHFYDEYTLALILAVLEVLKDN------ 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1592 rHVKFISCSATVanPEEHMKTIFGVEEVrltdFDGSPSGRKEFlcwntpfkdPGDPTSGRGDCMAE---TAKLFCQLMLR 1668
Cdd:cd09639    154 -DVPILLMSATL--PKFLKEYAEKIGYV----EENEPLDLKPN---------ERAPFIKIESDKVGeisSLERLLEFIKK 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1669 GVRAIAFCRVRKQCEALLAAVKtELTNLErpevipRVMSYRGGYTPQDRREIE----REMFDGKLCGIVATSALELGVDI 1744
Cdd:cd09639    218 GGSVAIIVNTVDRAQEFYQQLK-EKGPEE------EIMLIHSRFTEKDRAKKEaellLEFKKSEKFVIVATQVIEASLDI 290
                          330       340       350
                   ....*....|....*....|....*....|.
gi 1409590592 1745 gSLDAVVTVgfPYTIANLRQQSGRAGRRNKD 1775
Cdd:cd09639    291 -SVDVMITE--LAPIDSLIQRLGRLHRYGEK 318
DEADc_DDX28 cd17948
DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box ...
1426-1625 1.12e-07

DEAD-box helicase domain of DEAD box protein 28; DDX28 (also called mitochondrial DEAD-box polypeptide 28) plays an essential role in facilitating the proper assembly of the mitochondrial large ribosomal subunit and its helicase activity is essential for this function. DDX28 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350706 [Multi-domain]  Cd Length: 231  Bit Score: 55.07  E-value: 1.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1426 NITQLYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQL--------EQEPNTRAMYIFPTKALAQDQRKSMKEL 1497
Cdd:cd17948      9 GITKPTTVQKQGIPSILRGRNTLCAAETGSGKTLTYLLPIIQRLlrykllaeGPFNAPRGLVITPSRELAEQIGSVAQSL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1498 LRFMPgfedILVETFDGDTPMSD-RNYIRDEARIIFTNPDML------HITILPQedawrtylqnLRFVVVDELH-VYNG 1569
Cdd:cd17948     89 TEGLG----LKVKVITGGRTKRQiRNPHFEEVDILVATPGALsklltsRIYSLEQ----------LRHLVLDEADtLLDD 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1409590592 1570 LFGAHMAFIMRR----LRRICAAVG-NRHVKFISCSATVanPEehmktifGVEEV--RLTDFD 1625
Cdd:cd17948    155 SFNEKLSHFLRRfplaSRRSENTDGlDPGTQLVLVSATM--PS-------GVGEVlsKVIDVD 208
cas3_cyano TIGR03158
CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short ...
1433-1640 1.31e-07

CRISPR-associated helicase Cas3, subtype CYANO; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) is a widespread family of prokaryotic direct repeats with spacers of unique sequence between consecutive repeats. This protein family is a CRISPR-associated (Cas) family strictly associated with the Cyano subtype of CRISPR/Cas locus, found in several species of Cyanobacteria and several archaeal species. It contains helicase motifs and appears to represent the Cas3 protein of the Cyano subtype of CRISPR/Cas system.


Pssm-ID: 274457 [Multi-domain]  Cd Length: 357  Bit Score: 56.06  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1433 HQAEAINNLYDGH-NVIVSTS-TSSGKSLIYQIPVLHQleqepNTRAMYIFPTKALAQDQRKSMKELLRFMPGFEDILVE 1510
Cdd:TIGR03158    1 HQVATFEALQSKDaDIIFNTApTGAGKTLAWLTPLLHG-----ENDTIALYPTNALIEDQTEAIKEFVDVFKPERDVNLL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1511 TFDGDTPMSDRNYIRDEAR---------------------IIFTNPDMLH-----ITILPQEDAWRTYlQNLRFVVVDEL 1564
Cdd:TIGR03158   76 HVSKATLKDIKEYANDKVGsskgeklynllrnpigtstpiILLTNPDIFVyltrfAYIDRGDIAAGFY-TKFSTVIFDEF 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1565 HVYNGLFGAHMAFIMRRLRRIcaAVGNRHVKFISCSATvanPEEHMKTIF------GVEEVRLTDFDGSPSGRKEFLCWN 1638
Cdd:TIGR03158  155 HLYDAKQLVGMLFLLAYMQLI--RFFECRRKFVFLSAT---PDPALILRLqnakqaGVKIAPIDGEKYQFPDNPELEADN 229

                   ..
gi 1409590592 1639 TP 1640
Cdd:TIGR03158  230 KT 231
SF2_C_Ski2 cd18795
C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an ...
1672-1775 1.32e-07

C-terminal helicase domain of the Ski2 family helicases; Ski2-like RNA helicases play an important role in RNA degradation, processing, and splicing pathways. This family includes spliceosomal Brr2 RNA helicase, ASCC3 (involved in the repair of N-alkylated nucleotides), Mtr4 (involved in processing of structured RNAs), DDX60 (involved in viral RNA degradation), and other proteins. Ski2-like RNA helicases are DEAD-like helicases belonging to superfamily (SF)2, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Similar to SF1 helicases, SF2 helicases do not form toroidal structures like SF3-6 helicases. Their helicase core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350182 [Multi-domain]  Cd Length: 154  Bit Score: 53.33  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1672 AIAFCRVRKQCEAL---LAAVKTeltnlerpeviprvmsYRGGYTPQDRREIEREMFDGKLCGIVATSALELGVD----- 1743
Cdd:cd18795     46 VLVFCSSRKECEKTakdLAGIAF----------------HHAGLTREDRELVEELFREGLIKVLVATSTLAAGVNlpart 109
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1409590592 1744 --IGSLDAVVTVGF-PYTIANLRQQSGRAGRRNKD 1775
Cdd:cd18795    110 viIKGTQRYDGKGYrELSPLEYLQMIGRAGRPGFD 144
DEADc_DDX51 cd17956
DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by ...
1417-1563 1.87e-07

DEAD-box helicase domain of DEAD box protein 51; DDX51 aids cell cancer proliferation by regulating multiple signalling pathways. Mammalian DEAD box protein Ddx51 acts in 3' end maturation of 28S rRNA by promoting the release of U8 snoRNA.It is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350714 [Multi-domain]  Cd Length: 231  Bit Score: 54.56  E-value: 1.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1417 LVNALyNTRNITQLYAHQAEAINNL---------YDGHNVIVSTSTSSGKSLIYQIPVLHQLEQE--PNTRAMYIFPTKA 1485
Cdd:cd17956      1 LLKNL-QNNGITSAFPVQAAVIPWLlpsskstppYRPGDLCVSAPTGSGKTLAYVLPIVQALSKRvvPRLRALIVVPTKE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1486 LAQDQRKSMKELlrfMPGFeDILVETFDGDT----------PMSDRNYIrDEARIIFTNPDML--HITILPQEDawrtyL 1553
Cdd:cd17956     80 LVQQVYKVFESL---CKGT-GLKVVSLSGQKsfkkeqklllVDTSGRYL-SRVDILVATPGRLvdHLNSTPGFT-----L 149
                          170
                   ....*....|
gi 1409590592 1554 QNLRFVVVDE 1563
Cdd:cd17956    150 KHLRFLVIDE 159
Cas3_I-D cd09710
CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; ...
1433-1640 1.91e-07

CRISPR/Cas system-associated protein Cas3; Distinct diverged subfamily of Cas3 helicase domain; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Diverged DNA helicase Cas3'; signature gene for Type I and subtype I-D


Pssm-ID: 187841 [Multi-domain]  Cd Length: 353  Bit Score: 55.65  E-value: 1.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1433 HQAEAINNLYDGH-NVIVSTS-TSSGKSLIYQIPVLHQleqepNTRAMYIFPTKALAQDQRKSMKELLRFMPGFEDILVE 1510
Cdd:cd09710      1 HQVATFEALQSKDaDIIFNTApTGAGKTLAWLTPLLHG-----ENKAIALYPTNALIEDQTEAIKEFVDDANPRHQVKSL 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1511 TFDGDTPMSD----------------RNYI-RDEARIIFTNPDMLH-----ITILPQEDAWRTYlQNLRFVVVDELHVYN 1568
Cdd:cd09710     76 SASDITLWPNdknvgsskgeklynllRNDIgTSTPIILLTNPDIFVyltrfAYIDRGDIAAGFY-TKFSTVIFDEFHLYD 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1409590592 1569 GLFGAHMAFIMRRLRRIcaAVGNRHVKFISCSATvanPEEHMktifgVEEVRLTDFDGSPSGRKEFLCWNTP 1640
Cdd:cd09710    155 AKQLVGLLFYLAYMQLI--RFFECRRKFVFLSAT---PDPAL-----ILRLQNAKQAGVKIAPIDGEAGQFP 216
DEXHc_Brr2_1 cd18019
N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD ...
1446-1608 9.02e-07

N-terminal DEXH-box helicase domain of spliceosomal Brr2 RNA helicase; Brr2 is a type II DEAD box helicase that mediates spliceosome catalytic activation. It is a stable subunit of the spliceosome, required during splicing catalysis and spliceosome disassembly. Brr2 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350777 [Multi-domain]  Cd Length: 214  Bit Score: 51.99  E-value: 9.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1446 NVIVSTSTSSGKSLIYQIPVLHQLEQEPNT---------RAMYIFPTKALAQDQRKSMKELLRFMpgfeDILVETFDGDT 1516
Cdd:cd18019     35 NLLLCAPTGAGKTNVALLTILREIGKHRNPdgtinldafKIVYIAPMKALVQEMVGNFSKRLAPY----GITVAELTGDQ 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1517 PMSDRNYirDEARIIFTNPDMLHITILPQEDawRTYLQNLRFVVVDELHVYNGLFGAHM-AFIMRRLRRIcaAVGNRHVK 1595
Cdd:cd18019    111 QLTKEQI--SETQIIVTTPEKWDIITRKSGD--RTYTQLVRLIIIDEIHLLHDDRGPVLeSIVARTIRQI--EQTQEYVR 184
                          170
                   ....*....|...
gi 1409590592 1596 FISCSATVANPEE 1608
Cdd:cd18019    185 LVGLSATLPNYED 197
DEADc_DDX1 cd17938
DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ...
1434-1607 9.96e-07

DEAD-box helicase domain of DEAD box protein 1; DEAD box protein 1 (DDX1) acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. It possesses 5' single-stranded RNA overhang nuclease activity as well as ATPase activity on various RNA, but not DNA polynucleotides. DDX1 may play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. It may also be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. DDX1 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350696 [Multi-domain]  Cd Length: 204  Bit Score: 51.55  E-value: 9.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLhQLeqepnTRAMYIFPTKALAQDQRKSMKELLRFM--PGFEDILVEt 1511
Cdd:cd17938     26 QAEAIPLILGGGDVLMAAETGSGKTGAFCLPVL-QI-----VVALILEPSRELAEQTYNCIENFKKYLdnPKLRVALLI- 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1512 fdGDTPMSDR-NYIRDEARIIFTNPDMLHITILPQEDAwrtyLQNLRFVVVDELhvyNGLFG-AHMAFIMRRLRRICA-A 1588
Cdd:cd17938     99 --GGVKAREQlKRLESGVDIVVGTPGRLEDLIKTGKLD----LSSVRFFVLDEA---DRLLSqGNLETINRIYNRIPKiT 169
                          170
                   ....*....|....*....
gi 1409590592 1589 VGNRHVKFISCSATVANPE 1607
Cdd:cd17938    170 SDGKRLQVIVCSATLHSFE 188
DEADc_DDX21_DDX50 cd17944
DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and ...
1421-1564 1.71e-06

DEAD-box helicase domain of DEAD box proteins 21 and 50; DDX21 (also called Gu-Alpha and nucleolar RNA helicase 2) is an RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II. It promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) and binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs. DDX50 (also called Gu-Beta, Nucleolar Protein Gu2, and malignant cell derived RNA helicase). DDX21 and DDX50 have similar genomic structures and are in tandem orientation on chromosome 10, suggesting that the two genes arose by gene duplication in evolution. Diseases associated with DDX21 include stomach disease and cerebral creatine deficiency syndrome 3. Diseases associated with DDX50 include rectal disease. Both are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. Their name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350702 [Multi-domain]  Cd Length: 202  Bit Score: 51.00  E-value: 1.71e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1421 LYNTRNITQLYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEPNTRA-------MYIFPTKALAQDQRKS 1493
Cdd:cd17944      4 LLQARGVTYLFPIQVKTFHPVYSGKDLIAQARTGTGKTFSFAIPLIEKLQEDQQPRKrgrapkvLVLAPTRELANQVTKD 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1409590592 1494 MKELLRfmpgfeDILVETFDGDTPMSDR-NYIRDEARIIFTNPDMLhitilpqedawRTYLQN-------LRFVVVDEL 1564
Cdd:cd17944     84 FKDITR------KLSVACFYGGTPYQQQiFAIRNGIDILVGTPGRI-----------KDHLQNgrldltkLKHVVLDEV 145
ResIII pfam04851
Type III restriction enzyme, res subunit;
1429-1565 2.02e-06

Type III restriction enzyme, res subunit;


Pssm-ID: 398492 [Multi-domain]  Cd Length: 162  Bit Score: 49.98  E-value: 2.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1429 QLYAHQAEAINNL------YDGHNVIVSTsTSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQRKSMKELLrfmp 1502
Cdd:pfam04851    3 ELRPYQIEAIENLlesiknGQKRGLIVMA-TGSGKTLTAAKLIARLFKKGPIKKVLFLVPRKDLLEQALEEFKKFL---- 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1409590592 1503 GFEDILVETFDGDTpmsdRNYIRDEARIIFTNPDMLHItilpQEDAWRTYLQNLRF--VVVDELH 1565
Cdd:pfam04851   78 PNYVEIGEIISGDK----KDESVDDNKIVVTTIQSLYK----ALELASLELLPDFFdvIIIDEAH 134
SF2_C cd18785
C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases ...
1732-1775 2.40e-06

C-terminal helicase domain of superfamily 2 DEAD/H-box helicases; Superfamily (SF)2 helicases include DEAD-box helicases, UvrB, RecG, Ski2, Sucrose Non-Fermenting (SNF) family helicases, and dicer proteins, among others. Similar to SF1 helicases, they do not form toroidal structures like SF3-6 helicases. SF2 helicases are a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. Their helicase core is surrounded by C- and N-terminal domains with specific functions such as nucleases, RNA or DNA binding domains, or domains engaged in protein-protein interactions. The core consists of two similar protein domains that resemble the fold of the recombination protein RecA. This model describes the C-terminal domain, also called HelicC.


Pssm-ID: 350172 [Multi-domain]  Cd Length: 77  Bit Score: 47.31  E-value: 2.40e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1409590592 1732 IVATSALELGVDIGSLDAVVTVGFPYTIANLRQQSGRAGRRNKD 1775
Cdd:cd18785     26 LVATNVLGEGIDVPSLDTVIFFDPPSSAASYIQRVGRAGRGGKD 69
EF-hand_7 pfam13499
EF-hand domain pair;
2347-2401 2.41e-06

EF-hand domain pair;


Pssm-ID: 463900 [Multi-domain]  Cd Length: 67  Bit Score: 46.86  E-value: 2.41e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1409590592 2347 FQVFDKERSGFVGKGQIKYILTNL--GEKMSEEEVDELFKsTIDASNN-EVDYREFVK 2401
Cdd:pfam13499    8 FKLLDSDGDGYLDVEELKKLLRKLeeGEPLSDEEVEELFK-EFDLDKDgRISFEEFLE 64
FRQ1 COG5126
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
2258-2405 4.21e-06

Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];


Pssm-ID: 444056 [Multi-domain]  Cd Length: 137  Bit Score: 48.25  E-value: 4.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 2258 TMASTNYREAFQLFDKRGNGRVDRSALGDLLRACGQnpTLAEIADlergvgADSANKparaVDFDTFSKILNRPggfREP 2337
Cdd:COG5126      1 DLQRRKLDRRFDLLDADGDGVLERDDFEALFRRLWA--TLFSEAD------TDGDGR----ISREEFVAGMESL---FEA 65
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1409590592 2338 FDIEEYIRGFQVFDKERSGFVGKGQIKYILTNLGekMSEEEVDELFKStIDASNN-EVDYREFVKTIAE 2405
Cdd:COG5126     66 TVEPFARAAFDLLDTDGDGKISADEFRRLLTALG--VSEEEADELFAR-LDTDGDgKISFEEFVAAVRD 131
DEADc_EIF4A cd17939
DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation ...
1434-1563 6.53e-06

DEAD-box helicase domain of eukaryotic initiation factor 4A; The eukaryotic initiation factor-4A (eIF4A) family consists of 3 proteins EIF4A1, EIF4A2, and EIF4A3. These factors are required for the binding of mRNA to 40S ribosomal subunits. In addition these proteins are helicases that function to unwind double-stranded RNA. EIF4A proteins are members of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350697 [Multi-domain]  Cd Length: 199  Bit Score: 49.24  E-value: 6.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLE-QEPNTRAMYIFPTKALAQDQRKSMKELLRFMpgfeDILVETF 1512
Cdd:cd17939     24 QQRAIVPIIKGRDVIAQAQSGTGKTATFSIGALQRIDtTVRETQALVLAPTRELAQQIQKVVKALGDYM----GVKVHAC 99
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1409590592 1513 DGDTPMSDRNYIRDEA-RIIFTNP----DMLHITILpqedawrtYLQNLRFVVVDE 1563
Cdd:cd17939    100 IGGTSVREDRRKLQYGpHIVVGTPgrvfDMLQRRSL--------RTDKIKMFVLDE 147
DEXHc_cas3 cd17930
DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase ...
1444-1602 6.84e-06

DEXH/Q-box helicase domain of Cas3; CRISPR-associated (Cas) 3 is a nuclease-helicase responsible for degradation of dsDNA. The two enzymatic units of Cas3, a histidine-aspartate (HD) nuclease and a Superfamily 2 (SF2) helicase, may be expressed from separate genes as Cas3' (SF2 helicase) and Cas3'' (HD nuclease) or may be fused as a single HD-SF2 polypeptide. The nucleolytic activity of most Cas3 enzymes is transition metal ion-dependent. Cas3 is a member 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.


Pssm-ID: 350688 [Multi-domain]  Cd Length: 186  Bit Score: 48.83  E-value: 6.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1444 GHNVIVSTSTSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQRKSMKELLRFMPGFEDIL-------VETFDGDT 1516
Cdd:cd17930      1 PGLVILEAPTGSGKTEAALLWALKLAARGGKRRIIYALPTRATINQMYERIREILGRLDDEDKVLllhskaaLELLESDE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1517 PMSDRNYIRDE----------ARIIFTNPDMLHITILPQedawrtYLQNLRF-------VVVDELHVYNGLFgahMAFIM 1579
Cdd:cd17930     81 EPDDDPVEAVDwalllkrswlAPIVVTTIDQLLESLLKY------KHFERRLhglansvVVLDEVQAYDPEY---MALLL 151
                          170       180
                   ....*....|....*....|...
gi 1409590592 1580 RRLRRICAAVGnrhVKFISCSAT 1602
Cdd:cd17930    152 KALLELLGELG---GPVVLMTAT 171
DEADc_DDX59 cd17962
DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer ...
1434-1563 7.59e-06

DEAD-box helicase domain of DEAD box protein 59; DDX59 plays an important role in lung cancer development by promoting DNA replication. DDX59 knockdown mice showed reduced cell proliferation, anchorage-independent cell growth, and reduction of tumor formation. Recent work shows that EGFR and Ras regulate DDX59 during lung cancer development. Diseases associated with DDX59 (also called zinc finger HIT domain-containing protein 5) include orofaciodigital syndrome V and orofaciodigital syndrome. DDX59 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350720 [Multi-domain]  Cd Length: 193  Bit Score: 49.08  E-value: 7.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQ-LEQEPNTRAMYIFPTKALAQDQRKSMKELLRFMPGFEDILVEtf 1512
Cdd:cd17962     17 QMQMIPVGLLGRDILASADTGSGKTAAFLLPVIIRcLTEHRNPSALILTPTRELAVQIEDQAKELMKGLPPMKTALLV-- 94
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1409590592 1513 dGDTPMSDRNY-IRDEARIIFTNPDMLhITILPQEDawrTYLQNLRFVVVDE 1563
Cdd:cd17962     95 -GGLPLPPQLYrLQQGVKVIIATPGRL-LDILKQSS---VELDNIKIVVVDE 141
DEADc cd00268
DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family ...
1417-1563 9.96e-06

DEAD-box helicase domain of DEAD box helicases; DEAD-box helicases comprise a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350669 [Multi-domain]  Cd Length: 196  Bit Score: 48.59  E-value: 9.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1417 LVNALyNTRNITQLYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEP-----NTRAMYIFPTKALAQDQR 1491
Cdd:cd00268      1 LLKAL-KKLGFEKPTPIQAQAIPLILSGRDVIGQAQTGSGKTLAFLLPILEKLLPEPkkkgrGPQALVLAPTRELAMQIA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1492 KSMKELLRFMpgfeDILVETFDGDTPmsdrnyIRDEARIIFTNPDML---------HItilpQEDawRTYLQNLRFVVVD 1562
Cdd:cd00268     80 EVARKLGKGT----GLKVAAIYGGAP------IKKQIEALKKGPDIVvgtpgrlldLI----ERG--KLDLSNVKYLVLD 143

                   .
gi 1409590592 1563 E 1563
Cdd:cd00268    144 E 144
DEADc_DDX56 cd17961
DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of ...
1434-1563 1.24e-05

DEAD-box helicase domain of DEAD box protein 56; DDX56 is a helicase required for assembly of infectious West Nile virus particles. New research suggests that DDX56 relocalizes to the site of virus assembly during WNV infection and that its interaction with WNV capsid in the cytoplasm may occur transiently during virion morphogenesis. DDX56 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350719 [Multi-domain]  Cd Length: 206  Bit Score: 48.35  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQL-------EQEPNTRAMYIFPTKALAQDQRKSMKELLRFMpgFED 1506
Cdd:cd17961     21 QSKAIPLALEGKDILARARTGSGKTAAYALPIIQKIlkakaesGEEQGTRALILVPTRELAQQVSKVLEQLTAYC--RKD 98
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1507 ILVETFDGDTPMSD-RNYIRDEARIIFTNPDML--HItilpQEDAWRTyLQNLRFVVVDE 1563
Cdd:cd17961     99 VRVVNLSASSSDSVqRALLAEKPDIVVSTPARLlsHL----ESGSLLL-LSTLKYLVIDE 153
DEXHc_SKIV2L cd18027
DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also ...
1434-1608 1.36e-05

DEXH-box helicase domain of SKIV2L; Superkiller viralicidic activity 2-like (SKIV2L, also called SKI2 or DHX13) plays a role in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. SKIV2L belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350785 [Multi-domain]  Cd Length: 179  Bit Score: 48.03  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVlhQLEQEPNTRAMYIFPTKALAQDQRKSMKELlrfmpgFEDILVETfd 1513
Cdd:cd18027     13 QKQAILHLEAGDSVFVAAHTSAGKTVVAEYAI--ALAQKHMTRTIYTSPIKALSNQKFRDFKNT------FGDVGLIT-- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1514 GDTPmsdrnyIRDEARIIFTNPDMLHITILPQEDAWRtylqNLRFVVVDELHVYN----GLFGAHMAFIMrrlrricaav 1589
Cdd:cd18027     83 GDVQ------LNPEASCLIMTTEILRSMLYNGSDVIR----DLEWVIFDEVHYINdaerGVVWEEVLIML---------- 142
                          170
                   ....*....|....*....
gi 1409590592 1590 gNRHVKFISCSATVANPEE 1608
Cdd:cd18027    143 -PDHVSIILLSATVPNTVE 160
PLN00206 PLN00206
DEAD-box ATP-dependent RNA helicase; Provisional
1389-1780 2.56e-05

DEAD-box ATP-dependent RNA helicase; Provisional


Pssm-ID: 215103 [Multi-domain]  Cd Length: 518  Bit Score: 49.40  E-value: 2.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1389 GQIVPDghrvfdpqePV--YGDLNFA--MSQNLVNALYNTRNITQLyahqaEAINNLYDGHNVIVSTSTSSGKSLIYQIP 1464
Cdd:PLN00206   113 GEAVPP---------PIlsFSSCGLPpkLLLNLETAGYEFPTPIQM-----QAIPAALSGRSLLVSADTGSGKTASFLVP 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1465 VL--------HQLEQEPNTRAMYIFPTKALAQDQRKSMKELLRFMPgFEDILVetFDGDtPMSDRNY-IRDEARIIFTNP 1535
Cdd:PLN00206   179 IIsrcctirsGHPSEQRNPLAMVLTPTRELCVQVEDQAKVLGKGLP-FKTALV--VGGD-AMPQQLYrIQQGVELIVGTP 254
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1536 DMLhITILPQEDawrTYLQNLRFVVVDELHvynglfgahmAFIMRRLR----RICAAVGNRHVKFIScsATVANPEEHMK 1611
Cdd:PLN00206   255 GRL-IDLLSKHD---IELDNVSVLVLDEVD----------CMLERGFRdqvmQIFQALSQPQVLLFS--ATVSPEVEKFA 318
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1612 TIFGVEEVRLT-DFDGSPSGR-KEFLCWNTPFKdpgdptsgrgdcmaETAKLFCQLMLRG---VRAIAFCRVRKQCEaLL 1686
Cdd:PLN00206   319 SSLAKDIILISiGNPNRPNKAvKQLAIWVETKQ--------------KKQKLFDILKSKQhfkPPAVVFVSSRLGAD-LL 383
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1687 AAVKTELTNLerpevipRVMSYRGGYTPQDRREIEREMFDGKLCGIVATSALELGVDIGSLDAVVTVGFPYTIANLRQQS 1766
Cdd:PLN00206   384 ANAITVVTGL-------KALSIHGEKSMKERREVMKSFLVGEVPVIVATGVLGRGVDLLRVRQVIIFDMPNTIKEYIHQI 456
                          410
                   ....*....|....
gi 1409590592 1767 GRAGRRNKDSLSVL 1780
Cdd:PLN00206   457 GRASRMGEKGTAIV 470
DEADc_DDX54 cd17959
DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner ...
1434-1563 3.36e-05

DEAD-box helicase domain of DEAD box protein 54; DDX54 interacts in a hormone-dependent manner with nuclear receptors, and represses their transcriptional activity. DDX54 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350717 [Multi-domain]  Cd Length: 205  Bit Score: 47.30  E-value: 3.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQL---EQEPNTRAMYIFPTKALAQDQRKSMKELLRFMPGFEDILVe 1510
Cdd:cd17959     28 QRKTIPLILDGRDVVAMARTGSGKTAAFLIPMIEKLkahSPTVGARALILSPTRELALQTLKVTKELGKFTDLRTALLV- 106
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1409590592 1511 tfDGDTpmsdrnyIRDEARIIFTNPD--------MLHITIlpqEDAWRtyLQNLRFVVVDE 1563
Cdd:cd17959    107 --GGDS-------LEEQFEALASNPDiiiatpgrLLHLLV---EMNLK--LSSVEYVVFDE 153
DEXHc_RecQ4-like cd18018
DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) ...
1418-1565 3.43e-05

DEAH-box helicase domain of RecQ4 and similar proteins; ATP-dependent DNA helicase Q4 (RecQ4) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations cause Rothmund-Thomson/RAPADILINO/Baller-Gerold syndrome.


Pssm-ID: 350776 [Multi-domain]  Cd Length: 201  Bit Score: 47.25  E-value: 3.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1418 VNALYNTRNITQLYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEPNTrAMYIFPTKALAQDQrksMKEL 1497
Cdd:cd18018      1 LKLLRRVFGHPSFRPGQEEAIARLLSGRSTLVVLPTGAGKSLCYQLPALLLRRRGPGL-TLVVSPLIALMKDQ---VDAL 76
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1409590592 1498 LRFMPGfedilvETFDGDTPMSDRNYI-----RDEARIIFTNPDMLhitilpqedAWRTYLQNLR------FVVVDELH 1565
Cdd:cd18018     77 PRAIKA------AALNSSLTREERRRIleklrAGEVKILYVSPERL---------VNESFRELLRqtppisLLVVDEAH 140
EFh_calglandulin_like cd16252
EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The ...
2341-2399 5.47e-05

EF-hand, calcium binding motif, found in uncharacterized calglandulin-like proteins; The family corresponds to a group of uncharacterized calglandulin-like proteins. Although their biological function remain unclear, they show high sequence similarity with human calglandulin-like protein GAGLP, which is an ortholog of calglandulin from the venom glands of Bothrops insularis snake. Both GAGLP and calglandulin are putative Ca2+-binding proteins with four EF-hand motifs. However, members in this family contain only three EF-hand motifs. In this point, they may belong to the parvalbumin-like EF-hand family, which is characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix).


Pssm-ID: 319995 [Multi-domain]  Cd Length: 106  Bit Score: 44.44  E-value: 5.47e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1409590592 2341 EEYIR-GFQVFDKERSGFVGKGQIKYILTNLGEKM-----SEEEVDELFKSTIDASNNEVDYREF 2399
Cdd:cd16252     36 EEAIRkAFQMLDKDKSGFIEWNEIKYILSTVPSSMpvaplSDEEAEAMIQAADTDGDGRIDFQEF 100
PRK01297 PRK01297
ATP-dependent RNA helicase RhlB; Provisional
1346-1563 5.66e-05

ATP-dependent RNA helicase RhlB; Provisional


Pssm-ID: 234938 [Multi-domain]  Cd Length: 475  Bit Score: 48.37  E-value: 5.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1346 PAPAESRASTPGPERsliPASiptERKPIPDILNEMKTLewytgqivpdghrVFDPQEPVYGDLNFAMSQNLVNALYNTr 1425
Cdd:PRK01297    46 PAAAAPRAEKPKKDK---PRR---ERKPKPASLWKLEDF-------------VVEPQEGKTRFHDFNLAPELMHAIHDL- 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1426 NITQLYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEP--------NTRAMYIFPTKALAQDQRKSMKEL 1497
Cdd:PRK01297   106 GFPYCTPIQAQVLGYTLAGHDAIGRAQTGTGKTAAFLISIINQLLQTPppkerymgEPRALIIAPTRELVVQIAKDAAAL 185
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1409590592 1498 LRfmpgFEDILVETFDGDTPMsDRNYIRDEAR---IIFTNPDMLhITILPQEDAWrtyLQNLRFVVVDE 1563
Cdd:PRK01297   186 TK----YTGLNVMTFVGGMDF-DKQLKQLEARfcdILVATPGRL-LDFNQRGEVH---LDMVEVMVLDE 245
DEADc_DDX24 cd17946
DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box ...
1434-1500 7.50e-05

DEAD-box helicase domain of DEAD box protein 24; The human DDX24 gene encodes a DEAD box protein, which shows little similarity to any of the other known human DEAD box proteins, but shows a high similarity to mouse Ddx24 at the amino acid level. MDM2 mediates nonproteolytic polyubiquitylation of the DEAD-Box RNA helicase DDX24. DDX24 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP- binding region.


Pssm-ID: 350704 [Multi-domain]  Cd Length: 235  Bit Score: 46.46  E-value: 7.50e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1409590592 1434 QAEAINN-LYDGHNVIVSTSTSSGKSLIYQIPVLH----QLEQEPNT------RAMYIFPTKALAQDQRKSMKELLRF 1500
Cdd:cd17946     17 QALALPAaIRDGKDVIGAAETGSGKTLAFGIPILErllsQKSSNGVGgkqkplRALILTPTRELAVQVKDHLKAIAKY 94
DEXHc_RecQ5 cd18014
DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ ...
1446-1565 7.85e-05

DEAH-box helicase domain of RecQ5; ATP-dependent DNA helicase Q5 (RecQ5) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350772 [Multi-domain]  Cd Length: 205  Bit Score: 46.31  E-value: 7.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1446 NVIVSTSTSSGKSLIYQIPVLHQleqepNTRAMYIFPTKALAQDQRKSMKELlrfmpgfeDILVETFDGDTPMSDRNYIR 1525
Cdd:cd18014     31 DVFVCMPTGAGKSLCYQLPALLA-----KGITIVISPLIALIQDQVDHLKTL--------KIRVDSLNSKLSAQERKRII 97
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1409590592 1526 DEARIIFTNPDMLHITilPQEDAWRTYLQ---------NLRFVVVDELH 1565
Cdd:cd18014     98 ADLESEKPQTKFLYIT--PEMAATSSFQPllsslvsrnLLSYLVVDEAH 144
DEXHc_RecQ1 cd18015
DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ ...
1414-1497 9.18e-05

DEXH-box helicase domain of RecQ1; ATP-dependent DNA helicase Q1 (RecQ1) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350773 [Multi-domain]  Cd Length: 209  Bit Score: 45.82  E-value: 9.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1414 SQNLVNALYNTRNITQLYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQleqepNTRAMYIFPTKALAQDQRKS 1493
Cdd:cd18015      3 SGKVKDTLKNVFKLEKFRPLQLETINATMAGRDVFLVMPTGGGKSLCYQLPALCS-----DGFTLVVSPLISLMEDQLMA 77

                   ....
gi 1409590592 1494 MKEL 1497
Cdd:cd18015     78 LKKL 81
DEADc_DDX52 cd17957
DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ...
1434-1563 1.06e-04

DEAD-box helicase domain of DEAD box protein 52; DDX52 (also called ROK1 and HUSSY19) is ubiquitously expressed in testis, endometrium, and other tissues in humans. DDX52 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350715 [Multi-domain]  Cd Length: 198  Bit Score: 45.66  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEPNT---RAMYIFPTKALAQdqrKSMKELLRFMPG--FEDIL 1508
Cdd:cd17957     17 QMQAIPILLHGRDLLACAPTGSGKTLAFLIPILQKLGKPRKKkglRALILAPTRELAS---QIYRELLKLSKGtgLRIVL 93
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1409590592 1509 V----ETFDGDTPMSDRNYirDearIIFTNPDMLhITILpQEDAwrTYLQNLRFVVVDE 1563
Cdd:cd17957     94 LskslEAKAKDGPKSITKY--D---ILVSTPLRL-VFLL-KQGP--IDLSSVEYLVLDE 143
DEXDc_FANCM cd18033
DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ...
1445-1602 1.29e-04

DEAH-box helicase domain of FANCM; Fanconi anemia group M (FANCM) protein is a DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. It is required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, it binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA), and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, it efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, it strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA. FANCM is a member 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.


Pssm-ID: 350791 [Multi-domain]  Cd Length: 182  Bit Score: 45.01  E-value: 1.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1445 HNVIVSTSTSSGKSLIYQIPVLHQLEQEPNTRAMYIFPTKALAQDQRKSMKEllrFMPGFEDILVEtFDGDTPMSDRNYI 1524
Cdd:cd18033     17 QNTLVALPTGLGKTFIAAVVMLNYYRWFPKGKIVFMAPTKPLVSQQIEACYK---ITGIPSSQTAE-LTGSVPPTKRAEL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1525 RDEARIIFTNP-----DMLHITILPqedawrtylQNLRFVVVDELHVYNGLFGAHMafIMRRLRRIcaavgNRHVKFISC 1599
Cdd:cd18033     93 WASKRVFFLTPqtlenDLKEGDCDP---------KSIVCLVIDEAHRATGNYAYCQ--VVRELMRY-----NSHFRILAL 156

                   ...
gi 1409590592 1600 SAT 1602
Cdd:cd18033    157 TAT 159
DEXHc_ASCC3_1 cd18020
N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; ...
1446-1605 1.70e-04

N-terminal DEXH-box helicase domain of Activating signal cointegrator 1 complex subunit 3; Activating signal cointegrator 1 complex subunit 3 (ASCC3) is a type II DEAD box helicase that plays a role in the repair of N-alkylated nucleotides. ASCC3 belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350778 [Multi-domain]  Cd Length: 199  Bit Score: 45.11  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1446 NVIVSTSTSSGKSLIYQIPVLHQLEQ--EPNTRAM-------YIFPTKALAQDQRKSMKELLRFMpgfeDILVETFDGDT 1516
Cdd:cd18020     19 NMLICAPTGAGKTNIAMLTILHEIRQhvNQGGVIKkddfkivYIAPMKALAAEMVEKFSKRLAPL----GIKVKELTGDM 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1517 PMSDRNYIrdEARIIFTNPDMLHItILPQEDAWRTYLQNLRFVVVDELHVYNGLFGAHM-AFIMRRLRRICAAvgNRHVK 1595
Cdd:cd18020     95 QLTKKEIA--ETQIIVTTPEKWDV-VTRKSSGDVALSQLVRLLIIDEVHLLHDDRGPVIeSLVARTLRQVEST--QSMIR 169
                          170
                   ....*....|
gi 1409590592 1596 FISCSATVAN 1605
Cdd:cd18020    170 IVGLSATLPN 179
DEADc_DDX39 cd17950
DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and ...
1434-1563 1.73e-04

DEAD-box helicase domain of DEAD box protein 39; DDX39A is involved in pre-mRNA splicing and is required for the export of mRNA out of the nucleus. DDX39B is an essential splicing factor required for association of U2 small nuclear ribonucleoprotein with pre-mRNA, and it also plays an important role in mRNA export from the nucleus to the cytoplasm. Diseases associated with DDX39A (also called UAP56-Related Helicase, 49 kDa) include gastrointestinal stromal tumor and inflammatory bowel disease 6, while diseases associated with DDX39B (also called 56 kDa U2AF65-Associated Protein) include Plasmodium vivax malaria. DDX39 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350708 [Multi-domain]  Cd Length: 208  Bit Score: 45.03  E-value: 1.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEPN-TRAMYIFPTKALAQDQRKSMKELLRFMPgfeDILVETF 1512
Cdd:cd17950     29 QHECIPQAILGMDVLCQAKSGMGKTAVFVLSTLQQLEPVDGqVSVLVICHTRELAFQISNEYERFSKYMP---NVKTAVF 105
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1409590592 1513 DGDTPMS-DRNYIRDEA-RIIFTNPDmlHITILPQEDAWRtyLQNLRFVVVDE 1563
Cdd:cd17950    106 FGGVPIKkDIEVLKNKCpHIVVGTPG--RILALVREKKLK--LSHVKHFVLDE 154
DEADc_DDX31 cd17949
DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) ...
1413-1603 1.94e-04

DEAD-box helicase domain of DEAD box protein 31; DDX31 (also called helicain or G2 helicase) plays a role in ribosome biogenesis and TP53/p53 regulation through its interaction with NPM1. DDX31 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350707 [Multi-domain]  Cd Length: 214  Bit Score: 44.88  E-value: 1.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1413 MSQNLVNALyntrNITQLYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQL-EQEPN------TRAMYIFPTKA 1485
Cdd:cd17949      1 LVSHLKSKM----GIEKPTAIQKLAIPVLLQGRDVLVRSQTGSGKTLAYLLPIIQRLlSLEPRvdrsdgTLALVLVPTRE 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1486 LAQDQRKSMKELLRFM----PGfedILVetfDGDTPMSDRNYIRDEARIIFTNPDML--HITilpQEDAWRtyLQNLRFV 1559
Cdd:cd17949     77 LALQIYEVLEKLLKPFhwivPG---YLI---GGEKRKSEKARLRKGVNILIATPGRLldHLK---NTQSFD--VSNLRWL 145
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1409590592 1560 VVDE----LHVynGlFGAHMAFIMRRLRRICAAVGNRHVKFIS-----CSATV 1603
Cdd:cd17949    146 VLDEadrlLDM--G-FEKDITKILELLDDKRSKAGGEKSKPSRrqtvlVSATL 195
DEXHc_RecQ2_BLM cd18016
DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom ...
1413-1524 2.42e-04

DEAH-box helicase domain of RecQ2; ATP-dependent DNA helicase Q2 (RecQ2, also called Bloom syndrome protein homolog or BLM) is part of the RecQ family of highly conserved DNA repair helicases that is part of the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region. Mutations in RecQ2 cause Bloom syndrome.


Pssm-ID: 350774 [Multi-domain]  Cd Length: 208  Bit Score: 44.82  E-value: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1413 MSQNLVNALYNTRNITQLYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLhqleQEPNTrAMYIFPTKALAQDQRK 1492
Cdd:cd18016      1 HSKEMMKIFHKKFGLHQFRTNQLEAINAALLGEDCFVLMPTGGGKSLCYQLPAC----VSPGV-TVVISPLRSLIVDQVQ 75
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1409590592 1493 SMKELlrfmpgfeDILVETFDGDTPMSDRNYI 1524
Cdd:cd18016     76 KLTSL--------DIPATYLTGDKTDAEATKI 99
ELC_N cd22949
N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan ...
2263-2303 2.91e-04

N-terminal domain of Myosin essential light chain ELC; ELC is part of the apicomplexan membrane-associated protein complex called the glideosome, which is essential for parasite motility. The glideosome is composed of six proteins: myosin A (MyoA), essential light chain ELC, myosin light chain MLC1 (also called MTIP), and the glideosome-associated proteins GAP40, GAP45, and GAP50. MyoA is a Class XIV myosin implicated in gliding motility, as well as host cell and tissue invasion by parasites. ELC binds to the MyoA neck region adjacent to the MLC1-binding site, and both myosin light chains co-located to the glideosome. Although ELCs bind to a conserved MyoA sequence, P. falciparum ELC adopts a distinct structure in the free and MyoA-bound state. Therefore ELCs enhance MyoA performance by inducing alpha helical structure formation in MyoA and thus stiffening its lever arm. It has been shown that disruption of MyoA, MLC1, or ELC have dramatic effects on parasite motility but do not affect parasite shape or replication. The ELC N-terminal domain is part of the EF-hand calcium binding motif superfamily. Calcium binding has no effect on the structure of ELCs.


Pssm-ID: 439385 [Multi-domain]  Cd Length: 66  Bit Score: 41.18  E-value: 2.91e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1409590592 2263 NYREAFQLFDKRGNGRVDRSALGDLLRACGQNPTLAEIADL 2303
Cdd:cd22949      4 KFREAFILFDRDGDGELTMYEAVLAMRSCGIPLTNDEKDAL 44
DEADc_MSS116 cd17964
DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for ...
1441-1563 3.66e-04

DEAD-box helicase domain of DEAD-box helicase Mss116; Mss116 is an RNA chaperone important for mitochondrial group I and II intron splicing, translational activation, and RNA end processing. Mss116 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350722 [Multi-domain]  Cd Length: 211  Bit Score: 44.11  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1441 LYDGHNVIVSTSTSSGKSLIYQIPVLHQL------EQEPNTRAMYIFPTKALAQDQRKSMKELLRFMPGFEdilVETFDG 1514
Cdd:cd17964     29 LSTGDDVLARAKTGTGKTLAFLLPAIQSLlntkpaGRRSGVSALIISPTRELALQIAAEAKKLLQGLRKLR---VQSAVG 105
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1409590592 1515 DTPMSdrnyiRDEARIIFTNPDMLHIT------ILpQEDAWRTYLQNLRFVVVDE 1563
Cdd:cd17964    106 GTSRR-----AELNRLRRGRPDILVATpgrlidHL-ENPGVAKAFTDLDYLVLDE 154
EFh cd00051
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ...
2264-2328 3.69e-04

EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.


Pssm-ID: 238008 [Multi-domain]  Cd Length: 63  Bit Score: 40.61  E-value: 3.69e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1409590592 2264 YREAFQLFDKRGNGRVDRSALGDLLRACGQNPTLAEIADLERGVGADSANKparaVDFDTFSKIL 2328
Cdd:cd00051      2 LREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGK----IDFEEFLELM 62
DEADc_DDX55 cd17960
DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, ...
1434-1584 3.79e-04

DEAD-box helicase domain of DEAD box protein 55; DDX55 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350718 [Multi-domain]  Cd Length: 202  Bit Score: 44.10  E-value: 3.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1434 QAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQL------EQEPNTRAMYIFPTKALAQDQRKSMKELLRFmpGFEDI 1507
Cdd:cd17960     17 QAATIPLFLSNKDVVVEAVTGSGKTLAFLIPVLEILlkrkanLKKGQVGALIISPTRELATQIYEVLQSFLEH--HLPKL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1508 LVETFDGDTPMS--DRNYIRDEARIIFTNPDMLHiTILPQEDAWRTyLQNLRFVVVDELHVYNGL-FGAHMAFIMRRL-- 1582
Cdd:cd17960     95 KCQLLIGGTNVEedVKKFKRNGPNILVGTPGRLE-ELLSRKADKVK-VKSLEVLVLDEADRLLDLgFEADLNRILSKLpk 172

                   ...
gi 1409590592 1583 -RR 1584
Cdd:cd17960    173 qRR 175
DEADc_EIF4AII_EIF4AI_DDX2 cd18046
DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation ...
1432-1563 4.26e-04

DEAD-box helicase domain of eukaryotic initiation factor 4A-I and 4-II; Eukaryotic initiation factor 4A-I (DDX2A) and eukaryotic initiation factor 4A-II (DDX2B) are involved in cap recognition and are required for mRNA binding to ribosome. They are DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350804 [Multi-domain]  Cd Length: 201  Bit Score: 43.97  E-value: 4.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1432 AHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQE-PNTRAMYIFPTKALAQDQRKSMKELLRFMpgfeDILVE 1510
Cdd:cd18046     24 AIQQRAIMPCIKGYDVIAQAQSGTGKTATFSISILQQIDTSlKATQALVLAPTRELAQQIQKVVMALGDYM----GIKCH 99
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1409590592 1511 TFDGDTPM-SDRNYIRDEARIIFTNP----DMLhitilpQEDAWRTylQNLRFVVVDE 1563
Cdd:cd18046    100 ACIGGTSVrDDAQKLQAGPHIVVGTPgrvfDMI------NRRYLRT--DYIKMFVLDE 149
SrmB COG0513
Superfamily II DNA and RNA helicase [Replication, recombination and repair];
1408-1502 8.65e-04

Superfamily II DNA and RNA helicase [Replication, recombination and repair];


Pssm-ID: 440279 [Multi-domain]  Cd Length: 420  Bit Score: 44.37  E-value: 8.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1409590592 1408 DLNFamSQNLVNALyNTRNITQLYAHQAEAINNLYDGHNVIVSTSTSSGKSLIYQIPVLHQLEQEPN--TRAMYIFPTKA 1485
Cdd:COG0513      6 DLGL--SPPLLKAL-AELGYTTPTPIQAQAIPLILAGRDVLGQAQTGTGKTAAFLLPLLQRLDPSRPraPQALILAPTRE 82
                           90
                   ....*....|....*...
gi 1409590592 1486 LAQdQ-RKSMKELLRFMP 1502
Cdd:COG0513     83 LAL-QvAEELRKLAKYLG 99
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
86-110 1.07e-03

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 38.44  E-value: 1.07e-03
                           10        20
                   ....*....|....*....|....*
gi 1409590592   86 FECPHegCGKSYSRAEHLYRHQLNH 110
Cdd:pfam00096    1 YKCPD--CGKSFSRKSNLKRHLRTH 23
EF-hand_6 pfam13405
EF-hand domain;
2263-2292 2.92e-03

EF-hand domain;


Pssm-ID: 463869 [Multi-domain]  Cd Length: 30  Bit Score: 37.16  E-value: 2.92e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1409590592 2263 NYREAFQLFDKRGNGRVDRSALGDLLRACG 2292
Cdd:pfam13405    1 ELREAFKLFDKDGDGKISLEELRKALRSLG 30
EFh_parvalbumin_like cd16251
EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes ...
2347-2405 3.10e-03

EF-hand, calcium binding motif, found in parvalbumin-like EF-hand family; The family includes alpha- and beta-parvalbumins, and a group of uncharacterized calglandulin-like proteins. Parvalbumins are small, acidic, cytosolic EF-hand-containing Ca2+-buffer and Ca2+ transporter/shuttle proteins belonging to EF-hand superfamily. They are expressed by vertebrates in fast-twitch muscle cells, specific neurons of the central and peripheral nervous system, sensory cells of the mammalian auditory organ (Corti's cell), and some other cells, and characterized by the presence of three consecutive EF-hand motifs (helix-loop-helix) called AB, CD, and EF, but only CD and EF can chelate metal ions, such as Ca2+ and Mg2+. Thus, they may play an additional role in Mg2+ handling. Moreover, parvalbumins represent one of the major animal allergens. In metal-bound states, parvalbumins possess a rigid and stable tertiary structure and display strong allergenicity. In contrast, the metal-free parvalbumins are intrinsically disordered, and the loss of metal ions results in a conformational change that decreases their IgE binding capacity. Furthermore, parvalbumins have been widely used as a neuronal marker for a variety of functional brain systems. They also function as a Ca2+ shuttle transporting Ca2+ from troponin-C (TnC) to the sarcoplasmic reticulum (SR) Ca2+ pump during muscle relaxation. Thus they may facilitate myocardial relaxation and play important roles in cardiac diastolic dysfunction. Parvalbumins consists of alpha- and beta- sublineages, which can be distinguished on the basis of isoelectric point (pI > 5 for alpha; pI


Pssm-ID: 319994 [Multi-domain]  Cd Length: 101  Bit Score: 39.05  E-value: 3.10e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1409590592 2347 FQVFDKERSGFVGKGQIKYILTNL---GEKMSEEEVDELFKSTIDASNNEVDYREFVKTIAE 2405
Cdd:cd16251     40 FQILDKDKSGFIEEEELKYILKGFsiaGRDLTDEETKALLAAGDTDGDGKIGVEEFATLVAG 101
DEADc_DDX18 cd17942
DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein ...
1434-1500 4.04e-03

DEAD-box helicase domain of DEAD box protein 18; This DDX18 gene encodes a DEAD box protein and is activated by Myc protein. DDX18 is a member of the DEAD-box helicases, a diverse family of proteins involved in ATP-dependent RNA unwinding, needed in a variety of cellular processes including splicing, ribosome biogenesis and RNA degradation. The name derives from the sequence of the Walker B motif (motif II). This domain contains the ATP-binding region.


Pssm-ID: 350700 [Multi-domain]  Cd Length: 198  Bit Score: 40.81  E-value: 4.04e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1409590592 1434 QAEAINNLYDGHNVIVSTSTSSGKSLIYQIP---VLHQLEQEP--NTRAMYIFPTKALAQDQRKSMKELLRF 1500
Cdd:cd17942     17 QAKSIPPLLEGRDVLGAAKTGSGKTLAFLIPaieLLYKLKFKPrnGTGVIIISPTRELALQIYGVAKELLKY 88
PTZ00184 PTZ00184
calmodulin; Provisional
2339-2404 6.65e-03

calmodulin; Provisional


Pssm-ID: 185504 [Multi-domain]  Cd Length: 149  Bit Score: 39.36  E-value: 6.65e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1409590592 2339 DIEEYIRGFQVFDKERSGFVGKGQIKYILTNLGEKMSEEEVDELFKStIDASNN-EVDYREFVKTIA 2404
Cdd:PTZ00184     9 QIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINE-VDADGNgTIDFPEFLTLMA 74
EFh_PI-PLCdelta cd16202
EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta ...
2347-2401 8.44e-03

EF-hand motif found in phosphoinositide phospholipase C delta (PI-PLC-delta); PI-PLC-delta isozymes represent a class of metazoan PI-PLCs that are some of the most sensitive to calcium among all PLCs. Their activation is modulated by intracellular calcium ion concentration, phospholipids, polyamines, and other proteins, such as RhoAGAP. Like other PI-PLC isozymes, PI-PLC-delta isozymes contain a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C-terminal C2 domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. There are three PI-PLC-delta isozymes (1, 3 and 4). PI-PLC-delta1 is relatively well characterized. It is activated by high calcium levels generated by other PI-PLC family members, and therefore functions as a calcium amplifier within the cell. Different PI-PLC-delta isozymes have different tissue distribution and different subcellular locations. PI-PLC-delta1 is mostly a cytoplasmic protein, PI-PLC-delta3 is located in the membrane, and PI-PLC-delta4 is predominantly detected in the cell nucleus. PI-PLC-delta isozymes is evolutionarily conserved even in non-mammalian species, such as yeast, slime molds and plants.


Pssm-ID: 320032 [Multi-domain]  Cd Length: 140  Bit Score: 38.75  E-value: 8.44e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1409590592 2347 FQVFDKERSGFVGKGQIKYILTNLGEKMSEEEVDELFKSTIDASNNEVDYREFVK 2401
Cdd:cd16202      6 FRKADKNGDGKLSFKECKKLLKKLNVKVDKDYAKKLFQEADTSGEDVLDEEEFVQ 60
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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