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Conserved domains on  [gi|644440803|ref|WP_025315434|]
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primase-helicase zinc-binding domain-containing protein [Gilliamella apicola]

Protein Classification

TOPRIM and DUF927 domain-containing protein( domain architecture ID 11468653)

TOPRIM (topoisomerase-primase) and DUF927 domain-containing protein may function as a bifunctional DNA primase/helicase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3378 COG3378
DNA primase, phage- or plasmid-associated [Mobilome: prophages, transposons];
356-765 7.23e-95

DNA primase, phage- or plasmid-associated [Mobilome: prophages, transposons];


:

Pssm-ID: 442605 [Multi-domain]  Cd Length: 403  Bit Score: 301.47  E-value: 7.23e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 356 TNEVYIYKDNVWQMISEmDLKRELVQLFRQSNAH-----YSEKGIKSTIDTMKLQIPLKNEPARNLIGFKNGVFDLDTRT 430
Cdd:COG3378    5 TGKWYVYDGGRWEEDDG-EVRRLIKELLRAILAKwakksRSSRRIKAVLELLKAELPDELDADPNLINVKNGVLDLRTGE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 431 FKSHSKNHWLQSINNVNFidsvsneNLEHHAPNFYQWLSRSAKKDTIKMDAIKAALYMILANRYDWQLFLEVTGAGGSGK 510
Cdd:COG3378   84 LRPHSPEDYLTKVLPVEY-------DPDAKCPRWLKFLDEIFPGDKELIDLLQEALGYCLTGRTSEQKFFFLYGPGGNGK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 511 SVFADIATMLAGKNNTVSANMEAL-EKPRERSLIVGQSLIILPDQ-AKYIGEGNGIKAITGGDDVAIDEKYKKPYSTKIQ 588
Cdd:COG3378  157 STFLNLLTALLGKDNASSASLETLtENRFDLARLKGKRLNIASELeEGYRLDESLLKALTGGDPITARRKYKDPFSFKPT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 589 GVILAINNNPMTFSNDDGGISRRRVIFHFGEPVPANERDPILKDKIRGELSVIIRHLFNYFEDDNKAKLLLIEQQKSSEA 668
Cdd:COG3378  237 AKLLFATNHLPRIRDTDDGIWRRLLIIPFNVTFPEEERDPNLKEKLLEELPGILNWALEGLLRLLENGGLTEPESVKEAT 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 669 IEVKRLTNPLIDFCSYLFATDKPDgmmigkystpVQFKRFLYHAYITFIENNNLKnPLSLRNFVNALPAAMKEYgleviI 748
Cdd:COG3378  317 EEYREESDPLGAFLEECCELDPGA----------RVPKKDLYEAYREWCEDNGEK-PLSKRTFGKELKKLGFEY-----E 380
                        410       420
                 ....*....|....*....|
gi 644440803 749 RARHGEGRR---TNLHLDYD 765
Cdd:COG3378  381 KRRTNGGKRrgyRGIRLKDD 400
COG4643 COG4643
Uncharacterized domain associated with phage/plasmid primase [Mobilome: prophages, transposons] ...
1-424 1.90e-94

Uncharacterized domain associated with phage/plasmid primase [Mobilome: prophages, transposons];


:

Pssm-ID: 443681 [Multi-domain]  Cd Length: 435  Bit Score: 301.78  E-value: 1.90e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803   1 MKINEITTQAVDKWQSIFNSLGIVVGNGkHCPCPvCGGKDRFRFDNKNGR--GTYICNQCG--SGDGLNLIKNYYHCDAK 76
Cdd:COG4643    3 TNVKEVKAAARGRWPDILAALGLDPPAL-HGPCP-CGGKDRFRFDDKRGRksGWYVCNQCGppAGDGLDLLMKVFGWDFK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  77 EA----SSKV-----AECLNLRNTSTNSDLKSDLQDNIPENPVCKKVKYLLSKAI---LGQSDYLTEKGLT-FDLP---- 139
Cdd:COG4643   81 EAalglDAKGreltpEERAAARARAAAARAAREAEREARQAAAARRAAALWAEARpatPGDHPYLARKGLAaHGLRfhpa 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 140 -LLDNGRIFAPMLNLHNEYAGGQFIEPDGSKHLMKGSNKKSAFILVRSVLSRPAEvcanllahneIIICEGLATGISIAE 218
Cdd:COG4643  161 lLLPGGALLVPLTDADGELVTLQRIYLDGEKRFLKGGRKKGAFIRIGPLPPPGGT----------LLIAEGYATALSVHE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 219 FRlQSIVISAIDAGNLIHVAKGIRELNPTAKIIIAGDNDIGQSPNTGLAKAIEASQAVNGYYSVPDT--DYKCDWDDYRQ 296
Cdd:COG4643  231 AT-GLPVVAALDAGNLLPVAQALRERYPVAELIIAADNDRNTDGNPGQAAAEEAARAVGGLVALPPFppKKGTDFNDLHQ 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 297 QFGLEKVKQYFDSNIKNSLKGSFSEIKLksIPDLSQMQASQKADVLIEHYENNLSLDMVTNEVYIYKDNVWQMISEMDLK 376
Cdd:COG4643  310 ARGLEAVRAAFEAALYQPAGQTAAAVAL--ALAAVGSATAEVAAALALAPSAVEGVGLSEDDAAIAADLRWGAALRPSLG 387
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 644440803 377 RELVQLFRQSNAHYSEKGIKSTIDTMKLQIPLKNEPARNLIGFKNGVF 424
Cdd:COG4643  388 AAAGLRLLLAAEAGEDAAKKAALALTKLASLAAQLPLDGLSLSDALDG 435
 
Name Accession Description Interval E-value
COG3378 COG3378
DNA primase, phage- or plasmid-associated [Mobilome: prophages, transposons];
356-765 7.23e-95

DNA primase, phage- or plasmid-associated [Mobilome: prophages, transposons];


Pssm-ID: 442605 [Multi-domain]  Cd Length: 403  Bit Score: 301.47  E-value: 7.23e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 356 TNEVYIYKDNVWQMISEmDLKRELVQLFRQSNAH-----YSEKGIKSTIDTMKLQIPLKNEPARNLIGFKNGVFDLDTRT 430
Cdd:COG3378    5 TGKWYVYDGGRWEEDDG-EVRRLIKELLRAILAKwakksRSSRRIKAVLELLKAELPDELDADPNLINVKNGVLDLRTGE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 431 FKSHSKNHWLQSINNVNFidsvsneNLEHHAPNFYQWLSRSAKKDTIKMDAIKAALYMILANRYDWQLFLEVTGAGGSGK 510
Cdd:COG3378   84 LRPHSPEDYLTKVLPVEY-------DPDAKCPRWLKFLDEIFPGDKELIDLLQEALGYCLTGRTSEQKFFFLYGPGGNGK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 511 SVFADIATMLAGKNNTVSANMEAL-EKPRERSLIVGQSLIILPDQ-AKYIGEGNGIKAITGGDDVAIDEKYKKPYSTKIQ 588
Cdd:COG3378  157 STFLNLLTALLGKDNASSASLETLtENRFDLARLKGKRLNIASELeEGYRLDESLLKALTGGDPITARRKYKDPFSFKPT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 589 GVILAINNNPMTFSNDDGGISRRRVIFHFGEPVPANERDPILKDKIRGELSVIIRHLFNYFEDDNKAKLLLIEQQKSSEA 668
Cdd:COG3378  237 AKLLFATNHLPRIRDTDDGIWRRLLIIPFNVTFPEEERDPNLKEKLLEELPGILNWALEGLLRLLENGGLTEPESVKEAT 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 669 IEVKRLTNPLIDFCSYLFATDKPDgmmigkystpVQFKRFLYHAYITFIENNNLKnPLSLRNFVNALPAAMKEYgleviI 748
Cdd:COG3378  317 EEYREESDPLGAFLEECCELDPGA----------RVPKKDLYEAYREWCEDNGEK-PLSKRTFGKELKKLGFEY-----E 380
                        410       420
                 ....*....|....*....|
gi 644440803 749 RARHGEGRR---TNLHLDYD 765
Cdd:COG3378  381 KRRTNGGKRrgyRGIRLKDD 400
COG4643 COG4643
Uncharacterized domain associated with phage/plasmid primase [Mobilome: prophages, transposons] ...
1-424 1.90e-94

Uncharacterized domain associated with phage/plasmid primase [Mobilome: prophages, transposons];


Pssm-ID: 443681 [Multi-domain]  Cd Length: 435  Bit Score: 301.78  E-value: 1.90e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803   1 MKINEITTQAVDKWQSIFNSLGIVVGNGkHCPCPvCGGKDRFRFDNKNGR--GTYICNQCG--SGDGLNLIKNYYHCDAK 76
Cdd:COG4643    3 TNVKEVKAAARGRWPDILAALGLDPPAL-HGPCP-CGGKDRFRFDDKRGRksGWYVCNQCGppAGDGLDLLMKVFGWDFK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  77 EA----SSKV-----AECLNLRNTSTNSDLKSDLQDNIPENPVCKKVKYLLSKAI---LGQSDYLTEKGLT-FDLP---- 139
Cdd:COG4643   81 EAalglDAKGreltpEERAAARARAAAARAAREAEREARQAAAARRAAALWAEARpatPGDHPYLARKGLAaHGLRfhpa 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 140 -LLDNGRIFAPMLNLHNEYAGGQFIEPDGSKHLMKGSNKKSAFILVRSVLSRPAEvcanllahneIIICEGLATGISIAE 218
Cdd:COG4643  161 lLLPGGALLVPLTDADGELVTLQRIYLDGEKRFLKGGRKKGAFIRIGPLPPPGGT----------LLIAEGYATALSVHE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 219 FRlQSIVISAIDAGNLIHVAKGIRELNPTAKIIIAGDNDIGQSPNTGLAKAIEASQAVNGYYSVPDT--DYKCDWDDYRQ 296
Cdd:COG4643  231 AT-GLPVVAALDAGNLLPVAQALRERYPVAELIIAADNDRNTDGNPGQAAAEEAARAVGGLVALPPFppKKGTDFNDLHQ 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 297 QFGLEKVKQYFDSNIKNSLKGSFSEIKLksIPDLSQMQASQKADVLIEHYENNLSLDMVTNEVYIYKDNVWQMISEMDLK 376
Cdd:COG4643  310 ARGLEAVRAAFEAALYQPAGQTAAAVAL--ALAAVGSATAEVAAALALAPSAVEGVGLSEDDAAIAADLRWGAALRPSLG 387
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 644440803 377 RELVQLFRQSNAHYSEKGIKSTIDTMKLQIPLKNEPARNLIGFKNGVF 424
Cdd:COG4643  388 AAAGLRLLLAAEAGEDAAKKAALALTKLASLAAQLPLDGLSLSDALDG 435
primase_Cterm TIGR01613
phage/plasmid primase, P4 family, C-terminal domain; This model represents a clade within a ...
415-731 1.12e-25

phage/plasmid primase, P4 family, C-terminal domain; This model represents a clade within a larger family of proteins from viruses of bacteria and animals. Members of this family are found in phage and plasmids of bacteria and archaea only. The model describes a domain of about 300 residues, found generally toward the protein C-terminus. [DNA metabolism, DNA replication, recombination, and repair, Mobile and extrachromosomal element functions, Prophage functions]


Pssm-ID: 273716 [Multi-domain]  Cd Length: 304  Bit Score: 108.19  E-value: 1.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  415 NLIGFKNGVFDLDTRTFKSHSKNHWLQSInnvnfIDSVSNENLEhhAPNFYQWLSRSAKKDTIKMDAIKAALYMILANRY 494
Cdd:TIGR01613   1 YKLNVANGVYDLRTGQLEPHDPDEIHTRK-----ITTEYDPKAD--CPTWNGFLLETFGGDNELIEYLQRVIGYSLTGNY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  495 DWQLFLEVTGAGGSGKSVFAD-IATMLAGKNNTVSAN--MEALEKPR-ERSLIVGQSLIILPD-QAKYIGEGNGIKAITG 569
Cdd:TIGR01613  74 TEQKLFFLYGNGGNGKSTFQNlLSNLLGDYAITAVASlkMNELSEHRfGLARLEGKRAVIGDEvQKGYRDDESTFKSLTG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  570 GDDVAIDEKYKKPYS-TKIQGVILAINNNPmTFSNDDGGISRRRVIFHFGEPVPANERDPILKDKIRGELSVIIRHLFNY 648
Cdd:TIGR01613 154 GDTITARFKNKDPFEfTPKFTLVQSTNHLP-RIRGFDGGIKRRLRIIPFTKVFPGEKKNKALKEDYINEKDVILYWAVEG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  649 FEDDNKAKLLLIEQQKSSEAIEVKRLTNPLIDFCSYLFATDKPDgmmigkySTPVqfkRFLYHAYITFIENNNlKNPLSL 728
Cdd:TIGR01613 233 IRLDQRIGDFSIPKAVLEATEEYKEENDVVARFLEECCDDSEGE-------KVPV---RFVYEAYKEWCEEGG-YPILSR 301

                  ...
gi 644440803  729 RNF 731
Cdd:TIGR01613 302 NKF 304
Prim_Zn_Ribbon smart00778
Zinc-binding domain of primase-helicase; This region represents the zinc binding domain. It is ...
28-64 1.28e-19

Zinc-binding domain of primase-helicase; This region represents the zinc binding domain. It is found in the N-terminal region of the bacteriophage P4 alpha protein, which is a multifunctional protein with origin recognition, helicase and primase activities.


Pssm-ID: 129016 [Multi-domain]  Cd Length: 37  Bit Score: 82.38  E-value: 1.28e-19
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 644440803    28 GKHCPCPVCGGKDRFRFDNKNGRGTYICNQCGSGDGL 64
Cdd:smart00778   1 GRHGPCPNCGGSDRFRFDDKDGRGTWFCSVCGAGDGI 37
Prim_Zn_Ribbon pfam08273
Zinc-binding domain of primase-helicase;
28-64 3.17e-19

Zinc-binding domain of primase-helicase;


Pssm-ID: 400529  Cd Length: 37  Bit Score: 81.27  E-value: 3.17e-19
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 644440803   28 GKHCPCPVCGGKDRFRFDNKNGRGTYICNQCGSGDGL 64
Cdd:pfam08273   1 GYHGPCPVCGGRDRFRFDDKDGRGTWFCRVCGAGDGL 37
D5_N smart00885
D5 N terminal like; This domain is found in D5 proteins of DNA viruses and bacteriophage P4 ...
339-464 2.18e-15

D5 N terminal like; This domain is found in D5 proteins of DNA viruses and bacteriophage P4 DNA primases phages.


Pssm-ID: 197953 [Multi-domain]  Cd Length: 141  Bit Score: 73.55  E-value: 2.18e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803   339 ADVLIEHYENNLSLDMVTNEVYIYKDNVWQMISEMDLKRELVQLFR----------QSNAHYSEKGIKSTIDTMKLQIPL 408
Cdd:smart00885   1 AERLAEHYGDRLRYVPETGKWYVYDGGIWEPDEDLELARKLIRALLpeaaelserkKLRDEVKKALTASALEALLKEAPV 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 644440803   409 KNE---PARNLIGFKNGVFDLDTRTFKSHSKNHWLQSINNVNFIDSVSNENLEHHAPNF 464
Cdd:smart00885  81 TPEeldADPHLINFPNGVLDLRTGELRPHDPEDYITKKIPVAYDPNAKCPRWDGFLNEI 139
Pox_D5 pfam03288
Poxvirus D5 protein-like; This family includes D5 from Poxviruses which is necessary for viral ...
676-772 8.51e-10

Poxvirus D5 protein-like; This family includes D5 from Poxviruses which is necessary for viral DNA replication, and is a nucleic acid independent nucleoside triphosphatase. Members of this family are also found outside of poxviruses. This domain is a DNA-binding winged HTH domain.


Pssm-ID: 367437 [Multi-domain]  Cd Length: 85  Bit Score: 55.81  E-value: 8.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  676 NPLIDFCSYLFATDKpdgmmigkysTPVQFKRFLYHAYITFIENNNLKNPLSLRNFVNALPAAMKeyglEVIIRARHGEG 755
Cdd:pfam03288   3 DPVPDFLEELFVLDK----------SLRVPSDYLYHAYKAWCEKNGYKPVLSLRTFQKRLKKHLN----EGFIKKKKKYG 68
                          90
                  ....*....|....*..
gi 644440803  756 RRTNLHLDYDKCNDWFP 772
Cdd:pfam03288  69 NVPNEYLEYIFIDDLLP 85
TOPRIM_primases cd01029
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ...
202-278 2.75e-06

TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in the active site regions of bacterial DnaG-type primases and their homologs. Primases synthesize RNA primers for the initiation of DNA replication. DnaG type primases are often closely associated with DNA helicases in primosome assemblies. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. The prototypical bacterial primase. Escherichia coli DnaG is a single subunit enzyme.


Pssm-ID: 173779 [Multi-domain]  Cd Length: 79  Bit Score: 45.72  E-value: 2.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644440803 202 NEIIICEGLATGISIAEFRLQSiVISAIDAGNLIHVAKGIRELNPTakIIIAGDNDI-GQspnTGLAKAIEASQAVNG 278
Cdd:cd01029    1 DEVIIVEGYMDVLALHQAGIKN-VVAALGTANTEEQLRLLKRFART--VILAFDNDEaGK---KAAARALELLLALGG 72
PRK14709 PRK14709
hypothetical protein; Provisional
497-643 6.54e-04

hypothetical protein; Provisional


Pssm-ID: 173172 [Multi-domain]  Cd Length: 469  Bit Score: 43.17  E-value: 6.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 497 QLFLEVTGAGGSGKSVFADIATMLAGkNNTVSANMEAL------EKPRERSLIVGQSLIilpdQAKYIGEGNG-----IK 565
Cdd:PRK14709 205 HALVFVFGGGGNGKSVFLNVLAGILG-DYATTAAMDTFtaskhdRHPTDLAMLRGARLV----TASETEEGRAwaearIK 279
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644440803 566 AITGGDDVAIDEKYKKPYSTKIQGVILAINNNPMTFSNDDGGISRRRVIFHF-GEPvpaNERDPILKDKIRGELSVIIR 643
Cdd:PRK14709 280 QMTGGDTITARFMRQDFFEFVPQFKLTIVGNHKPRLRNVDEAARRRFNIVPFtRKP---ARPDPDLEAKLRAEWPAILR 355
anti_R_Lar TIGR03655
restriction alleviation protein, Lar family; Restriction alleviation proteins provide a ...
32-60 7.70e-03

restriction alleviation protein, Lar family; Restriction alleviation proteins provide a countermeasure to host cell restriction enzyme defense against foreign DNA such as phage or plasmids. This family consists of homologs to the phage antirestriction protein Lar, and most members belong to phage genomes or prophage regions of bacterial genomes. [Mobile and extrachromosomal element functions, Prophage functions, DNA metabolism, Restriction/modification]


Pssm-ID: 274704  Cd Length: 53  Bit Score: 35.13  E-value: 7.70e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 644440803   32 PCPVCGGKD---RFRFDNKNGRGTYICNQCGS 60
Cdd:TIGR03655   3 PCPFCGGADvylRRGFDPLDLSHYFECSDCGA 34
 
Name Accession Description Interval E-value
COG3378 COG3378
DNA primase, phage- or plasmid-associated [Mobilome: prophages, transposons];
356-765 7.23e-95

DNA primase, phage- or plasmid-associated [Mobilome: prophages, transposons];


Pssm-ID: 442605 [Multi-domain]  Cd Length: 403  Bit Score: 301.47  E-value: 7.23e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 356 TNEVYIYKDNVWQMISEmDLKRELVQLFRQSNAH-----YSEKGIKSTIDTMKLQIPLKNEPARNLIGFKNGVFDLDTRT 430
Cdd:COG3378    5 TGKWYVYDGGRWEEDDG-EVRRLIKELLRAILAKwakksRSSRRIKAVLELLKAELPDELDADPNLINVKNGVLDLRTGE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 431 FKSHSKNHWLQSINNVNFidsvsneNLEHHAPNFYQWLSRSAKKDTIKMDAIKAALYMILANRYDWQLFLEVTGAGGSGK 510
Cdd:COG3378   84 LRPHSPEDYLTKVLPVEY-------DPDAKCPRWLKFLDEIFPGDKELIDLLQEALGYCLTGRTSEQKFFFLYGPGGNGK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 511 SVFADIATMLAGKNNTVSANMEAL-EKPRERSLIVGQSLIILPDQ-AKYIGEGNGIKAITGGDDVAIDEKYKKPYSTKIQ 588
Cdd:COG3378  157 STFLNLLTALLGKDNASSASLETLtENRFDLARLKGKRLNIASELeEGYRLDESLLKALTGGDPITARRKYKDPFSFKPT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 589 GVILAINNNPMTFSNDDGGISRRRVIFHFGEPVPANERDPILKDKIRGELSVIIRHLFNYFEDDNKAKLLLIEQQKSSEA 668
Cdd:COG3378  237 AKLLFATNHLPRIRDTDDGIWRRLLIIPFNVTFPEEERDPNLKEKLLEELPGILNWALEGLLRLLENGGLTEPESVKEAT 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 669 IEVKRLTNPLIDFCSYLFATDKPDgmmigkystpVQFKRFLYHAYITFIENNNLKnPLSLRNFVNALPAAMKEYgleviI 748
Cdd:COG3378  317 EEYREESDPLGAFLEECCELDPGA----------RVPKKDLYEAYREWCEDNGEK-PLSKRTFGKELKKLGFEY-----E 380
                        410       420
                 ....*....|....*....|
gi 644440803 749 RARHGEGRR---TNLHLDYD 765
Cdd:COG3378  381 KRRTNGGKRrgyRGIRLKDD 400
COG4643 COG4643
Uncharacterized domain associated with phage/plasmid primase [Mobilome: prophages, transposons] ...
1-424 1.90e-94

Uncharacterized domain associated with phage/plasmid primase [Mobilome: prophages, transposons];


Pssm-ID: 443681 [Multi-domain]  Cd Length: 435  Bit Score: 301.78  E-value: 1.90e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803   1 MKINEITTQAVDKWQSIFNSLGIVVGNGkHCPCPvCGGKDRFRFDNKNGR--GTYICNQCG--SGDGLNLIKNYYHCDAK 76
Cdd:COG4643    3 TNVKEVKAAARGRWPDILAALGLDPPAL-HGPCP-CGGKDRFRFDDKRGRksGWYVCNQCGppAGDGLDLLMKVFGWDFK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  77 EA----SSKV-----AECLNLRNTSTNSDLKSDLQDNIPENPVCKKVKYLLSKAI---LGQSDYLTEKGLT-FDLP---- 139
Cdd:COG4643   81 EAalglDAKGreltpEERAAARARAAAARAAREAEREARQAAAARRAAALWAEARpatPGDHPYLARKGLAaHGLRfhpa 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 140 -LLDNGRIFAPMLNLHNEYAGGQFIEPDGSKHLMKGSNKKSAFILVRSVLSRPAEvcanllahneIIICEGLATGISIAE 218
Cdd:COG4643  161 lLLPGGALLVPLTDADGELVTLQRIYLDGEKRFLKGGRKKGAFIRIGPLPPPGGT----------LLIAEGYATALSVHE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 219 FRlQSIVISAIDAGNLIHVAKGIRELNPTAKIIIAGDNDIGQSPNTGLAKAIEASQAVNGYYSVPDT--DYKCDWDDYRQ 296
Cdd:COG4643  231 AT-GLPVVAALDAGNLLPVAQALRERYPVAELIIAADNDRNTDGNPGQAAAEEAARAVGGLVALPPFppKKGTDFNDLHQ 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 297 QFGLEKVKQYFDSNIKNSLKGSFSEIKLksIPDLSQMQASQKADVLIEHYENNLSLDMVTNEVYIYKDNVWQMISEMDLK 376
Cdd:COG4643  310 ARGLEAVRAAFEAALYQPAGQTAAAVAL--ALAAVGSATAEVAAALALAPSAVEGVGLSEDDAAIAADLRWGAALRPSLG 387
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 644440803 377 RELVQLFRQSNAHYSEKGIKSTIDTMKLQIPLKNEPARNLIGFKNGVF 424
Cdd:COG4643  388 AAAGLRLLLAAEAGEDAAKKAALALTKLASLAAQLPLDGLSLSDALDG 435
primase_Cterm TIGR01613
phage/plasmid primase, P4 family, C-terminal domain; This model represents a clade within a ...
415-731 1.12e-25

phage/plasmid primase, P4 family, C-terminal domain; This model represents a clade within a larger family of proteins from viruses of bacteria and animals. Members of this family are found in phage and plasmids of bacteria and archaea only. The model describes a domain of about 300 residues, found generally toward the protein C-terminus. [DNA metabolism, DNA replication, recombination, and repair, Mobile and extrachromosomal element functions, Prophage functions]


Pssm-ID: 273716 [Multi-domain]  Cd Length: 304  Bit Score: 108.19  E-value: 1.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  415 NLIGFKNGVFDLDTRTFKSHSKNHWLQSInnvnfIDSVSNENLEhhAPNFYQWLSRSAKKDTIKMDAIKAALYMILANRY 494
Cdd:TIGR01613   1 YKLNVANGVYDLRTGQLEPHDPDEIHTRK-----ITTEYDPKAD--CPTWNGFLLETFGGDNELIEYLQRVIGYSLTGNY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  495 DWQLFLEVTGAGGSGKSVFAD-IATMLAGKNNTVSAN--MEALEKPR-ERSLIVGQSLIILPD-QAKYIGEGNGIKAITG 569
Cdd:TIGR01613  74 TEQKLFFLYGNGGNGKSTFQNlLSNLLGDYAITAVASlkMNELSEHRfGLARLEGKRAVIGDEvQKGYRDDESTFKSLTG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  570 GDDVAIDEKYKKPYS-TKIQGVILAINNNPmTFSNDDGGISRRRVIFHFGEPVPANERDPILKDKIRGELSVIIRHLFNY 648
Cdd:TIGR01613 154 GDTITARFKNKDPFEfTPKFTLVQSTNHLP-RIRGFDGGIKRRLRIIPFTKVFPGEKKNKALKEDYINEKDVILYWAVEG 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  649 FEDDNKAKLLLIEQQKSSEAIEVKRLTNPLIDFCSYLFATDKPDgmmigkySTPVqfkRFLYHAYITFIENNNlKNPLSL 728
Cdd:TIGR01613 233 IRLDQRIGDFSIPKAVLEATEEYKEENDVVARFLEECCDDSEGE-------KVPV---RFVYEAYKEWCEEGG-YPILSR 301

                  ...
gi 644440803  729 RNF 731
Cdd:TIGR01613 302 NKF 304
Prim_Zn_Ribbon smart00778
Zinc-binding domain of primase-helicase; This region represents the zinc binding domain. It is ...
28-64 1.28e-19

Zinc-binding domain of primase-helicase; This region represents the zinc binding domain. It is found in the N-terminal region of the bacteriophage P4 alpha protein, which is a multifunctional protein with origin recognition, helicase and primase activities.


Pssm-ID: 129016 [Multi-domain]  Cd Length: 37  Bit Score: 82.38  E-value: 1.28e-19
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 644440803    28 GKHCPCPVCGGKDRFRFDNKNGRGTYICNQCGSGDGL 64
Cdd:smart00778   1 GRHGPCPNCGGSDRFRFDDKDGRGTWFCSVCGAGDGI 37
Prim_Zn_Ribbon pfam08273
Zinc-binding domain of primase-helicase;
28-64 3.17e-19

Zinc-binding domain of primase-helicase;


Pssm-ID: 400529  Cd Length: 37  Bit Score: 81.27  E-value: 3.17e-19
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 644440803   28 GKHCPCPVCGGKDRFRFDNKNGRGTYICNQCGSGDGL 64
Cdd:pfam08273   1 GYHGPCPVCGGRDRFRFDDKDGRGTWFCRVCGAGDGL 37
D5_N smart00885
D5 N terminal like; This domain is found in D5 proteins of DNA viruses and bacteriophage P4 ...
339-464 2.18e-15

D5 N terminal like; This domain is found in D5 proteins of DNA viruses and bacteriophage P4 DNA primases phages.


Pssm-ID: 197953 [Multi-domain]  Cd Length: 141  Bit Score: 73.55  E-value: 2.18e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803   339 ADVLIEHYENNLSLDMVTNEVYIYKDNVWQMISEMDLKRELVQLFR----------QSNAHYSEKGIKSTIDTMKLQIPL 408
Cdd:smart00885   1 AERLAEHYGDRLRYVPETGKWYVYDGGIWEPDEDLELARKLIRALLpeaaelserkKLRDEVKKALTASALEALLKEAPV 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 644440803   409 KNE---PARNLIGFKNGVFDLDTRTFKSHSKNHWLQSINNVNFIDSVSNENLEHHAPNF 464
Cdd:smart00885  81 TPEeldADPHLINFPNGVLDLRTGELRPHDPEDYITKKIPVAYDPNAKCPRWDGFLNEI 139
Pox_D5 pfam03288
Poxvirus D5 protein-like; This family includes D5 from Poxviruses which is necessary for viral ...
676-772 8.51e-10

Poxvirus D5 protein-like; This family includes D5 from Poxviruses which is necessary for viral DNA replication, and is a nucleic acid independent nucleoside triphosphatase. Members of this family are also found outside of poxviruses. This domain is a DNA-binding winged HTH domain.


Pssm-ID: 367437 [Multi-domain]  Cd Length: 85  Bit Score: 55.81  E-value: 8.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  676 NPLIDFCSYLFATDKpdgmmigkysTPVQFKRFLYHAYITFIENNNLKNPLSLRNFVNALPAAMKeyglEVIIRARHGEG 755
Cdd:pfam03288   3 DPVPDFLEELFVLDK----------SLRVPSDYLYHAYKAWCEKNGYKPVLSLRTFQKRLKKHLN----EGFIKKKKKYG 68
                          90
                  ....*....|....*..
gi 644440803  756 RRTNLHLDYDKCNDWFP 772
Cdd:pfam03288  69 NVPNEYLEYIFIDDLLP 85
D5_N pfam08706
D5 N terminal like; This domain is found in D5 proteins of DNA viruses and bacteriophage P4 ...
339-468 1.33e-09

D5 N terminal like; This domain is found in D5 proteins of DNA viruses and bacteriophage P4 DNA primases phages.


Pssm-ID: 378029 [Multi-domain]  Cd Length: 145  Bit Score: 57.09  E-value: 1.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  339 ADVLIEHYENNLSLDMVTNEVYIYKDNVWQmISEMDLKRELVQ---------------LFRQSNAHYSEKGIKSTIDTMK 403
Cdd:pfam08706   1 AERLRDRYGKDLRYVPGLGGWYVWDGKRWR-EDSKKAIRELADkllrkilreaealkeLRKFAKRSRSKKGVKNVLKEAK 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644440803  404 LQIPLKNEP---ARNLIGFKNGVFDLDTRTFKSHSKNHWLQSINNVNFIDSVSnenlehhAPNFYQWL 468
Cdd:pfam08706  80 AMLDVTLDEldaDPYLLNFPNGVLDLRTGELRPHDPEDRLTKITPVDYDPDAD-------CPEWKQFL 140
Toprim_3 pfam13362
Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic ...
204-299 5.10e-08

Toprim domain; The toprim domain is found in a wide variety of enzymes involved in nucleic acid manipulation.


Pssm-ID: 433146 [Multi-domain]  Cd Length: 97  Bit Score: 51.25  E-value: 5.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  204 IIICEGLATGISIAEFRLQS--IVISAIDAGNLihvaKGIRELNPTAKIIIAGDND---IGQSpntGLAKAIEASQAVNG 278
Cdd:pfam13362   2 LIIGEGIETALSLTQRLNPPgtPVIALLSAANL----KAVAWPERVKRVYIAADNDaanDGQA---AAEKLAERLEAAGI 74
                          90       100
                  ....*....|....*....|.
gi 644440803  279 YYSVPDTDYKCDWDDYRQQFG 299
Cdd:pfam13362  75 EAVLLEPEAGEDWNDDLQQTG 95
TOPRIM_primases cd01029
TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain ...
202-278 2.75e-06

TOPRIM_primases: The topoisomerase-primase (TOPRIM) nucleotidyl transferase/hydrolase domain found in the active site regions of bacterial DnaG-type primases and their homologs. Primases synthesize RNA primers for the initiation of DNA replication. DnaG type primases are often closely associated with DNA helicases in primosome assemblies. The TOPRIM domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function. The prototypical bacterial primase. Escherichia coli DnaG is a single subunit enzyme.


Pssm-ID: 173779 [Multi-domain]  Cd Length: 79  Bit Score: 45.72  E-value: 2.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 644440803 202 NEIIICEGLATGISIAEFRLQSiVISAIDAGNLIHVAKGIRELNPTakIIIAGDNDI-GQspnTGLAKAIEASQAVNG 278
Cdd:cd01029    1 DEVIIVEGYMDVLALHQAGIKN-VVAALGTANTEEQLRLLKRFART--VILAFDNDEaGK---KAAARALELLLALGG 72
DUF5906 pfam19263
Family of unknown function (DUF5906); This is a family of proteins of unknown function found ...
506-612 5.38e-06

Family of unknown function (DUF5906); This is a family of proteins of unknown function found in viruses. This family is a P-loop member whose proteins are thought to be SF3 helicases, which are involved in replication initiation.


Pssm-ID: 466016 [Multi-domain]  Cd Length: 114  Bit Score: 45.83  E-value: 5.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803  506 GGSGKSVFAD--IATMLAGKNNTVSANMEALEKPRERSLiVGQSLIILPDQAKYIGEGNG----IKAITGGDdVAIDEKY 579
Cdd:pfam19263   6 QGTGKSTLLEfiLGKLLGPSNVTALSDLLKLLGRFNSAL-QGKLLIIIDEIGMASGEWHKangrLKSLITEP-ISIERKG 83
                          90       100       110
                  ....*....|....*....|....*....|...
gi 644440803  580 KKPYSTKIQGVILAINNNPMTFSNDDGgiSRRR 612
Cdd:pfam19263  84 KDPYEVKNYARFIFTSNHNWPLPAEDD--DDRR 114
PRK14709 PRK14709
hypothetical protein; Provisional
497-643 6.54e-04

hypothetical protein; Provisional


Pssm-ID: 173172 [Multi-domain]  Cd Length: 469  Bit Score: 43.17  E-value: 6.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 497 QLFLEVTGAGGSGKSVFADIATMLAGkNNTVSANMEAL------EKPRERSLIVGQSLIilpdQAKYIGEGNG-----IK 565
Cdd:PRK14709 205 HALVFVFGGGGNGKSVFLNVLAGILG-DYATTAAMDTFtaskhdRHPTDLAMLRGARLV----TASETEEGRAwaearIK 279
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644440803 566 AITGGDDVAIDEKYKKPYSTKIQGVILAINNNPMTFSNDDGGISRRRVIFHF-GEPvpaNERDPILKDKIRGELSVIIR 643
Cdd:PRK14709 280 QMTGGDTITARFMRQDFFEFVPQFKLTIVGNHKPRLRNVDEAARRRFNIVPFtRKP---ARPDPDLEAKLRAEWPAILR 355
zf-RRN7 pfam11781
Zinc-finger of RNA-polymerase I-specific TFIIB, Rrn7; This is the zinc-finger at the start of ...
32-60 2.71e-03

Zinc-finger of RNA-polymerase I-specific TFIIB, Rrn7; This is the zinc-finger at the start of transcription-binding factor that associates strongly with both Rrn6 and Rrn7 to form a complex which itself binds the TATA-binding protein and is required for transcription by the core domain of the RNA PolI promoter.


Pssm-ID: 463348  Cd Length: 32  Bit Score: 36.03  E-value: 2.71e-03
                          10        20
                  ....*....|....*....|....*....
gi 644440803   32 PCPVCGGkDRFRFDNkngrGTYICNQCGS 60
Cdd:pfam11781   6 PCGVCGC-RLFYLDD----GFYYCRRCHT 29
TOPRIM cd00188
Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type ...
202-257 3.76e-03

Topoisomerase-primase domain. This is a nucleotidyl transferase/hydrolase domain found in type IA, type IIA and type IIB topoisomerases, bacterial DnaG-type primases, small primase-like proteins from bacteria and archaea, OLD family nucleases from bacterial and archaea, and bacterial DNA repair proteins of the RecR/M family. This domain has two conserved motifs, one of which centers at a conserved glutamate and the other one at two conserved aspartates (DxD). This glutamate and two aspartates, cluster together to form a highly acid surface patch. The conserved glutamate may act as a general base in nucleotide polymerization by primases and in strand joining in topoisomerases and, as a general acid in strand cleavage by topisomerases and nucleases. The DXD motif may co-ordinate Mg2+, a cofactor required for full catalytic function.


Pssm-ID: 173773 [Multi-domain]  Cd Length: 83  Bit Score: 37.02  E-value: 3.76e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 644440803 202 NEIIICEGLATGISIAEFRLQSIVISAIDAGNLIHVAKGIRELNPTAK-IIIAGDND 257
Cdd:cd00188    1 KKLIIVEGPSDALALAQAGGYGGAVVALGGHALNKTRELLKRLLGEAKeVIIATDAD 57
TOPRIM smart00493
topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;
202-279 4.96e-03

topoisomerases, DnaG-type primases, OLD family nucleases and RecR proteins;


Pssm-ID: 214695 [Multi-domain]  Cd Length: 75  Bit Score: 36.47  E-value: 4.96e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 644440803   202 NEIIICEGLATGISIAEFR-LQSIVISAIDAGNLIHVAKGIRELNPTAKIIIAGDNDIGqspntGLAKAIEASQAVNGY 279
Cdd:smart00493   1 KVLIIVEGPADAIALEKAGgKRGNVVALGGHLLSKEQIKLLKKLAKKAEVILATDPDRE-----GEAIAWELAELLKPA 74
anti_R_Lar TIGR03655
restriction alleviation protein, Lar family; Restriction alleviation proteins provide a ...
32-60 7.70e-03

restriction alleviation protein, Lar family; Restriction alleviation proteins provide a countermeasure to host cell restriction enzyme defense against foreign DNA such as phage or plasmids. This family consists of homologs to the phage antirestriction protein Lar, and most members belong to phage genomes or prophage regions of bacterial genomes. [Mobile and extrachromosomal element functions, Prophage functions, DNA metabolism, Restriction/modification]


Pssm-ID: 274704  Cd Length: 53  Bit Score: 35.13  E-value: 7.70e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 644440803   32 PCPVCGGKD---RFRFDNKNGRGTYICNQCGS 60
Cdd:TIGR03655   3 PCPFCGGADvylRRGFDPLDLSHYFECSDCGA 34
PRK08417 PRK08417
metal-dependent hydrolase;
267-471 8.50e-03

metal-dependent hydrolase;


Pssm-ID: 236262 [Multi-domain]  Cd Length: 386  Bit Score: 39.30  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 267 AKAIEASQAVNGYYSVPDTDYKcdwddyrQQFGLEKVKQYFDSNIKNS---LKGSFS-EIKLKSIPDLSQMQASQKADVL 342
Cdd:PRK08417 118 AKALELSSDLDANLLKVIAQYA-------KMLDVPIFCRCEDSSFDDSgvmNDGELSfELGLPGIPSIAETKEVAKMKEL 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 644440803 343 IEHYENNLSLDMVTNEVYIYKDNvwqmisemDLKRELVQLFRQSNAHY---SEKGIKSTIDTMKLQIPLKNEPARNLI-- 417
Cdd:PRK08417 191 AKFYKNKVLFDTLALPRSLELLD--------KFKSEGEKLLKEVSIHHlilDDSACENFNTAAKLNPPLRSKEDRLALle 262
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 644440803 418 GFKNGVFDLDTRTFKSHSKNHWLQSINNVNF-IDSvsnenLEHHAPNFYQWLSRS 471
Cdd:PRK08417 263 ALKEGKIDFLTSLHSAKSNSKKDLAFDEAAFgIDS-----ICEYFSLCYTYLVKE 312
 
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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