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Conserved domains on  [gi|1125288690|gb|OLC32717|]
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single-stranded DNA-binding protein [Armatimonadetes bacterium 13_1_40CM_64_14]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SpoIIIAA COG3854
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ...
 17-297 7.28e-124

Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 443063  Cd Length: 309  Bit Score: 364.47  E-value: 7.28e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690  17 AVLPDRVRDVLQQ--QGDLEMLLEVVLDLGRHLEARFPNRVLHLGDDY-ATHDDIRHVTSRVGA---------------- 77
Cdd:COG3854     7 AILPPTIREALEKlpDPVLDKLEEIRLRLGRPLELRFPGGEYFLSEAYpVTREDLERTLNRISNyslyaleeelrqgyit 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690  78 FGKDNRAGIERTLHRISAIRNRQGEVIGLTCRVGRAVVGTVDIVRDVIESGK---SILLLGRPGVGKTTLLREAARVMAD 154
Cdd:COG3854    87 IPGGHRVGIAGTVVRESGIVKRIKDISGLNIRIAREVKGTADPILPYIISGGriyNTLIISPPGCGKTTLLRDIARVLSD 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 155 EF----AKRVVVVDTSNEIAGD-GDIPHPGIGRarRMQVPHPELQHAVMIEAVENHMPQVIVIDEIGTEAEALAARTIAE 229
Cdd:COG3854   167 GLlgfpGKRVGVVDERSEIAGCyGGIPQPDIGI--RTDVLDGCPKAEGMIMAIRSMSPEVIVVDEIGREEDAEALREAAN 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125288690 230 RGVQLIATAHGNTLDNLLQNPTLCDLIGGI---QAVTLSDEEArrRGTQKTVLERKApptfDVVIEIQDKD 297
Cdd:COG3854   245 AGVQLIATAHGNSLEDLLKRPTLSDLIGGGvfeRYVTLSRREG--PGTVETILDRKA----DVLVEMLERD 309
R3H_AAA cd02645
R3H domain of a group of proteins with unknown function, who also contain a AAA-ATPase (AAA) ...
 454-511 2.49e-16

R3H domain of a group of proteins with unknown function, who also contain a AAA-ATPase (AAA) domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA or ssRNA in a sequence-specific manner.


:

Pssm-ID: 100074  Cd Length: 60  Bit Score: 73.08  E-value: 2.49e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1125288690 454 ALREVEGAISEVLKS-TQPVELSPQNSYVRRLQHQLIQRYGLASESRGEEPFRRVVVFP 511
Cdd:cd02645     2 ALEEARLAIEQVVIPkGEPVELLPRSAYIRRLQHDLVERYQLRSESFGSEPNRRLRILP 60
 
Name Accession Description Interval E-value
SpoIIIAA COG3854
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ...
 17-297 7.28e-124

Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443063  Cd Length: 309  Bit Score: 364.47  E-value: 7.28e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690  17 AVLPDRVRDVLQQ--QGDLEMLLEVVLDLGRHLEARFPNRVLHLGDDY-ATHDDIRHVTSRVGA---------------- 77
Cdd:COG3854     7 AILPPTIREALEKlpDPVLDKLEEIRLRLGRPLELRFPGGEYFLSEAYpVTREDLERTLNRISNyslyaleeelrqgyit 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690  78 FGKDNRAGIERTLHRISAIRNRQGEVIGLTCRVGRAVVGTVDIVRDVIESGK---SILLLGRPGVGKTTLLREAARVMAD 154
Cdd:COG3854    87 IPGGHRVGIAGTVVRESGIVKRIKDISGLNIRIAREVKGTADPILPYIISGGriyNTLIISPPGCGKTTLLRDIARVLSD 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 155 EF----AKRVVVVDTSNEIAGD-GDIPHPGIGRarRMQVPHPELQHAVMIEAVENHMPQVIVIDEIGTEAEALAARTIAE 229
Cdd:COG3854   167 GLlgfpGKRVGVVDERSEIAGCyGGIPQPDIGI--RTDVLDGCPKAEGMIMAIRSMSPEVIVVDEIGREEDAEALREAAN 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125288690 230 RGVQLIATAHGNTLDNLLQNPTLCDLIGGI---QAVTLSDEEArrRGTQKTVLERKApptfDVVIEIQDKD 297
Cdd:COG3854   245 AGVQLIATAHGNSLEDLLKRPTLSDLIGGGvfeRYVTLSRREG--PGTVETILDRKA----DVLVEMLERD 309
spore_III_AA TIGR02858
stage III sporulation protein AA; Members of this protein are the stage III sporulation ...
 62-256 3.16e-19

stage III sporulation protein AA; Members of this protein are the stage III sporulation protein AA, encoded by one of several genes in the spoIIIA locus. It seems that this protein is found in a species if and only if that species is capable of endospore formation. [Cellular processes, Sporulation and germination]


Pssm-ID: 274324  Cd Length: 270  Bit Score: 87.40  E-value: 3.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690  62 YATHDDIR--HVT----SRVGAFGKDNRAGiertlHRISAIRNrqgeVIGLTCRVGRAVVGTVD-IVRDVIESGK--SIL 132
Cdd:TIGR02858  45 YAFEEELKqgYITieggHRVGLAGRCVTEN-----GKVKTIKN----VSSLNIRIAREKLGAADkLLPYLVRNNRvlNTL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 133 LLGRPGVGKTTLLREAARVMADEFAK------RVVVVDTSNEIAG--DGdIPHPGIGRarRMQV----PHPElqhaVMIE 200
Cdd:TIGR02858 116 IISPPQCGKTTLLRDLARILSTGISQlglrgkKVGIVDERSEIAGcvNG-VPQHDVGI--RTDVldgcPKAE----GMMM 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1125288690 201 AVENHMPQVIVIDEIGTEAEALAARTIAERGVQLIATAHGNTLDNLLQNPTLCDLI 256
Cdd:TIGR02858 189 LIRSMSPDVIVVDEIGREEDVEALLEALHAGVSIIATAHGRDVEDLYKRPVFKELI 244
R3H_AAA cd02645
R3H domain of a group of proteins with unknown function, who also contain a AAA-ATPase (AAA) ...
 454-511 2.49e-16

R3H domain of a group of proteins with unknown function, who also contain a AAA-ATPase (AAA) domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100074  Cd Length: 60  Bit Score: 73.08  E-value: 2.49e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1125288690 454 ALREVEGAISEVLKS-TQPVELSPQNSYVRRLQHQLIQRYGLASESRGEEPFRRVVVFP 511
Cdd:cd02645     2 ALEEARLAIEQVVIPkGEPVELLPRSAYIRRLQHDLVERYQLRSESFGSEPNRRLRILP 60
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
436-512 3.75e-14

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 67.71  E-value: 3.75e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125288690  436 QKFLRSLFEVEDVDEQEVALREVEGAISEVLKSTQPVELSPQNSYVRRLQHQLIQRYGLASESRGEEPFRRVVVFPR 512
Cdd:smart00393   3 FLPVTLDALSYRPRRREELIELELEIARFVKSTKESVELPPMNSYERKIVHELAEKYGLESESFGEGPKRRVVISKK 79
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
 455-511 1.60e-13

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 65.21  E-value: 1.60e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1125288690 455 LREVEGAISEVLKST-QPVELSPQNSYVRRLQHQLIQRYGLASESRGEEPFRRVVVFP 511
Cdd:pfam01424   3 LEQLAEKLAEFVKDTgKSLELPPMSSYERRIIHELAQKYGLESESEGEEPNRRVVVYK 60
Jag COG1847
Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General ...
 424-512 1.04e-11

Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General function prediction only];


Pssm-ID: 441452 [Multi-domain]  Cd Length: 143  Bit Score: 62.44  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 424 QHVLKSNTANQIQKFLRSLFEVEDVDE-QEVALRE-VEGAISEVLKSTQPVELSPQNSYVRRLQHQLIQRY-GLASESRG 500
Cdd:COG1847    51 QYLTNLAVNRKTGERSRVILDVEGYRErREEELEElARRAAEKVKRTGKPVELEPMSPYERRIIHDALADDpGVETESEG 130

                          90
                  ....*....|..
gi 1125288690 501 EEPFRRVVVFPR 512
Cdd:COG1847   131 EEPYRRVVISPK 142
Spore_III_AA pfam19568
Sporulation stage III, protein AA;
106-256 1.18e-09

Sporulation stage III, protein AA;


Pssm-ID: 437400  Cd Length: 306  Bit Score: 59.42  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 106 LTCRVGRAVVGTVDIVRDVIESGKSI---LLLGRPGVGKTTLLREAARVMADEFAKR----VVVVDTSNEIAG-DGDIPH 177
Cdd:pfam19568 119 LNIRLAHEVRGCADGVMPYIWCNEEVrhtLIISPPRCGKTTLLRDMIRQISDGNQYVpgvtVGVVDERSELGAcYLGVPQ 198

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125288690 178 PGIGRARRMQVPHPELQHAVMIeaVENHMPQVIVIDEIGTEAEALAARTIAERGVQLIATAHGNTLDNLLQNPTLCDLI 256
Cdd:pfam19568 199 NDLGRRTDILDCCPKAEGMIML--IRSMSPTVVAVDEIGGQEDIEALEYAMNCGCTIIATVHGACMEDISNRPVLRRLI 275
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 127-239 1.19e-09

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 57.00  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690  127 SGKSILLLGRPGVGKTTLLREAARvMADEFAKRVVVVDTSNEIAGDGDIPHpGIGRARRMQVPHPELQHAVMIEAVENHM 206
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAR-ELGPPGGGVIYIDGEDILEEVLDQLL-LIIVGGKKASGSGELRLRLALALARKLK 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1125288690  207 PQVIVIDEIGT-------------EAEALAARTIAERGVQLIATAH 239
Cdd:smart00382  79 PDVLILDEITSlldaeqealllllEELRLLLLLKSEKNLTVILTTN 124
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 118-225 1.33e-07

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 50.99  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 118 VDIVRDVIE--SGKSILLLGRPGVGKTTLLREAARVMADEFAkRVVVVDTSNEIAGDGDIPHPGIGRARRMQvphpelqh 195
Cdd:cd00009     7 IEALREALElpPPKNLLLYGPPGTGKTTLARAIANELFRPGA-PFLYLNASDLLEGLVVAELFGHFLVRLLF-------- 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1125288690 196 avmiEAVENHMPQVIVIDEIGTEAEALAAR 225
Cdd:cd00009    78 ----ELAEKAKPGVLFIDEIDSLSRGAQNA 103
Jag_EloR NF041568
RNA-binding cell elongation regulator Jag/EloR; Members of this family are nucleic ...
 465-511 8.79e-05

RNA-binding cell elongation regulator Jag/EloR; Members of this family are nucleic acid-binding proteins (RNA or single-stranded DNA) with a KH domain at the N-terminus, an R3H domain at the C-terminus, and additional regions of homology. The founding member of this family was JAG (spoIIIJ Associated Gene) from Bacillus subtilis, but later work in other lineages, such as Streptococcus pneumoniae, as established a role in controlling cell elongation and the operation of the elongasome. The S. pneumoniae protein, a protein that undergoes regulatory phosphorylation and dephosphorylation, is also called RNA-binding cell elongation regulator EloR, and also KhpB.


Pssm-ID: 469453 [Multi-domain]  Cd Length: 203  Bit Score: 43.58  E-value: 8.79e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1125288690 465 VLKSTQPVELSPQNSYVRRLQHQLIQRY-GLASESRGEEPFRRVVVFP 511
Cdd:NF041568  156 VKRTKKPVVLEPMPSYERKIIHTALQNHpDVETYSEGEEPNRKVVIAP 203
flhF PRK14722
flagellar biosynthesis regulator FlhF; Provisional
 124-284 1.16e-04

flagellar biosynthesis regulator FlhF; Provisional


Pssm-ID: 173185 [Multi-domain]  Cd Length: 374  Bit Score: 44.33  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 124 VIESGKSILLLGRPGVGKTTLLRE-AARVMADEFAKRVVVVDT-SNEIAGDGD---------IPHPGIGRARRMQVPHPE 192
Cdd:PRK14722  133 LMERGGVFALMGPTGVGKTTTTAKlAARCVMRFGASKVALLTTdSYRIGGHEQlrifgkilgVPVHAVKDGGDLQLALAE 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 193 L--QHAVMIEAVENHMPQVIVIDEIgteAEALAARTIAERGVQLIATAHGNTLDNLLQ---------NPTLCDLIGGIqa 261
Cdd:PRK14722  213 LrnKHMVLIDTIGMSQRDRTVSDQI---AMLHGADTPVQRLLLLNATSHGDTLNEVVQayrsaagqpKAALPDLAGCI-- 287

                         170       180
                  ....*....|....*....|...
gi 1125288690 262 VTLSDEEARRRGTQKTVLERKAP 284
Cdd:PRK14722  288 LTKLDEASNLGGVLDTVIRYKLP 310
 
Name Accession Description Interval E-value
SpoIIIAA COG3854
Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ...
 17-297 7.28e-124

Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443063  Cd Length: 309  Bit Score: 364.47  E-value: 7.28e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690  17 AVLPDRVRDVLQQ--QGDLEMLLEVVLDLGRHLEARFPNRVLHLGDDY-ATHDDIRHVTSRVGA---------------- 77
Cdd:COG3854     7 AILPPTIREALEKlpDPVLDKLEEIRLRLGRPLELRFPGGEYFLSEAYpVTREDLERTLNRISNyslyaleeelrqgyit 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690  78 FGKDNRAGIERTLHRISAIRNRQGEVIGLTCRVGRAVVGTVDIVRDVIESGK---SILLLGRPGVGKTTLLREAARVMAD 154
Cdd:COG3854    87 IPGGHRVGIAGTVVRESGIVKRIKDISGLNIRIAREVKGTADPILPYIISGGriyNTLIISPPGCGKTTLLRDIARVLSD 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 155 EF----AKRVVVVDTSNEIAGD-GDIPHPGIGRarRMQVPHPELQHAVMIEAVENHMPQVIVIDEIGTEAEALAARTIAE 229
Cdd:COG3854   167 GLlgfpGKRVGVVDERSEIAGCyGGIPQPDIGI--RTDVLDGCPKAEGMIMAIRSMSPEVIVVDEIGREEDAEALREAAN 244

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1125288690 230 RGVQLIATAHGNTLDNLLQNPTLCDLIGGI---QAVTLSDEEArrRGTQKTVLERKApptfDVVIEIQDKD 297
Cdd:COG3854   245 AGVQLIATAHGNSLEDLLKRPTLSDLIGGGvfeRYVTLSRREG--PGTVETILDRKA----DVLVEMLERD 309
spore_III_AA TIGR02858
stage III sporulation protein AA; Members of this protein are the stage III sporulation ...
 62-256 3.16e-19

stage III sporulation protein AA; Members of this protein are the stage III sporulation protein AA, encoded by one of several genes in the spoIIIA locus. It seems that this protein is found in a species if and only if that species is capable of endospore formation. [Cellular processes, Sporulation and germination]


Pssm-ID: 274324  Cd Length: 270  Bit Score: 87.40  E-value: 3.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690  62 YATHDDIR--HVT----SRVGAFGKDNRAGiertlHRISAIRNrqgeVIGLTCRVGRAVVGTVD-IVRDVIESGK--SIL 132
Cdd:TIGR02858  45 YAFEEELKqgYITieggHRVGLAGRCVTEN-----GKVKTIKN----VSSLNIRIAREKLGAADkLLPYLVRNNRvlNTL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 133 LLGRPGVGKTTLLREAARVMADEFAK------RVVVVDTSNEIAG--DGdIPHPGIGRarRMQV----PHPElqhaVMIE 200
Cdd:TIGR02858 116 IISPPQCGKTTLLRDLARILSTGISQlglrgkKVGIVDERSEIAGcvNG-VPQHDVGI--RTDVldgcPKAE----GMMM 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1125288690 201 AVENHMPQVIVIDEIGTEAEALAARTIAERGVQLIATAHGNTLDNLLQNPTLCDLI 256
Cdd:TIGR02858 189 LIRSMSPDVIVVDEIGREEDVEALLEALHAGVSIIATAHGRDVEDLYKRPVFKELI 244
R3H_AAA cd02645
R3H domain of a group of proteins with unknown function, who also contain a AAA-ATPase (AAA) ...
 454-511 2.49e-16

R3H domain of a group of proteins with unknown function, who also contain a AAA-ATPase (AAA) domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100074  Cd Length: 60  Bit Score: 73.08  E-value: 2.49e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1125288690 454 ALREVEGAISEVLKS-TQPVELSPQNSYVRRLQHQLIQRYGLASESRGEEPFRRVVVFP 511
Cdd:cd02645     2 ALEEARLAIEQVVIPkGEPVELLPRSAYIRRLQHDLVERYQLRSESFGSEPNRRLRILP 60
R3H smart00393
Putative single-stranded nucleic acids-binding domain;
436-512 3.75e-14

Putative single-stranded nucleic acids-binding domain;


Pssm-ID: 214647  Cd Length: 79  Bit Score: 67.71  E-value: 3.75e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1125288690  436 QKFLRSLFEVEDVDEQEVALREVEGAISEVLKSTQPVELSPQNSYVRRLQHQLIQRYGLASESRGEEPFRRVVVFPR 512
Cdd:smart00393   3 FLPVTLDALSYRPRRREELIELELEIARFVKSTKESVELPPMNSYERKIVHELAEKYGLESESFGEGPKRRVVISKK 79
R3H pfam01424
R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most ...
 455-511 1.60e-13

R3H domain; The name of the R3H domain comes from the characteriztic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to be binding ssDNA.


Pssm-ID: 460206  Cd Length: 60  Bit Score: 65.21  E-value: 1.60e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1125288690 455 LREVEGAISEVLKST-QPVELSPQNSYVRRLQHQLIQRYGLASESRGEEPFRRVVVFP 511
Cdd:pfam01424   3 LEQLAEKLAEFVKDTgKSLELPPMSSYERRIIHELAQKYGLESESEGEEPNRRVVVYK 60
R3H cd02325
R3H domain. The name of the R3H domain comes from the characteristic spacing of the most ...
 455-511 2.18e-13

R3H domain. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. R3H domains are found in proteins together with ATPase domains, SF1 helicase domains, SF2 DEAH helicase domains, Cys-rich repeats, ring-type zinc fingers, and KH domains. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100064  Cd Length: 59  Bit Score: 64.56  E-value: 2.18e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1125288690 455 LREVEGAISEVLKST--QPVELSPQNSYVRRLQHQLIQRYGLASESRGEEPFRRVVVFP 511
Cdd:cd02325     1 REEREEELEAFAKDAagKSLELPPMNSYERKLIHDLAEYYGLKSESEGEGPNRRVVITK 59
Jag COG1847
Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General ...
 424-512 1.04e-11

Predicted RNA-binding protein Jag (SpoIIIJ-associated), conains KH and R3H domains [General function prediction only];


Pssm-ID: 441452 [Multi-domain]  Cd Length: 143  Bit Score: 62.44  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 424 QHVLKSNTANQIQKFLRSLFEVEDVDE-QEVALRE-VEGAISEVLKSTQPVELSPQNSYVRRLQHQLIQRY-GLASESRG 500
Cdd:COG1847    51 QYLTNLAVNRKTGERSRVILDVEGYRErREEELEElARRAAEKVKRTGKPVELEPMSPYERRIIHDALADDpGVETESEG 130

                          90
                  ....*....|..
gi 1125288690 501 EEPFRRVVVFPR 512
Cdd:COG1847   131 EEPYRRVVISPK 142
R3H_jag cd02644
R3H domain found in proteins homologous to Bacillus subtilus Jag, which is associated with ...
 449-512 3.35e-10

R3H domain found in proteins homologous to Bacillus subtilus Jag, which is associated with SpoIIIJ. SpoIIIJ is necessary for the third stage of sporulation. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100073  Cd Length: 67  Bit Score: 55.94  E-value: 3.35e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1125288690 449 DEQEVALRE-VEGAISEVLKSTQPVELSPQNSYVRRLQHQLIQRY-GLASESRGEEPFRRVVVFPR 512
Cdd:cd02644     2 ERREETLIRlAERAAEKVRRTGKPVKLEPMNAYERRIIHDALANDeDVETESEGEGPYRRVVISPK 67
Spore_III_AA pfam19568
Sporulation stage III, protein AA;
106-256 1.18e-09

Sporulation stage III, protein AA;


Pssm-ID: 437400  Cd Length: 306  Bit Score: 59.42  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 106 LTCRVGRAVVGTVDIVRDVIESGKSI---LLLGRPGVGKTTLLREAARVMADEFAKR----VVVVDTSNEIAG-DGDIPH 177
Cdd:pfam19568 119 LNIRLAHEVRGCADGVMPYIWCNEEVrhtLIISPPRCGKTTLLRDMIRQISDGNQYVpgvtVGVVDERSELGAcYLGVPQ 198

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1125288690 178 PGIGRARRMQVPHPELQHAVMIeaVENHMPQVIVIDEIGTEAEALAARTIAERGVQLIATAHGNTLDNLLQNPTLCDLI 256
Cdd:pfam19568 199 NDLGRRTDILDCCPKAEGMIML--IRSMSPTVVAVDEIGGQEDIEALEYAMNCGCTIIATVHGACMEDISNRPVLRRLI 275
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 127-239 1.19e-09

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 57.00  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690  127 SGKSILLLGRPGVGKTTLLREAARvMADEFAKRVVVVDTSNEIAGDGDIPHpGIGRARRMQVPHPELQHAVMIEAVENHM 206
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALAR-ELGPPGGGVIYIDGEDILEEVLDQLL-LIIVGGKKASGSGELRLRLALALARKLK 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1125288690  207 PQVIVIDEIGT-------------EAEALAARTIAERGVQLIATAH 239
Cdd:smart00382  79 PDVLILDEITSlldaeqealllllEELRLLLLLKSEKNLTVILTTN 124
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 118-225 1.33e-07

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 50.99  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 118 VDIVRDVIE--SGKSILLLGRPGVGKTTLLREAARVMADEFAkRVVVVDTSNEIAGDGDIPHPGIGRARRMQvphpelqh 195
Cdd:cd00009     7 IEALREALElpPPKNLLLYGPPGTGKTTLARAIANELFRPGA-PFLYLNASDLLEGLVVAELFGHFLVRLLF-------- 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 1125288690 196 avmiEAVENHMPQVIVIDEIGTEAEALAAR 225
Cdd:cd00009    78 ----ELAEKAKPGVLFIDEIDSLSRGAQNA 103
RadA_SMS_N cd01121
bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a ...
 131-217 3.52e-06

bacterial RadA DNA repair protein; Sms or bacterial RadA is a DNA repair protein that plays a role in recombination and recombinational repair of DNA damaged by UV radiation, X-rays, and chemical agent and is responsible for the stabilization or processing of branched DNA molecules.


Pssm-ID: 410866 [Multi-domain]  Cd Length: 268  Bit Score: 48.68  E-value: 3.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 131 ILLLGRPGVGKTTLLREAARVMADEfAKRVVVV---DTSNEIAgdgdiphpgiGRARRMQVPHPELQHA------VMIEA 201
Cdd:cd01121    85 VLIGGDPGIGKSTLLLQVAARLAQR-GGKVLYVsgeESLSQIK----------LRAERLGLGSDNLYLLaetnleAILAE 153

                          90
                  ....*....|....*.
gi 1125288690 202 VENHMPQVIVIDEIGT 217
Cdd:cd01121   154 IEELKPSLVVIDSIQT 169
Sms COG1066
DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and ...
 131-217 4.12e-05

DNA repair protein RadA/Sms, contains AAA+ ATPase domain [Replication, recombination and repair];


Pssm-ID: 440685 [Multi-domain]  Cd Length: 453  Bit Score: 45.81  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 131 ILLLGRPGVGKTTLLREAARVMADEfAKRVVVVdtSNE-----IAgdgdiphpgiGRARRMQVPHPELQHA------VMI 199
Cdd:COG1066    92 VLIGGEPGIGKSTLLLQVAARLAKK-GGKVLYV--SGEesasqIK----------LRAERLGLLSDNLYLLaetdleAIL 158

                          90
                  ....*....|....*...
gi 1125288690 200 EAVENHMPQVIVIDEIGT 217
Cdd:COG1066   159 ATIEELKPDLLVIDSIQT 176
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
129-239 4.86e-05

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 44.12  E-value: 4.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 129 KSILLLGRPGVGKTTLLREAARVMADEFAK------------------RVVVVDT--SNEIAGDGDIPHPGIGRARrmqv 188
Cdd:COG1618     1 MKIFITGRPGVGKTTLLLKVVEELRDEGLRvggfitpevreggrrvgfKLVDLATgeEAILASVDIDSGPRVGKYG---- 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1125288690 189 PHPELQHAVMIEAVENHM--PQVIVIDEIGT-EAEAL----AARTIAERGVQLIATAH 239
Cdd:COG1618    77 VDPEALEAIAVEALERALeeADLIVIDEIGKmELKSKgfreAIEEALDSDKPVLATVH 134
Jag_EloR NF041568
RNA-binding cell elongation regulator Jag/EloR; Members of this family are nucleic ...
 465-511 8.79e-05

RNA-binding cell elongation regulator Jag/EloR; Members of this family are nucleic acid-binding proteins (RNA or single-stranded DNA) with a KH domain at the N-terminus, an R3H domain at the C-terminus, and additional regions of homology. The founding member of this family was JAG (spoIIIJ Associated Gene) from Bacillus subtilis, but later work in other lineages, such as Streptococcus pneumoniae, as established a role in controlling cell elongation and the operation of the elongasome. The S. pneumoniae protein, a protein that undergoes regulatory phosphorylation and dephosphorylation, is also called RNA-binding cell elongation regulator EloR, and also KhpB.


Pssm-ID: 469453 [Multi-domain]  Cd Length: 203  Bit Score: 43.58  E-value: 8.79e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1125288690 465 VLKSTQPVELSPQNSYVRRLQHQLIQRY-GLASESRGEEPFRRVVVFP 511
Cdd:NF041568  156 VKRTKKPVVLEPMPSYERKIIHTALQNHpDVETYSEGEEPNRKVVIAP 203
flhF PRK14722
flagellar biosynthesis regulator FlhF; Provisional
 124-284 1.16e-04

flagellar biosynthesis regulator FlhF; Provisional


Pssm-ID: 173185 [Multi-domain]  Cd Length: 374  Bit Score: 44.33  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 124 VIESGKSILLLGRPGVGKTTLLRE-AARVMADEFAKRVVVVDT-SNEIAGDGD---------IPHPGIGRARRMQVPHPE 192
Cdd:PRK14722  133 LMERGGVFALMGPTGVGKTTTTAKlAARCVMRFGASKVALLTTdSYRIGGHEQlrifgkilgVPVHAVKDGGDLQLALAE 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 193 L--QHAVMIEAVENHMPQVIVIDEIgteAEALAARTIAERGVQLIATAHGNTLDNLLQ---------NPTLCDLIGGIqa 261
Cdd:PRK14722  213 LrnKHMVLIDTIGMSQRDRTVSDQI---AMLHGADTPVQRLLLLNATSHGDTLNEVVQayrsaagqpKAALPDLAGCI-- 287

                         170       180
                  ....*....|....*....|...
gi 1125288690 262 VTLSDEEARRRGTQKTVLERKAP 284
Cdd:PRK14722  288 LTKLDEASNLGGVLDTVIRYKLP 310
AAA_24 pfam13479
AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.
 127-223 1.95e-04

AAA domain; This AAA domain is found in a wide variety of presumed phage proteins.


Pssm-ID: 433243  Cd Length: 199  Bit Score: 42.70  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 127 SGKSILLLGRPGVGKTTLLREaarvmadefAKRVVVVDTSneiAGDGDIphpgigRARRMQVPHPELQHAVMIEAV---- 202
Cdd:pfam13479   1 KKLKILIYGPSGIGKTTFAKT---------LPKPLFLDTE---KGSKAL------DGDRFPDIVIRDSWQDFLDAIdelt 62

                          90       100
                  ....*....|....*....|...
gi 1125288690 203 --ENHMPQVIVIDEIgTEAEALA 223
Cdd:pfam13479  63 aaELADYKTIVIDTV-DWLERLC 84
PRK13695 PRK13695
NTPase;
131-248 3.24e-04

NTPase;


Pssm-ID: 237475  Cd Length: 174  Bit Score: 41.44  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 131 ILLLGRPGVGKTTLLREAARVMADEFAK------------------RVVVVDTSNE--IAGDGDIPHPGIGRarrmQVPH 190
Cdd:PRK13695    3 IGITGPPGVGKTTLVLKIAELLKEEGYKvggfyteevreggkrigfKIIDLDTGEEgiLARVGFPSRPRVGK----YVVN 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125288690 191 PELQHAVMIEAVENHM--PQVIVIDEIG-----TEAEALAARTIAERGVQLIATAHGNTLDNLLQ 248
Cdd:PRK13695   79 LEDLERIGIPALERALeeADVIIIDEIGkmelkSPKFVKAVEEVLDSEKPVIATLHRRSVHPFVQ 143
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 92-153 4.35e-04

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 41.75  E-value: 4.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1125288690  92 RISAIRNRQGEVIGLTCRVGRavVGTVDIVRDV---IESGKSILLLGRPGVGKTTLLREAARVMA 153
Cdd:cd03220    11 PTYKGGSSSLKKLGILGRKGE--VGEFWALKDVsfeVPRGERIGLIGRNGAGKSTLLRLLAGIYP 73
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 117-231 7.72e-04

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 42.40  E-value: 7.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690  117 TVDIVRDV---IESGKSILLLGRPGVGKTTLLREAArVMADEFAKRVvvvdtSNEIAGDGDIPHPgIGRARRMQVphpel 193
Cdd:TIGR00956   73 TFDILKPMdglIKPGELTVVLGRPGSGCSTLLKTIA-SNTDGFHIGV-----EGVITYDGITPEE-IKKHYRGDV----- 140

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1125288690  194 qhaVMIEAVENHMPQVIVIDEIGTEAealAARTIAERG 231
Cdd:TIGR00956  141 ---VYNAETDVHFPHLTVGETLDFAA---RCKTPQNRP 172
AAA_22 pfam13401
AAA domain;
125-215 1.01e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 39.25  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 125 IESGKSILLL-GRPGVGKTTLLREAARvMADEFAKRVVVVDTSN---------EIAGDGDIPHPGIGRARrmqvphpELQ 194
Cdd:pfam13401   1 IRFGAGILVLtGESGTGKTTLLRRLLE-QLPEVRDSVVFVDLPSgtspkdllrALLRALGLPLSGRLSKE-------ELL 72

                          90       100
                  ....*....|....*....|.
gi 1125288690 195 HAVMIEAVENHMPQVIVIDEI 215
Cdd:pfam13401  73 AALQQLLLALAVAVVLIIDEA 93
R3H_NF-X1 cd02643
R3H domain of the X1 box binding protein (NF-X1) and related proteins. Human NF-X1 is a ...
 445-509 1.19e-03

R3H domain of the X1 box binding protein (NF-X1) and related proteins. Human NF-X1 is a transcription factor that regulates the expression of class II major histocompatibility complex (MHC) genes. The Drosophila homolog shuttle craft (STC) has been shown to be a DNA- or RNA-binding protein required for proper axon guidance in the central nervous system and, the yeast homolog FAP1 encodes a dosage suppressor of rapamycin toxicity. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100072  Cd Length: 74  Bit Score: 37.72  E-value: 1.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1125288690 445 VEDVDEqevalrEVEGAISEVLKSTQPVE---LSPQNSYVRRLQHQLIQRYGLASESRGEEPFRRVVV 509
Cdd:cd02643    11 VKDVEK------DLIELVESVNKGKQTSRshsFPPMNREKRRIVHELAEHFGIESVSYDQEPKRNVVA 72
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 119-211 1.27e-03

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 40.32  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 119 DIVRD---VIESGKSILLLGRPGVGKTTLLreaarvmadefakRVVVVDTSNEIAGDGDIPHPGIGRARRMQVPHPElqh 195
Cdd:cd03233    21 PILKDfsgVVKPGEMVLVLGRPGSGCSTLL-------------KALANRTEGNVSVEGDIHYNGIPYKEFAEKYPGE--- 84

                          90
                  ....*....|....*.
gi 1125288690 196 AVMIEAVENHMPQVIV 211
Cdd:cd03233    85 IIYVSEEDVHFPTLTV 100
R3H_encore_like cd02642
R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the ...
 467-512 1.49e-03

R3H domain of encore-like and DIP1-like proteins. Drosophila encore is involved in the germline exit after four mitotic divisions, by facilitating SCF-ubiquitin-proteasome-dependent proteolysis. Maize DBF1-interactor protein 1 (DIP1) containing an R3H domain is a potential regulator of DBF1 activity in stress responses. The name of the R3H domain comes from the characteristic spacing of the most conserved arginine and histidine residues. The function of the domain is predicted to bind ssDNA or ssRNA in a sequence-specific manner.


Pssm-ID: 100071  Cd Length: 63  Bit Score: 37.20  E-value: 1.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1125288690 467 KSTQPVELSPQNSYVRRLQHQLIQRYGLASESRGEEpFRRVVVFPR 512
Cdd:cd02642    19 STRQSLELPPMNSYYRLLAHRVAQYYGLDHNVDNSG-GKCVIVNKT 63
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 102-146 2.66e-03

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 39.38  E-value: 2.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1125288690 102 EVIGLTCRVGRAVvgtvdIVRDV---IESGKSILLLGRPGVGKTTLLR 146
Cdd:COG4133     4 EAENLSCRRGERL-----LFSGLsftLAAGEALALTGPNGSGKTTLLR 46
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 109-160 2.72e-03

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 39.77  E-value: 2.72e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1125288690 109 RVGRAVVGTVDIVRDV---IESGKSILLLGRPGVGKTTLLREAARVMADEFaKRV 160
Cdd:COG0714     9 EIGKVYVGQEELIELVliaLLAGGHLLLEGVPGVGKTTLAKALARALGLPF-IRI 62
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 102-239 3.28e-03

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 38.38  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 102 EVIGLTCRVGRAVVgtVDIVRDVIESGKSILLLGRPGVGKTTLLREAARvmadefakrvVVVDTSNEIAGDGDIPHPGIG 181
Cdd:cd00267     1 EIENLSFRYGGRTA--LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAG----------LLKPTSGEILIDGKDIAKLPL 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 182 RARRMQVPH-PEL----QHAVMIEAVENHMPQVIVIDEIGT-----EAEALAA--RTIAERGVQLIATAH 239
Cdd:cd00267    69 EELRRRIGYvPQLsggqRQRVALARALLLNPDLLLLDEPTSgldpaSRERLLEllRELAEEGRTVIIVTH 138
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 120-161 3.36e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 39.68  E-value: 3.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1125288690 120 IVRDVIESGK--SILLLGRPGVGKTTLlreaARVMADEFAKRVV 161
Cdd:PRK13342   26 PLRRMIEAGRlsSMILWGPPGTGKTTL----ARIIAGATDAPFE 65
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 125-229 5.38e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 38.62  E-value: 5.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1125288690 125 IESGKSILLL-GRPGVGKTTLLREAARVMADEFakRVVVVDTSN--------EIAGDGDIPHPGIGRARRMQvphpELQH 195
Cdd:COG3267    39 LAQGGGFVVLtGEVGTGKTTLLRRLLERLPDDV--KVAYIPNPQlspaellrAIADELGLEPKGASKADLLR----QLQE 112

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1125288690 196 AvMIEAVENHMPQVIVIDeigtEAEALAARTIAE 229
Cdd:COG3267   113 F-LLELAAAGRRVVLIID----EAQNLPPETLEE 141
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 102-146 7.66e-03

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 38.30  E-value: 7.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1125288690 102 EVIGLTCRVGRAVVgtvdiVRDV---IESGKSILLLGRPGVGKTTLLR 146
Cdd:COG4555     3 EVENLSKKYGKVPA-----LKDVsftAKDGEITGLLGPNGAGKTTLLR 45
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 125-161 9.76e-03

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 38.50  E-value: 9.76e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1125288690 125 IESGK--SILLLGRPGVGKTTLlreaARVMADEFAKRVV 161
Cdd:COG2256    44 IEAGRlsSMILWGPPGTGKTTL----ARLIANATDAEFV 78
 
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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