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Conserved domains on  [gi|1995381470|ref|WP_205568041|]
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AAA family ATPase [Pectobacterium brasiliense]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3910 COG3910
Predicted ATPase [General function prediction only];
7-241 5.77e-153

Predicted ATPase [General function prediction only];


:

Pssm-ID: 443116 [Multi-domain]  Cd Length: 239  Bit Score: 425.33  E-value: 5.77e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470   7 PYLQRIYFHPQKTLDPQAYPLIIPAINDLEKIRFHPDVTFLVGENGSGKSTLLEAVAIAMGFNPEGGSRNFNFSTRDSHS 86
Cdd:COG3910     2 PYLRRVSLKREKVPDRDAYPFNLPAVRNLEGLEFHPPVTFFVGENGSGKSTLLEAIAVAAGFNPEGGSKNFRFSTRESES 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  87 NLSDYLRIVKGIKRPRTGYFLRAESFFNVATEIENID--PGLIQLAYGGVSLHQQSHGESFMALLNHRFGANGFYLLDEP 164
Cdd:COG3910    82 ALGEYLRLSRGLPKPRDGFFLRAESFFNVATYLDELAaeGPGILDSYGGRSLHEQSHGESFLALFENRFRGNGLYLLDEP 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1995381470 165 EAALSPTRQLTALARIHQLVNTGCQFIIATHSPIILAYPNSVIYQFNENGIQQVAWQDTEHYQITRQFLNNPQGMMK 241
Cdd:COG3910   162 EAALSPSRQLALLALIHDLVREGSQFIIATHSPILMAYPGATIYEFDEDGIREVAYEDTEHYQLTRRFLNNPERFLR 238
 
Name Accession Description Interval E-value
COG3910 COG3910
Predicted ATPase [General function prediction only];
7-241 5.77e-153

Predicted ATPase [General function prediction only];


Pssm-ID: 443116 [Multi-domain]  Cd Length: 239  Bit Score: 425.33  E-value: 5.77e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470   7 PYLQRIYFHPQKTLDPQAYPLIIPAINDLEKIRFHPDVTFLVGENGSGKSTLLEAVAIAMGFNPEGGSRNFNFSTRDSHS 86
Cdd:COG3910     2 PYLRRVSLKREKVPDRDAYPFNLPAVRNLEGLEFHPPVTFFVGENGSGKSTLLEAIAVAAGFNPEGGSKNFRFSTRESES 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  87 NLSDYLRIVKGIKRPRTGYFLRAESFFNVATEIENID--PGLIQLAYGGVSLHQQSHGESFMALLNHRFGANGFYLLDEP 164
Cdd:COG3910    82 ALGEYLRLSRGLPKPRDGFFLRAESFFNVATYLDELAaeGPGILDSYGGRSLHEQSHGESFLALFENRFRGNGLYLLDEP 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1995381470 165 EAALSPTRQLTALARIHQLVNTGCQFIIATHSPIILAYPNSVIYQFNENGIQQVAWQDTEHYQITRQFLNNPQGMMK 241
Cdd:COG3910   162 EAALSPSRQLALLALIHDLVREGSQFIIATHSPILMAYPGATIYEFDEDGIREVAYEDTEHYQLTRRFLNNPERFLR 238
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
40-207 2.83e-14

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 68.54  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  40 FHPDVTFLVGENGSGKSTLLEAVAIAMGFnpeggsrnfnfstrdshsnlsdylrivKGIKRPRTGYFLRAEsffNVATei 119
Cdd:cd03227    19 GEGSLTIITGPNGSGKSTILDAIGLALGG---------------------------AQSATRRRSGVKAGC---IVAA-- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 120 enIDPGLIqlayggVSLHQQSHGESFMALL-----NHRFGANGFYLLDEPEAALSPTRQLTALARIHQLVNTGCQFIIAT 194
Cdd:cd03227    67 --VSAELI------FTRLQLSGGEKELSALalilaLASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVIT 138
                         170
                  ....*....|...
gi 1995381470 195 HSPIILAYPNSVI 207
Cdd:cd03227   139 HLPELAELADKLI 151
AAA_23 pfam13476
AAA domain;
36-114 3.55e-07

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 49.03  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  36 EKIRFHPDVTFLVGENGSGKSTLLEAVAIAMGFNPEGGSRNF--NFSTRDSHSNLS----DYLRIVKGIKRPRTGYFLRA 109
Cdd:pfam13476  12 QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSggGFVKGDIRIGLEgkgkAYVEITFENNDGRYTYAIER 91

                  ....*
gi 1995381470 110 ESFFN 114
Cdd:pfam13476  92 SRELS 96
recF PRK00064
recombination protein F; Reviewed
38-62 8.02e-06

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 46.30  E-value: 8.02e-06
                          10        20
                  ....*....|....*....|....*
gi 1995381470  38 IRFHPDVTFLVGENGSGKSTLLEAV 62
Cdd:PRK00064   19 LELSPGVNVLVGENGQGKTNLLEAI 43
recf TIGR00611
recF protein; All proteins in this family for which functions are known are DNA binding ...
40-62 1.03e-04

recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273173 [Multi-domain]  Cd Length: 365  Bit Score: 42.73  E-value: 1.03e-04
                          10        20
                  ....*....|....*....|...
gi 1995381470  40 FHPDVTFLVGENGSGKSTLLEAV 62
Cdd:TIGR00611  21 LSPGVNVIVGPNGQGKTNLLEAI 43
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
44-197 2.26e-04

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 41.07  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  44 VTFLVGENGSGKSTLLEAVAIAMgfNPEGGSRNFNFSTRDS----HSNLSDYL----RIVKGIKR-PRTGYF--LRAESF 112
Cdd:NF040873   20 LTAVVGPNGSGKSTLLKVLAGVL--RPTSGTVRRAGGARVAyvpqRSEVPDSLpltvRDLVAMGRwARRGLWrrLTRDDR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 113 FNVATEIENIdpGLIQLAygGVSLHQQSHGESFMALLnhrfgANGF------YLLDEPEAALSP-TRQLTALArIHQLVN 185
Cdd:NF040873   98 AAVDDALERV--GLADLA--GRQLGELSGGQRQRALL-----AQGLaqeadlLLLDEPTTGLDAeSRERIIAL-LAEEHA 167
                         170
                  ....*....|..
gi 1995381470 186 TGCQFIIATHSP 197
Cdd:NF040873  168 RGATVVVVTHDL 179
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
41-200 9.59e-04

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: 38.51  E-value: 9.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470   41 HPDVTFLVGENGSGKSTLLEAVAiamGFNPEGGSRNFNFSTRDSHSNLSDYLRIVKGIKRPRTGYflRAESFFNVATEIE 120
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALA---RELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS--GELRLRLALALAR 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  121 NIDPGLIqlayggvslhqqshgesfmallnhrfgangfyLLDEPEAALSPTRQLTALARIHQLVN------TGCQFIIAT 194
Cdd:smart00382  76 KLKPDVL--------------------------------ILDEITSLLDAEQEALLLLLEELRLLlllkseKNLTVILTT 123

                   ....*.
gi 1995381470  195 HSPIIL 200
Cdd:smart00382 124 NDEKDL 129
 
Name Accession Description Interval E-value
COG3910 COG3910
Predicted ATPase [General function prediction only];
7-241 5.77e-153

Predicted ATPase [General function prediction only];


Pssm-ID: 443116 [Multi-domain]  Cd Length: 239  Bit Score: 425.33  E-value: 5.77e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470   7 PYLQRIYFHPQKTLDPQAYPLIIPAINDLEKIRFHPDVTFLVGENGSGKSTLLEAVAIAMGFNPEGGSRNFNFSTRDSHS 86
Cdd:COG3910     2 PYLRRVSLKREKVPDRDAYPFNLPAVRNLEGLEFHPPVTFFVGENGSGKSTLLEAIAVAAGFNPEGGSKNFRFSTRESES 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  87 NLSDYLRIVKGIKRPRTGYFLRAESFFNVATEIENID--PGLIQLAYGGVSLHQQSHGESFMALLNHRFGANGFYLLDEP 164
Cdd:COG3910    82 ALGEYLRLSRGLPKPRDGFFLRAESFFNVATYLDELAaeGPGILDSYGGRSLHEQSHGESFLALFENRFRGNGLYLLDEP 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1995381470 165 EAALSPTRQLTALARIHQLVNTGCQFIIATHSPIILAYPNSVIYQFNENGIQQVAWQDTEHYQITRQFLNNPQGMMK 241
Cdd:COG3910   162 EAALSPSRQLALLALIHDLVREGSQFIIATHSPILMAYPGATIYEFDEDGIREVAYEDTEHYQLTRRFLNNPERFLR 238
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
32-252 2.04e-20

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 88.91  E-value: 2.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  32 INDLEkIRFHPDVTFLVGENGSGKSTLLEAVAIAMGfnpegGSRNFNFSTRDSH-----------------SNLSDYLR- 93
Cdd:COG3593    14 IKDLS-IELSDDLTVLVGENNSGKSSILEALRLLLG-----PSSSRKFDEEDFYlgddpdlpeieieltfgSLLSRLLRl 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  94 ---------IVKGIKRPR--------------TGYFLRAESFFNV-----ATEIENIDPGL-IQLAYG-GVSLHQQSHGE 143
Cdd:COG3593    88 llkeedkeeLEEALEELNeelkealkalnellSEYLKELLDGLDLelelsLDELEDLLKSLsLRIEDGkELPLDRLGSGF 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 144 S---FMALLN-----HRFGANGFYLLDEPEAALSPTRQLTALARIHQLVNTGCQFIIATHSPIILAY--PNSVIYQFNEN 213
Cdd:COG3593   168 QrliLLALLSalaelKRAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEvpLENIRRLRRDS 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1995381470 214 G---IQQVAWQDTEHYQITRQFLNNPQGMM----KILLAdEDDTDE 252
Cdd:COG3593   248 GgttSTKLIDLDDEDLRKLLRYLGVTRSELlfarKVILV-EGDTEV 292
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
40-207 2.83e-14

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 68.54  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  40 FHPDVTFLVGENGSGKSTLLEAVAIAMGFnpeggsrnfnfstrdshsnlsdylrivKGIKRPRTGYFLRAEsffNVATei 119
Cdd:cd03227    19 GEGSLTIITGPNGSGKSTILDAIGLALGG---------------------------AQSATRRRSGVKAGC---IVAA-- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 120 enIDPGLIqlayggVSLHQQSHGESFMALL-----NHRFGANGFYLLDEPEAALSPTRQLTALARIHQLVNTGCQFIIAT 194
Cdd:cd03227    67 --VSAELI------FTRLQLSGGEKELSALalilaLASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVIT 138
                         170
                  ....*....|...
gi 1995381470 195 HSPIILAYPNSVI 207
Cdd:cd03227   139 HLPELAELADKLI 151
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
32-214 3.69e-14

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 70.03  E-value: 3.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  32 INDLEkIRFH--PDVTFLVGENGSGKSTLLEAVAIAMG--------------------FNPE-------GGSRNFN---- 78
Cdd:COG3950    14 FEDLE-IDFDnpPRLTVLVGENGSGKTTLLEAIALALSgllsrlddvkfrkllirngeFGDSaklilyyGTSRLLLdgpl 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  79 --------------------FSTRDSHSNLSDYLR--IVKGIKRPRTGYFLRAESFFNV---------ATEIENIDPGLI 127
Cdd:COG3950    93 kklerlkeeyfsrldgydslLDEDSNLREFLEWLReyLEDLENKLSDELDEKLEAVREAlnkllpdfkDIRIDRDPGRLV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 128 QLAYGG--VSLHQQSHGE-SFMAL--------------LNHRFGANGFYLLDEPEAALSPTRQLTALARIHQlVNTGCQF 190
Cdd:COG3950   173 ILDKNGeeLPLNQLSDGErSLLALvgdlarrlaelnpaLENPLEGEGIVLIDEIDLHLHPKWQRRILPDLRK-IFPNIQF 251
                         250       260
                  ....*....|....*....|....*
gi 1995381470 191 IIATHSP-IILAYPNSVIYQFNENG 214
Cdd:COG3950   252 IVTTHSPlILSSLEDEEVIVLERDE 276
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
43-212 1.64e-13

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: 66.11  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  43 DVTFLVGENGSGKSTLLEAVAiamgfnpeggsrnfnfstrdshsnlsdylrivkGIKRPRTGYFLraesFFNVATEIENI 122
Cdd:cd00267    26 EIVALVGPNGSGKSTLLRAIA---------------------------------GLLKPTSGEIL----IDGKDIAKLPL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 123 DPGLIQLAYggvsLHQQSHGESF-----MALLNHRfganGFYLLDEPEAALSPTRQLTALARIHQLVNTGCQFIIATHSP 197
Cdd:cd00267    69 EELRRRIGY----VPQLSGGQRQrvalaRALLLNP----DLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDP 140
                         170
                  ....*....|....*
gi 1995381470 198 IILAYPNSVIYQFNE 212
Cdd:cd00267   141 ELAELAADRVIVLKD 155
COG4938 COG4938
Predicted ATPase [General function prediction only];
43-218 1.58e-10

Predicted ATPase [General function prediction only];


Pssm-ID: 443965 [Multi-domain]  Cd Length: 277  Bit Score: 59.98  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  43 DVTFLVGENGSGKSTLLEAVAIAMGFNPE------GGSRNFNFSTRDSHSNL-------SDYLRIVKGIKRPRT------ 103
Cdd:COG4938    21 PLTLLIGPNGSGKSTLIQALLLLLQSNFIylpaerSGPARLYPSLVRELSDLgsrgeytADFLAELENLEILDDkskell 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 104 -GYFLRAESFFNVATEIeNIDPGLIQLAYGG------VSLHQQSHGESFMA----LLNHRFGANGFYLLDEPEAALSPTR 172
Cdd:COG4938   101 eQVEEWLEKIFPGKVEV-DASSDLVRLVFRPsgngkrIPLSNVGSGVSELLpillALLSAAKPGSLLIIEEPEAHLHPKA 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 173 QlTALAR-IHQLVNTGCQFIIATHSPIIL------------AYPNSV-IYQFNENGIQQV 218
Cdd:COG4938   180 Q-SALAElLAELANSGVQVIIETHSDYILnglrnlikegklLDPDDVaVYFFERDGGGSE 238
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
37-207 7.43e-08

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 51.31  E-value: 7.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  37 KIRFHPDVTFLVGENGSGKSTLLEAVAIAMGfnpEGGSRNFnfstRDshSNLSDYlrIVKGIK-RPRTGYflrAEsffnV 115
Cdd:cd03278    17 TIPFPPGLTAIVGPNGSGKSNIIDAIRWVLG---EQSAKSL----RG--EKMSDV--IFAGSEtRKPANF---AE----V 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 116 ATEIENID--PGLI-Q------LAYGG---VSLHQQSHGE---SFMALLNHRFGANG--FYLLDEPEAALSPTRqltaLA 178
Cdd:cd03278    79 TLTFDNSDgrYSIIsQgdvseiIEAPGkkvQRLSLLSGGEkalTALALLFAIFRVRPspFCVLDEVDAALDDAN----VE 154
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1995381470 179 RIHQLVN---TGCQFIIATHSPIILAYPNSVI 207
Cdd:cd03278   155 RFARLLKefsKETQFIVITHRKGTMEAADRLY 186
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
43-198 1.21e-07

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: 50.56  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  43 DVTFLVGENGSGKSTLLEAVAiamGF-NPEGGSRNFNfsTRDSHSNLSDYLRIV------KGIKRPRTGY----FLRAes 111
Cdd:COG4133    29 EALALTGPNGSGKTTLLRILA---GLlPPSAGEVLWN--GEPIRDAREDYRRRLaylghaDGLKPELTVRenlrFWAA-- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 112 FFNVATEIENIDPGLIQL---AYGGVSLHQQSHGesfM--------ALLNHRfganGFYLLDEPEAALSPTRQLTALARI 180
Cdd:COG4133   102 LYGLRADREAIDEALEAVglaGLADLPVRQLSAG---QkrrvalarLLLSPA----PLWLLDEPFTALDAAGVALLAELI 174
                         170
                  ....*....|....*...
gi 1995381470 181 HQLVNTGCQFIIATHSPI 198
Cdd:COG4133   175 AAHLARGGAVLLTTHQPL 192
AAA_23 pfam13476
AAA domain;
36-114 3.55e-07

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 49.03  E-value: 3.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  36 EKIRFHPDVTFLVGENGSGKSTLLEAVAIAMGFNPEGGSRNF--NFSTRDSHSNLS----DYLRIVKGIKRPRTGYFLRA 109
Cdd:pfam13476  12 QTIDFSKGLTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSggGFVKGDIRIGLEgkgkAYVEITFENNDGRYTYAIER 91

                  ....*
gi 1995381470 110 ESFFN 114
Cdd:pfam13476  92 SRELS 96
ABC_SMC6_euk cd03276
ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of ...
37-67 1.59e-06

ATP-binding cassette domain of eukaryotic SM6 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213243 [Multi-domain]  Cd Length: 198  Bit Score: 47.21  E-value: 1.59e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1995381470  37 KIRFHPDVTFLVGENGSGKSTLLEAVAIAMG 67
Cdd:cd03276    16 QIEFGPRVNFIVGNNGSGKSAILTALTIGLG 46
RecF COG1195
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
38-62 7.62e-06

Recombinational DNA repair ATPase RecF [Replication, recombination and repair];


Pssm-ID: 440808 [Multi-domain]  Cd Length: 352  Bit Score: 46.30  E-value: 7.62e-06
                          10        20
                  ....*....|....*....|....*
gi 1995381470  38 IRFHPDVTFLVGENGSGKSTLLEAV 62
Cdd:COG1195    18 LEFSPGINVLVGPNGQGKTNLLEAI 42
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
34-65 7.90e-06

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 45.39  E-value: 7.90e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1995381470  34 DLEKIRFHPDVTFLVGENGSGKSTLLEAVAIA 65
Cdd:COG0419    15 DTETIDFDDGLNLIVGPNGAGKSTILEAIRYA 46
recF PRK00064
recombination protein F; Reviewed
38-62 8.02e-06

recombination protein F; Reviewed


Pssm-ID: 234608 [Multi-domain]  Cd Length: 361  Bit Score: 46.30  E-value: 8.02e-06
                          10        20
                  ....*....|....*....|....*
gi 1995381470  38 IRFHPDVTFLVGENGSGKSTLLEAV 62
Cdd:PRK00064   19 LELSPGVNVLVGENGQGKTNLLEAI 43
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
30-208 8.59e-06

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 45.33  E-value: 8.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  30 PAINDLEkIRFHP-DVTFLVGENGSGKSTLLEAVAIAMGFNPEGGSrnFNFSTRDSHSNLSdylrIVKGIKRPRTgyflr 108
Cdd:COG2401    44 YVLRDLN-LEIEPgEIVLIVGASGSGKSTLLRLLAGALKGTPVAGC--VDVPDNQFGREAS----LIDAIGRKGD----- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 109 aesfFNVATEIENI----DPGLIQLAYggvslHQQSHGESFMA----LLNHRfgaNGFYLLDEPEAALSPTrqlTA--LA 178
Cdd:COG2401   112 ----FKDAVELLNAvglsDAVLWLRRF-----KELSTGQKFRFrlalLLAER---PKLLVIDEFCSHLDRQ---TAkrVA 176
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1995381470 179 RIHQLV--NTGCQFIIATHSPIILAY--PNSVIY 208
Cdd:COG2401   177 RNLQKLarRAGITLVVATHHYDVIDDlqPDLLIF 210
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
32-93 1.01e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 1.01e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1995381470   32 INDLEKIRFHPDVTFLVGENGSGKSTLLEAVAIAMGFNPEggsRNFNFSTRDSHS---NLSDYLR 93
Cdd:COG4913     14 FDGVHTIDFDGRGTLLTGDNGSGKSTLLDAIQTLLVPAKR---PRFNKAANDAGKsdrTLLSYVR 75
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
38-68 1.97e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 45.35  E-value: 1.97e-05
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1995381470   38 IRFHPDVTFLVGENGSGKSTLLEAVAIAMGF 68
Cdd:pfam02463   19 LPFSPGFTAIVGPNGSGKSNILDAILFVLGE 49
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
36-207 2.07e-05

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 44.14  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  36 EKIRFHPDVTFLVGENGSGKSTLLEAVAIAMgfnpeggsrnfnFSTRDSHSNLSDYLRIVKGIKRPRTGYFLRAESFFNV 115
Cdd:cd03240    16 SEIEFFSPLTLIVGQNGAGKTTIIEALKYAL------------TGELPPNSKGGAHDPKLIREGEVRAQVKLAFENANGK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 116 ATEIENIDPGLIQLAYggvsLHQQ-------------SHGESFMALLNHR------FGAN-GFYLLDEPEAALSPTRQLT 175
Cdd:cd03240    84 KYTITRSLAILENVIF----CHQGesnwplldmrgrcSGGEKVLASLIIRlalaetFGSNcGILALDEPTTNLDEENIEE 159
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1995381470 176 ALARI--HQLVNTGCQFIIATHSPIILAYPNSVI 207
Cdd:cd03240   160 SLAEIieERKSQKNFQLIVITHDEELVDAADHIY 193
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
44-200 2.77e-05

ATPase/GTPase, AAA15 family [General function prediction only];


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 44.65  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  44 VTFLVGENGSGKSTLLEAVAIA--------------------------------MGFNPEGGSRNFNFSTRDSH------ 85
Cdd:COG1106    31 VNLIYGANASGKSNLLEALYFLrnlvlnssqpgdklvepflldsesknepsefeILFLLDGVRYEYGFELDKERiisewl 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  86 --------------SNLSDYLR---IVKGIKRPRTGYFLRAESFFNVATE-IENIDPGLIQLAY---------------- 131
Cdd:COG1106   111 yflstaaqlnvpllSPLYDWFDnniSLDTSSDGLTLLLKEDESLKEELLElLKIADPGIEDIEVeeeeiedlverklifk 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1995381470 132 -----GGVSLHQQSHGE----SFMALLNHRFGANGFYLLDEPEAALSPTRQLTALARIHQLVN-TGCQFIIATHSPIIL 200
Cdd:COG1106   191 hkggnVPLPLSEESDGTkrllALAGALLDALAKGGVLLIDEIEASLHPSLLRKLLKLFLDLANkNNAQLIFTTHSTELL 269
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
30-208 2.96e-05

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 43.61  E-value: 2.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  30 PAINDLEkIRFHP-DVTFLVGENGSGKSTLLEavAIAMGFNPEGGSRNFNfSTRDSHSNLSDYLRIVkgikrprtGY-FL 107
Cdd:cd03225    15 PALDDIS-LTIKKgEFVLIVGPNGSGKSTLLR--LLNGLLGPTSGEVLVD-GKDLTKLSLKELRRKV--------GLvFQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 108 RAES-FFN--VATEI----EN--IDPGLIQ------LAYGGV------SLHQQSHGE-------SFMAlLNHRfgangFY 159
Cdd:cd03225    83 NPDDqFFGptVEEEVafglENlgLPEEEIEerveeaLELVGLeglrdrSPFTLSGGQkqrvaiaGVLA-MDPD-----IL 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1995381470 160 LLDEPEAALSP--TRQLTALarIHQLVNTGCQFIIATHSP-IILAYPNSVIY 208
Cdd:cd03225   157 LLDEPTAGLDPagRRELLEL--LKKLKAEGKTIIIVTHDLdLLLELADRVIV 206
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
44-201 3.37e-05

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 42.64  E-value: 3.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  44 VTFLVGENGSGKSTLLEavAIAMGFNPEGGSRNFNFstRDSHSNLSDYLRivKGIkrprtGYFLRAESFFNVATEIENID 123
Cdd:pfam00005  13 ILALVGPNGAGKSTLLK--LIAGLLSPTEGTILLDG--QDLTDDERKSLR--KEI-----GYVFQDPQLFPRLTVRENLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 124 PGLIQLAYGGVSLHQQshgesfMALLNHRFGANGFY--LLDEPEAALSP-TRQLTALARihqlvntgcqfIIATHSPIIL 200
Cdd:pfam00005  82 LGLLLKGLSKREKDAR------AEEALEKLGLGDLAdrPVGERPGTLSGgQRQRVAIAR-----------ALLTKPKLLL 144

                  .
gi 1995381470 201 A 201
Cdd:pfam00005 145 L 145
ABC_RecF cd03242
ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that ...
37-62 8.95e-05

ATP-binding cassette domain of RecF; RecF is a recombinational DNA repair ATPase that maintains replication in the presence of DNA damage. When replication is prematurely disrupted by DNA damage, several recF pathway gene products play critical roles processing the arrested replication fork, allowing it to resume and complete its task. This CD represents the nucleotide binding domain of RecF. RecF belongs to a large superfamily of ABC transporters 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 with 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: 213209 [Multi-domain]  Cd Length: 270  Bit Score: 42.67  E-value: 8.95e-05
                          10        20
                  ....*....|....*....|....*.
gi 1995381470  37 KIRFHPDVTFLVGENGSGKSTLLEAV 62
Cdd:cd03242    16 ELEFEPGVTVLVGENAQGKTNLLEAI 41
recf TIGR00611
recF protein; All proteins in this family for which functions are known are DNA binding ...
40-62 1.03e-04

recF protein; All proteins in this family for which functions are known are DNA binding proteins that assist the filamentation of RecA onto DNA for the initiation of recombination or recombinational repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273173 [Multi-domain]  Cd Length: 365  Bit Score: 42.73  E-value: 1.03e-04
                          10        20
                  ....*....|....*....|...
gi 1995381470  40 FHPDVTFLVGENGSGKSTLLEAV 62
Cdd:TIGR00611  21 LSPGVNVIVGPNGQGKTNLLEAI 43
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
44-93 1.58e-04

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 41.99  E-value: 1.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1995381470  44 VTFLVGENGSGKSTLLEAVAIAMGFNPEGGSRNFNFSTRDSHSNLSDYLR 93
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLN 50
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
156-201 1.97e-04

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 41.99  E-value: 1.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1995381470 156 NGFYLLDEPEAALSPTRQLTALARIHQLVNTGCQFIIATHSPIILA 201
Cdd:pfam13304 258 GGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
37-124 2.00e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  37 KIRFHPDVTFLVGENGSGKSTLLEAVAIAM----GFNPEGGSRNfNFsTRDSHS----------NLSDYlRIVKGIKR-- 100
Cdd:PRK03918   18 VVEFDDGINLIIGQNGSGKSSILEAILVGLywghGSKPKGLKKD-DF-TRIGGSgteielkfekNGRKY-RIVRSFNRge 94
                          90       100
                  ....*....|....*....|....*...
gi 1995381470 101 ----PRTGYFLRAESFFNVATEIENIDP 124
Cdd:PRK03918   95 sylkYLDGSEVLEEGDSSVREWVERLIP 122
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
44-197 2.26e-04

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 41.07  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  44 VTFLVGENGSGKSTLLEAVAIAMgfNPEGGSRNFNFSTRDS----HSNLSDYL----RIVKGIKR-PRTGYF--LRAESF 112
Cdd:NF040873   20 LTAVVGPNGSGKSTLLKVLAGVL--RPTSGTVRRAGGARVAyvpqRSEVPDSLpltvRDLVAMGRwARRGLWrrLTRDDR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 113 FNVATEIENIdpGLIQLAygGVSLHQQSHGESFMALLnhrfgANGF------YLLDEPEAALSP-TRQLTALArIHQLVN 185
Cdd:NF040873   98 AAVDDALERV--GLADLA--GRQLGELSGGQRQRALL-----AQGLaqeadlLLLDEPTTGLDAeSRERIIAL-LAEEHA 167
                         170
                  ....*....|..
gi 1995381470 186 TGCQFIIATHSP 197
Cdd:NF040873  168 RGATVVVVTHDL 179
AAA_29 pfam13555
P-loop containing region of AAA domain;
38-63 3.24e-04

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 37.96  E-value: 3.24e-04
                          10        20
                  ....*....|....*....|....*..
gi 1995381470  38 IRFHPD-VTFLVGENGSGKSTLLEAVA 63
Cdd:pfam13555  17 IPIDPRgNTLLTGPSGSGKSTLLDAIQ 43
recF PRK14079
recombination protein F; Provisional
35-67 3.73e-04

recombination protein F; Provisional


Pssm-ID: 184491 [Multi-domain]  Cd Length: 349  Bit Score: 41.31  E-value: 3.73e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1995381470  35 LEKIRFHPDVTFLVGENGSGKSTLLEAVAIAMG 67
Cdd:PRK14079   16 PPTLAFPPGVTAVVGENAAGKTNLLEAIYLALT 48
COG4637 COG4637
Predicted ATPase [General function prediction only];
31-89 6.54e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 40.30  E-value: 6.54e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1995381470  31 AINDLEkIRFHPdVTFLVGENGSGKSTLLEAV----AIAMG-----FNPEGGSRN-FNFSTRDSHSNLS 89
Cdd:COG4637    12 SLRDLE-LPLGP-LTVLIGANGSGKSNLLDALrflsDAARGglqdaLARRGGLEElLWRGPRTITEPIR 78
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
109-200 6.55e-04

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433011 [Multi-domain]  Cd Length: 392  Bit Score: 40.27  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 109 AESFFNVATEIENI-----DPGLIQLAYGGVSL--HQQSHGE------SFMALLNHRFGA-----NGFYLLDEPEAALSP 170
Cdd:pfam13175 282 KNILFKKIDKLKDFgyppfLNPEIEIKKDDEDLplNKNGSGVqrlillIFFIAEAERKEDeieekNVILAIEEPEAHLHP 361
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1995381470 171 TRQlTALAR-IHQLVNTG-CQFIIATHSPIIL 200
Cdd:pfam13175 362 QAQ-RVLIKlLKELANDNkTQVIITTHSPHII 392
ABC_SMC5_euk cd03277
ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of ...
39-71 7.17e-04

ATP-binding cassette domain of eukaryotic SMC5 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213244 [Multi-domain]  Cd Length: 213  Bit Score: 39.50  E-value: 7.17e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1995381470  39 RFHPDVTFLVGENGSGKSTLLEAVAIAMGFNPE 71
Cdd:cd03277    20 RPGPSLNMIIGPNGSGKSSIVCAICLGLGGKPK 52
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
41-200 9.59e-04

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: 38.51  E-value: 9.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470   41 HPDVTFLVGENGSGKSTLLEAVAiamGFNPEGGSRNFNFSTRDSHSNLSDYLRIVKGIKRPRTGYflRAESFFNVATEIE 120
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALA---RELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS--GELRLRLALALAR 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  121 NIDPGLIqlayggvslhqqshgesfmallnhrfgangfyLLDEPEAALSPTRQLTALARIHQLVN------TGCQFIIAT 194
Cdd:smart00382  76 KLKPDVL--------------------------------ILDEITSLLDAEQEALLLLLEELRLLlllkseKNLTVILTT 123

                   ....*.
gi 1995381470  195 HSPIIL 200
Cdd:smart00382 124 NDEKDL 129
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
36-61 1.09e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433011 [Multi-domain]  Cd Length: 392  Bit Score: 39.89  E-value: 1.09e-03
                          10        20
                  ....*....|....*....|....*.
gi 1995381470  36 EKIRFHPDVTFLVGENGSGKSTLLEA 61
Cdd:pfam13175  17 TEIDLDEDLTVLIGKNNSGKSSILEA 42
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
43-208 1.11e-03

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: 39.05  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  43 DVTF---------LVGENGSGKSTLLEAVA---------------------IAMGFNPEggsrnfnFSTRDshsNLsdYL 92
Cdd:cd03220    40 DVSFevprgerigLIGRNGAGKSTLLRLLAgiyppdsgtvtvrgrvssllgLGGGFNPE-------LTGRE---NI--YL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  93 R-IVKGIKRPRTGYFLRA-ESFfnvaTEIEN-ID-P------G-LIQLAYgGVSLHqqshgesfmalLNHRfgangFYLL 161
Cdd:cd03220   108 NgRLLGLSRKEIDEKIDEiIEF----SELGDfIDlPvktyssGmKARLAF-AIATA-----------LEPD-----ILLI 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1995381470 162 DEPEAALSPTRQLTALARIHQLVNTGCQFIIATHSP-IILAYPNSVIY 208
Cdd:cd03220   167 DEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPsSIKRLCDRALV 214
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-67 1.26e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 1.26e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1995381470  37 KIRFHPDVTFLVGENGSGKSTLLEAVAIAMG 67
Cdd:COG1196    19 TIPFEPGITAIVGPNGSGKSNIVDAIRWVLG 49
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
44-197 1.30e-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: 39.07  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470  44 VTFLVGENGSGKSTLLEavAIAMGFNPEGGSRNFNFstRDSHSNLSDYLRivkgikrpRTGYFLRAESFFNVATEIENID 123
Cdd:COG4555    29 ITGLLGPNGAGKTTLLR--MLAGLLKPDSGSILIDG--EDVRKEPREARR--------QIGVLPDERGLYDRLTVRENIR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995381470 124 pgliqlAYGgvSLHQQSHGE--SFMALLNHRFG--------ANGF--------------------YLLDEPEAALSPTRQ 173
Cdd:COG4555    97 ------YFA--ELYGLFDEElkKRIEELIELLGleefldrrVGELstgmkkkvalaralvhdpkvLLLDEPTNGLDVMAR 168
                         170       180
                  ....*....|....*....|....
gi 1995381470 174 LTALARIHQLVNTGCQFIIATHSP 197
Cdd:COG4555   169 RLLREILRALKKEGKTVLFSSHIM 192
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
34-67 1.40e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.65  E-value: 1.40e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1995381470   34 DLEKIRFHPDVTFLVGENGSGKSTLLEAVAIAMG 67
Cdd:TIGR02168   15 DPTTINFDKGITGIVGPNGCGKSNIVDAIRWVLG 48
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
34-59 1.57e-03

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 39.40  E-value: 1.57e-03
                          10        20
                  ....*....|....*....|....*..
gi 1995381470  34 DLEkirFHP-DVTFLVGENGSGKSTLL 59
Cdd:COG4615   352 DLT---IRRgELVFIVGGNGSGKSTLA 375
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
43-70 2.53e-03

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 38.15  E-value: 2.53e-03
                          10        20
                  ....*....|....*....|....*...
gi 1995381470  43 DVTFLVGENGSGKSTLLEAVaiaMGFNP 70
Cdd:COG1121    33 EFVAIVGPNGAGKSTLLKAI---LGLLP 57
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
43-71 2.64e-03

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 38.14  E-value: 2.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1995381470  43 DVTF---------LVGENGSGKSTLLEAVA---------------------IAMGFNPE 71
Cdd:COG1134    44 DVSFevergesvgIIGRNGAGKSTLLKLIAgileptsgrvevngrvsalleLGAGFHPE 102
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
43-63 4.21e-03

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 37.96  E-value: 4.21e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1995381470  43 DVTF---------LVGENGSGKSTLLEAVA 63
Cdd:COG1123   283 DVSLtlrrgetlgLVGESGSGKSTLARLLL 312
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
47-78 5.44e-03

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 37.13  E-value: 5.44e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1995381470  47 LVGENGSGKSTLLEAVAiamGFNPEGGSRNFN 78
Cdd:COG4138    27 LIGPNGAGKSTLLARMA---GLLPGQGEILLN 55
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
38-66 6.64e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 37.71  E-value: 6.64e-03
                          10        20
                  ....*....|....*....|....*....
gi 1995381470  38 IRFHPDVTFLVGENGSGKSTLLEAVAIAM 66
Cdd:PRK02224   19 LRLEDGVTVIHGVNGSGKSSLLEACFFAL 47
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
47-78 7.26e-03

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 36.71  E-value: 7.26e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1995381470  47 LVGENGSGKSTLLEAVaiaMGFN-PEGGSRNFN 78
Cdd:cd03257    36 LVGESGSGKSTLARAI---LGLLkPTSGSIIFD 65
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
24-74 9.24e-03

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 37.04  E-value: 9.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1995381470  24 AYPLIIPAINDLEkIRFHP-DVTFLVGENGSGKSTLLEAVaiaMGFN-PEGGS 74
Cdd:COG4988   345 SYPGGRPALDGLS-LTIPPgERVALVGPSGAGKSTLLNLL---LGFLpPYSGS 393
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
158-202 9.45e-03

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 36.47  E-value: 9.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1995381470 158 FYLLDEPEAALSpTRQLTALAR-IHQLVNtGCQFIIATHSPIILAY 202
Cdd:cd03272   183 FYLFDEIDAALD-AQYRTAVANmIKELSD-GAQFITTTFRPELLEV 226
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
42-70 9.68e-03

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 36.36  E-value: 9.68e-03
                          10        20
                  ....*....|....*....|....*....
gi 1995381470  42 PDVTFLVGENGSGKSTLLEAVaiaMGFNP 70
Cdd:cd03235    25 GEFLAIVGPNGAGKSTLLKAI---LGLLK 50
 
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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