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Conserved domains on  [gi|829777421|ref|WP_047345412|]
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MULTISPECIES: AAA family ATPase [Enterobacterales]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA_partition super family cl49513
ParA family partition ATPase;
9-209 9.71e-31

ParA family partition ATPase;


The actual alignment was detected with superfamily member NF041546:

Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 111.88  E-value: 9.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   9 KGGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAKHHAEREAsgiEPTFTLIE-KFDNLTQTLRALDEKYDHVIVDVA 87
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAARED---ERPFPVVGlARPTLHRELPSLARDYDFVVIDGP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  88 GRNSrEFITSGV-VAHQIIAPLQCSQPDLDTLTELAQQIEAMRDLNPELKVYCLQSMATTNPVLrgneRKEFLEYLEEFP 166
Cdd:NF041546  85 PRAE-DLARSAIkAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIARTAL----GREVAEALAEYG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 829777421 167 tIETLQTVICFRKVYRDCMSNGTGVVETN-NEAAKAEIMQLMKE 209
Cdd:NF041546 160 -LPVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
9-209 9.71e-31

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 111.88  E-value: 9.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   9 KGGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAKHHAEREAsgiEPTFTLIE-KFDNLTQTLRALDEKYDHVIVDVA 87
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAARED---ERPFPVVGlARPTLHRELPSLARDYDFVVIDGP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  88 GRNSrEFITSGV-VAHQIIAPLQCSQPDLDTLTELAQQIEAMRDLNPELKVYCLQSMATTNPVLrgneRKEFLEYLEEFP 166
Cdd:NF041546  85 PRAE-DLARSAIkAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIARTAL----GREVAEALAEYG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 829777421 167 tIETLQTVICFRKVYRDCMSNGTGVVETN-NEAAKAEIMQLMKE 209
Cdd:NF041546 160 -LPVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 1-211 1.03e-29

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 109.55  E-value: 1.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   1 MITVVGGNKGGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAKHHAEREasGIEPTFTLIEKFDNLTQTLRALDEKYD 80
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEARE--EGEPLIPVVRMGKSIRADLPKVASGYD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  81 HVIVDVAGRNSREFITSGVVAHQIIAPLQCSQPDLDTLTELAQQIEAMRDLNPELKVYCLQSMATTNPVLRGNERKEFLE 160
Cdd:PHA02518  79 YVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYREARKALA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 829777421 161 YLEefptIETLQTVICFRKVYRDCMSNGTGVVETNNE-AAKAEIMQLMKEVF 211
Cdd:PHA02518 159 GYG----LPILRNGTTQRVAYADAAEAGGSVLELPEDdKAAEEIIQLVKELF 206
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-163 2.94e-25

partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 95.30  E-value: 2.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   1 MITVVGGNKGGSGKTTTASNLAIALAHEGQDVCLLNGDLQRtaakhhaereasgieptftliekfdNLTQTLraldekYD 80
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQG-------------------------SLTSWL------YD 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  81 HVIVDVAGRNSREFITSGVVAHQIIAPLQCSQPDLDTLTELAQQI-EAMRDLNPELKVYC-LQSMATTnpvlRGNERKEF 158
Cdd:cd02042   50 YILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLeELKKQLNPPLLILGiLLTRVDP----RTKLAREV 125


                 ....*
gi 829777421 159 LEYLE 163
Cdd:cd02042  126 LEELK 130
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 8-210 7.52e-20

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 84.52  E-value: 7.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   8 NKGGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAKHH-------------------------------------AER 50
Cdd:COG1192    9 QKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLgldpddldptlydlllddapledaivpteipgldlipANI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  51 EASGIEPTFTLIEKFDN-LTQTLRALDEKYDHVIVDVAGrnSREFIT-SGVVA-HQIIAPLQCSQPDLDTLTELAQQIEA 127
Cdd:COG1192   89 DLAGAEIELVSRPGRELrLKRALAPLADDYDYILIDCPP--SLGLLTlNALAAaDSVLIPVQPEYLSLEGLAQLLETIEE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421 128 MR-DLNPELKV-YCLQSMATTnpvlRGNERKEFLEYLEEFPTIETLQTVICFRKVYRDCMSNGTGVVETNNEAAKAE-IM 204
Cdd:COG1192  167 VReDLNPKLEIlGILLTMVDP----RTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKaYR 242


                 ....*.
gi 829777421 205 QLMKEV 210
Cdd:COG1192  243 ALAEEL 248
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 2-137 1.47e-12

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 64.29  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421    2 ITVVGGnKGGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAKHH---------------------------------- 47
Cdd:pfam01656   1 IAIAGT-KGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEglegdiapalqalaeglkgrvnldpillkeksde 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   48 -------AEREASGIEPTFTLIEKFDNLTQTLRALDEKYDHVIVDVA---GRNSREFITSgvvAHQIIAPLQCSQPDLDT 117
Cdd:pfam01656  80 ggldlipGNIDLEKFEKELLGPRKEERLREALEALKEDYDYVIIDGApglGELLRNALIA---ADYVIIPLEPEVILVED 156

                         170       180
                  ....*....|....*....|
gi 829777421  118 LTELAQQIEAMRDLNPELKV 137
Cdd:pfam01656 157 AKRLGGVIAALVGGYALLGL 176
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
 2-93 3.09e-09

SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.


Pssm-ID: 214940  Cd Length: 197  Bit Score: 54.34  E-value: 3.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421     2 ITVVGGNkgGSGKTTTASNLAIALAHEGQD-VCLLNGDLQRTAA----KHHAEReaSGIEPTFTLIEK------FDNLTq 70
Cdd:smart00962   4 ILLVGPN--GVGKTTTIAKLAARLKLKGGKkVLLVAADTFRAAAveqlKTYAEI--LGVVPVAGGEGAdpvavaKDAVE- 78

                           90       100
                   ....*....|....*....|...
gi 829777421    71 tlRALDEKYDHVIVDVAGRNSRE 93
Cdd:smart00962  79 --LAKARGYDVVLIDTAGRLHND 99
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 2-39 4.12e-07

cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 48.96  E-value: 4.12e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 829777421    2 ITVVGGnKGGSGKTTTASNLAIALAHEGQDVCLLNGDL 39
Cdd:TIGR01969   3 ITIASG-KGGTGKTTITANLGVALAKLGKKVLALDADI 39
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
9-209 9.71e-31

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 111.88  E-value: 9.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   9 KGGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAKHHAEREAsgiEPTFTLIE-KFDNLTQTLRALDEKYDHVIVDVA 87
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAARED---ERPFPVVGlARPTLHRELPSLARDYDFVVIDGP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  88 GRNSrEFITSGV-VAHQIIAPLQCSQPDLDTLTELAQQIEAMRDLNPELKVYCLQSMATTNPVLrgneRKEFLEYLEEFP 166
Cdd:NF041546  85 PRAE-DLARSAIkAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIARTAL----GREVAEALAEYG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 829777421 167 tIETLQTVICFRKVYRDCMSNGTGVVETN-NEAAKAEIMQLMKE 209
Cdd:NF041546 160 -LPVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
 1-211 1.03e-29

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 109.55  E-value: 1.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   1 MITVVGGNKGGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAKHHAEREasGIEPTFTLIEKFDNLTQTLRALDEKYD 80
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEARE--EGEPLIPVVRMGKSIRADLPKVASGYD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  81 HVIVDVAGRNSREFITSGVVAHQIIAPLQCSQPDLDTLTELAQQIEAMRDLNPELKVYCLQSMATTNPVLRGNERKEFLE 160
Cdd:PHA02518  79 YVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYREARKALA 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 829777421 161 YLEefptIETLQTVICFRKVYRDCMSNGTGVVETNNE-AAKAEIMQLMKEVF 211
Cdd:PHA02518 159 GYG----LPILRNGTTQRVAYADAAEAGGSVLELPEDdKAAEEIIQLVKELF 206
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 1-163 2.94e-25

partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved family of bacterial proteins implicated in chromosome segregation. ParB binds to DNA sequences adjacent to the origin of replication and localizes to opposite cell poles shortly following the initiation of DNA replication. ParB regulates the ParA ATPase activity by promoting nucleotide exchange in a fashion reminiscent of the exchange factors of eukaryotic G proteins. ADP-bound ParA binds single-stranded DNA, whereas the ATP-bound form dissociates ParB from its DNA binding sites. Increasing the fraction of ParA-ADP in the cell inhibits cell division, suggesting that this simple nucleotide switch may regulate cytokinesis. ParA shares sequence similarity to a conserved and widespread family of ATPases which includes the repA protein of the repABC operon in Rhizobium etli symbiotic plasmid. This operon is involved in the plasmid replication and partition.


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 95.30  E-value: 2.94e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   1 MITVVGGNKGGSGKTTTASNLAIALAHEGQDVCLLNGDLQRtaakhhaereasgieptftliekfdNLTQTLraldekYD 80
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQG-------------------------SLTSWL------YD 49

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  81 HVIVDVAGRNSREFITSGVVAHQIIAPLQCSQPDLDTLTELAQQI-EAMRDLNPELKVYC-LQSMATTnpvlRGNERKEF 158
Cdd:cd02042   50 YILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLeELKKQLNPPLLILGiLLTRVDP----RTKLAREV 125


                 ....*
gi 829777421 159 LEYLE 163
Cdd:cd02042  126 LEELK 130
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 8-210 7.52e-20

ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein BcsQ [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440805 [Multi-domain]  Cd Length: 253  Bit Score: 84.52  E-value: 7.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   8 NKGGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAKHH-------------------------------------AER 50
Cdd:COG1192    9 QKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLgldpddldptlydlllddapledaivpteipgldlipANI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  51 EASGIEPTFTLIEKFDN-LTQTLRALDEKYDHVIVDVAGrnSREFIT-SGVVA-HQIIAPLQCSQPDLDTLTELAQQIEA 127
Cdd:COG1192   89 DLAGAEIELVSRPGRELrLKRALAPLADDYDYILIDCPP--SLGLLTlNALAAaDSVLIPVQPEYLSLEGLAQLLETIEE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421 128 MR-DLNPELKV-YCLQSMATTnpvlRGNERKEFLEYLEEFPTIETLQTVICFRKVYRDCMSNGTGVVETNNEAAKAE-IM 204
Cdd:COG1192  167 VReDLNPKLEIlGILLTMVDP----RTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSKGAKaYR 242


                 ....*.
gi 829777421 205 QLMKEV 210
Cdd:COG1192  243 ALAEEL 248
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 2-137 1.47e-12

CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid a,c-diamide synthases. These include CbiA and CbiP from S.typhimurium, and CobQ from R. capsulatus. These amidases catalyze amidations to various side chains of hydrogenobyrinic acid or cobyrinic acid a,c-diamide in the biosynthesis of cobalamin (vitamin B12) from uroporphyrinogen III. Vitamin B12 is an important cofactor and an essential nutrient for many plants and animals and is primarily produced by bacteria. The family also contains dethiobiotin synthetases as well as the plasmid partitioning proteins of the MinD/ParA family.


Pssm-ID: 426369 [Multi-domain]  Cd Length: 228  Bit Score: 64.29  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421    2 ITVVGGnKGGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAKHH---------------------------------- 47
Cdd:pfam01656   1 IAIAGT-KGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEglegdiapalqalaeglkgrvnldpillkeksde 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   48 -------AEREASGIEPTFTLIEKFDNLTQTLRALDEKYDHVIVDVA---GRNSREFITSgvvAHQIIAPLQCSQPDLDT 117
Cdd:pfam01656  80 ggldlipGNIDLEKFEKELLGPRKEERLREALEALKEDYDYVIIDGApglGELLRNALIA---ADYVIIPLEPEVILVED 156

                         170       180
                  ....*....|....*....|
gi 829777421  118 LTELAQQIEAMRDLNPELKV 137
Cdd:pfam01656 157 AKRLGGVIAALVGGYALLGL 176
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 1-133 6.58e-12

Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 443989 [Multi-domain]  Cd Length: 358  Bit Score: 63.59  E-value: 6.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   1 MITVVGGnKGGSGKTTTASNLAIALAHE-GQDVCLLNGDLQ-------------------------------RTAAKHHA 48
Cdd:COG4963  104 VIAVVGA-KGGVGATTLAVNLAWALAREsGRRVLLVDLDLQfgdvalyldleprrgladalrnpdrldetllDRALTRHS 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  49 ER-----------EASGIEPtftliekfDNLTQTLRALDEKYDHVIVDVAGRNSREFITSGVVAHQIIAPLqcsQPDLDT 117
Cdd:COG4963  183 SGlsvlaapadleRAEEVSP--------EAVERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVT---EPDLPS 251

                        170
                 ....*....|....*.
gi 829777421 118 LTELAQQIEAMRDLNP 133
Cdd:COG4963  252 LRNAKRLLDLLRELGL 267
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 2-118 1.09e-11

ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ParB near the chromosomal origin of replication. It is responsible for the temporal and spatial regulation of FtsZ ring formation.


Pssm-ID: 401181 [Multi-domain]  Cd Length: 262  Bit Score: 62.09  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421    2 ITVVGGNKGGSGKTTTASNLAIALAHEGQDVCLLNGDL-QRTAAKHHAEREA----SGIE---PTFTLI----------- 62
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYFENRSAtadrTGLSlptPEHLNLpdndvaevpdg 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 829777421   63 --EKFDNLTQTLRALDEKYDHVIVDVAGRNSREFITSGVVAHQIIAPLQCSQPDLDTL 118
Cdd:pfam09140  82 enIDDARLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTPLNDSFVDFDLL 139
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 2-144 6.41e-11

GTPase domain similar to the signal recognition particle subunit 54; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognate receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349769 [Multi-domain]  Cd Length: 193  Bit Score: 58.92  E-value: 6.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   2 ITVVGGNkgGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAA----KHHAEREASGIEPTFTLIEKFDNLTQTLRALDE 77
Cdd:cd03115    3 ILLVGLQ--GSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAveqlKTLAEKLGVPVFESYTGTDPASIAQEAVEKAKL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 829777421  78 K-YDHVIVDVAGRnsrefitsgvvaHQIIAPLqcsqpdldtLTELAQQIEAmrdLNPELKVYCLQSMA 144
Cdd:cd03115   81 EgYDVLLVDTAGR------------LQKDEPL---------MEELKKVKEV---ESPDEVLLVLDATT 124
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
 2-90 1.17e-10

SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.


Pssm-ID: 459814 [Multi-domain]  Cd Length: 193  Bit Score: 58.32  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421    2 ITVVGGNkgGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAA----KHHAER----------EASGIEPTFTLIEKFDN 67
Cdd:pfam00448   3 ILLVGLQ--GSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAieqlKQLAEKlgvpvfgsktGADPAAVAFDAVEKAKA 80

                          90       100
                  ....*....|....*....|...
gi 829777421   68 ltqtlraldEKYDHVIVDVAGRN 90
Cdd:pfam00448  81 ---------ENYDVVLVDTAGRL 94
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 2-137 5.60e-10

AAA domain; This family includes a wide variety of AAA domains including some that have lost essential nucleotide binding residues in the P-loop.


Pssm-ID: 433350 [Multi-domain]  Cd Length: 177  Bit Score: 56.05  E-value: 5.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421    2 ITVVGGNKGGSGKTTTASNLAIALAHEGQDVCLLNGDLQ-------------RTAAKHHAEREASGIE------------ 56
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQgnatsglgidknnVEKTIYELLIGECNIEeaiiktvienld 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   57 --PT-----------FTLIEKFDNLTQTLRALDEKYDHVIVDVAgrNSREFIT--SGVVAHQIIAPLQCSQPDLDTLTEL 121
Cdd:pfam13614  83 liPSnidlagaeielIGIENRENILKEALEPVKDNYDYIIIDCP--PSLGLLTinALTASDSVLIPVQCEYYALEGLSQL 160

                         170
                  ....*....|....*..
gi 829777421  122 AQQIEAMRD-LNPELKV 137
Cdd:pfam13614 161 LNTIKLVKKrLNPSLEI 177
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
 2-93 3.09e-09

SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 component, a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 of the signal recognition particle has a three-domain structure: an N-terminal helical bundle domain, a GTPase domain, and the M-domain that binds the 7s RNA and also binds the signal sequence. The extreme C-terminal region is glycine-rich and lower in complexity and poorly conserved between species. The GTPase domain is evolutionary related to P-loop NTPase domains found in a variety of other proteins.


Pssm-ID: 214940  Cd Length: 197  Bit Score: 54.34  E-value: 3.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421     2 ITVVGGNkgGSGKTTTASNLAIALAHEGQD-VCLLNGDLQRTAA----KHHAEReaSGIEPTFTLIEK------FDNLTq 70
Cdd:smart00962   4 ILLVGPN--GVGKTTTIAKLAARLKLKGGKkVLLVAADTFRAAAveqlKTYAEI--LGVVPVAGGEGAdpvavaKDAVE- 78

                           90       100
                   ....*....|....*....|...
gi 829777421    71 tlRALDEKYDHVIVDVAGRNSRE 93
Cdd:smart00962  79 --LAKARGYDVVLIDTAGRLHND 99
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 1-124 1.26e-08

bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on a C-terminal tyrosine cluster and also phosphorylate endogenous protein substrates by using ATP as phosphoryl donor. Besides their capacity to function as tyrosine kinase, most of these proteins are also involved in the production and transport of exopolysaccharides. BY-kinases are involved in a number of physiological processes ranging from stress resistance to pathogenicity.


Pssm-ID: 349772 [Multi-domain]  Cd Length: 190  Bit Score: 52.57  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   1 MITvvgGNKGGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAkhhaeREASGIEPTFTliekfdnLTQTLRALDEKYD 80
Cdd:cd05387   23 AVT---SASPGEGKSTVAANLAVALAQSGKRVLLIDADLRRPSL-----HRLLGLPNEPG-------LSEVLSGQASLED 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 829777421  81 HVIVDVAGRNSreFITSGVVAHQiIAPLQCSQPDLDTLTELAQQ 124
Cdd:cd05387   88 VIQSTNIPNLD--VLPAGTVPPN-PSELLSSPRFAELLEELKEQ 128
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 2-85 1.43e-08

Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440255 [Multi-domain]  Cd Length: 289  Bit Score: 53.65  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   2 ITVVGGnKGGSGKTTTASNLAIALAHEGQDVCLLNGDLQR---------TAAKHHAEREASGIEPTFTL----IEKFD-- 66
Cdd:COG0489   95 IAVTSG-KGGEGKSTVAANLALALAQSGKRVLLIDADLRGpslhrmlglENRPGLSDVLAGEASLEDVIqpteVEGLDvl 173

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 829777421  67 ----------------NLTQTLRALDEKYDHVIVD 85
Cdd:COG0489  174 pagplppnpsellaskRLKQLLEELRGRYDYVIID 208
SRP_G cd18539
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ...
 11-89 2.23e-08

GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349786  Cd Length: 193  Bit Score: 51.83  E-value: 2.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  11 GSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAKHHAEREASGIE-PTFTLIEKFDNLTQTLRALD----EKYDHVIVD 85
Cdd:cd18539   10 GSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQTLGEQVGvPVFESGDGQSPVDIAKRALEkakeEGFDVVIVD 89


                 ....
gi 829777421  86 VAGR 89
Cdd:cd18539   90 TAGR 93
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 2-39 2.49e-08

Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically iron-sulfur (FeS) cluster scaffolds that function to assemble nascent FeS clusters for transfer to FeS-requiring enzymes. Members include the eukaryotic nucleotide-binding protein 1 (NUBP1) which is a component of the cytosolic iron-sulfur (Fe/S) protein assembly (CIA) machinery and the archael [NiFe] hydrogenase maturation protein HypB which is required for nickel insertion into [NiFe] hydrogenase.


Pssm-ID: 349757 [Multi-domain]  Cd Length: 213  Bit Score: 52.12  E-value: 2.49e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 829777421   2 ITVVGGnKGGSGKTTTASNLAIALAHEGQDVCLLNGDL 39
Cdd:cd02037    3 IAVLSG-KGGVGKSTVAVNLALALAKKGYKVGLLDADI 39
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 2-39 7.28e-08

NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid partitioning. It also contains the cytosolic Fe-S cluster assembling factor NBP35 which is required for biogenesis and export of both ribosomal subunits.


Pssm-ID: 431392 [Multi-domain]  Cd Length: 246  Bit Score: 51.30  E-value: 7.28e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 829777421    2 ITVVGGnKGGSGKTTTASNLAIALAHEGQDVCLLNGDL 39
Cdd:pfam10609   6 IAVASG-KGGVGKSTVAVNLALALARLGYKVGLLDADI 42
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 2-39 2.04e-07

septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein.


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 49.89  E-value: 2.04e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 829777421   2 ITVVGGnKGGSGKTTTASNLAIALAHEGQDVCLLNGDL 39
Cdd:cd02036    3 IVITSG-KGGVGKTTTTANLGVALAKLGKKVLLIDADI 39
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 2-39 4.12e-07

cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD family. MinD, a weak ATPase, works in bacteria with MinC as a generalized cell division inhibitor and, through interaction with MinE, prevents septum placement inappropriate sites. Often several members of this family are found in archaeal genomes, and the function is uncharacterized. More distantly related proteins ParA chromosome partitioning proteins. The exact roles of the various archaeal MinD homologs are unknown.


Pssm-ID: 131024 [Multi-domain]  Cd Length: 251  Bit Score: 48.96  E-value: 4.12e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 829777421    2 ITVVGGnKGGSGKTTTASNLAIALAHEGQDVCLLNGDL 39
Cdd:TIGR01969   3 ITIASG-KGGTGKTTITANLGVALAKLGKKVLALDADI 39
Ffh COG0541
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ...
 11-89 6.78e-07

Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440307 [Multi-domain]  Cd Length: 423  Bit Score: 48.86  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  11 GSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAKHHAEREASGIE-PTFTLIEKFDNLTQTLRALDE----KYDHVIVD 85
Cdd:COG0541  110 GSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAIEQLKTLGEQIGvPVFPEEDGKDPVDIAKRALEYakknGYDVVIVD 189


                 ....
gi 829777421  86 VAGR 89
Cdd:COG0541  190 TAGR 193
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 2-134 7.01e-07

pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE protein of the Caulobacter pilus assembly and the orf4 protein of Actinobacillus pilus formation gene cluster. The function of these proteins are unkown. The Caulobacter pilus assembly contains 7 genes: pilA, cpaA, cpaB, cpaC, cpaD, cpaE and cpaF. These genes are clustered together on chromosome.


Pssm-ID: 349765 [Multi-domain]  Cd Length: 235  Bit Score: 48.04  E-value: 7.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   2 ITVVGGnKGGSGKTTTASNLAIALAHEGQD-VCLLNGDLQ-------------------------------RTAAKHHAE 49
Cdd:cd03111    3 VAVVGA-KGGVGASTLAVNLAQELAQRAKDkVLLIDLDLPfgdlglylnlrpdydladviqnldrldrtllDSAVTRHSS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  50 R--------EASGIEPTFTliEKFDNLTQTLRAldeKYDHVIVDvAGRNSREFITSGVV-AHQIiapLQCSQPDLDTLTE 120
Cdd:cd03111   82 GlsllpapqELEDLEALGA--EQVDKLLQVLRA---FYDHIIVD-LGHFLDEVTLAVLEaADEI---LLVTQQDLPSLRN 152

                        170
                 ....*....|....
gi 829777421 121 LAQQIEAMRDLNPE 134
Cdd:cd03111  153 ARRLLDSLRELEGS 166
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 2-38 9.06e-07

Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 48.13  E-value: 9.06e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 829777421   2 ITVVGGnKGGSGKTTTASNLAIALAHEGQDVCLLNGD 38
Cdd:COG2894    5 IVVTSG-KGGVGKTTTTANLGTALALLGKKVVLIDAD 40
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 2-39 1.44e-06

MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) is a major determinant for a variety of flagellation patterns. It effects location and number of bacterial flagella during C-ring assembly.


Pssm-ID: 349758 [Multi-domain]  Cd Length: 230  Bit Score: 47.18  E-value: 1.44e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 829777421   2 ITVVGGnKGGSGKTTTASNLAIALAHEGQDVCLLNGDL 39
Cdd:cd02038    3 IAVTSG-KGGVGKTNVSANLALALSKLGKRVLLLDADL 39
PRK10416 PRK10416
signal recognition particle-docking protein FtsY; Provisional
 2-89 2.55e-06

signal recognition particle-docking protein FtsY; Provisional


Pssm-ID: 236686 [Multi-domain]  Cd Length: 318  Bit Score: 47.02  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   2 ITVVGGNkgGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAA----KHHAEReaSGIePTFTLIEK-------FDNLTq 70
Cdd:PRK10416 117 ILVVGVN--GVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAieqlQVWGER--VGV-PVIAQKEGadpasvaFDAIQ- 190

                         90
                 ....*....|....*....
gi 829777421  71 tlRALDEKYDHVIVDVAGR 89
Cdd:PRK10416 191 --AAKARGIDVLIIDTAGR 207
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 1-38 2.56e-06

SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349751 [Multi-domain]  Cd Length: 107  Bit Score: 44.73  E-value: 2.56e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 829777421   1 MITVVGGNKGGSGKTTTASNLAIALAHEGQDVCLLNGD 38
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
FlhF cd17873
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ...
 11-92 3.78e-06

signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP)-type GTPase that is essential for the placement and assembly of polar flagella. It is similar to the 54 kd subunit (SRP54) of the signal recognition particle (SRP) that mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR).


Pssm-ID: 349782 [Multi-domain]  Cd Length: 189  Bit Score: 45.62  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  11 GSGKTTTASNLA-IALAHEGQDVCLLNGDLQRTAAKHHAEREASGIEPTFTLIEKFDNLTQTLRALDEkYDHVIVDVAGR 89
Cdd:cd17873   10 GVGKTTTLAKLAaRYVLKKGKKVALITTDTYRIGAVEQLKTYAEIMGIPVEVAEDPEDLADALERLSD-RDLILIDTAGR 88


                 ...
gi 829777421  90 NSR 92
Cdd:cd17873   89 SPR 91
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 2-35 3.83e-06

Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the inner membrane of the cell. This ATP-driven oxyanion pump catalyzes the extrusion of arsenite, antimonite and arsenate. Maintenance of a low intracellular concentration of oxyanion produces resistance to the toxic agents. The pump is composed of two subunits, the catalytic ArsA subunit and the membrane subunit ArsB, which are encoded by arsA and arsB genes, respectively. Arsenic efflux in bacteria is catalyzed by either ArsB alone or by ArsAB complex. The ATP-coupled pump, however, is more efficient. ArsA is composed of two homologous halves, A1 and A2, connected by a short linker sequence.


Pssm-ID: 349755 [Multi-domain]  Cd Length: 250  Bit Score: 45.96  E-value: 3.83e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 829777421   2 ITVVGgnKGGSGKTTTASNLAIALAHEGQDVCLL 35
Cdd:cd02035    3 IFFGG--KGGVGKTTIAAATAVRLAEQGKRVLLV 34
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 2-39 4.26e-06

septum site-determining protein MinD; This model describes the bacterial and chloroplast form of MinD, a multifunctional cell division protein that guides correct placement of the septum. The homologous archaeal MinD proteins, with many archaeal genomes having two or more forms, are described by a separate model. [Cellular processes, Cell division]


Pssm-ID: 131023 [Multi-domain]  Cd Length: 261  Bit Score: 46.18  E-value: 4.26e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 829777421    2 ITVVGGNKGGSGKTTTASNLAIALAHEGQDVCLLNGDL 39
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADI 40
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
2-39 5.05e-06

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 46.19  E-value: 5.05e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 829777421   2 ITVVGGNKGGSGKTTTASNLAIALAHEGQDVCLLNGDL 39
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADI 146
FtsY cd17874
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ...
 2-89 9.60e-06

signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle (SRP) receptor (SR), is homologous to the SRP receptor alpha-subunit (SRalpha) of the eukaryotic SR. It interacts with the signal-recognition particle (SRP) and is required for the co-translational membrane targeting of proteins.


Pssm-ID: 349783  Cd Length: 199  Bit Score: 44.48  E-value: 9.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   2 ITVVGGNkgGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAA----KHHAEReaSGIEptftLIEK----------FDN 67
Cdd:cd17874    3 ILFVGVN--GVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAveqlEEWAER--LGVP----VISQnegadpaavaFDA 74

                         90       100
                 ....*....|....*....|..
gi 829777421  68 LtqtLRALDEKYDHVIVDVAGR 89
Cdd:cd17874   75 I---QAAKARGIDVVLIDTAGR 93
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 16-146 1.52e-05

MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell division, chromosome partitioning, Cell motility];


Pssm-ID: 440223 [Multi-domain]  Cd Length: 230  Bit Score: 44.11  E-value: 1.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  16 TTASNLAIALAHEGQDVCLLNGDL----------------------QRTAAKHHAEREASGIE--------PTFTLIEKF 65
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLglanldvllglepkatladvlaGEADLEDAIVQGPGGLDvlpggsgpAELAELDPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  66 DNLTQTLRALDEKYDHVIVDVA---GRNSREFITsgvVAHQIIAPlqcSQPDLDTLTELAQQIEAMRDLNPELKVYCLQS 142
Cdd:COG0455   81 ERLIRVLEELERFYDVVLVDTGagiSDSVLLFLA---AADEVVVV---TTPEPTSITDAYALLKLLRRRLGVRRAGVVVN 154


                 ....
gi 829777421 143 MATT 146
Cdd:COG0455  155 RVRS 158
SRP54_G cd17875
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ...
 11-93 2.39e-05

GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) mediates the transport to or across the plasma membrane in bacteria and the endoplasmic reticulum in eukaryotes. SRP recognizes N-terminal signal sequences of newly synthesized polypeptides at the ribosome. The SRP-polypeptide complex is then targeted to the membrane by an interaction between SRP and its cognated receptor (SR). In mammals, SRP consists of six protein subunits and a 7SL RNA. One of these subunits is a 54 kd protein (SRP54), which is a GTP-binding protein that interacts with the signal sequence when it emerges from the ribosome. SRP54 is a multidomain protein that consists of an N-terminal domain, followed by a central G (GTPase) domain and a C-terminal M domain.


Pssm-ID: 349784  Cd Length: 193  Bit Score: 43.34  E-value: 2.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  11 GSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAKHHAEREASGIEPTFTLIEKFDNLTQTLRA-----LDEKYDHVIVD 85
Cdd:cd17875   10 GSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAFDQLKQNATKARVPFYGSYTEKDPVKIAKEgvekfKKEKFDIIIVD 89


                 ....*...
gi 829777421  86 VAGRNSRE 93
Cdd:cd17875   90 TSGRHKQE 97
PRK00771 PRK00771
signal recognition particle protein Srp54; Provisional
 11-93 2.86e-05

signal recognition particle protein Srp54; Provisional


Pssm-ID: 179118 [Multi-domain]  Cd Length: 437  Bit Score: 44.04  E-value: 2.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  11 GSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAKHHAEREASGIE-PTFTLIEKFDNLTQTLRALDE--KYDHVIVDVA 87
Cdd:PRK00771 105 GSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQLAEKIGvPFYGDPDNKDAVEIAKEGLEKfkKADVIIVDTA 184


                 ....*.
gi 829777421  88 GRNSRE 93
Cdd:PRK00771 185 GRHALE 190
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 1-88 6.85e-05

NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) of the protochlorophyllide reductase, and the BchX subunit of the Chlorophyllide reductase. Members of this family use energy from ATP hydrolysis and transfer electrons through a Fe4-S4 cluster to other subunit for substrate reduction


Pssm-ID: 349761  Cd Length: 266  Bit Score: 42.35  E-value: 6.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   1 MITVVGGnKGGSGKTTTASNLAIALAHEGQDV----C---------LLNGDLQRT-----AAKHHAER------------ 50
Cdd:cd02117    1 ESIVVYG-KGGIGKSTTASNLSAALAEGGKKVlhvgCdpkhdstllLTGGKVPPTidemlTEDGTAEElrredllfsgfn 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 829777421  51 -----EASGIEP-----------TFTLIEKFdnltqtlRALDEKYDHVIVDVAG 88
Cdd:cd02117   80 gvdcvEAGGPEPgvgcggrgigtMLELLEEH-------GLLDDDYDVVIFDVLG 126
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
11-93 9.10e-05

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 42.55  E-value: 9.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  11 GSGKTTTASNLA-IALAHEGQDVCLLNGDLQRTAA----KHHAerEASGIEptFTLIEKFDNLTQTLRALdEKYDHVIVD 85
Cdd:COG1419  174 GVGKTTTIAKLAaRFVLRGKKKVALITTDTYRIGAveqlKTYA--RILGVP--VEVAYDPEELKEALERL-RDKDLVLID 248


                 ....*...
gi 829777421  86 VAGRNSRE 93
Cdd:COG1419  249 TAGRSPRD 256
minD CHL00175
septum-site determining protein; Validated
 2-39 9.86e-05

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 42.06  E-value: 9.86e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 829777421   2 ITVVGGNKGGSGKTTTASNLAIALAHEGQDVCLLNGDL 39
Cdd:CHL00175  17 IIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADI 54
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
 1-85 1.19e-04

tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) [Translation, ribosomal structure and biogenesis, Defense mechanisms];


Pssm-ID: 443264 [Multi-domain]  Cd Length: 179  Bit Score: 41.25  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   1 MITVVGGNKGgSGKTTTASNLAIALAHEGQDVCLLNGDLQRtaakHHAEREasgIEPTFTLIEKFDNLTQTLR--ALDEK 78
Cdd:COG4088    5 MLLILTGPPG-SGKTTFAKALAQRLYAEGIAVALLHSDDFR----RFLVNE---SFPKETYEEVVEDVRTTTAdnALDNG 76


                 ....*..
gi 829777421  79 YdHVIVD 85
Cdd:COG4088   77 Y-SVIVD 82
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 9-88 3.77e-04

nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. Nitrogenase is responsible for the biological nitrogen fixation, i.e. reduction of molecular nitrogen to ammonia. NifH consists of two oxygen-sensitive metallosulfur proteins: the mollybdenum-iron (alternatively, vanadium-iron or iron-iron) protein (commonly referred to as component 1), and the iron protein (commonly referred to as component 2). The iron protein is a homodimer, with an Fe4S4 cluster bound between the subunits and two ATP-binding domains. It supplies energy by ATP hydrolysis, and transfers electrons from reduced ferredoxin or flavodoxin to component 1 for the reduction of molecular nitrogen to ammonia.


Pssm-ID: 349759  Cd Length: 265  Bit Score: 40.19  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   9 KGGSGKTTTASNLAIALAHEGQDV-------------CLLNGDLQRTAAKHHAER--------------------EASGI 55
Cdd:cd02040    8 KGGIGKSTTASNLSAALAEMGKKVlhvgcdpkadstrLLLGGKAIPTVLDTLREKgeveeledvikegfngikcvESGGP 87

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 829777421  56 EP-----------TFTLIEKfdnltqtLRALDEKYDHVIVDVAG 88
Cdd:cd02040   88 EPgvgcagrgiitAINLLEE-------LGAYEEDLDVVFYDVLG 124
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 1-32 4.27e-04

CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 40.15  E-value: 4.27e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 829777421   1 MITVVGGnKGGSGKTTTASNLAIALAHEGQDV 32
Cdd:COG3640    1 MKIAVAG-KGGVGKTTLSALLARYLAEKGKPV 31
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
2-35 4.32e-04

Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];


Pssm-ID: 439774  Cd Length: 299  Bit Score: 40.19  E-value: 4.32e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 829777421   2 ITVVGGnKGGSGKTTTASNLAIALAHEGQDVCLL 35
Cdd:COG0003    5 IIFFTG-KGGVGKTTVAAATALALAERGKRTLLV 37
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 9-58 5.44e-04

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 39.75  E-value: 5.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 829777421   9 KGGSGKTTTASNLAIALAHEGQDVCLLNGDlqrtaAKHHAEREASGIE-PT 58
Cdd:PRK13230   9 KGGIGKSTTVCNIAAALAESGKKVLVVGCD-----PKADCTRNLVGEKiPT 54
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 1-32 6.03e-04

L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. Protochlorophyllide reductase catalyzes the reductive formation of chlorophyllide from protochlorophyllide during biosynthesis of chlorophylls and bacteriochlorophylls. Three genes, bchL, bchN and bchB, are involved in light-independent protochlorophyllide reduction in bacteriochlorophyll biosynthesis. In cyanobacteria, algae, and gymnosperms, three similar genes, chlL, chlN and chlB are involved in protochlorophyllide reduction during chlorophylls biosynthesis. BchL/chlL, bchN/chlN and bchB/chlB exhibit significant sequence similarity to the nifH, nifD and nifK subunits of nitrogenase, respectively. Nitrogenase catalyzes the reductive formation of ammonia from dinitrogen.


Pssm-ID: 349752  Cd Length: 267  Bit Score: 39.59  E-value: 6.03e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 829777421   1 MITVVGGnKGGSGKTTTASNLAIALAHEGQDV 32
Cdd:cd02032    1 LVIAVYG-KGGIGKSTTSSNLSAAFAKRGKKV 31
SRP54_euk TIGR01425
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ...
 11-93 9.03e-04

signal recognition particle protein SRP54; This model represents examples from the eukaryotic cytosol of the signal recognition particle protein component, SRP54. This GTP-binding protein is a component of the eukaryotic signal recognition particle, along with several other protein subunits and a 7S RNA. Some species, including Arabidopsis, have several closely related forms. The extreme C-terminal region is glycine-rich and lower in complexity, poorly conserved between species, and excluded from this model.


Pssm-ID: 273615 [Multi-domain]  Cd Length: 428  Bit Score: 39.43  E-value: 9.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421   11 GSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAA----KHHAER----------EASGIEPTFTLIEKFDNltqtlrald 76
Cdd:TIGR01425 110 GAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAfdqlKQNATKagipfygsyeESDPVKIASEGVEKFRK--------- 180

                          90
                  ....*....|....*..
gi 829777421   77 EKYDHVIVDVAGRNSRE 93
Cdd:TIGR01425 181 EKFDIIIVDTSGRHKQE 197
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 9-41 1.56e-03

capsular exopolysaccharide family; This model describes the capsular exopolysaccharide proteins in bacteria. The exopolysaccharide gene cluster consists of several genes which encode a number of proteins which regulate the exoploysaccharide biosynthesis(EPS). Atleast 13 genes espA to espM in streptococcus species seem to direct the EPS proteins and all of which share high homology. Functional roles were characterized by gene disruption experiments which resulted in exopolysaccharide-deficient phenotypes. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 38.19  E-value: 1.56e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 829777421    9 KGGSGKTTTASNLAIALAHEGQDVCLLNGDLQR 41
Cdd:TIGR01007  26 KPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRN 58
BioD COG0132
Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part ...
 11-88 1.65e-03

Dethiobiotin synthetase [Coenzyme transport and metabolism]; Dethiobiotin synthetase is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 439902 [Multi-domain]  Cd Length: 222  Bit Score: 38.22  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421  11 GSGKTTTASNLAIALAHEGQDVC---------------LLNGDlqrtAAKHhaeREASGIEPTFTLIE------------ 63
Cdd:COG0132   12 DVGKTVVTAALAAALRAAGLRVGyykpvqtgceetdggLRNGD----AELL---RRLSGLPLSYELVNpyrfeeplsphl 84

                         90       100       110
                 ....*....|....*....|....*....|....
gi 829777421  64 ---------KFDNLTQTLRALDEKYDHVIVDVAG 88
Cdd:COG0132   85 aarlegvpiDLDKILAALRALAARYDLVLVEGAG 118
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 2-85 2.90e-03

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: 36.97  E-value: 2.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829777421     2 ITVVGGNkgGSGKTTTASNLAIALAHEGQDVCLLNGDLQRTAAKHHAEREASGIEPTFTL-IEKFDNLTQtlRALDEKYD 80
Cdd:smart00382   5 ILIVGPP--GSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSgELRLRLALA--LARKLKPD 80


                   ....*
gi 829777421    81 HVIVD 85
Cdd:smart00382  81 VLILD 85
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
9-38 4.60e-03

4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;


Pssm-ID: 395090  Cd Length: 271  Bit Score: 37.04  E-value: 4.60e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 829777421    9 KGGSGKTTTASNLAIALAHEGQDVCLLNGD 38
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCD 37
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 9-60 6.87e-03

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 36.99  E-value: 6.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 829777421    9 KGGSGKTTTASNLAIALAHEGQDVCLLNGDlqrTAAkhHAEREASGIEPTFT 60
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSD---PAA--HLSVTLTGSLNNLQ 375
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 9-38 6.94e-03

arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family belongs consists of transport-energizing ATPases, including to TRC40/GET3 family involved in post-translational insertion of protein C-terminal transmembrane anchors into membranes from the cyotosolic face. This family, however, is restricted to ATPases that energize pumps that export arsenite (or antimonite).


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 36.99  E-value: 6.94e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 829777421    9 KGGSGKTTTASNLAIALAHEGQDVCLLNGD 38
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTD 40
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
 11-42 7.20e-03

Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; Adenylylsulfate kinase or related kinase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440295 [Multi-domain]  Cd Length: 189  Bit Score: 36.22  E-value: 7.20e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 829777421  11 GSGKTTTASNLAIALAHEGQDVCLLNGDLQRT 42
Cdd:COG0529   26 GSGKSTLANALERRLFERGRHVYLLDGDNVRH 57
 
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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