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Conserved domains on  [gi|446556567|ref|WP_000633913|]
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MULTISPECIES: division plane positioning ATPase MipZ [Enterobacteriaceae]

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 3.11e-33

ParA family partition ATPase;


The actual alignment was detected with superfamily member NF041546:

Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 118.04  E-value: 3.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   9 KGGSGKTTIASNLAIALANKGREVCLLNGDLQRTAAKHHAEREAAGLLPAITLveKFDNLTQTLQALNEKFDDVIVDVAG 88
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVVGL--ARPTLHRELPSLARDYDFVVIDGPP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  89 RNSKEFITSGVVAHQIIAPLQCSQPDLDTLTELEQQIDAMRNLNPELKVYCLQSMATTNPVLrgneRKEFLEYLEEFPtI 168
Cdd:NF041546  86 RAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIARTAL----GREVAEALAEYG-L 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446556567 169 QVLDSVICFRKVYRDCMSNGTGVVETN-NTAARAEIEHLMNE 209
Cdd:NF041546 161 PVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
9-209 3.11e-33

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 118.04  E-value: 3.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   9 KGGSGKTTIASNLAIALANKGREVCLLNGDLQRTAAKHHAEREAAGLLPAITLveKFDNLTQTLQALNEKFDDVIVDVAG 88
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVVGL--ARPTLHRELPSLARDYDFVVIDGPP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  89 RNSKEFITSGVVAHQIIAPLQCSQPDLDTLTELEQQIDAMRNLNPELKVYCLQSMATTNPVLrgneRKEFLEYLEEFPtI 168
Cdd:NF041546  86 RAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIARTAL----GREVAEALAEYG-L 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446556567 169 QVLDSVICFRKVYRDCMSNGTGVVETN-NTAARAEIEHLMNE 209
Cdd:NF041546 161 PVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
1-211 8.74e-29

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 106.86  E-value: 8.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   1 MITVVGGNKGGSGKTTIASNLAIALANKGREVCLLNGDLQRTAAKHHAEREAAGllPAITLVEKFDNLTQTLQALNEKFD 80
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGE--PLIPVVRMGKSIRADLPKVASGYD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  81 DVIVDVAGRNSKEFITSGVVAHQIIAPLQCSQPDLDTLTELEQQIDAMRNLNPELKVYCLQSMATTNPVLRGNERKEFLE 160
Cdd:PHA02518  79 YVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYREARKALA 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446556567 161 YLEefptIQVLDSVICFRKVYRDCMSNGTGVVE-TNNTAARAEIEHLMNEVF 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 1.23e-22

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: 88.75  E-value: 1.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   1 MITVVGGNKGGSGKTTIASNLAIALANKGREVCLLNGDLQRtaakhhaereaagllpaitlvekfdNLTQTLqalnekFD 80
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQG-------------------------SLTSWL------YD 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  81 DVIVDVAGRNSKEFITSGVVAHQIIAPLQCSQPDLDTLTELEQQI-DAMRNLNPELKVYC-LQSMATTnpvlRGNERKEF 158
Cdd:cd02042   50 YILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLeELKKQLNPPLLILGiLLTRVDP----RTKLAREV 125

                 ....*
gi 446556567 159 LEYLE 163
Cdd:cd02042  126 LEELK 130
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
8-210 9.89e-18

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: 78.75  E-value: 9.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   8 NKGGSGKTTIASNLAIALANKGREVCLLNGDLQRTAAKHHAEREAAG---------------------------LLPA-- 58
Cdd:COG1192    9 QKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLdptlydlllddapledaivpteipgldLIPAni 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  59 ------ITLVEKFDN---LTQTLQALNEKFDDVIVDVAGrnSKEFIT-SGVVA-HQIIAPLQCSQPDLDTLTELEQQIDA 127
Cdd:COG1192   89 dlagaeIELVSRPGRelrLKRALAPLADDYDYILIDCPP--SLGLLTlNALAAaDSVLIPVQPEYLSLEGLAQLLETIEE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567 128 MR-NLNPELKV-YCLQSMATTnpvlRGNERKEFLEYLEEFPTIQVLDSVICFRKVYRDCMSNGTGVVE-TNNTAARAEIE 204
Cdd:COG1192  167 VReDLNPKLEIlGILLTMVDP----RTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEyDPKSKGAKAYR 242

                 ....*.
gi 446556567 205 HLMNEV 210
Cdd:COG1192  243 ALAEEL 248
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
2-137 7.33e-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: 62.36  E-value: 7.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567    2 ITVVGGnKGGSGKTTIASNLAIALANKGREVCLLNGDLQRTAA-------------------------------KHHAER 50
Cdd:pfam01656   1 IAIAGT-KGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSsveglegdiapalqalaeglkgrvnldpillKEKSDE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   51 EAAGLLPAITLVEKFDN----------LTQTLQALNEKFDDVIVDVAGRNSKEFITSGVVAHQIIAPLQCSQPDLDTLTE 120
Cdd:pfam01656  80 GGLDLIPGNIDLEKFEKellgprkeerLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159
                         170
                  ....*....|....*..
gi 446556567  121 LEQQIDAMRNLNPELKV 137
Cdd:pfam01656 160 LGGVIAALVGGYALLGL 176
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
2-39 4.11e-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: 4.11e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 446556567    2 ITVVGGnKGGSGKTTIASNLAIALANKGREVCLLNGDL 39
Cdd:TIGR01969   3 ITIASG-KGGTGKTTITANLGVALAKLGKKVLALDADI 39
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
2-93 5.69e-07

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: 48.17  E-value: 5.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567     2 ITVVGGNkgGSGKTTIASNLAIALANKG-REVCLLNGDLQRTAA----KHHAEREAAGLLPAITLVEKFDNLTQTLQ-AL 75
Cdd:smart00962   4 ILLVGPN--GVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAveqlKTYAEILGVVPVAGGEGADPVAVAKDAVElAK 81
                           90
                   ....*....|....*...
gi 446556567    76 NEKFDDVIVDVAGRNSKE 93
Cdd:smart00962  82 ARGYDVVLIDTAGRLHND 99
 
Name Accession Description Interval E-value
ParA_partition NF041546
ParA family partition ATPase;
9-209 3.11e-33

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 118.04  E-value: 3.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   9 KGGSGKTTIASNLAIALANKGREVCLLNGDLQRTAAKHHAEREAAGLLPAITLveKFDNLTQTLQALNEKFDDVIVDVAG 88
Cdd:NF041546   8 KGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDWAAAREDERPFPVVGL--ARPTLHRELPSLARDYDFVVIDGPP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  89 RNSKEFITSGVVAHQIIAPLQCSQPDLDTLTELEQQIDAMRNLNPELKVYCLQSMATTNPVLrgneRKEFLEYLEEFPtI 168
Cdd:NF041546  86 RAEDLARSAIKAADLVLIPVQPSPYDLWASADTVDLIKEAREYTPGLKAAFVLNRAIARTAL----GREVAEALAEYG-L 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446556567 169 QVLDSVICFRKVYRDCMSNGTGVVETN-NTAARAEIEHLMNE 209
Cdd:NF041546 161 PVLKTRIGQRVAFAESAAEGLTVFEAEpDGKAAREIRALAKE 202
PHA02518 PHA02518
ParA-like protein; Provisional
1-211 8.74e-29

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 106.86  E-value: 8.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   1 MITVVGGNKGGSGKTTIASNLAIALANKGREVCLLNGDLQRTAAKHHAEREAAGllPAITLVEKFDNLTQTLQALNEKFD 80
Cdd:PHA02518   1 KIIAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGE--PLIPVVRMGKSIRADLPKVASGYD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  81 DVIVDVAGRNSKEFITSGVVAHQIIAPLQCSQPDLDTLTELEQQIDAMRNLNPELKVYCLQSMATTNPVLRGNERKEFLE 160
Cdd:PHA02518  79 YVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPDLVELIKARQEVTDGLPKFAFIISRAIKNTQLYREARKALA 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446556567 161 YLEefptIQVLDSVICFRKVYRDCMSNGTGVVE-TNNTAARAEIEHLMNEVF 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 1.23e-22

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: 88.75  E-value: 1.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   1 MITVVGGNKGGSGKTTIASNLAIALANKGREVCLLNGDLQRtaakhhaereaagllpaitlvekfdNLTQTLqalnekFD 80
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQG-------------------------SLTSWL------YD 49
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  81 DVIVDVAGRNSKEFITSGVVAHQIIAPLQCSQPDLDTLTELEQQI-DAMRNLNPELKVYC-LQSMATTnpvlRGNERKEF 158
Cdd:cd02042   50 YILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGLAKLLDTLeELKKQLNPPLLILGiLLTRVDP----RTKLAREV 125

                 ....*
gi 446556567 159 LEYLE 163
Cdd:cd02042  126 LEELK 130
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
8-210 9.89e-18

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: 78.75  E-value: 9.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   8 NKGGSGKTTIASNLAIALANKGREVCLLNGDLQRTAAKHHAEREAAG---------------------------LLPA-- 58
Cdd:COG1192    9 QKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLdptlydlllddapledaivpteipgldLIPAni 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  59 ------ITLVEKFDN---LTQTLQALNEKFDDVIVDVAGrnSKEFIT-SGVVA-HQIIAPLQCSQPDLDTLTELEQQIDA 127
Cdd:COG1192   89 dlagaeIELVSRPGRelrLKRALAPLADDYDYILIDCPP--SLGLLTlNALAAaDSVLIPVQPEYLSLEGLAQLLETIEE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567 128 MR-NLNPELKV-YCLQSMATTnpvlRGNERKEFLEYLEEFPTIQVLDSVICFRKVYRDCMSNGTGVVE-TNNTAARAEIE 204
Cdd:COG1192  167 VReDLNPKLEIlGILLTMVDP----RTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEyDPKSKGAKAYR 242

                 ....*.
gi 446556567 205 HLMNEV 210
Cdd:COG1192  243 ALAEEL 248
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
2-137 7.33e-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: 62.36  E-value: 7.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567    2 ITVVGGnKGGSGKTTIASNLAIALANKGREVCLLNGDLQRTAA-------------------------------KHHAER 50
Cdd:pfam01656   1 IAIAGT-KGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSsveglegdiapalqalaeglkgrvnldpillKEKSDE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   51 EAAGLLPAITLVEKFDN----------LTQTLQALNEKFDDVIVDVAGRNSKEFITSGVVAHQIIAPLQCSQPDLDTLTE 120
Cdd:pfam01656  80 GGLDLIPGNIDLEKFEKellgprkeerLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVEDAKR 159
                         170
                  ....*....|....*..
gi 446556567  121 LEQQIDAMRNLNPELKV 137
Cdd:pfam01656 160 LGGVIAALVGGYALLGL 176
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
1-212 3.95e-11

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: 61.28  E-value: 3.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   1 MITVVGGnKGGSGKTTIASNLAIALA-NKGREVCLLNGDLQ-------------------------------RTAAKHHA 48
Cdd:COG4963  104 VIAVVGA-KGGVGATTLAVNLAWALArESGRRVLLVDLDLQfgdvalyldleprrgladalrnpdrldetllDRALTRHS 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  49 EReaAGLLPAITLVEKFDNLT-----QTLQALNEKFDDVIVDVAGRNSKEFITSGVVAHQIIAPLqcsQPDLDTLTELEQ 123
Cdd:COG4963  183 SG--LSVLAAPADLERAEEVSpeaveRLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVVLVT---EPDLPSLRNAKR 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567 124 QIDAMRNLN-PELKVYCLQSMATTNPVLRgneRKEFLEYLeEFPtiqvLDSVICF-RKVYRDCMSNGTGVVETN-NTAAR 200
Cdd:COG4963  258 LLDLLRELGlPDDKVRLVLNRVPKRGEIS---AKDIEEAL-GLP----VAAVLPNdPKAVAEAANQGRPLAEVApKSPLA 329
                        250
                 ....*....|..
gi 446556567 201 AEIEHLMNEVFG 212
Cdd:COG4963  330 KAIRKLAARLTG 341
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
2-93 4.22e-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: 59.69  E-value: 4.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   2 ITVVGGNkgGSGKTTIASNLAIALANKGREVCLLNGDLQRTAA----KHHAEREAAGLLPAITLVEKFDNLTQTLQAL-N 76
Cdd:cd03115    3 ILLVGLQ--GSGKTTTLAKLARYYQEKGKKVLLIAADTFRAAAveqlKTLAEKLGVPVFESYTGTDPASIAQEAVEKAkL 80
                         90
                 ....*....|....*..
gi 446556567  77 EKFDDVIVDVAGRNSKE 93
Cdd:cd03115   81 EGYDVLLVDTAGRLQKD 97
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
2-127 7.00e-10

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: 57.08  E-value: 7.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567    2 ITVVGGNKGGSGKTTIASNLAIALANKGREVCLLNGDL-QRTAAKHHAEREA-------------AGLLPAITLVEKFDN 67
Cdd:pfam09140   2 VIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLrQRTFHRYFENRSAtadrtglslptpeHLNLPDNDVAEVPDG 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446556567   68 LTQTLQALNEKFDD-------VIVDVAGRNSKEFITSGVVAHQIIAPLQCSQPDLDTLTeleqQIDA 127
Cdd:pfam09140  82 ENIDDARLEEAFADlearcdfIVIDTPGSDSPLSRLAHSRADTLVTPLNDSFVDFDLLG----QVDP 144
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
2-39 1.11e-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: 53.61  E-value: 1.11e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 446556567    2 ITVVGGnKGGSGKTTIASNLAIALANKGREVCLLNGDL 39
Cdd:pfam10609   6 IAVASG-KGGVGKSTVAVNLALALARLGYKVGLLDADI 42
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
2-90 1.20e-08

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: 52.93  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567    2 ITVVGGNkgGSGKTTIASNLAIALANKGREVCLLNGDLQRTAA----KHHAER-------EAAGLLPAITLVEKFDnltq 70
Cdd:pfam00448   3 ILLVGLQ--GSGKTTTIAKLAAYLKKKGKKVLLVAADTFRAAAieqlKQLAEKlgvpvfgSKTGADPAAVAFDAVE---- 76
                          90       100
                  ....*....|....*....|
gi 446556567   71 tlQALNEKFDDVIVDVAGRN 90
Cdd:pfam00448  77 --KAKAENYDVVLVDTAGRL 94
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
2-39 1.47e-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: 52.89  E-value: 1.47e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446556567   2 ITVVGGnKGGSGKTTIASNLAIALANKGREVCLLNGDL 39
Cdd:cd02037    3 IAVLSG-KGGVGKSTVAVNLALALAKKGYKVGLLDADI 39
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
2-137 4.70e-08

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: 51.05  E-value: 4.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567    2 ITVVGGNKGGSGKTTIASNLAIALANKGREVCLLNGDLQRTA---------------------------AKHHAEREAAG 54
Cdd:pfam13614   3 VIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNAtsglgidknnvektiyelligecnieeAIIKTVIENLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   55 LLPA-ITLVEKFDNLTQT----------LQALNEKFDDVIVDVAGRNSKEFITSGVVAHQIIAPLQCSQPDLDTLTELEQ 123
Cdd:pfam13614  83 LIPSnIDLAGAEIELIGIenrenilkeaLEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEGLSQLLN 162
                         170
                  ....*....|....*
gi 446556567  124 QID-AMRNLNPELKV 137
Cdd:pfam13614 163 TIKlVKKRLNPSLEI 177
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
2-39 5.71e-08

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: 51.42  E-value: 5.71e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446556567   2 ITVVGGnKGGSGKTTIASNLAIALANKGREVCLLNGDL 39
Cdd:cd02038    3 IAVTSG-KGGVGKTNVSANLALALSKLGKRVLLLDADL 39
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
2-85 6.16e-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: 51.73  E-value: 6.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   2 ITVVGGnKGGSGKTTIASNLAIALANKGREVCLLNGDLQR-------------------------TAAKHHAEREAAGLL 56
Cdd:COG0489   95 IAVTSG-KGGEGKSTVAANLALALAQSGKRVLLIDADLRGpslhrmlglenrpglsdvlageaslEDVIQPTEVEGLDVL 173
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 446556567  57 PAITLVE------KFDNLTQTLQALNEKFDDVIVD 85
Cdd:COG0489  174 PAGPLPPnpsellASKRLKQLLEELRGRYDYVIID 208
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
2-39 1.26e-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: 50.28  E-value: 1.26e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446556567   2 ITVVGGnKGGSGKTTIASNLAIALANKGREVCLLNGDL 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 4.11e-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: 4.11e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 446556567    2 ITVVGGnKGGSGKTTIASNLAIALANKGREVCLLNGDL 39
Cdd:TIGR01969   3 ITIASG-KGGTGKTTITANLGVALAKLGKKVLALDADI 39
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
2-93 5.69e-07

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: 48.17  E-value: 5.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567     2 ITVVGGNkgGSGKTTIASNLAIALANKG-REVCLLNGDLQRTAA----KHHAEREAAGLLPAITLVEKFDNLTQTLQ-AL 75
Cdd:smart00962   4 ILLVGPN--GVGKTTTIAKLAARLKLKGgKKVLLVAADTFRAAAveqlKTYAEILGVVPVAGGEGADPVAVAKDAVElAK 81
                           90
                   ....*....|....*...
gi 446556567    76 NEKFDDVIVDVAGRNSKE 93
Cdd:smart00962  82 ARGYDVVLIDTAGRLHND 99
SRP_G cd18539
GTPase domain of signal recognition particle protein; The signal recognition particle (SRP) ...
11-89 1.10e-06

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: 47.21  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  11 GSGKTTIASNLAIALANKGREVCLLNGDLQRTAAKHHAEreaagLLPAITLVEKFDNLTQ------TLQALN----EKFD 80
Cdd:cd18539   10 GSGKTTTAAKLALYLKKKGKKVLLVAADVYRPAAIEQLQ-----TLGEQVGVPVFESGDGqspvdiAKRALEkakeEGFD 84

                 ....*....
gi 446556567  81 DVIVDVAGR 89
Cdd:cd18539   85 VVIVDTAGR 93
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
1-38 1.16e-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: 45.50  E-value: 1.16e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446556567   1 MITVVGGNKGGSGKTTIASNLAIALANKGREVCLLNGD 38
Cdd:cd01983    1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
2-35 1.20e-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: 47.50  E-value: 1.20e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446556567   2 ITVVGgnKGGSGKTTIASNLAIALANKGREVCLL 35
Cdd:cd02035    3 IFFGG--KGGVGKTTIAAATAVRLAEQGKRVLLV 34
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
2-91 1.21e-06

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: 47.66  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   2 ITVVGGnKGGSGKTTIASNLAIALANK-GREVCLLNGDLQ-------------------------------RTAAKHHAE 49
Cdd:cd03111    3 VAVVGA-KGGVGASTLAVNLAQELAQRaKDKVLLIDLDLPfgdlglylnlrpdydladviqnldrldrtllDSAVTRHSS 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446556567  50 REAagLLPAITLVEKFDNL-----TQTLQALNEKFDDVIVDVAGRNS 91
Cdd:cd03111   82 GLS--LLPAPQELEDLEALgaeqvDKLLQVLRAFYDHIIVDLGHFLD 126
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
2-38 3.06e-06

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 46.59  E-value: 3.06e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 446556567   2 ITVVGGnKGGSGKTTIASNLAIALANKGREVCLLNGD 38
Cdd:COG2894    5 IVVTSG-KGGVGKTTTTANLGTALALLGKKVVLIDAD 40
SRP54_G cd17875
GTPase domain of the signal recognition 54 kDa subunit; The signal recognition particle (SRP) ...
11-93 3.54e-06

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: 45.65  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  11 GSGKTTIASNLAIALANKGREVCLLNGDLQRTAA----KHHAER----------EAAGLLPAITLVEKFdnltqtlqaLN 76
Cdd:cd17875   10 GSGKTTTAAKLAYYYQKKGYKVGLVCADTFRAGAfdqlKQNATKarvpfygsytEKDPVKIAKEGVEKF---------KK 80
                         90
                 ....*....|....*..
gi 446556567  77 EKFDDVIVDVAGRNSKE 93
Cdd:cd17875   81 EKFDIIIVDTSGRHKQE 97
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
2-39 9.62e-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: 45.02  E-value: 9.62e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 446556567    2 ITVVGGNKGGSGKTTIASNLAIALANKGREVCLLNGDL 39
Cdd:TIGR01968   3 VIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADI 40
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
2-35 1.10e-05

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 45.20  E-value: 1.10e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446556567   2 ITVVGGnKGGSGKTTIASNLAIALANKGREVCLL 35
Cdd:COG0003    5 IIFFTG-KGGVGKTTVAAATALALAERGKRTLLV 37
CysC COG0529
Adenylylsulfate kinase or related kinase [Inorganic ion transport and metabolism]; ...
11-42 4.12e-05

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: 42.77  E-value: 4.12e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446556567  11 GSGKTTIASNLAIALANKGREVCLLNGDLQRT 42
Cdd:COG0529   26 GSGKSTLANALERRLFERGRHVYLLDGDNVRH 57
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
1-32 5.06e-05

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 42.85  E-value: 5.06e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446556567   1 MITVVGGnKGGSGKTTIASNLAIALANKGREV 32
Cdd:COG3640    1 MKIAVAG-KGGVGKTTLSALLARYLAEKGKPV 31
SRP54_euk TIGR01425
signal recognition particle protein SRP54; This model represents examples from the eukaryotic ...
11-93 5.37e-05

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: 43.28  E-value: 5.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   11 GSGKTTIASNLAIALANKGREVCLLNGDLQRTAA----KHHAER----------EAAGLLPAITLVEKFDnltqtlqalN 76
Cdd:TIGR01425 110 GAGKTTTCTKLAYYYKRRGFKPALVCADTFRAGAfdqlKQNATKagipfygsyeESDPVKIASEGVEKFR---------K 180
                          90
                  ....*....|....*..
gi 446556567   77 EKFDDVIVDVAGRNSKE 93
Cdd:TIGR01425 181 EKFDIIIVDTSGRHKQE 197
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
1-41 6.00e-05

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: 42.17  E-value: 6.00e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446556567   1 MITvvgGNKGGSGKTTIASNLAIALANKGREVCLLNGDLQR 41
Cdd:cd05387   23 AVT---SASPGEGKSTVAANLAVALAQSGKRVLLIDADLRR 60
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
2-39 6.03e-05

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 43.11  E-value: 6.03e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446556567   2 ITVVGGNKGGSGKTTIASNLAIALANKGREVCLLNGDL 39
Cdd:PRK11670 109 IIAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADI 146
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
16-138 1.14e-04

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: 41.80  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  16 TIASNLAIALANKGREVCLLNGDL----------------------QRTAAKHHAEREAAGL--LPAITLVEKFDNLT-- 69
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLglanldvllglepkatladvlaGEADLEDAIVQGPGGLdvLPGGSGPAELAELDpe 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446556567  70 ----QTLQALNEKFDDVIVDVAGRNSKEFITSGVVAHQIIAPlqcSQPDLDTLTELEQQIDAMRNLNPELKVY 138
Cdd:COG0455   81 erliRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVV---TTPEPTSITDAYALLKLLRRRLGVRRAG 150
FtsY cd17874
signal recognition particle receptor FtsY; FtsY, the bacterial signal-recognition particle ...
2-89 1.38e-04

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: 41.40  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   2 ITVVGGNkgGSGKTTIASNLAIALANKGREVCLLNGDLQRTAA----KHHAEREAAGLL-------PAITLvekFDNLtq 70
Cdd:cd17874    3 ILFVGVN--GVGKTTTIGKLAHYLKNQGKKVVLAAGDTFRAAAveqlEEWAERLGVPVIsqnegadPAAVA---FDAI-- 75
                         90
                 ....*....|....*....
gi 446556567  71 tLQALNEKFDDVIVDVAGR 89
Cdd:cd17874   76 -QAAKARGIDVVLIDTAGR 93
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
1-38 1.97e-04

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: 41.20  E-value: 1.97e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446556567   1 MITVVGGnKGGSGKTTIASNLAIALANKGREVCLLNGD 38
Cdd:cd02117    1 ESIVVYG-KGGIGKSTTASNLSAALAEGGKKVLHVGCD 37
Kti12 COG4088
tRNA uridine 5-carbamoylmethylation protein Kti12 (Killer toxin insensitivity protein) ...
1-85 3.86e-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: 39.71  E-value: 3.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   1 MITVVGGNKGgSGKTTIASNLAIALANKGREVCLLNGDLQRtaakHHAEREAAGLLPAITLVEKFdnLTQTLQALNEKFD 80
Cdd:COG4088    5 MLLILTGPPG-SGKTTFAKALAQRLYAEGIAVALLHSDDFR----RFLVNESFPKETYEEVVEDV--RTTTADNALDNGY 77

                 ....*
gi 446556567  81 DVIVD 85
Cdd:COG4088   78 SVIVD 82
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
9-38 4.20e-04

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: 40.46  E-value: 4.20e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 446556567    9 KGGSGKTTIASNLAIALANKGREVCLLNGD 38
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTD 40
VirC1 pfam07015
VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium ...
9-206 4.23e-04

VirC1 protein; This family consists of several bacterial VirC1 proteins. In Agrobacterium tumefaciens, a cis-active 24-base-pair sequence adjacent to the right border of the T-DNA, called overdrive, stimulates tumour formation by increasing the level of T-DNA processing. It is thought that the virC operon which enhances T-DNA processing probably does so because the VirC1 protein interacts with overdrive. It has now been shown that the virC1 gene product binds to overdrive but not to the right border of T-DNA.


Pssm-ID: 148565 [Multi-domain]  Cd Length: 231  Bit Score: 40.25  E-value: 4.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567    9 KGGSGKTTIASNLAIALANKGREVCLLNGDLQR--TAAKHHAEREAA-GLLPAITLVEKFDNLTQTLQ-ALNEKFDDVIV 84
Cdd:pfam07015  10 KGGAGKTTALMGLCSALASDGKRVALFEADENRplTKWRENALRKGTwDPACEIFNADELPLLEQAYEhAEGSGFDYALA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   85 DVAGRNSKefITSGVVAHQ--IIAPLQCSQPDLD-TLTELEQQIDAMRNLNPELKVYCLQsmaTTNPVLRGNERKEF-LE 160
Cdd:pfam07015  90 DTHGGSSE--LNNTIIASSdlLLIPTMLTPLDIDeALATYRYVIELLLTENLAIPTAILR---QRVPVGRLTSSQRFcSD 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  161 YLEEFPtiqVLDSVICFRKVYRDCMSNG--------------TGVVETNNTAARAEIEHL 206
Cdd:pfam07015 165 MLEQLP---VFDCPMHERDAFAAMKERGmlhitlenlsqipsMRLALRNLRTAMEDLDRL 221
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
9-42 4.38e-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: 4.38e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446556567   9 KGGSGKTTIASNLAIALANKGREV-------------CLLNGDLQRT 42
Cdd:cd02040    8 KGGIGKSTTASNLSAALAEMGKKVlhvgcdpkadstrLLLGGKAIPT 54
Ffh COG0541
Signal recognition particle GTPase [Intracellular trafficking, secretion, and vesicular ...
11-89 7.55e-04

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


Pssm-ID: 440307 [Multi-domain]  Cd Length: 423  Bit Score: 39.62  E-value: 7.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  11 GSGKTTIASNLAIALANKGREVCLLNGDLQRTAA----KHHAEREAAGLLPAITLVEKFDNLTQTLQALNEKFDDV-IVD 85
Cdd:COG0541  110 GSGKTTTAAKLAKYLKKKGKKPLLVAADVYRPAAieqlKTLGEQIGVPVFPEEDGKDPVDIAKRALEYAKKNGYDVvIVD 189

                 ....
gi 446556567  86 VAGR 89
Cdd:COG0541  190 TAGR 193
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
1-32 1.03e-03

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: 39.20  E-value: 1.03e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446556567   1 MITVVGGnKGGSGKTTIASNLAIALANKGREV 32
Cdd:cd02032    1 LVIAVYG-KGGIGKSTTSSNLSAAFAKRGKKV 31
minD CHL00175
septum-site determining protein; Validated
2-39 1.19e-03

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 38.98  E-value: 1.19e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446556567   2 ITVVGGNKGGSGKTTIASNLAIALANKGREVCLLNGDL 39
Cdd:CHL00175  17 IIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADI 54
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
10-42 1.48e-03

pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a variant of type IV pili. It is part of the SIMIBI superfamily which contains a variety of proteins which share a common ATP-binding domain. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion.


Pssm-ID: 349778 [Multi-domain]  Cd Length: 219  Bit Score: 38.29  E-value: 1.48e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 446556567  10 GGSGKTTIASNLAIALANKGREVCLLN-GDLQRT 42
Cdd:cd17869   13 GGSGKSTVAAACAYTLAEKGKKTLYLNmERLQST 46
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
1-38 1.59e-03

accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in the incorporation of nickel into the complex active site ([Ni-4Fe-4S]) cluster of Ni,Fe-dependent carbon monoxide dehydrogenase (CODH). CODH from Rhodospirillum rubrum catalyzes the reversible oxidation of CO to CO2. CODH contains a nickel-iron-sulfur cluster (C-center) and an iron-sulfur cluster (B-center). CO oxidation occurs at the C-center. Three accessory proteins encoded by cooCTJ genes are involved in nickel incorporation into a nickel site. CooC functions as a nickel insertase that mobilizes nickel to apoCODH using energy released from ATP hydrolysis. CooC is a homodimer and has NTPase activities. Mutation at the P-loop abolishs its function.


Pssm-ID: 349754 [Multi-domain]  Cd Length: 249  Bit Score: 38.45  E-value: 1.59e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446556567   1 MITVVGGnKGGSGKTTIASNLAIALANKGREVCLLNGD 38
Cdd:cd02034    1 MKIAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDAD 37
PRK00889 PRK00889
adenylylsulfate kinase; Provisional
11-42 2.19e-03

adenylylsulfate kinase; Provisional


Pssm-ID: 179157  Cd Length: 175  Bit Score: 37.69  E-value: 2.19e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446556567  11 GSGKTTIASNLAIALANKGREVCLLNGDLQRT 42
Cdd:PRK00889  14 GAGKTTIARALAEKLREAGYPVEVLDGDAVRT 45
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
9-60 2.30e-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: 38.53  E-value: 2.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446556567    9 KGGSGKTTIASNLAIALANKGREVCLLNGDlqrTAAkhHAEREAAGLLPAIT 60
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSD---PAA--HLSVTLTGSLNNLQ 375
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
2-28 3.25e-03

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 37.36  E-value: 3.25e-03
                         10        20
                 ....*....|....*....|....*..
gi 446556567   2 ITVVGGnKGGSGKTTIASNLAIALANK 28
Cdd:cd03110    2 IAVLSG-KGGTGKTTITANLAVLLYNV 27
PRK00771 PRK00771
signal recognition particle protein Srp54; Provisional
11-93 3.38e-03

signal recognition particle protein Srp54; Provisional


Pssm-ID: 179118 [Multi-domain]  Cd Length: 437  Bit Score: 37.88  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567  11 GSGKTTIASNLAIALANKGREVCLLNGDLQRTAAKHHAER--EAAGLL--------PAITLVEKfdnltqTLQALnEKFD 80
Cdd:PRK00771 105 GSGKTTTAAKLARYFKKKGLKVGLVAADTYRPAAYDQLKQlaEKIGVPfygdpdnkDAVEIAKE------GLEKF-KKAD 177
                         90
                 ....*....|...
gi 446556567  81 DVIVDVAGRNSKE 93
Cdd:PRK00771 178 VIIVDTAGRHALE 190
PRK13849 PRK13849
conjugal transfer ATPase VirC1;
9-53 3.44e-03

conjugal transfer ATPase VirC1;


Pssm-ID: 139909  Cd Length: 231  Bit Score: 37.51  E-value: 3.44e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446556567   9 KGGSGKTTIASNLAIALANKGREVCLLNGDLQR--TAAKHHAEREAA 53
Cdd:PRK13849  10 KGGAGKTTALMGLCAALASDGKRVALFEADENRplTRWKENALRSNT 56
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
9-41 4.05e-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: 37.03  E-value: 4.05e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 446556567    9 KGGSGKTTIASNLAIALANKGREVCLLNGDLQR 41
Cdd:TIGR01007  26 KPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRN 58
Zeta_toxin pfam06414
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ...
4-96 4.26e-03

Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.


Pssm-ID: 428926  Cd Length: 192  Bit Score: 36.96  E-value: 4.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567    4 VVGGnKGGSGKTTIASNLAIALAnKGREVCLLNGDLQRTAAKHHAEREAAGLLPAITLVEKFDN--LTQTLQALNEKFDD 81
Cdd:pfam06414  15 LLGG-QPGAGKTELARALLDELG-RQGNVVRIDPDDFRELHPHYRELQAADPKTASEYTQPDASrwVEKLLQHAIENGYN 92
                          90
                  ....*....|....*
gi 446556567   82 VIVDVAGRNSKEFIT 96
Cdd:pfam06414  93 IILEGTLRSPDVAKK 107
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
2-40 4.49e-03

cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found immediately upsteam of bacterial cellulose synthase (bcs) genes in a broad range of bacteria, including both copies of the bcs locus in Klebsiella pneumoniae. In several species it is seen clearly as part of the bcs operon. It is identified as a probable component of the bacterial cellulose metabolic process not only by gene location, but also by partial phylogenetic profiling, or Haft-Selengut algorithm (), based on a bacterial cellulose biosynthesis genome property profile. Cellulose plays an important role in biofilm formation and structural integrity in some bacteria. Mutants in yhjQ in Escherichia coli, show altered morphology an growth, but the function of YhjQ has not yet been determined. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 36.94  E-value: 4.49e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 446556567    2 ITVVGGnKGGSGKTTIASNLAIALANKGREVCLLNGDLQ 40
Cdd:TIGR03371   4 IAIVSV-RGGVGKTTLTANLASALKLLGEPVLAIDLDPQ 41
CobB_N cd05388
N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase ...
4-32 5.15e-03

N-terminal domain of cobyrinic acid a,c-diamide synthase; Cobyrinic acid a,c-diamide synthase (CobB, CbiA). Biosynthesis of cobalamin (vitamin B12) requires more than two dozen different enzymes. CobB catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of cobyrinic acid, via the formation of a phosphorylated intermediate, using glutamine or ammonia as the nitrogen source. CobB is comprised of two protein domains: the C-terminal glutaminase domain and the N-terminal ATP-binding domain. The glutaminase domain catalyzes the hydrolysis of glutamine to glutamate and ammonia. It belongs to the triad class of glutamine amidotransferases. This classification is based on the N-terminal domain which catalyzes the ultimate synthesis of the diamide product by using energy from the hydrolysis of ATP and ammonia transferred from the C-terminal domain.


Pssm-ID: 349773 [Multi-domain]  Cd Length: 193  Bit Score: 36.43  E-value: 5.15e-03
                         10        20
                 ....*....|....*....|....*....
gi 446556567   4 VVGGNKGGSGKTTIASNLAIALANKGREV 32
Cdd:cd05388    4 VIAGTSSGSGKTTITLGLMRALARRGLRV 32
PRK10416 PRK10416
signal recognition particle-docking protein FtsY; Provisional
2-89 6.33e-03

signal recognition particle-docking protein FtsY; Provisional


Pssm-ID: 236686 [Multi-domain]  Cd Length: 318  Bit Score: 36.61  E-value: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446556567   2 ITVVGGNkgGSGKTTIASNLAIALANKGREVCLLNGDLQRTAA----KHHAEReaAGlLPAITLVEK-------FDNLTq 70
Cdd:PRK10416 117 ILVVGVN--GVGKTTTIGKLAHKYKAQGKKVLLAAGDTFRAAAieqlQVWGER--VG-VPVIAQKEGadpasvaFDAIQ- 190
                         90
                 ....*....|....*....
gi 446556567  71 tlQALNEKFDDVIVDVAGR 89
Cdd:PRK10416 191 --AAKARGIDVLIIDTAGR 207
PRK05537 PRK05537
bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;
11-42 6.33e-03

bifunctional sulfate adenylyltransferase/adenylylsulfate kinase;


Pssm-ID: 180124 [Multi-domain]  Cd Length: 568  Bit Score: 36.96  E-value: 6.33e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 446556567  11 GSGKTTIASNLAIAL-ANKGREVCLLNGDLQRT 42
Cdd:PRK05537 402 GAGKSTIAKALMVKLmEMRGRPVTLLDGDVVRK 434
CobB COG1797
Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a, ...
4-32 6.47e-03

Cobyrinic acid a,c-diamide synthase [Coenzyme transport and metabolism]; Cobyrinic acid a,c-diamide synthase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441402 [Multi-domain]  Cd Length: 459  Bit Score: 37.01  E-value: 6.47e-03
                         10        20
                 ....*....|....*....|....*....
gi 446556567   4 VVGGNKGGSGKTTIASNLAIALANKGREV 32
Cdd:COG1797    7 VIAAPHSGSGKTTVTLGLLAALRRRGLKV 35
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
11-42 7.63e-03

Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.


Pssm-ID: 396247 [Multi-domain]  Cd Length: 154  Bit Score: 35.76  E-value: 7.63e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 446556567   11 GSGKTTIASNLAIALANKGREVCLLNGDLQRT 42
Cdd:pfam01583  12 GAGKSTIANALERKLFEQGRSVYVLDGDNVRH 43
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
9-32 8.13e-03

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 36.48  E-value: 8.13e-03
                         10        20
                 ....*....|....*....|....
gi 446556567   9 KGGSGKTTIASNLAIALANKGREV 32
Cdd:PRK13185  10 KGGIGKSTTSSNLSAAFAKLGKKV 33
 
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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