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Conserved domains on  [gi|1250768313|gb|PCY62999|]
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chromosome partitioning protein ParA [Listeria monocytogenes]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PrgP super family cl49321
ParA superfamily DNA segregation protein PrgP;
24-319 1.93e-133

ParA superfamily DNA segregation protein PrgP;


The actual alignment was detected with superfamily member NF041283:

Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 381.02  E-value: 1.93e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  24 RVIINANQKGGVGKTTNTTMEAIILAHVFNKKVLLIDEDMQGNETSFMSKTYDVIEFPMSLMKAIEEGDLTKAIVNLDEN 103
Cdd:NF041283    3 YVIVLANQKGGVGKTTDTVMEAVVASSVFNKKVLVIDTDLQGNATQFLSKTFNVPNFPQSFMKCVEDGDLEKGIVHLTPN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 104 IDIIPGSYDMRKMVNFLIGKFKTEEAQTFYLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVVQETQQFALEG 183
Cdd:NF041283   83 LDLIAGDYDTRELGDFLADKFKSEYDRTFYLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYVIVIQETQQFAFEG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 184 SNTFISTYLNTLVDDFGSRFKTEIIGILPVLLQKKRKLHEKILETTKEKFGKENIFGTTINNHARLELYGKFGVQFEDHW 263
Cdd:NF041283  163 SKKLILTYLQTLVDDFGDEINVQVAGILPVLLQARRPLQQKIVDETIEYFGKDNVFNNIIKNHARLEWYGEQGIQFEDYH 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1250768313 264 DRTMFALYTDIVQEMLERMQLIENGSDLDNYQYKPIFYNPKigKVTALGKEIVVNG 319
Cdd:NF041283  243 DRRMFALFADIFCELEERIKSFEKTGDVENFTYTHQYINQN--KLTPKGKEITING 296
 
Name Accession Description Interval E-value
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
24-319 1.93e-133

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 381.02  E-value: 1.93e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  24 RVIINANQKGGVGKTTNTTMEAIILAHVFNKKVLLIDEDMQGNETSFMSKTYDVIEFPMSLMKAIEEGDLTKAIVNLDEN 103
Cdd:NF041283    3 YVIVLANQKGGVGKTTDTVMEAVVASSVFNKKVLVIDTDLQGNATQFLSKTFNVPNFPQSFMKCVEDGDLEKGIVHLTPN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 104 IDIIPGSYDMRKMVNFLIGKFKTEEAQTFYLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVVQETQQFALEG 183
Cdd:NF041283   83 LDLIAGDYDTRELGDFLADKFKSEYDRTFYLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYVIVIQETQQFAFEG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 184 SNTFISTYLNTLVDDFGSRFKTEIIGILPVLLQKKRKLHEKILETTKEKFGKENIFGTTINNHARLELYGKFGVQFEDHW 263
Cdd:NF041283  163 SKKLILTYLQTLVDDFGDEINVQVAGILPVLLQARRPLQQKIVDETIEYFGKDNVFNNIIKNHARLEWYGEQGIQFEDYH 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1250768313 264 DRTMFALYTDIVQEMLERMQLIENGSDLDNYQYKPIFYNPKigKVTALGKEIVVNG 319
Cdd:NF041283  243 DRRMFALFADIFCELEERIKSFEKTGDVENFTYTHQYINQN--KLTPKGKEITING 296
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 29-283 4.16e-47

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: 159.25  E-value: 4.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  29 ANQKGGVGKTTNTTMEAIILAHvFNKKVLLIDEDMQGNETSFMSktYDVIEFPMSLMKAI-EEGDLTKAIVNLD-ENIDI 106
Cdd:COG1192     7 ANQKGGVGKTTTAVNLAAALAR-RGKRVLLIDLDPQGNLTSGLG--LDPDDLDPTLYDLLlDDAPLEDAIVPTEiPGLDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 107 IPGSYDMRKMVNFLIGKFKTEeaqtFYLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVVQETQQFALEGSNT 186
Cdd:COG1192    84 IPANIDLAGAEIELVSRPGRE----LRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 187 FISTyLNTLVDDFGSRFKteIIGILPVLLQKKRKLHEKILETTKEKFGkENIFGTTINNHARLELYGKFGVQFEDHWDRT 266
Cdd:COG1192   160 LLET-IEEVREDLNPKLE--ILGILLTMVDPRTRLSREVLEELREEFG-DKVLDTVIPRSVALAEAPSAGKPVFEYDPKS 235

                         250
                  ....*....|....*...
gi 1250768313 267 MFAL-YTDIVQEMLERMQ 283
Cdd:COG1192   236 KGAKaYRALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 23-195 1.02e-37

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: 132.32  E-value: 1.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  23 CRVIINANQKGGVGKTTNTTMEAIILAHvFNKKVLLIDEDMQGNETSFMSKTYDVIEFPM-SLMkaIEEGDLTKAIVNLD 101
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAK-KGKKVLLIDLDPQGNATSGLGIDKNNVEKTIyELL--IGECNIEEAIIKTV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 102 -ENIDIIPGSYDMRKMVNFLIGKFKTEEAqtfyLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVVQETQQFA 180
Cdd:pfam13614  78 iENLDLIPSNIDLAGAEIELIGIENRENI----LKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYA 153

                         170
                  ....*....|....*
gi 1250768313 181 LEGsntfISTYLNTL 195
Cdd:pfam13614 154 LEG----LSQLLNTI 164
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 24-228 9.14e-24

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: 94.14  E-value: 9.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  24 RVIINANQKGGVGKTTNTTMEAIILAHVfNKKVLLIDEDMQGNETSFMsktydviefpmslmkaieegdltkaivnlden 103
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALR-GKRVLLIDLDPQGSLTSWL-------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 104 idiipgsydmrkmvnfligkfkteeaqtfylsslidkirddYDFIFIDVPPSTDLKVDNAVVAADYLVVVQETQQFALEG 183
Cdd:cd02042    48 -----------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDG 86

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1250768313 184 SNTFISTyLNTLVDDFGSRFKteIIGILPVLLQKKRKLHEKILET 228
Cdd:cd02042    87 LAKLLDT-LEELKKQLNPPLL--ILGILLTRVDPRTKLAREVLEE 128
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 24-173 4.79e-11

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: 62.06  E-value: 4.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  24 RVIINANQKGGVGKTTNTTMEAIILAHvFNKKVLLIDEDMQGNETSFMSKTYDViefPMSLMKAI-EEGDLTKAIVNLDE 102
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAK-LGKKVLALDADITMANLELILGMEDK---PVTLHDVLaGEADIKDAIYEGPF 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250768313 103 NIDIIPGSYDMRKmvnflIGKFKTEEaqtfyLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVV 173
Cdd:TIGR01969  77 GVKVIPAGVSLEG-----LRKADPDK-----LEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLV 137
ParA_partition NF041546
ParA family partition ATPase;
25-174 1.79e-09

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 56.79  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  25 VIINANQKGGVGKTTNttmeAIILAHVF---NKKVLLIDEDMQGnetsfmsktydviefpmSLMK--AIEEGDLTKAIVN 99
Cdd:NF041546    1 IIAVLNQKGGVGKTTL----ATHLAAALarrGYRVLLVDADPQG-----------------SALDwaAAREDERPFPVVG 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1250768313 100 LD-ENidiipgsydmrkmvnfligkfkteeaqtfyLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADY-LVVVQ 174
Cdd:NF041546   60 LArPT------------------------------LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLvLIPVQ 106
minD CHL00175
septum-site determining protein; Validated
 9-173 2.94e-06

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 47.84  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313   9 EEYKKVQKVLSDNRCRVIINANQKGGVGKTTNTTMEAIILAHVfNKKVLLIDED--------MQGNETSFMSKTYDVIEF 80
Cdd:CHL00175    1 EQITTEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARL-GYRVALIDADiglrnldlLLGLENRVLYTAMDVLEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  81 PMSLMKAIEEGDLTKaivnldeNIDIIPGSYDmRKMVNFligkfkTEEAqtfyLSSLIDKIRD-DYDFIFIDVPPSTDLK 159
Cdd:CHL00175   80 ECRLDQALIRDKRWK-------NLSLLAISKN-RQRYNV------TRKN----MNMLVDSLKNrGYDYILIDCPAGIDVG 141

                         170
                  ....*....|....
gi 1250768313 160 VDNAVVAADYLVVV 173
Cdd:CHL00175  142 FINAIAPAQEAIVV 155
 
Name Accession Description Interval E-value
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
24-319 1.93e-133

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 381.02  E-value: 1.93e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  24 RVIINANQKGGVGKTTNTTMEAIILAHVFNKKVLLIDEDMQGNETSFMSKTYDVIEFPMSLMKAIEEGDLTKAIVNLDEN 103
Cdd:NF041283    3 YVIVLANQKGGVGKTTDTVMEAVVASSVFNKKVLVIDTDLQGNATQFLSKTFNVPNFPQSFMKCVEDGDLEKGIVHLTPN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 104 IDIIPGSYDMRKMVNFLIGKFKTEEAQTFYLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVVQETQQFALEG 183
Cdd:NF041283   83 LDLIAGDYDTRELGDFLADKFKSEYDRTFYLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYVIVIQETQQFAFEG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 184 SNTFISTYLNTLVDDFGSRFKTEIIGILPVLLQKKRKLHEKILETTKEKFGKENIFGTTINNHARLELYGKFGVQFEDHW 263
Cdd:NF041283  163 SKKLILTYLQTLVDDFGDEINVQVAGILPVLLQARRPLQQKIVDETIEYFGKDNVFNNIIKNHARLEWYGEQGIQFEDYH 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1250768313 264 DRTMFALYTDIVQEMLERMQLIENGSDLDNYQYKPIFYNPKigKVTALGKEIVVNG 319
Cdd:NF041283  243 DRRMFALFADIFCELEERIKSFEKTGDVENFTYTHQYINQN--KLTPKGKEITING 296
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 29-283 4.16e-47

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: 159.25  E-value: 4.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  29 ANQKGGVGKTTNTTMEAIILAHvFNKKVLLIDEDMQGNETSFMSktYDVIEFPMSLMKAI-EEGDLTKAIVNLD-ENIDI 106
Cdd:COG1192     7 ANQKGGVGKTTTAVNLAAALAR-RGKRVLLIDLDPQGNLTSGLG--LDPDDLDPTLYDLLlDDAPLEDAIVPTEiPGLDL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 107 IPGSYDMRKMVNFLIGKFKTEeaqtFYLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVVQETQQFALEGSNT 186
Cdd:COG1192    84 IPANIDLAGAEIELVSRPGRE----LRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEGLAQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 187 FISTyLNTLVDDFGSRFKteIIGILPVLLQKKRKLHEKILETTKEKFGkENIFGTTINNHARLELYGKFGVQFEDHWDRT 266
Cdd:COG1192   160 LLET-IEEVREDLNPKLE--ILGILLTMVDPRTRLSREVLEELREEFG-DKVLDTVIPRSVALAEAPSAGKPVFEYDPKS 235

                         250
                  ....*....|....*...
gi 1250768313 267 MFAL-YTDIVQEMLERMQ 283
Cdd:COG1192   236 KGAKaYRALAEELLERLE 253
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 23-195 1.02e-37

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: 132.32  E-value: 1.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  23 CRVIINANQKGGVGKTTNTTMEAIILAHvFNKKVLLIDEDMQGNETSFMSKTYDVIEFPM-SLMkaIEEGDLTKAIVNLD 101
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAK-KGKKVLLIDLDPQGNATSGLGIDKNNVEKTIyELL--IGECNIEEAIIKTV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 102 -ENIDIIPGSYDMRKMVNFLIGKFKTEEAqtfyLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVVQETQQFA 180
Cdd:pfam13614  78 iENLDLIPSNIDLAGAEIELIGIENRENI----LKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYA 153

                         170
                  ....*....|....*
gi 1250768313 181 LEGsntfISTYLNTL 195
Cdd:pfam13614 154 LEG----LSQLLNTI 164
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 24-228 9.14e-24

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: 94.14  E-value: 9.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  24 RVIINANQKGGVGKTTNTTMEAIILAHVfNKKVLLIDEDMQGNETSFMsktydviefpmslmkaieegdltkaivnlden 103
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALR-GKRVLLIDLDPQGSLTSWL-------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 104 idiipgsydmrkmvnfligkfkteeaqtfylsslidkirddYDFIFIDVPPSTDLKVDNAVVAADYLVVVQETQQFALEG 183
Cdd:cd02042    48 -----------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDG 86

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1250768313 184 SNTFISTyLNTLVDDFGSRFKteIIGILPVLLQKKRKLHEKILET 228
Cdd:cd02042    87 LAKLLDT-LEELKKQLNPPLL--ILGILLTRVDPRTKLAREVLEE 128
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 26-232 5.86e-20

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: 86.63  E-value: 5.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  26 IINANQKGGVGKTTNTTMEAIILAhVFNKKVLLIDEDMQGNETSFMSKTYDVIEFPMSLMKAIEEGDLTKAIV----NLD 101
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALA-RRGLRVLLIDLDPQSNNSSVEGLEGDIAPALQALAEGLKGRVNLDPILlkekSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 102 ENIDIIPGSYDMRKMVNFLIGKFKTEEaqtfyLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVVQETQQFAL 181
Cdd:pfam01656  80 GGLDLIPGNIDLEKFEKELLGPRKEER-----LREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILV 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1250768313 182 EGSNTFIstylnTLVDDFGSRFKTEIIGILPVLLQKKR-----KLHEKILETTKEK 232
Cdd:pfam01656 155 EDAKRLG-----GVIAALVGGYALLGLKIIGVVLNKVDgdnhgKLLKEALEELLRG 205
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 24-173 4.75e-12

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: 64.51  E-value: 4.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  24 RVIINANQKGGVGKTTNTTMEAIILAHvFNKKVLLIDEDMQGNETSFM-----SKT-YDVIEFPMSLMKAIEEGDltkai 97
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSK-LGKRVLLLDADLGLANLDILlglapKKTlGDVLKGRVSLEDIIVEGP----- 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1250768313  98 vnldENIDIIPGSYDMRKMVNFligkfkTEEAQTFYLSSLiDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVV 173
Cdd:cd02038    75 ----EGLDIIPGGSGMEELANL------DPEQKAKLIEEL-SSLESNYDYLLIDTGAGISRNVLDFLLAADEVIVV 139
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 45-173 2.89e-11

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: 62.21  E-value: 2.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  45 AIILAHVfNKKVLLIDEDMQ-GNETSFMSKT-----YDVIEfpmslmkaiEEGDLTKAIVNLDENIDIIPGSYDMRKMVN 118
Cdd:COG0455     7 AAALARL-GKRVLLVDADLGlANLDVLLGLEpkatlADVLA---------GEADLEDAIVQGPGGLDVLPGGSGPAELAE 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1250768313 119 FligkfkTEEAQtfyLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVV 173
Cdd:COG0455    77 L------DPEER---LIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVV 122
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 24-173 4.79e-11

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: 62.06  E-value: 4.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  24 RVIINANQKGGVGKTTNTTMEAIILAHvFNKKVLLIDEDMQGNETSFMSKTYDViefPMSLMKAI-EEGDLTKAIVNLDE 102
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAK-LGKKVLALDADITMANLELILGMEDK---PVTLHDVLaGEADIKDAIYEGPF 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1250768313 103 NIDIIPGSYDMRKmvnflIGKFKTEEaqtfyLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVV 173
Cdd:TIGR01969  77 GVKVIPAGVSLEG-----LRKADPDK-----LEDVLKEIIDDTDFLLIDAPAGLERDAVTALAAADELLLV 137
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 19-173 6.91e-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: 62.44  E-value: 6.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  19 SDNRCRVI--INAnqKGGVGKTTNTTMEAIILAHVFNKKVLLIDEDMQ-GNETSFMSktydvIEFPMSLMKAIEEGD--- 92
Cdd:COG4963    98 AARRGRVIavVGA--KGGVGATTLAVNLAWALARESGRRVLLVDLDLQfGDVALYLD-----LEPRRGLADALRNPDrld 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  93 ---LTKAIVNLDENIDIIPGSYDMRKMVNFligkfkTEEAqtfyLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADY 169
Cdd:COG4963   171 etlLDRALTRHSSGLSVLAAPADLERAEEV------SPEA----VERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADE 240


                  ....
gi 1250768313 170 LVVV 173
Cdd:COG4963   241 VVLV 244
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 32-182 6.23e-10

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: 59.04  E-value: 6.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  32 KGGVGKTTNTTMEAIILAHVfNKKVLLIDEDMQGnetSFMSKTYDVIEFPMSLMKAIEEGDLTKAIVNLD-ENIDIIPgs 110
Cdd:COG0489   101 KGGEGKSTVAANLALALAQS-GKRVLLIDADLRG---PSLHRMLGLENRPGLSDVLAGEASLEDVIQPTEvEGLDVLP-- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 111 ydmrkmvnflIGKFKTEEAQtfYLSS-----LIDKIRDDYDFIFIDVPPSTDlkVDNAVVAADY----LVVV--QETQQF 179
Cdd:COG0489   175 ----------AGPLPPNPSE--LLASkrlkqLLEELRGRYDYVIIDTPPGLG--VADATLLASLvdgvLLVVrpGKTALD 240


                  ...
gi 1250768313 180 ALE 182
Cdd:COG0489   241 DVR 243
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 24-173 9.80e-10

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: 57.98  E-value: 9.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  24 RVIINANQKGGVGKTTNTTMEAIILAHvFNKKVLLIDED--------MQGNETSFMSKTYDVIEfpmslmkaiEEGDLTK 95
Cdd:cd02036     1 RVIVITSGKGGVGKTTTTANLGVALAK-LGKKVLLIDADiglrnldlILGLENRIVYTLVDVLE---------GECRLEQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  96 AIV--NLDENIDIIPGSYDMRKMvnfligKFKTEEaqtfyLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVV 173
Cdd:cd02036    71 ALIkdKRWENLYLLPASQTRDKD------ALTPEK-----LEELVKELKDSFDFILIDSPAGIESGFINAIAPADEAIIV 139
ParA_partition NF041546
ParA family partition ATPase;
25-174 1.79e-09

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 56.79  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  25 VIINANQKGGVGKTTNttmeAIILAHVF---NKKVLLIDEDMQGnetsfmsktydviefpmSLMK--AIEEGDLTKAIVN 99
Cdd:NF041546    1 IIAVLNQKGGVGKTTL----ATHLAAALarrGYRVLLVDADPQG-----------------SALDwaAAREDERPFPVVG 59

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1250768313 100 LD-ENidiipgsydmrkmvnfligkfkteeaqtfyLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADY-LVVVQ 174
Cdd:NF041546   60 LArPT------------------------------LHRELPSLARDYDFVVIDGPPRAEDLARSAIKAADLvLIPVQ 106
minD CHL00175
septum-site determining protein; Validated
 9-173 2.94e-06

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 47.84  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313   9 EEYKKVQKVLSDNRCRVIINANQKGGVGKTTNTTMEAIILAHVfNKKVLLIDED--------MQGNETSFMSKTYDVIEF 80
Cdd:CHL00175    1 EQITTEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARL-GYRVALIDADiglrnldlLLGLENRVLYTAMDVLEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  81 PMSLMKAIEEGDLTKaivnldeNIDIIPGSYDmRKMVNFligkfkTEEAqtfyLSSLIDKIRD-DYDFIFIDVPPSTDLK 159
Cdd:CHL00175   80 ECRLDQALIRDKRWK-------NLSLLAISKN-RQRYNV------TRKN----MNMLVDSLKNrGYDYILIDCPAGIDVG 141

                         170
                  ....*....|....
gi 1250768313 160 VDNAVVAADYLVVV 173
Cdd:CHL00175  142 FINAIAPAQEAIVV 155
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 18-166 2.97e-06

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: 47.05  E-value: 2.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  18 LSDNRCRVIINANQKGGVGKTTNTTMEAIILAHVfNKKVLLIDEDMQgneTSFMSKTYDVIEFPMSLMKAIE-EGDLTKA 96
Cdd:TIGR01007  12 FSGAEIKVLLITSVKPGEGKSTTSANIAIAFAQA-GYKTLLIDGDMR---NSVMSGTFKSQNKITGLTNFLSgTTDLSDA 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1250768313  97 IVNLD-ENIDIIP-GSydmrkmvnflIGKFKTEEAQTFYLSSLIDKIRDDYDFIFIDVPPsTDLKVDNAVVA 166
Cdd:TIGR01007  88 ICDTNiENLDVITaGP----------VPPNPTELLQSSNFKTLIETLRKRFDYIIIDTPP-IGTVTDAAIIA 148
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 23-155 3.80e-06

plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein involved in replicon partitioning. All known examples occur in bacterial species with two or more replicons, on a plasmid or the smaller chromosome. Note that an apparent exception may be seen as a pseudomolecule from assembly of an incompletely sequenced genome. Members of this family belong to a larger family that also includes the enzyme cobyrinic acid a,c-diamide synthase, but assignment of that name to members of this family would be in error. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274585 [Multi-domain]  Cd Length: 387  Bit Score: 48.05  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  23 CRVIINANQKGGVGKTTNttmeAIILAHVF---NKKVLLIDEDMQGNETSFMS--KTYDVIEFPmSLMKAIEEGDLTKAI 97
Cdd:TIGR03453 104 LQVIAVTNFKGGSGKTTT----AAHLAQYLalrGYRVLAIDLDPQASLSALFGyqPEFDVGENE-TLYGAIRYDDERRPI 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1250768313  98 VNLDE-----NIDIIPGsydmrkmvNFLIGKFKTE----------EAQTFY--LSSLIDKIRDDYDFIFIDVPPS 155
Cdd:TIGR03453 179 SEIIRktyfpGLDLVPG--------NLELMEFEHEtpralsrgqgGDTIFFarVGEALAEVEDDYDVVVIDCPPQ 245
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 24-211 4.89e-06

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 47.75  E-value: 4.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  24 RVIINANQKGGVGKTTNTTMEAIILAhVFNKKVLLIDEDMQG----------------NETSFMSKTYDVIEFPMSlmka 87
Cdd:PRK13869  122 QVIAVTNFKGGSGKTTTSAHLAQYLA-LQGYRVLAVDLDPQAslsallgvlpetdvgaNETLYAAIRYDDTRRPLR---- 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  88 ieegDLTKAivNLDENIDIIPGSYDMRKMVNFLI----------GKFKTEEAQTFylssliDKIRDDYDFIFIDVPPSTD 157
Cdd:PRK13869  197 ----DVIRP--TYFDGLHLVPGNLELMEFEHTTPkalsdkgtrdGLFFTRVAQAF------DEVADDYDVVVIDCPPQLG 264

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1250768313 158 LKVDNAVVAADYLVVVQETQQFALEGSNTFISTYLNTL--VDDFGSRFKTEIIGIL 211
Cdd:PRK13869  265 FLTLSGLCAATSMVITVHPQMLDIASMSQFLLMTRDLLgvVKEAGGNLQYDFIRYL 320
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 25-172 6.88e-06

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 47.28  E-value: 6.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  25 VIINANQKGGVGKTTNTTMEAIILAhVFNKKVLLID-EDMQGNETSFMSKTYDV-IEFPMSLMKAI--EEGDLTKAIV-N 99
Cdd:PRK13705  108 VIGVAAHKGGVYKTSVSVHLAQDLA-LKGLRVLLVEgNDPQGTASMYHGWVPDLhIHAEDTLLPFYlgEKDDATYAIKpT 186

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1250768313 100 LDENIDIIPGSYDMRKMVNFLIGKF---KTEEAQTFYLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVV 172
Cdd:PRK13705  187 CWPGLDIIPSCLALHRIETELMGKFdegKLPTDPHLMLRLAIETVAHDYDVIVIDSAPNLGIGTINVVCAADVLIV 262
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 24-173 1.06e-05

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: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  24 RVIINANQKGGVGKTTNTTMEAIILAHVfNKKVLLIDED--------MQGNETSFMSKTYDVIEFPMSLMKAIEEGDLTK 95
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARL-GKKVVLIDADiglrnldlLLGLENRIVYTLVDVVEGECRLQQALIKDKRLK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1250768313  96 aivnldeNIDIIPGSYDMRK-MVnfligkfkTEEAqtfyLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVV 173
Cdd:TIGR01968  81 -------NLYLLPASQTRDKdAV--------TPEQ----MKKLVNELKEEFDYVIIDCPAGIESGFRNAVAPADEAIVV 140
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 25-195 3.44e-05

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 45.00  E-value: 3.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  25 VIINANQKGGVGKTTNTTMEAIILAhVFNKKVLLID-EDMQGNETSFMSKTYDV-IEFPMSLMKAI--EEGDLTKAIV-N 99
Cdd:PHA02519  108 VLAVMSHKGGVYKTSSAVHTAQWLA-LQGHRVLLIEgNDPQGTASMYHGYVPDLhIHADDTLLPFYlgERDNAEYAIKpT 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313 100 LDENIDIIPGSYDMRKMVNFLI---GKFKTEEAQTFYLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADYLVVVQET 176
Cdd:PHA02519  187 CWPGLDIIPSCLALHRIETDLMqyhDAGKLPHPPHLMLRAAIESVWDNYDIIVIDSAPNLGTGTINVVCAADVIVVATPA 266

                         170
                  ....*....|....*....
gi 1250768313 177 QQFALEGSNTFISTYLNTL 195
Cdd:PHA02519  267 ELFDYVSVLQFFTMLLDLL 285
PHA02518 PHA02518
ParA-like protein; Provisional
 24-168 3.79e-05

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 44.07  E-value: 3.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  24 RVIINANQKGGVGKTTNTTMEAIILaHVFNKKVLLIDEDMQGNETSFmsktydviefpmslMKAIEEGDLTKAIVNLDEN 103
Cdd:PHA02518    1 KIIAVLNQKGGAGKTTVATNLASWL-HADGHKVLLVDLDPQGSSTDW--------------AEAREEGEPLIPVVRMGKS 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1250768313 104 IdiipgsydmrkmvnfligkfkteeaqtfylSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAAD 168
Cdd:PHA02518   66 I------------------------------RADLPKVASGYDYVVVDGAPQDSELARAALRIAD 100
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 24-173 2.27e-04

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 41.97  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  24 RVIINANQKGGVGKTTNTTMEAIILAhVFNKKVLLIDEDM--------QGNETSFMsktYDVIEfpmslmkaIEEGD--L 93
Cdd:COG2894     3 KVIVVTSGKGGVGKTTTTANLGTALA-LLGKKVVLIDADIglrnldlvMGLENRIV---YDLVD--------VIEGEcrL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  94 TKAIVNlD---ENIDIIPGSYDMRK-MVnfligkfkTEEAqtfyLSSLIDKIRDDYDFIFIDVPPSTDLKVDNAVVAADY 169
Cdd:COG2894    71 KQALIK-DkrfENLYLLPASQTRDKdAL--------TPEQ----MKKLVEELKEEFDYILIDSPAGIEQGFKNAIAGADE 137


                  ....
gi 1250768313 170 LVVV 173
Cdd:COG2894   138 AIVV 141
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 32-151 2.41e-04

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 42.08  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1250768313  32 KGGVGKTTNTTMeaiiLAHVF---NKKVLLIDEDMQGN--ETSFMSKTYDVIEfPMSLMKA-IEE--GDLTKAIVNLDEN 103
Cdd:COG3640     8 KGGVGKTTLSAL----LARYLaekGKPVLAVDADPNANlaEALGLEVEADLIK-PLGEMRElIKErtGAPGGGMFKLNPK 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1250768313 104 IDIIPGSYdMRKM--VNFL-IGKFKTEE------AQTFyLSSLIDKIRD-DYDFIFID 151
Cdd:COG3640    83 VDDIPEEY-LVEGdgVDLLvMGTIEEGGsgcycpENAL-LRALLNHLVLgNYEYVVVD 138
 
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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