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Conserved domains on  [gi|504955354|ref|WP_015142456|]
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AAA family ATPase [Pleurocapsa sp. PCC 7327]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 174-451 6.27e-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: 162.33  E-value: 6.27e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPqQGDLTASL--RKQEGKVKLSDCLIDhKINVRDTIqkfqirfk 251
Cdd:COG1192    4 IAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDP-QGNLTSGLglDPDDLDPTLYDLLLD-DAPLEDAI-------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 252 nQPTPKNIFDLIPSDSVLEKYmePGEQAKIQGGSSRLKRLIEPLLQEYDYIIFDCPTNWTFFSQSCVYASDVILIPTQHN 331
Cdd:COG1192   74 -VPTEIPGLDLIPANIDLAGA--EIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 332 NFaSLKNsqkvIQQFIPQIQNKKEDGRPIALP--IFFNHHKPTaasmKKTHNFIQSLLTTssgginknllpyyypkaslg 409
Cdd:COG1192  151 YL-SLEG----LAQLLETIEEVREDLNPKLEIlgILLTMVDPR----TRLSREVLEELRE-------------------- 201

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 504955354 410 NFNKSIF--TIPAYPIVASAGFSGIPA---ALTHKIAHTsYLALVEE 451
Cdd:COG1192  202 EFGDKVLdtVIPRSVALAEAPSAGKPVfeyDPKSKGAKA-YRALAEE 247
HSDR_N super family cl29110
Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N ...
 28-135 1.94e-06

Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N terminal regions found in type I restriction enzyme R (HSDR) proteins. Restriction and modification (R/M) systems are found in a wide variety of prokaryotes and are thought to protect the host bacterium from the uptake of foreign DNA. Type I restriction and modification systems are encoded by three genes: hsdR, hsdM, and hsdS. The three polypeptides, HsdR, HsdM, and HsdS, often assemble to give an enzyme (R2M2S1) that modifies hemimethylated DNA and restricts unmethylated DNA.


The actual alignment was detected with superfamily member pfam13588:

Pssm-ID: 452924 [Multi-domain]  Cd Length: 110  Bit Score: 46.43  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354   28 FVEPLLEELGFTK----LEWFPQFPTGKGAVDYaarknsvgnIFKNTKTNPYVLIEVKgrgtvagtqinlADGTPQYKAT 103
Cdd:pfam13588   9 FVRYLINELGYPKeliaVEKPLQLGSKKKRADI---------VVYNKDGKPYILVECK------------APSIKISQKV 67

                          90       100       110
                  ....*....|....*....|....*....|..
gi 504955354  104 KEQIKRYLLSPKCQtarWGIITNATHIQLFQR 135
Cdd:pfam13588  68 FDQLARYNSVLGAP---FLVVTNGLQHICFKV 96
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 174-451 6.27e-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: 162.33  E-value: 6.27e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPqQGDLTASL--RKQEGKVKLSDCLIDhKINVRDTIqkfqirfk 251
Cdd:COG1192    4 IAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDP-QGNLTSGLglDPDDLDPTLYDLLLD-DAPLEDAI-------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 252 nQPTPKNIFDLIPSDSVLEKYmePGEQAKIQGGSSRLKRLIEPLLQEYDYIIFDCPTNWTFFSQSCVYASDVILIPTQHN 331
Cdd:COG1192   74 -VPTEIPGLDLIPANIDLAGA--EIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 332 NFaSLKNsqkvIQQFIPQIQNKKEDGRPIALP--IFFNHHKPTaasmKKTHNFIQSLLTTssgginknllpyyypkaslg 409
Cdd:COG1192  151 YL-SLEG----LAQLLETIEEVREDLNPKLEIlgILLTMVDPR----TRLSREVLEELRE-------------------- 201

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 504955354 410 NFNKSIF--TIPAYPIVASAGFSGIPA---ALTHKIAHTsYLALVEE 451
Cdd:COG1192  202 EFGDKVLdtVIPRSVALAEAPSAGKPVfeyDPKSKGAKA-YRALAEE 247
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 174-329 2.34e-33

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: 123.85  E-value: 2.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPqQGDLTASLR--KQEGKVKLSDCLIDHKiNVRDTIQKfqirfk 251
Cdd:pfam13614   4 IAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDP-QGNATSGLGidKNNVEKTIYELLIGEC-NIEEAIIK------ 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504955354  252 nqpTPKNIFDLIPSDSVLEKYmePGEQAKIQGGSSRLKRLIEPLLQEYDYIIFDCPTNWTFFSQSCVYASDVILIPTQ 329
Cdd:pfam13614  76 ---TVIENLDLIPSNIDLAGA--EIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQ 148
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 174-384 4.97e-25

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


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 99.54  E-value: 4.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPqQGDLTASLrkqegkvklsdclidhkinvrdtiqkfqirfknq 253
Cdd:cd02042    3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDP-QGSLTSWL---------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 254 ptpknifdlipsdsvlekymepgeqakiqggssrlkrliepllqeYDYIIFDCPTNWTFFSQSCVYASDVILIPTQHNNF 333
Cdd:cd02042   48 ---------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPF 82

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504955354 334 A--SLKNSQKVIQQFIPQIQNKKEDGRpialpIFFNHHKPTAASMKKTHNFIQ 384
Cdd:cd02042   83 DldGLAKLLDTLEELKKQLNPPLLILG-----ILLTRVDPRTKLAREVLEELK 130
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 173-307 2.08e-16

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: 78.62  E-value: 2.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  173 SICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQGDLTASLRKQEGKVKLSDCLIDhKINVRDTIQKfqirfkn 252
Cdd:TIGR01969   2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPVTLHDVLAG-EADIKDAIYE------- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 504955354  253 qpTPKNIFdLIPSDSVLEKYMepgeQAKIQggssRLKRLIEPLLQEYDYIIFDCP 307
Cdd:TIGR01969  74 --GPFGVK-VIPAGVSLEGLR----KADPD----KLEDVLKEIIDDTDFLLIDAP 117
ParA_partition NF041546
ParA family partition ATPase;
174-329 5.28e-15

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 73.36  E-value: 5.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQGDLT-ASLRKQEGKVKLSDClidhkinVRDTIQKFqirfkn 252
Cdd:NF041546   2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDwAAAREDERPFPVVGL-------ARPTLHRE------ 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504955354 253 qptpknifdlipsdsvlekymepgeqakiqggssrlkrlIEPLLQEYDYIIFDCPTNWTFFSQSCVYASDVILIPTQ 329
Cdd:NF041546  69 ---------------------------------------LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQ 106
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 174-336 1.22e-12

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 69.32  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQqgdltASLRKQEGKVKLSDCLIDHKI--NVRDTIQKFQIRFK 251
Cdd:PRK13869 124 IAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQ-----ASLSALLGVLPETDVGANETLyaAIRYDDTRRPLRDV 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 252 NQPTPKNIFDLIPSDSVLEKYMEPGEQAKIQGGS------SRLKRLIEPLLQEYDYIIFDCPTNWTFFSQS--CVYASDV 323
Cdd:PRK13869 199 IRPTYFDGLHLVPGNLELMEFEHTTPKALSDKGTrdglffTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSglCAATSMV 278

                        170
                 ....*....|...
gi 504955354 324 ILIPTQHNNFASL 336
Cdd:PRK13869 279 ITVHPQMLDIASM 291
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
178-347 1.36e-10

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 62.08  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 178 NNKGGVGKTTTVANLAAILAYL-GKKVLVIDFDpQQGDLTASLRKQEGKVKLSDCLIdHKINVRDtiqkfqirFKNQPTP 256
Cdd:NF041283   9 NQKGGVGKTTDTVMEAVVASSVfNKKVLVIDTD-LQGNATQFLSKTFNVPNFPQSFM-KCVEDGD--------LEKGIVH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 257 --KNIfDLIPSDSVLEKYMEPGEQaKIQGGSSR---LKRLIEPLLQEYDYIIFDCPTNWTFFSQSCVYASDVIlIPTQHN 331
Cdd:NF041283  79 ltPNL-DLIAGDYDTRELGDFLAD-KFKSEYDRtfyLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYV-IVIQET 155

                        170
                 ....*....|....*.
gi 504955354 332 NFASLKNSQKVIQQFI 347
Cdd:NF041283 156 QQFAFEGSKKLILTYL 171
HSDR_N_2 pfam13588
Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N ...
 28-135 1.94e-06

Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N terminal regions found in type I restriction enzyme R (HSDR) proteins. Restriction and modification (R/M) systems are found in a wide variety of prokaryotes and are thought to protect the host bacterium from the uptake of foreign DNA. Type I restriction and modification systems are encoded by three genes: hsdR, hsdM, and hsdS. The three polypeptides, HsdR, HsdM, and HsdS, often assemble to give an enzyme (R2M2S1) that modifies hemimethylated DNA and restricts unmethylated DNA.


Pssm-ID: 433331 [Multi-domain]  Cd Length: 110  Bit Score: 46.43  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354   28 FVEPLLEELGFTK----LEWFPQFPTGKGAVDYaarknsvgnIFKNTKTNPYVLIEVKgrgtvagtqinlADGTPQYKAT 103
Cdd:pfam13588   9 FVRYLINELGYPKeliaVEKPLQLGSKKKRADI---------VVYNKDGKPYILVECK------------APSIKISQKV 67

                          90       100       110
                  ....*....|....*....|....*....|..
gi 504955354  104 KEQIKRYLLSPKCQtarWGIITNATHIQLFQR 135
Cdd:pfam13588  68 FDQLARYNSVLGAP---FLVVTNGLQHICFKV 96
COG4748 COG4748
Uncharacterized conserved protein, contains restriction enzyme R protein N terminal (HSDR_N) ...
 26-135 1.68e-04

Uncharacterized conserved protein, contains restriction enzyme R protein N terminal (HSDR_N) domain [Function unknown];


Pssm-ID: 443782  Cd Length: 355  Bit Score: 43.72  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  26 NDFVEPLLEELG---FTKLEWFPQFP----TGKGA-VDYAarknsvgnIFKNTKtnPYVLIEVKGRGTvagtqiNLADgt 97
Cdd:COG4748   29 NALIMPFIQILGydvFNPTEVVPEYTadvgTKKGEkVDYA--------ILKDGQ--PVILIECKGVGE------DLDI-- 90

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 504955354  98 pqykATKEQIKRYLlspKCQTARWGIITNATHIQLFQR 135
Cdd:COG4748   91 ----NHASQLFRYF---HVTEARFGILTNGIEYRFYTD 121
PoNe cd20702
Polymorphic Nuclease effector (PoNe) domain is a deoxyribonuclease; This family contains the ...
 29-96 1.33e-03

Polymorphic Nuclease effector (PoNe) domain is a deoxyribonuclease; This family contains the DNase toxin domain called PoNe (Polymorphic Nuclease effector), which belongs to a diverse superfamily of PD-(D/E)xK phosphodiesterases, and is associated with several toxin delivery systems including type V, type VI, and type VII. PoNe toxicity is antagonized by cognate immunity proteins (PoNi) containing DUF1911 and DUF1910 domains. The PoNe domain co-occurs with a variety of N-terminal domains such as filamentous hemagglutinin, nuclease, HINT, DUFs, PAAR, RHS repeat, or LXG domains. Some members of this family also co-occur with the FIX (Found in type sIX effector) domain of unknown function, as identified by Jana et al., who have also identified this PoNe domain.


Pssm-ID: 410637  Cd Length: 77  Bit Score: 37.34  E-value: 1.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504955354  29 VEPLLEELGFTKLEWFPQFPTGKGaVDyaarknsvgNIFKNTKTNPYVLIEVKGRGTVAGTQINLADG 96
Cdd:cd20702    9 ADLYLKSQGYTKLIGGSKGGGGNG-ID---------GVYKDPKGPEYIIVEAKFGSASLKGGVSLGTT 66
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
 182-206 1.51e-03

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: 39.70  E-value: 1.51e-03
                           10        20
                   ....*....|....*....|....*.
gi 504955354   182 GVGKTTTVANLAAILAYLG-KKVLVI 206
Cdd:smart00962  11 GVGKTTTIAKLAARLKLKGgKKVLLV 36
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 174-451 6.27e-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: 162.33  E-value: 6.27e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPqQGDLTASL--RKQEGKVKLSDCLIDhKINVRDTIqkfqirfk 251
Cdd:COG1192    4 IAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDP-QGNLTSGLglDPDDLDPTLYDLLLD-DAPLEDAI-------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 252 nQPTPKNIFDLIPSDSVLEKYmePGEQAKIQGGSSRLKRLIEPLLQEYDYIIFDCPTNWTFFSQSCVYASDVILIPTQHN 331
Cdd:COG1192   74 -VPTEIPGLDLIPANIDLAGA--EIELVSRPGRELRLKRALAPLADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 332 NFaSLKNsqkvIQQFIPQIQNKKEDGRPIALP--IFFNHHKPTaasmKKTHNFIQSLLTTssgginknllpyyypkaslg 409
Cdd:COG1192  151 YL-SLEG----LAQLLETIEEVREDLNPKLEIlgILLTMVDPR----TRLSREVLEELRE-------------------- 201

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 504955354 410 NFNKSIF--TIPAYPIVASAGFSGIPA---ALTHKIAHTsYLALVEE 451
Cdd:COG1192  202 EFGDKVLdtVIPRSVALAEAPSAGKPVfeyDPKSKGAKA-YRALAEE 247
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 174-329 2.34e-33

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: 123.85  E-value: 2.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPqQGDLTASLR--KQEGKVKLSDCLIDHKiNVRDTIQKfqirfk 251
Cdd:pfam13614   4 IAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDP-QGNATSGLGidKNNVEKTIYELLIGEC-NIEEAIIK------ 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504955354  252 nqpTPKNIFDLIPSDSVLEKYmePGEQAKIQGGSSRLKRLIEPLLQEYDYIIFDCPTNWTFFSQSCVYASDVILIPTQ 329
Cdd:pfam13614  76 ---TVIENLDLIPSNIDLAGA--EIELIGIENRENILKEALEPVKDNYDYIIIDCPPSLGLLTINALTASDSVLIPVQ 148
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 174-329 3.00e-28

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: 111.67  E-value: 3.00e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPqQGDLTASLRKQEGKVKLSDCLIDhkiNVRDTIQKFQIRFKNQ 253
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDP-QSNNSSVEGLEGDIAPALQALAE---GLKGRVNLDPILLKEK 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504955354  254 PTPKNiFDLIPSDSVLEKYMEPGEQAkiqGGSSRLKRLIEPLLQEYDYIIFDCPTNWTFFSQSCVYASDVILIPTQ 329
Cdd:pfam01656  77 SDEGG-LDLIPGNIDLEKFEKELLGP---RKEERLREALEALKEDYDYVIIDGAPGLGELLRNALIAADYVIIPLE 148
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 174-384 4.97e-25

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


Pssm-ID: 349760 [Multi-domain]  Cd Length: 130  Bit Score: 99.54  E-value: 4.97e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPqQGDLTASLrkqegkvklsdclidhkinvrdtiqkfqirfknq 253
Cdd:cd02042    3 IAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDP-QGSLTSWL---------------------------------- 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 254 ptpknifdlipsdsvlekymepgeqakiqggssrlkrliepllqeYDYIIFDCPTNWTFFSQSCVYASDVILIPTQHNNF 333
Cdd:cd02042   48 ---------------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPF 82

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504955354 334 A--SLKNSQKVIQQFIPQIQNKKEDGRpialpIFFNHHKPTAASMKKTHNFIQ 384
Cdd:cd02042   83 DldGLAKLLDTLEELKKQLNPPLLILG-----ILLTRVDPRTKLAREVLEELK 130
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 180-307 7.17e-21

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: 92.17  E-value: 7.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 180 KGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQGDLTASLrKQEGKVKLSDCLIDhKINVRDTIqkfqirfknQPTPKNI 259
Cdd:COG0489  101 KGGEGKSTVAANLALALAQSGKRVLLIDADLRGPSLHRML-GLENRPGLSDVLAG-EASLEDVI---------QPTEVEG 169

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 504955354 260 FDLIPSDSVLEKYMEPgeqakIqgGSSRLKRLIEPLLQEYDYIIFDCP 307
Cdd:COG0489  170 LDVLPAGPLPPNPSEL-----L--ASKRLKQLLEELRGRYDYVIIDTP 210
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 168-346 4.26e-18

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: 85.17  E-value: 4.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 168 PPRALSICVYNNKGGVGKTTTVANLAAILA-YLGKKVLVIDFDPQQGDLTASLrKQEGKVKLSDCLID-HKINvRDTIQK 245
Cdd:COG4963   99 ARRGRVIAVVGAKGGVGATTLAVNLAWALArESGRRVLLVDLDLQFGDVALYL-DLEPRRGLADALRNpDRLD-ETLLDR 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 246 FQIRFKNQptpkniFDLIPSDSVLEKYMEPGEQAkiqggssrLKRLIEPLLQEYDYIIFDCPTNWTFFSQSCVYASDVIL 325
Cdd:COG4963  177 ALTRHSSG------LSVLAAPADLERAEEVSPEA--------VERLLDLLRRHFDYVVVDLPRGLNPWTLAALEAADEVV 242

                        170       180
                 ....*....|....*....|.
gi 504955354 326 IPTQhNNFASLKNSQKVIQQF 346
Cdd:COG4963  243 LVTE-PDLPSLRNAKRLLDLL 262
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 182-307 1.33e-17

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: 80.69  E-value: 1.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 182 GVGKTTTVANLAAILAYLGKKVLVIDFDPQQGDLTASLrKQEGKVKLSDcLIDHKINVRDTIqkfqirfknQPTPKNIFD 261
Cdd:cd05387   30 GEGKSTVAANLAVALAQSGKRVLLIDADLRRPSLHRLL-GLPNEPGLSE-VLSGQASLEDVI---------QSTNIPNLD 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 504955354 262 LIPSDSVLekyMEPGEQAkiqgGSSRLKRLIEPLLQEYDYIIFDCP 307
Cdd:cd05387   99 VLPAGTVP---PNPSELL----SSPRFAELLEELKEQYDYVIIDTP 137
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 187-328 4.12e-17

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: 80.32  E-value: 4.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 187 TTVANLAAILAYLGKKVLVIDFDPQQGDLTASLRKQEGKVkLSDcLIDHKINVRDTIqkfqirfknQPTPKNiFDLIPSD 266
Cdd:COG0455    1 TVAVNLAAALARLGKRVLLVDADLGLANLDVLLGLEPKAT-LAD-VLAGEADLEDAI---------VQGPGG-LDVLPGG 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504955354 267 SVLEKYMEPGEQAkiqggssRLKRLIEPLLQEYDYIIFDCPTNWTFFSQSCVYASDVILIPT 328
Cdd:COG0455   69 SGPAELAELDPEE-------RLIRVLEELERFYDVVLVDTGAGISDSVLLFLAAADEVVVVT 123
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 174-307 5.30e-17

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 80.49  E-value: 5.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDpqQG----DLTASLRKQ---------EGKVKLSDCLIDHKinvr 240
Cdd:COG2894    5 IVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD--IGlrnlDLVMGLENRivydlvdviEGECRLKQALIKDK---- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504955354 241 dtiqkfqiRFKNqptpkniFDLIPSDSVLEKYMEPGEQakiqggssrLKRLIEPLLQEYDYIIFDCP 307
Cdd:COG2894   79 --------RFEN-------LYLLPASQTRDKDALTPEQ---------MKKLVEELKEEFDYILIDSP 121
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 173-307 7.38e-17

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: 79.55  E-value: 7.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 173 SICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDpqQG----DLTASLRKQ---------EGKVKLSDCLIDHKinv 239
Cdd:cd02036    2 VIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDAD--IGlrnlDLILGLENRivytlvdvlEGECRLEQALIKDK--- 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504955354 240 rdtiqkfqiRFKNqptpkniFDLIPSDSVLEKYMEPGEQakiqggssrLKRLIEPLLQEYDYIIFDCP 307
Cdd:cd02036   77 ---------RWEN-------LYLLPASQTRDKDALTPEK---------LEELVKELKDSFDFILIDSP 119
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 173-307 2.08e-16

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: 78.62  E-value: 2.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  173 SICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQGDLTASLRKQEGKVKLSDCLIDhKINVRDTIQKfqirfkn 252
Cdd:TIGR01969   2 IITIASGKGGTGKTTITANLGVALAKLGKKVLALDADITMANLELILGMEDKPVTLHDVLAG-EADIKDAIYE------- 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 504955354  253 qpTPKNIFdLIPSDSVLEKYMepgeQAKIQggssRLKRLIEPLLQEYDYIIFDCP 307
Cdd:TIGR01969  74 --GPFGVK-VIPAGVSLEGLR----KADPD----KLEDVLKEIIDDTDFLLIDAP 117
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 174-307 2.35e-16

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: 78.53  E-value: 2.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDP--QQGDLTASLRKQ---------EGKVKLSDCLIDHKinvrdt 242
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALARLGKKVVLIDADIglRNLDLLLGLENRivytlvdvvEGECRLQQALIKDK------ 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504955354  243 iqkfqiRFKNqptpkniFDLIPSDSVLEKYMEPGEQakiqggssrLKRLIEPLLQEYDYIIFDCP 307
Cdd:TIGR01968  78 ------RLKN-------LYLLPASQTRDKDAVTPEQ---------MKKLVNELKEEFDYVIIDCP 120
COG2810 COG2810
Predicted type IV restriction endonuclease [Defense mechanisms];
1-368 3.59e-15

Predicted type IV restriction endonuclease [Defense mechanisms];


Pssm-ID: 442059 [Multi-domain]  Cd Length: 340  Bit Score: 76.56  E-value: 3.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354   1 MTRDQEM---WNHILDSI----PNDAHEAIICNDFVEPLLEELGFTKL---EWFPQFPTGKGAVDYAARKNSVgnifknt 70
Cdd:COG2810    1 MTAPADLqslVERILRNLdylsLRSANEAATRQEFIDPLLEALGWDIDnpeEVIPEERVEGGRPDYALRLNGK------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  71 ktnPYVLIEVKGRGtvagtqINLADgtpqykATKEQIKRYLLSpkcQTARWGIITNATHIQLFQRHGKVIVPATSnylik 150
Cdd:COG2810   74 ---RKLFVEAKKPG------VNLKD------KPARQARSYAWS---SGVRWAILTNGREWRVYDAQEKTSPRPIE----- 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 151 KDNITQIVSQIKNLIDcppralsicvynnkggvgkTTTVANLAAIlaylgkkvlvIDFDPQQGDLTASLRKQEGKVKLSD 230
Cdd:COG2810  131 LDTALEARLLLLEYEE-------------------LSSELDLILS----------RIIVDTDLLARLTLGLLDSELKERK 181

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 231 CLIDHKINVRdtIQKFQIRFKNQPTPKNIFDLIPSDSVLEKYMEPGEQAKIQGGSSRLKRLIEPLLQEYDYIIFDCPTNW 310
Cdd:COG2810  182 LLSDSDPLLL--EIDARLKETLGTAIKSTVLSGPILTDLREDRELSVVGLSKSLDELLEELELKKDADEVLKGLGPPDRK 259

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504955354 311 TFFSQSCVYASDVILIPTQHNNFASLKNSQKViqqfIPQIQNKKEDGRPIALPIFFNH 368
Cdd:COG2810  260 YSGRSLRRSKSEVLGIKDDIAISIYLLLLPLV----TLELVLKLIEDRLSIGEIGHLQ 313
ParA_partition NF041546
ParA family partition ATPase;
174-329 5.28e-15

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 73.36  E-value: 5.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQGDLT-ASLRKQEGKVKLSDClidhkinVRDTIQKFqirfkn 252
Cdd:NF041546   2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDwAAAREDERPFPVVGL-------ARPTLHRE------ 68

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504955354 253 qptpknifdlipsdsvlekymepgeqakiqggssrlkrlIEPLLQEYDYIIFDCPTNWTFFSQSCVYASDVILIPTQ 329
Cdd:NF041546  69 ---------------------------------------LPSLARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQ 106
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 173-328 7.10e-15

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: 73.76  E-value: 7.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 173 SICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDfdpqqGDL-TASLRKQEG---KVKLSDcLIDHKINVRDTIQKfqi 248
Cdd:cd02038    2 IIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLD-----ADLgLANLDILLGlapKKTLGD-VLKGRVSLEDIIVE--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 249 rfknqpTPKNIfDLIPSDSvlekymepGEQAKIQGGSSRLKRLIE---PLLQEYDYIIFDCPTNWTFFSQSCVYASDVIL 325
Cdd:cd02038   73 ------GPEGL-DIIPGGS--------GMEELANLDPEQKAKLIEelsSLESNYDYLLIDTGAGISRNVLDFLLAADEVI 137


                 ...
gi 504955354 326 IPT 328
Cdd:cd02038  138 VVT 140
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 174-327 2.19e-13

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: 71.55  E-value: 2.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQqgdltASLRKQEGkvklsdclIDHKINVR--DTIQKfQIRFK 251
Cdd:TIGR03453 107 IAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQ-----ASLSALFG--------YQPEFDVGenETLYG-AIRYD 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  252 NQPTP-KNI--------FDLIPSDSVLekyME-----PGEQAKIQGGSS----RLKRLIEPLLQEYDYIIFDCPTNWTFF 313
Cdd:TIGR03453 173 DERRPiSEIirktyfpgLDLVPGNLEL---MEfehetPRALSRGQGGDTiffaRVGEALAEVEDDYDVVVIDCPPQLGFL 249

                         170
                  ....*....|....
gi 504955354  314 SQSCVYASDVILIP 327
Cdd:TIGR03453 250 TLSALCAATGVLIT 263
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 174-336 1.22e-12

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 69.32  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQqgdltASLRKQEGKVKLSDCLIDHKI--NVRDTIQKFQIRFK 251
Cdd:PRK13869 124 IAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQ-----ASLSALLGVLPETDVGANETLyaAIRYDDTRRPLRDV 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 252 NQPTPKNIFDLIPSDSVLEKYMEPGEQAKIQGGS------SRLKRLIEPLLQEYDYIIFDCPTNWTFFSQS--CVYASDV 323
Cdd:PRK13869 199 IRPTYFDGLHLVPGNLELMEFEHTTPKALSDKGTrdglffTRVAQAFDEVADDYDVVVIDCPPQLGFLTLSglCAATSMV 278

                        170
                 ....*....|...
gi 504955354 324 ILIPTQHNNFASL 336
Cdd:PRK13869 279 ITVHPQMLDIASM 291
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 174-346 2.56e-11

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: 63.45  E-value: 2.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILA-YLGKKVLVIDFDPQQGDLTASLrkqegkvklsDCLIDHKIN-------------V 239
Cdd:cd03111    3 VAVVGAKGGVGASTLAVNLAQELAqRAKDKVLLIDLDLPFGDLGLYL----------NLRPDYDLAdviqnldrldrtlL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 240 RDTIQKFQIRFKNQPTPKNIFDLIPsdsvlekymepgeqakIQGGSSRlkRLIEPLLQEYDYIIFDCPTNWTFFSQSCVY 319
Cdd:cd03111   73 DSAVTRHSSGLSLLPAPQELEDLEA----------------LGAEQVD--KLLQVLRAFYDHIIVDLGHFLDEVTLAVLE 134

                        170       180
                 ....*....|....*....|....*..
gi 504955354 320 ASDVILIPTQHnNFASLKNSQKVIQQF 346
Cdd:cd03111  135 AADEILLVTQQ-DLPSLRNARRLLDSL 160
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 173-307 8.44e-11

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: 61.30  E-value: 8.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  173 SICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQGDLTASLRKQEGKVKLSDCLIdHKINVRDTIQkfQIRFKN 252
Cdd:TIGR01007  19 VLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRNSVMSGTFKSQNKITGLTNFLS-GTTDLSDAIC--DTNIEN 95

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 504955354  253 qptpkniFDLIPSDSVlekymEPGEQAKIQggSSRLKRLIEPLLQEYDYIIFDCP 307
Cdd:TIGR01007  96 -------LDVITAGPV-----PPNPTELLQ--SSNFKTLIETLRKRFDYIIIDTP 136
PrgP NF041283
ParA superfamily DNA segregation protein PrgP;
178-347 1.36e-10

ParA superfamily DNA segregation protein PrgP;


Pssm-ID: 469180 [Multi-domain]  Cd Length: 297  Bit Score: 62.08  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 178 NNKGGVGKTTTVANLAAILAYL-GKKVLVIDFDpQQGDLTASLRKQEGKVKLSDCLIdHKINVRDtiqkfqirFKNQPTP 256
Cdd:NF041283   9 NQKGGVGKTTDTVMEAVVASSVfNKKVLVIDTD-LQGNATQFLSKTFNVPNFPQSFM-KCVEDGD--------LEKGIVH 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 257 --KNIfDLIPSDSVLEKYMEPGEQaKIQGGSSR---LKRLIEPLLQEYDYIIFDCPTNWTFFSQSCVYASDVIlIPTQHN 331
Cdd:NF041283  79 ltPNL-DLIAGDYDTRELGDFLAD-KFKSEYDRtfyLKKLLDKIKDDYDFIFIDVPPSTDIKVDNAMVAADYV-IVIQET 155

                        170
                 ....*....|....*.
gi 504955354 332 NFASLKNSQKVIQQFI 347
Cdd:NF041283 156 QQFAFEGSKKLILTYL 171
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 180-306 1.86e-10

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 60.95  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 180 KGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQGdLTASLrkqeGkVKLSDCLIDHKINVRDTIQKfqirfKNQPTPKNI 259
Cdd:COG3640    8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNAN-LAEAL----G-LEVEADLIKPLGEMRELIKE-----RTGAPGGGM 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504955354 260 FDLIPS-DSVLEKYMEPGEQAKI-------QGGS-------SRLKRLIEPL-LQEYDYIIFDC 306
Cdd:COG3640   77 FKLNPKvDDIPEEYLVEGDGVDLlvmgtieEGGSgcycpenALLRALLNHLvLGNYEYVVVDM 139
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 174-327 2.64e-09

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: 57.85  E-value: 2.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQGDLTaslRKQEgkvklsdclidhkiNVRDTIQKFQIRFknq 253
Cdd:pfam09140   3 IVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLRQRTFH---RYFE--------------NRSATADRTGLSL--- 62

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504955354  254 PTPKniFDLIPSDSVLEKYmepgEQAKIQggSSRLKRLIEPLLQEYDYIIFDCPTNWTFFSQSCVYASDVILIP 327
Cdd:pfam09140  63 PTPE--HLNLPDNDVAEVP----DGENID--DARLEEAFADLEARCDFIVIDTPGSDSPLSRLAHSRADTLVTP 128
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 180-308 3.29e-09

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: 57.13  E-value: 3.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 180 KGGVGKTTTVANLAAILAYLGKKVLVIDFDPQ--QGDLTASLRKQEGKVKLSDCLIDHKINVRDTIQKFQIRFKnqptpK 257
Cdd:cd02035    8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAhsLSDAFGQKLGGETPVKGAPNLWAMEIDPEEALEEYWEEVK-----E 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504955354 258 NIFDLIPSDSVLEKYMEpgEQAKIQG-----GSSRLKRLIEplLQEYDYIIFDC-PT 308
Cdd:cd02035   83 LLAQYLRLPGLDEVYAE--ELLSLPGmdeaaAFDELREYVE--SGEYDVIVFDTaPT 135
PHA02518 PHA02518
ParA-like protein; Provisional
 174-333 3.97e-09

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 56.40  E-value: 3.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQGDLTASLRKQEGKvklsdclidhkinvrdtiqkfqirfknq 253
Cdd:PHA02518   3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDWAEAREEGE---------------------------- 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 254 ptpknifdliPSDSVLEkymepgeqakiQGGSsrLKRLIEPLLQEYDYIIFDCPTNWTFFSQSCVYASDVILIPTQHNNF 333
Cdd:PHA02518  55 ----------PLIPVVR-----------MGKS--IRADLPKVASGYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPF 111
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 174-219 9.07e-09

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 56.32  E-value: 9.07e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 504955354 174 ICVYNnKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQgDLTASL 219
Cdd:PRK13230   4 FCFYG-KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKA-DCTRNL 47
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 174-209 1.06e-08

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: 52.82  E-value: 1.06e-08
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFD 209
Cdd:cd01983    3 IAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 174-328 1.19e-08

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 56.91  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQGdlTASLrkQEGKVKlsdcliDHKINVRDTIQKFQIRFKN- 252
Cdd:PRK13705 109 IGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEGNDPQG--TASM--YHGWVP------DLHIHAEDTLLPFYLGEKDd 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 253 -----QPTPKNIFDLIPSDSVLEK----YMEPGEQAKIQGGSSRLKRL-IEPLLQEYDYIIFDCPTNWTFFSQSCVYASD 322
Cdd:PRK13705 179 atyaiKPTCWPGLDIIPSCLALHRieteLMGKFDEGKLPTDPHLMLRLaIETVAHDYDVIVIDSAPNLGIGTINVVCAAD 258


                 ....*.
gi 504955354 323 VILIPT 328
Cdd:PRK13705 259 VLIVPT 264
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 174-219 1.75e-08

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: 55.45  E-value: 1.75e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPqQGDLTASL 219
Cdd:cd02117    2 SIVVYGKGGIGKSTTASNLSAALAEGGKKVLHVGCDP-KHDSTLLL 46
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
180-307 2.16e-08

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 55.21  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 180 KGGVGKTTTVANLAAILAYLGKKVLVIDFDPqqgdltASlrkqegkvKLSDCL---IDHK-------------INVRDTI 243
Cdd:COG0003   11 KGGVGKTTVAAATALALAERGKRTLLVSTDP------AH--------SLGDVLgteLGNEptevavpnlyaleIDPEAEL 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504955354 244 QKFQIRFKNQptPKNIFDLIPSDSVLEkyMEPG--EQAKIQggssRLKRLIEplLQEYDYIIFDCP 307
Cdd:COG0003   77 EEYWERVRAP--LRGLLPSAGVDELAE--SLPGteELAALD----ELLELLE--EGEYDVIVVDTA 132
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 172-305 2.46e-08

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: 55.00  E-value: 2.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 172 LSICVYNnKGGVGKTTTVANLAAILAYLGKKVLVIDFDPqqgdltaslrKQEGKVKLSDCLIDHKInvrDTIQKFQIRFK 251
Cdd:cd02032    1 LVIAVYG-KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDP----------KHDSTFTLTGFLIPTVI---DVLQSVDFHYE 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504955354 252 nqptpknifDLIPSDSVLEKYME--------P-----------GEQAKIqggssrLKRLiePLLQEYDYIIFD 305
Cdd:cd02032   67 ---------EVWPEDVIFTGYGGvdcveaggPpagtgcggyvvGETVKL------LKEL--NAFDEYDVILFD 122
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 174-210 4.14e-08

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: 54.06  E-value: 4.14e-08
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 504955354 174 ICVYNnKGGVGKTTTVANLAAILAYLGKKVLVIDFDP 210
Cdd:cd02040    3 IAIYG-KGGIGKSTTASNLSAALAEMGKKVLHVGCDP 38
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 174-209 7.42e-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: 7.42e-08
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFD 209
Cdd:cd02037    3 IAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
minD CHL00175
septum-site determining protein; Validated
 174-307 1.08e-07

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 53.24  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDP--QQGDLTASLRKQ---------EGKVKLSDCLIDHKinvrdt 242
Cdd:CHL00175  18 IVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADIglRNLDLLLGLENRvlytamdvlEGECRLDQALIRDK------ 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504955354 243 iqkfqiRFKNqptpkniFDLIPSDSVLEKYMEPGEQakiqggssrLKRLIEPL-LQEYDYIIFDCP 307
Cdd:CHL00175  92 ------RWKN-------LSLLAISKNRQRYNVTRKN---------MNMLVDSLkNRGYDYILIDCP 135
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 170-211 1.35e-07

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 52.66  E-value: 1.35e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 504955354 170 RALSICVYNnKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQ 211
Cdd:PRK13185   1 MALVLAVYG-KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPK 41
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
174-211 1.76e-07

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 52.45  E-value: 1.76e-07
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 504955354  174 ICVYNnKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQ 211
Cdd:pfam00142   3 IAIYG-KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPK 39
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 113-346 1.90e-07

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 53.09  E-value: 1.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 113 SPKCQ--TARWGIITNATHIQL------------------FQRHGKVivPATSNYLIkkDNITQIVSQIKNLIDCP---- 168
Cdd:PHA02519  30 SPEARaiTRRWGITEVADLIGVtpqairdaeksgrlpppdFETRGRV--ERRAGYTI--DQISHMRDHFGNPNQRPddkn 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 169 PRALSICVYnnKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQGdlTASLrkQEGKVKlsdcliDHKINVRDTIQKFQI 248
Cdd:PHA02519 106 PVVLAVMSH--KGGVYKTSSAVHTAQWLALQGHRVLLIEGNDPQG--TASM--YHGYVP------DLHIHADDTLLPFYL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 249 ------RFKNQPTPKNIFDLIPSDSVLEK----YMEPGEQAKI-QGGSSRLKRLIEPLLQEYDYIIFDCPTNWTFFSQSC 317
Cdd:PHA02519 174 gerdnaEYAIKPTCWPGLDIIPSCLALHRietdLMQYHDAGKLpHPPHLMLRAAIESVWDNYDIIVIDSAPNLGTGTINV 253

                        250       260
                 ....*....|....*....|....*....
gi 504955354 318 VYASDVILIPTQhnnfASLKNSQKVIQQF 346
Cdd:PHA02519 254 VCAADVIVVATP----AELFDYVSVLQFF 278
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 180-211 3.54e-07

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: 51.19  E-value: 3.54e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 504955354  180 KGGVGKTTTVANLAAILAYLGKKVLVIDFDPQ 211
Cdd:TIGR03371  10 RGGVGKTTLTANLASALKLLGEPVLAIDLDPQ 41
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 180-311 6.03e-07

Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes repeated, in an anion-transporting ATPase. The ATPase is involved in the removal of arsenate, antimonite, and arsenate from the cell.


Pssm-ID: 396792  Cd Length: 302  Bit Score: 50.81  E-value: 6.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  180 KGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQgDLTASLRKQEGKV--KLSDCL----IDHKINVRDTIQKFQiRFKNQ 253
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAH-SLSDSFNQKFGHEptKVKENLsameIDPNMELEEYWQEVQ-KYMNA 86

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504955354  254 ptpknIFDLIPSDSVLEKYME--PG-EQAKIQGgssRLKRLIEPLlqEYDYIIFD-CPTNWT 311
Cdd:pfam02374  87 -----LLGLRMLEGILAEELAslPGiDEAASFD---EFKKYMDEG--EYDVVVFDtAPTGHT 138
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 180-326 7.75e-07

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: 50.00  E-value: 7.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 180 KGGVGKTTTVANLAAILAYLGKKVLVIDFDPQqgdltASLRKQEGKVKLSDCLIDHKINVRDTIQkfqirfKNQPTPKNI 259
Cdd:cd02034    8 KGGVGKTTIAALLIRYLAKKGGKVLAVDADPN-----SNLAETLGVEVEKLPLIKTIGDIRERTG------AKKGEPPEG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 260 FDLIPS-DSVLEKYMEPGEQ------AKIQGGSSR--------LKRLIEPL-LQEYDYIIFDCPTNWTFFSQSCVYASDV 323
Cdd:cd02034   77 MSLNPYvDDIIKEIIVEPDGidllvmGRPEGGGSGcycpvnalLRELLRHLaLKNYEYVVIDMEAGIEHLSRGTIRAVDL 156


                 ...
gi 504955354 324 ILI 326
Cdd:cd02034  157 LII 159
HSDR_N_2 pfam13588
Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N ...
 28-135 1.94e-06

Type I restriction enzyme R protein N terminus (HSDR_N); This family consists of a number of N terminal regions found in type I restriction enzyme R (HSDR) proteins. Restriction and modification (R/M) systems are found in a wide variety of prokaryotes and are thought to protect the host bacterium from the uptake of foreign DNA. Type I restriction and modification systems are encoded by three genes: hsdR, hsdM, and hsdS. The three polypeptides, HsdR, HsdM, and HsdS, often assemble to give an enzyme (R2M2S1) that modifies hemimethylated DNA and restricts unmethylated DNA.


Pssm-ID: 433331 [Multi-domain]  Cd Length: 110  Bit Score: 46.43  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354   28 FVEPLLEELGFTK----LEWFPQFPTGKGAVDYaarknsvgnIFKNTKTNPYVLIEVKgrgtvagtqinlADGTPQYKAT 103
Cdd:pfam13588   9 FVRYLINELGYPKeliaVEKPLQLGSKKKRADI---------VVYNKDGKPYILVECK------------APSIKISQKV 67

                          90       100       110
                  ....*....|....*....|....*....|..
gi 504955354  104 KEQIKRYLLSPKCQtarWGIITNATHIQLFQR 135
Cdd:pfam13588  68 FDQLARYNSVLGAP---FLVVTNGLQHICFKV 96
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 174-209 3.32e-06

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: 48.22  E-value: 3.32e-06
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 504955354  174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFD 209
Cdd:pfam10609   6 IAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 182-307 9.26e-06

exopolysaccharide transport protein family; The model describes the exopolysaccharide transport protein family in bacteria. The transport protein is part of a large genetic locus which is associated with exopolysaccharide (EPS) biosynthesis. Detailed molecular characterization and gene fusion analysis revealed atleast seven gene products are involved in the overall regulation, which among other things, include exopolysaccharide biosynthesis, property of conferring virulence and exopolysaccharide export. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273391 [Multi-domain]  Cd Length: 764  Bit Score: 48.18  E-value: 9.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  182 GVGKTTTVANLAAILAYLGKKVLVIDFDPQQGDLTASLRKQEgKVKLSDCLIDHKinvrdtiqKFQIRFKNQPTPKniFD 261
Cdd:TIGR01005 564 DEGKSFIAANFAALIAAGGKRTLLIDADIRKGGLHQMFGKAP-KPGLLDLLAGEA--------SIEAGIHRDQRPG--LA 632

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 504955354  262 LIPSDSVLEKYMEPGEQAkiqgGSSRLKRLIEPLLQEYDYIIFDCP 307
Cdd:TIGR01005 633 FIAAGGASHFPHNPNELL----ANPAMAELIDNARNAFDLVLVDLA 674
PRK10818 PRK10818
septum site-determining protein MinD;
174-209 1.64e-05

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 46.47  E-value: 1.64e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFD 209
Cdd:PRK10818   5 IVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFD 40
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
182-307 7.13e-05

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 45.14  E-value: 7.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 182 GVGKTTTVANLAAILAYLGKKVLVIDFDPQQGdLTASLRKQEGKVKLSDCLIDhKINVRDTIqkfqirfknQPTPKNIFD 261
Cdd:PRK11519 537 SIGKTFVCANLAAVISQTNKRVLLIDCDMRKG-YTHELLGTNNVNGLSDILIG-QGDITTAA---------KPTSIANFD 605

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 504955354 262 LIPSDSVLEKymePGEQAKiqggSSRLKRLIEPLLQEYDYIIFDCP 307
Cdd:PRK11519 606 LIPRGQVPPN---PSELLM----SERFAELVNWASKNYDLVLIDTP 644
PRK09841 PRK09841
tyrosine-protein kinase;
184-307 8.71e-05

tyrosine-protein kinase;


Pssm-ID: 182106 [Multi-domain]  Cd Length: 726  Bit Score: 44.90  E-value: 8.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 184 GKTTTVANLAAILAYLGKKVLVIDFDPQQGDLTA--SLRKQEGkvkLSDCLiDHKINVRDTIQKFQirfknqptpKNIFD 261
Cdd:PRK09841 544 GKTFVSSTLAAVIAQSDQKVLFIDADLRRGYSHNlfTVSNEHG---LSEYL-AGKDELNKVIQHFG---------KGGFD 610

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 504955354 262 LIPSDSVlekymePGEQAKIQGGsSRLKRLIEPLLQEYDYIIFDCP 307
Cdd:PRK09841 611 VITRGQV------PPNPSELLMR-DRMRQLLEWANDHYDLVIVDTP 649
GPN cd17868
GPN-loop GTPase; GPN-loop GTPases are deeply evolutionarily conserved family of three small ...
 182-316 9.26e-05

GPN-loop GTPase; GPN-loop GTPases are deeply evolutionarily conserved family of three small GTPases, Gpn1, 2, and 3. They form heterodimers, interact with RNA polymerase II and may function in nuclear import of RNA polymerase II.


Pssm-ID: 349777 [Multi-domain]  Cd Length: 198  Bit Score: 43.46  E-value: 9.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 182 GVGKTTTVANLAAILAYLGKKVLVIDFDPQQgdltaslrkqegkvklSDCLIDHKINVRDTIqKFQIRFKNqptpkniFD 261
Cdd:cd17868   10 GSGKTTFCKNMKEHLRARKRNPYVINLDPGN----------------INEPLDYDIDIRDLI-KYDDIMEE-------LD 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504955354 262 LIPSDSVLE--KYMEPGEqakiqggsSRLKRLIEPLLQEYDYIIFDCPTNWTFFSQS 316
Cdd:cd17868   66 LGPNGSIVYslEYFEKNF--------DWFEKKLENEDKNPHYILFDCPGQIELFTHS 114
BchX cd02033
X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls ...
 174-219 1.65e-04

X-subunit of protochlorophyllide reductase; Chlorophyllide reductase converts chlorophylls into bacteriochlorophylls by reducing the chlorin B-ring. This family contains the X subunit of this three-subunit enzyme. Sequence and structure similarity between bchX, protochlorophyllide reductase L subunit (bchL and chlL) and nitrogenase Fe protein (nifH gene) suggest their functional similarity. Members of the BchX family serve as the unique electron donors to their respective catalytic subunits (bchN-bchB, bchY-bchZ and nitrogenase component 1). Mechanistically, they hydrolyze ATP and transfer electrons through a Fe4-S4 cluster.


Pssm-ID: 349753  Cd Length: 329  Bit Score: 43.67  E-value: 1.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 504955354 174 ICVYNnKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQgDLTASL 219
Cdd:cd02033   34 IAIYG-KGGIGKSFTLANLSYMMAQQGKRVLLIGCDPKS-DTTSLL 77
COG4748 COG4748
Uncharacterized conserved protein, contains restriction enzyme R protein N terminal (HSDR_N) ...
 26-135 1.68e-04

Uncharacterized conserved protein, contains restriction enzyme R protein N terminal (HSDR_N) domain [Function unknown];


Pssm-ID: 443782  Cd Length: 355  Bit Score: 43.72  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  26 NDFVEPLLEELG---FTKLEWFPQFP----TGKGA-VDYAarknsvgnIFKNTKtnPYVLIEVKGRGTvagtqiNLADgt 97
Cdd:COG4748   29 NALIMPFIQILGydvFNPTEVVPEYTadvgTKKGEkVDYA--------ILKDGQ--PVILIECKGVGE------DLDI-- 90

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 504955354  98 pqykATKEQIKRYLlspKCQTARWGIITNATHIQLFQR 135
Cdd:COG4748   91 ----NHASQLFRYF---HVTEARFGILTNGIEYRFYTD 121
chlL CHL00072
photochlorophyllide reductase subunit L
 172-219 3.22e-04

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 42.42  E-value: 3.22e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 504955354 172 LSICVYNnKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQgDLTASL 219
Cdd:CHL00072   1 MKLAVYG-KGGIGKSTTSCNISIALARRGKKVLQIGCDPKH-DSTFTL 46
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
 182-209 6.06e-04

flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 41.55  E-value: 6.06e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 504955354  182 GVGKTTTVANLAAILA--YLGKKVLVIDFD 209
Cdd:TIGR03499 204 GVGKTTTLAKLAARFAleHGKKKVALITTD 233
flhF PRK05703
flagellar biosynthesis protein FlhF;
156-206 6.89e-04

flagellar biosynthesis protein FlhF;


Pssm-ID: 235570 [Multi-domain]  Cd Length: 424  Bit Score: 41.80  E-value: 6.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504955354 156 QIVSQIKNLIDCPPRALSIcvynNKG--------GVGKTTTVANLAAILAYL--GKKVLVI 206
Cdd:PRK05703 201 YLLELLANMIPVRVEDILK----QGGvvalvgptGVGKTTTLAKLAARYALLygKKKVALI 257
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 180-210 7.47e-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: 42.00  E-value: 7.47e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 504955354  180 KGGVGKTTTVANLAAILAYLGKKVLVIDFDP 210
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDP 359
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 180-311 9.77e-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: 41.61  E-value: 9.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  180 KGGVGKTTTVANLAAILAYLGKKVLVIDFDPqqgdltASlrkqegkvklsdclidhkiNVRDTiqkFQIRFKNQPTPkni 259
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDP------AS-------------------NVGQV---FGQTIGNKITA--- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354  260 FDLIPSDSVLEkyMEPGEQAkiqgGSSRlKRLIEP---------------------------------------LLQEYD 300
Cdd:TIGR04291  60 IAGVPGLFALE--IDPQAAA----QAYR-ARIVDPvrgvlpddvvssieeqlsgactteiaafdeftglltdaeLTQDFD 132

                         170
                  ....*....|..
gi 504955354  301 YIIFD-CPTNWT 311
Cdd:TIGR04291 133 HIIFDtAPTGHT 144
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
158-209 1.19e-03

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 40.80  E-value: 1.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504955354 158 VSQIKNLIdcppralsiCVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFD 209
Cdd:PRK11670 103 VNGVKNII---------AVSSGKGGVGKSSTAVNLALALAAEGAKVGILDAD 145
PoNe cd20702
Polymorphic Nuclease effector (PoNe) domain is a deoxyribonuclease; This family contains the ...
 29-96 1.33e-03

Polymorphic Nuclease effector (PoNe) domain is a deoxyribonuclease; This family contains the DNase toxin domain called PoNe (Polymorphic Nuclease effector), which belongs to a diverse superfamily of PD-(D/E)xK phosphodiesterases, and is associated with several toxin delivery systems including type V, type VI, and type VII. PoNe toxicity is antagonized by cognate immunity proteins (PoNi) containing DUF1911 and DUF1910 domains. The PoNe domain co-occurs with a variety of N-terminal domains such as filamentous hemagglutinin, nuclease, HINT, DUFs, PAAR, RHS repeat, or LXG domains. Some members of this family also co-occur with the FIX (Found in type sIX effector) domain of unknown function, as identified by Jana et al., who have also identified this PoNe domain.


Pssm-ID: 410637  Cd Length: 77  Bit Score: 37.34  E-value: 1.33e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504955354  29 VEPLLEELGFTKLEWFPQFPTGKGaVDyaarknsvgNIFKNTKTNPYVLIEVKGRGTVAGTQINLADG 96
Cdd:cd20702    9 ADLYLKSQGYTKLIGGSKGGGGNG-ID---------GVYKDPKGPEYIIVEAKFGSASLKGGVSLGTT 66
SRP54 smart00962
SRP54-type protein, GTPase domain; This entry represents the GTPase domain of the 54 kDa SRP54 ...
 182-206 1.51e-03

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: 39.70  E-value: 1.51e-03
                           10        20
                   ....*....|....*....|....*.
gi 504955354   182 GVGKTTTVANLAAILAYLG-KKVLVI 206
Cdd:smart00962  11 GVGKTTTIAKLAARLKLKGgKKVLLV 36
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
 182-206 2.51e-03

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: 39.06  E-value: 2.51e-03
                          10        20
                  ....*....|....*....|....*
gi 504955354  182 GVGKTTTVANLAAILAYLGKKVLVI 206
Cdd:pfam00448  10 GSGKTTTIAKLAAYLKKKGKKVLLV 34
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
182-206 2.66e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 39.85  E-value: 2.66e-03
                         10        20
                 ....*....|....*....|....*.
gi 504955354 182 GVGKTTTVANLAAILAYLG-KKVLVI 206
Cdd:COG1419  174 GVGKTTTIAKLAARFVLRGkKKVALI 199
SRP_G_like cd03115
GTPase domain similar to the signal recognition particle subunit 54; The signal recognition ...
 182-209 2.87e-03

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: 38.89  E-value: 2.87e-03
                         10        20
                 ....*....|....*....|....*...
gi 504955354 182 GVGKTTTVANLAAILAYLGKKVLVIDFD 209
Cdd:cd03115   10 GSGKTTTLAKLARYYQEKGKKVLLIAAD 37
nifH PRK13233
nitrogenase iron protein;
174-211 3.23e-03

nitrogenase iron protein;


Pssm-ID: 183905  Cd Length: 275  Bit Score: 39.42  E-value: 3.23e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 504955354 174 ICVYNnKGGVGKTTTVANLAAILAYL-GKKVLVIDFDPQ 211
Cdd:PRK13233   5 IAIYG-KGGIGKSTTTQNTAAAMAYFhDKKVFIHGCDPK 42
PRK13231 PRK13231
nitrogenase reductase-like protein; Reviewed
 174-219 3.29e-03

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183904  Cd Length: 264  Bit Score: 39.40  E-value: 3.29e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 504955354 174 ICVYNnKGGVGKTTTVANLAAILAYlGKKVLVIDFDPqQGDLTASL 219
Cdd:PRK13231   5 IAIYG-KGGIGKSTTVSNMAAAYSN-DHRVLVIGCDP-KADTTRTL 47
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 174-353 3.65e-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: 38.67  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 174 ICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDPQQGdlTASLRKQEGKVKLSDCLIDHKINVRDTIQKFQIRFKNQ 253
Cdd:cd17869    6 ITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQS--TDVFFGASGRYLMSDHLYTLKSRKANLADKLESCVKQH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504955354 254 PTPKNIFDliPSDSVLEkymepgeqaKIQGGSSRLKRLIEPL--LQEYDYIIFDCPtnWTFFSQSC--VYASDVILIPTQ 329
Cdd:cd17869   84 ESGVYYFS--PFKSALD---------ILEIKKDDILHMITKLveAHAYDYIIMDLS--FEFSSTVCklLQASHNNVVIAL 150

                        170       180
                 ....*....|....*....|....
gi 504955354 330 HNNFASLKNsQKVIQQFIPQIQNK 353
Cdd:cd17869  151 QDANSSYKL-NKFLRALEDLFQEN 173
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 173-210 4.84e-03

Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in cellulose biosynthesis. (Roemling U. and Galperin M.Y. "Bacterial cellulose biosynthesis. Diversity of operons and subunits" (manuscript in preparation)). A second component of the extracellular matrix of the multicellular morphotype (rdar) of Salmonella typhimurium and Escherichia coli is cellulose. The family does contain a P-loop sequence motif suggesting a nucleotide binding function, but this has not been confirmed.


Pssm-ID: 429004 [Multi-domain]  Cd Length: 234  Bit Score: 38.51  E-value: 4.84e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 504955354  173 SICVYNNKGGVGKTTTVANLAAILAYLGKKVLVIDFDP 210
Cdd:pfam06564   3 ILALQGVRGGVGTTSILAALAWALQRLGERVLLIDLSP 40
FlhF cd17873
signal-recognition particle GTPase FlhF; FlhF protein is a signal-recognition particle (SRP) ...
 182-209 4.99e-03

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


Pssm-ID: 349782 [Multi-domain]  Cd Length: 189  Bit Score: 37.91  E-value: 4.99e-03
                         10        20
                 ....*....|....*....|....*....
gi 504955354 182 GVGKTTTVANLAAILA-YLGKKVLVIDFD 209
Cdd:cd17873   10 GVGKTTTLAKLAARYVlKKGKKVALITTD 38
PRK10416 PRK10416
signal recognition particle-docking protein FtsY; Provisional
 182-204 8.36e-03

signal recognition particle-docking protein FtsY; Provisional


Pssm-ID: 236686 [Multi-domain]  Cd Length: 318  Bit Score: 38.16  E-value: 8.36e-03
                         10        20
                 ....*....|....*....|...
gi 504955354 182 GVGKTTTVANLAAILAYLGKKVL 204
Cdd:PRK10416 124 GVGKTTTIGKLAHKYKAQGKKVL 146
FtsY COG0552
Signal recognition particle GTPase FtsY [Intracellular trafficking, secretion, and vesicular ...
 182-205 9.20e-03

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


Pssm-ID: 440318 [Multi-domain]  Cd Length: 303  Bit Score: 38.08  E-value: 9.20e-03
                         10        20
                 ....*....|....*....|....
gi 504955354 182 GVGKTTTVANLAAILAYLGKKVLV 205
Cdd:COG0552  110 GVGKTTTIGKLAHRLKAEGKSVLL 133
 
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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