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Conserved domains on  [gi|1519253200|gb|AZA12430|]
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Sporulation initiation inhibitor protein Soj [Corynebacterium gerontici]

Protein Classification

ParA family protein( domain architecture ID 11439703)

ParA (plasmid partition protein A) family protein similar to ParA, which is essential for plasmid partition, ensuring the proper distribution of newly replicated plasmids to daughter cells during cell division

CATH:  3.40.50.300
Gene Ontology:  GO:0005524|GO:0016887
PubMed:  17161598|2149583|26339031|11522360
SCOP:  4003982

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 ...
 35-289 1.69e-125

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: 359.17  E-value: 1.69e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  35 TRRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALGAEHRAGTLSSYELLIGECTAEQAMQQSSAsE 114
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEI-P 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 115 NLWCIPATIDLAGAEIELVSMVRREYRLHDALSStfiEEAGFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEG 194
Cdd:COG1192    80 GLDLIPANIDLAGAEIELVSRPGRELRLKRALAP---LADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 195 VGQLLNNIVMIRQHLNANLHISAILLTMYDARTKLAEQVSEEVRGHFGDVVLRTKIPRSVKVSEAPGYGQTVLAYDPGSR 274
Cdd:COG1192   157 LAQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSK 236

                         250
                  ....*....|....*
gi 1519253200 275 GAMAYVDAARELSKR 289
Cdd:COG1192   237 GAKAYRALAEELLER 251
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 35-289 1.69e-125

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: 359.17  E-value: 1.69e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  35 TRRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALGAEHRAGTLSSYELLIGECTAEQAMQQSSAsE 114
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEI-P 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 115 NLWCIPATIDLAGAEIELVSMVRREYRLHDALSStfiEEAGFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEG 194
Cdd:COG1192    80 GLDLIPANIDLAGAEIELVSRPGRELRLKRALAP---LADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 195 VGQLLNNIVMIRQHLNANLHISAILLTMYDARTKLAEQVSEEVRGHFGDVVLRTKIPRSVKVSEAPGYGQTVLAYDPGSR 274
Cdd:COG1192   157 LAQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSK 236

                         250
                  ....*....|....*
gi 1519253200 275 GAMAYVDAARELSKR 289
Cdd:COG1192   237 GAKAYRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 35-215 5.89e-81

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: 243.26  E-value: 5.89e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  35 TRRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALGAEHRAGTLSSYELLIGECTAEQAMQQSSAsE 114
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVI-E 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 115 NLWCIPATIDLAGAEIELVSMVRREYRLHDALSStfIEEAgFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEG 194
Cdd:pfam13614  80 NLDLIPSNIDLAGAEIELIGIENRENILKEALEP--VKDN-YDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEG 156

                         170       180
                  ....*....|....*....|.
gi 1519253200 195 VGQLLNNIVMIRQHLNANLHI 215
Cdd:pfam13614 157 LSQLLNTIKLVKKRLNPSLEI 177
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 36-238 3.51e-50

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: 163.09  E-value: 3.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  36 RRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALgaehragtlssyelligectaeqamqqssasen 115
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 116 lwcipatidlagaeielvsmvrreyrlhdalsstfieeagFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEGV 195
Cdd:cd02042    48 ----------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGL 87

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1519253200 196 GQLLNNIVMIRQHLNANLHISAILLTMYDARTKLAEQVSEEVR 238
Cdd:cd02042    88 AKLLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
38-285 2.54e-31

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 116.50  E-value: 2.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  38 ITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTAlgaehragtlssyelligectaeqamqqSSASEnlw 117
Cdd:NF041546    2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDW----------------------------AAARE--- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 118 cipatidlAGAEIELVSMVRreYRLHDALSSTfieEAGFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEGVGQ 197
Cdd:NF041546   51 --------DERPFPVVGLAR--PTLHRELPSL---ARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASAD 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 198 LLnNIVMIRQHLNANLHiSAILLTMYDARTKLAEQVSEEVRGhFGDVVLRTKIPRSVKVSEAPGYGQTVLAYDPGSrgam 277
Cdd:NF041546  118 TV-DLIKEAREYTPGLK-AAFVLNRAIARTALGREVAEALAE-YGLPVLKTRIGQRVAFAESAAEGLTVFEAEPDG---- 190


                  ....*...
gi 1519253200 278 ayvDAARE 285
Cdd:NF041546  191 ---KAARE 195
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 36-288 4.62e-21

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: 90.18  E-value: 4.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  36 RRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLD-PQGNASTALGAEHRAGTLssYELLIGECTAEQAMQQSsaSE 114
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGMEDKPVTL--HDVLAGEADIKDAIYEG--PF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 115 NLWCIPATIDLAG---AEIElvsmvrreyRLHDALSStFIEEagFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYA 191
Cdd:TIGR01969  77 GVKVIPAGVSLEGlrkADPD---------KLEDVLKE-IIDD--TDFLLIDAPAGLERDAVTALAAADELLLVVNPEISS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 192 LegVGQLLNNIVMIRQHLNAnlhISAILLTMYDARTKLAEQVSEEVRghfgDVVLRTKIPRSVKVSEAPGYGQTVLAYDP 271
Cdd:TIGR01969 145 I--TDALKTKIVAEKLGTAI---LGVVLNRVTRDKTELGREEIETIL----EVPVLGVVPEDPEVRRAAAFGEPVVIYNP 215

                         250
                  ....*....|....*..
gi 1519253200 272 GSRGAMAYVDAARELSK 288
Cdd:TIGR01969 216 NSPAAQAFMELAAELAG 232
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 20-282 4.70e-21

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 92.82  E-value: 4.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  20 HRRGTrgaaltkpERTRRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALgaehraGTLSSYELLIG 99
Cdd:PRK13869  114 HRRGS--------EHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALL------GVLPETDVGAN 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 100 EcTAEQAMQQSSASENLW-CIPAT----IDLAGAEIELVSMvrrEYRLHDALS-------------STFIEEAG--FDFI 159
Cdd:PRK13869  180 E-TLYAAIRYDDTRRPLRdVIRPTyfdgLHLVPGNLELMEF---EHTTPKALSdkgtrdglfftrvAQAFDEVAddYDVV 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 160 FIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEGVGQLL---NNIVMIRQHLNANLHISAI--LLTMYDARTKLAEQVS 234
Cdd:PRK13869  256 VIDCPPQLGFLTLSGLCAATSMVITVHPQMLDIASMSQFLlmtRDLLGVVKEAGGNLQYDFIryLLTRYEPQDAPQTKVA 335

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1519253200 235 EEVRGHFGDVVLRTKIPRSVKVSEAPGYGQTVlaYDPGSRG--------AMAYVDA 282
Cdd:PRK13869  336 ALLRNMFEDHVLTNPMVKSAAVSDAGLTKQTL--YEIGRENltrstydrAMESLDA 389
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 31-83 1.79e-03

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 39.86  E-value: 1.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1519253200  31 KPERTRRITVANqKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALG 83
Cdd:NF041417    8 RGEDTEFVFFSG-KGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFG 59
 
Name Accession Description Interval E-value
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 35-289 1.69e-125

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: 359.17  E-value: 1.69e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  35 TRRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALGAEHRAGTLSSYELLIGECTAEQAMQQSSAsE 114
Cdd:COG1192     1 MKVIAVANQKGGVGKTTTAVNLAAALARRGKRVLLIDLDPQGNLTSGLGLDPDDLDPTLYDLLLDDAPLEDAIVPTEI-P 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 115 NLWCIPATIDLAGAEIELVSMVRREYRLHDALSStfiEEAGFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEG 194
Cdd:COG1192    80 GLDLIPANIDLAGAEIELVSRPGRELRLKRALAP---LADDYDYILIDCPPSLGLLTLNALAAADSVLIPVQPEYLSLEG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 195 VGQLLNNIVMIRQHLNANLHISAILLTMYDARTKLAEQVSEEVRGHFGDVVLRTKIPRSVKVSEAPGYGQTVLAYDPGSR 274
Cdd:COG1192   157 LAQLLETIEEVREDLNPKLEILGILLTMVDPRTRLSREVLEELREEFGDKVLDTVIPRSVALAEAPSAGKPVFEYDPKSK 236

                         250
                  ....*....|....*
gi 1519253200 275 GAMAYVDAARELSKR 289
Cdd:COG1192   237 GAKAYRALAEELLER 251
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 35-215 5.89e-81

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: 243.26  E-value: 5.89e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  35 TRRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALGAEHRAGTLSSYELLIGECTAEQAMQQSSAsE 114
Cdd:pfam13614   1 GKVIAIANQKGGVGKTTTSVNLAAALAKKGKKVLLIDLDPQGNATSGLGIDKNNVEKTIYELLIGECNIEEAIIKTVI-E 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 115 NLWCIPATIDLAGAEIELVSMVRREYRLHDALSStfIEEAgFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEG 194
Cdd:pfam13614  80 NLDLIPSNIDLAGAEIELIGIENRENILKEALEP--VKDN-YDYIIIDCPPSLGLLTINALTASDSVLIPVQCEYYALEG 156

                         170       180
                  ....*....|....*....|.
gi 1519253200 195 VGQLLNNIVMIRQHLNANLHI 215
Cdd:pfam13614 157 LSQLLNTIKLVKKRLNPSLEI 177
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 38-266 2.38e-52

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: 172.15  E-value: 2.38e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  38 ITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALGAE--HRAGTLSSYELLIGECTAEQAMQQS-SASE 114
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGLRVLLIDLDPQSNNSSVEGLEgdIAPALQALAEGLKGRVNLDPILLKEkSDEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 115 NLWCIPATIDLAGAEIELVSMvRREYRLHDALSstFIEEaGFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEG 194
Cdd:pfam01656  81 GLDLIPGNIDLEKFEKELLGP-RKEERLREALE--ALKE-DYDYVIIDGAPGLGELLRNALIAADYVIIPLEPEVILVED 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519253200 195 VGQLLNNIVMIRQHLN-ANLHISAILLTMYDARTKLAEQVSEEVRGHFGDVVLrTKIPRSVKVSEAPGYGQTV 266
Cdd:pfam01656 157 AKRLGGVIAALVGGYAlLGLKIIGVVLNKVDGDNHGKLLKEALEELLRGLPVL-GVIPRDEAVAEAPARGLPV 228
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 36-238 3.51e-50

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: 163.09  E-value: 3.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  36 RRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALgaehragtlssyelligectaeqamqqssasen 115
Cdd:cd02042     1 KVIAVANQKGGVGKTTLAVNLAAALALRGKRVLLIDLDPQGSLTSWL--------------------------------- 47

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 116 lwcipatidlagaeielvsmvrreyrlhdalsstfieeagFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEGV 195
Cdd:cd02042    48 ----------------------------------------YDYILIDTPPSLGLLTRNALAAADLVLIPVQPSPFDLDGL 87

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1519253200 196 GQLLNNIVMIRQHLNANLHISAILLTMYDARTKLAEQVSEEVR 238
Cdd:cd02042    88 AKLLDTLEELKKQLNPPLLILGILLTRVDPRTKLAREVLEELK 130
ParA_partition NF041546
ParA family partition ATPase;
38-285 2.54e-31

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 116.50  E-value: 2.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  38 ITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTAlgaehragtlssyelligectaeqamqqSSASEnlw 117
Cdd:NF041546    2 IAVLNQKGGVGKTTLATHLAAALARRGYRVLLVDADPQGSALDW----------------------------AAARE--- 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 118 cipatidlAGAEIELVSMVRreYRLHDALSSTfieEAGFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEGVGQ 197
Cdd:NF041546   51 --------DERPFPVVGLAR--PTLHRELPSL---ARDYDFVVIDGPPRAEDLARSAIKAADLVLIPVQPSPYDLWASAD 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 198 LLnNIVMIRQHLNANLHiSAILLTMYDARTKLAEQVSEEVRGhFGDVVLRTKIPRSVKVSEAPGYGQTVLAYDPGSrgam 277
Cdd:NF041546  118 TV-DLIKEAREYTPGLK-AAFVLNRAIARTALGREVAEALAE-YGLPVLKTRIGQRVAFAESAAEGLTVFEAEPDG---- 190


                  ....*...
gi 1519253200 278 ayvDAARE 285
Cdd:NF041546  191 ---KAARE 195
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 36-286 1.26e-25

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: 102.28  E-value: 1.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  36 RRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLD-PQGNASTALGAEHRAG-TLSsyELLIGECTAEQAMQQSSAS 113
Cdd:cd02036     1 RVIVITSGKGGVGKTTTTANLGVALAKLGKKVLLIDADiGLRNLDLILGLENRIVyTLV--DVLEGECRLEQALIKDKRW 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 114 ENLWCIPATIDLAGAEIELVSMVrreyRLHDALSstfieeAGFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALE 193
Cdd:cd02036    79 ENLYLLPASQTRDKDALTPEKLE----ELVKELK------DSFDFILIDSPAGIESGFINAIAPADEAIIVTNPEISSVR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 194 G---VGQLLNNIVMIRQHLnanlhisaiLLTMYD-ARTKLAEQVS-EEVRGHFGDVVLRTkIPRSVKVSEAPGYGQTVLA 268
Cdd:cd02036   149 DadrVIGLLESKGIVNIGL---------IVNRYRpEMVKSGDMLSvEDIQEILGIPLLGV-IPEDPEVIVATNRGEPLVL 218

                         250
                  ....*....|....*...
gi 1519253200 269 YDPGSRGAMAYVDAAREL 286
Cdd:cd02036   219 YKPNSLAAKAFENIARRL 236
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 51-289 1.58e-23

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: 96.50  E-value: 1.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  51 TSSVNLAAGLAQNGLKVLVVDLDPQ-GNASTALGAEHRAgTLSsyELLIGECTAEQAMQQSsaSENLWCIPATIDLAGAE 129
Cdd:COG0455     1 TVAVNLAAALARLGKRVLLVDADLGlANLDVLLGLEPKA-TLA--DVLAGEADLEDAIVQG--PGGLDVLPGGSGPAELA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 130 ielvsMVRREYRLHDALSSTfieEAGFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEGVGQLLNNIVmiRQHL 209
Cdd:COG0455    76 -----ELDPEERLIRVLEEL---ERFYDVVLVDTGAGISDSVLLFLAAADEVVVVTTPEPTSITDAYALLKLLR--RRLG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 210 NANLHisaILLTMYDART---KLAEQVSEEVRGHFG-DVVLRTKIPRSVKVSEAPGYGQTVLAYDPGSRGAMAYVDAARE 285
Cdd:COG0455   146 VRRAG---VVVNRVRSEAearDVFERLEQVAERFLGvRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAAR 222


                  ....
gi 1519253200 286 LSKR 289
Cdd:COG0455   223 LAGW 226
minD_arch TIGR01969
cell division ATPase MinD, archaeal; This model represents the archaeal branch of the MinD ...
 36-288 4.62e-21

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: 90.18  E-value: 4.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  36 RRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLD-PQGNASTALGAEHRAGTLssYELLIGECTAEQAMQQSsaSE 114
Cdd:TIGR01969   1 RIITIASGKGGTGKTTITANLGVALAKLGKKVLALDADiTMANLELILGMEDKPVTL--HDVLAGEADIKDAIYEG--PF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 115 NLWCIPATIDLAG---AEIElvsmvrreyRLHDALSStFIEEagFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYA 191
Cdd:TIGR01969  77 GVKVIPAGVSLEGlrkADPD---------KLEDVLKE-IIDD--TDFLLIDAPAGLERDAVTALAAADELLLVVNPEISS 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 192 LegVGQLLNNIVMIRQHLNAnlhISAILLTMYDARTKLAEQVSEEVRghfgDVVLRTKIPRSVKVSEAPGYGQTVLAYDP 271
Cdd:TIGR01969 145 I--TDALKTKIVAEKLGTAI---LGVVLNRVTRDKTELGREEIETIL----EVPVLGVVPEDPEVRRAAAFGEPVVIYNP 215

                         250
                  ....*....|....*..
gi 1519253200 272 GSRGAMAYVDAARELSK 288
Cdd:TIGR01969 216 NSPAAQAFMELAAELAG 232
PRK13869 PRK13869
plasmid-partitioning protein RepA; Provisional
 20-282 4.70e-21

plasmid-partitioning protein RepA; Provisional


Pssm-ID: 139929 [Multi-domain]  Cd Length: 405  Bit Score: 92.82  E-value: 4.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  20 HRRGTrgaaltkpERTRRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALgaehraGTLSSYELLIG 99
Cdd:PRK13869  114 HRRGS--------EHLQVIAVTNFKGGSGKTTTSAHLAQYLALQGYRVLAVDLDPQASLSALL------GVLPETDVGAN 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 100 EcTAEQAMQQSSASENLW-CIPAT----IDLAGAEIELVSMvrrEYRLHDALS-------------STFIEEAG--FDFI 159
Cdd:PRK13869  180 E-TLYAAIRYDDTRRPLRdVIRPTyfdgLHLVPGNLELMEF---EHTTPKALSdkgtrdglfftrvAQAFDEVAddYDVV 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 160 FIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEGVGQLL---NNIVMIRQHLNANLHISAI--LLTMYDARTKLAEQVS 234
Cdd:PRK13869  256 VIDCPPQLGFLTLSGLCAATSMVITVHPQMLDIASMSQFLlmtRDLLGVVKEAGGNLQYDFIryLLTRYEPQDAPQTKVA 335

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1519253200 235 EEVRGHFGDVVLRTKIPRSVKVSEAPGYGQTVlaYDPGSRG--------AMAYVDA 282
Cdd:PRK13869  336 ALLRNMFEDHVLTNPMVKSAAVSDAGLTKQTL--YEIGRENltrstydrAMESLDA 389
partition_RepA TIGR03453
plasmid partitioning protein RepA; Members of this family are the RepA (or ParA) protein ...
 6-285 5.99e-21

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: 92.35  E-value: 5.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200   6 REH-EQTAAMGRR-AAHRRGTrgaaltkpERTRRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQgnAStaLG 83
Cdd:TIGR03453  81 RRHlAQRGREARRyLPHRRGG--------EHLQVIAVTNFKGGSGKTTTAAHLAQYLALRGYRVLAIDLDPQ--AS--LS 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  84 AEHraGTLSSYELLIGEcTAEQAM----QQSSASE--------NLWCIPATIDLAGAEIE--LVSMVRREY------RLH 143
Cdd:TIGR03453 149 ALF--GYQPEFDVGENE-TLYGAIryddERRPISEiirktyfpGLDLVPGNLELMEFEHEtpRALSRGQGGdtiffaRVG 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 144 DALSSTfieEAGFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEGVGQLLNNIVMIRQHLN---ANLHISAI-- 218
Cdd:TIGR03453 226 EALAEV---EDDYDVVVIDCPPQLGFLTLSALCAATGVLITVHPQMLDVMSMSQFLLMTGDLLGVVReagGNLSYDFMry 302

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519253200 219 LLTMYDARTKLAEQVSEEVRGHFGDVVLRTKIPRSVKVSEAPGYGQTVLAYDPGSRGAMAYvDAARE 285
Cdd:TIGR03453 303 LVTRYEPNDGPQAQMVAFLRSLFGDHVLTNPMLKSTAISDAGLTKQTLYEVERSQFTRSTY-DRAME 368
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 12-168 4.90e-18

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: 82.54  E-value: 4.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  12 AAMGRRAAHRRGTRGAALTKPERTRRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQG-NASTALGAEHRAGt 90
Cdd:COG0489    69 LLLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQSGKRVLLIDADLRGpSLHRMLGLENRPG- 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  91 LSsyELLIGECTAEQAMQQSSAsENLWCIPatidlAGAEIELVSmvrrEYRLHDALsSTFIEEA--GFDFIFIDCPPSLG 168
Cdd:COG0489   148 LS--DVLAGEASLEDVIQPTEV-EGLDVLP-----AGPLPPNPS----ELLASKRL-KQLLEELrgRYDYVIIDTPPGLG 214
PRK13705 PRK13705
plasmid-partitioning protein SopA; Provisional
 8-264 9.27e-18

plasmid-partitioning protein SopA; Provisional


Pssm-ID: 184261 [Multi-domain]  Cd Length: 388  Bit Score: 83.10  E-value: 9.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200   8 HEQTAAMGR----------RAAHRRGTRGAALTKPERTRR--ITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVD-LDP 74
Cdd:PRK13705   67 HPDMEMRGRveqrvgytieQINHMRDVFGTRLRRAEDVFPpvIGVAAHKGGVYKTSVSVHLAQDLALKGLRVLLVEgNDP 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  75 QGNASTALGAE-----HRAGTLSSYELliGECTAEQAMQQSSASENLWCIPATIDLAGAEIELvsmvrreYRLHDA---- 145
Cdd:PRK13705  147 QGTASMYHGWVpdlhiHAEDTLLPFYL--GEKDDATYAIKPTCWPGLDIIPSCLALHRIETEL-------MGKFDEgklp 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 146 -----LSSTFIEEA--GFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEGVGQLLNnivMIRQhLNANLHISA- 217
Cdd:PRK13705  218 tdphlMLRLAIETVahDYDVIVIDSAPNLGIGTINVVCAADVLIVPTPAELFDYTSALQFFD---MLRD-LLKNVDLKGf 293

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1519253200 218 -----ILLTMY-DARTKLAEQVSEEVRGHFGDVVLRtkipRSVKVSEAPGYGQ 264
Cdd:PRK13705  294 epdvrILLTKYsNSNGSQSPWMEEQIRDAWGSMVLK----NVVRETDEVGKGQ 342
PHA02518 PHA02518
ParA-like protein; Provisional
 38-289 1.61e-16

ParA-like protein; Provisional


Pssm-ID: 222854 [Multi-domain]  Cd Length: 211  Bit Score: 76.81  E-value: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  38 ITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTAlgAEHRAGTLSSyelligectaeqamqqssasenlw 117
Cdd:PHA02518    3 IAVLNQKGGAGKTTVATNLASWLHADGHKVLLVDLDPQGSSTDW--AEAREEGEPL------------------------ 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 118 cIPAtidlagaeIELVSMVRREyrLHDALSstfieeaGFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALEGVGQ 197
Cdd:PHA02518   57 -IPV--------VRMGKSIRAD--LPKVAS-------GYDYVVVDGAPQDSELARAALRIADMVLIPVQPSPFDIWAAPD 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 198 LLnNIVMIRQHLNANLHISAILLTMYDARTKLAEQVSEEVRGhFGDVVLRTKIPRSVKVSEAPGYGQTVLAYDPGSRGAM 277
Cdd:PHA02518  119 LV-ELIKARQEVTDGLPKFAFIISRAIKNTQLYREARKALAG-YGLPILRNGTTQRVAYADAAEAGGSVLELPEDDKAAE 196

                         250
                  ....*....|..
gi 1519253200 278 AYVDAARELSKR 289
Cdd:PHA02518  197 EIIQLVKELFRG 208
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 38-183 5.69e-16

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 76.25  E-value: 5.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  38 ITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDpQG--NASTALGAEHRAgtlsSYEL---LIGECTAEQAMQQSSA 112
Cdd:COG2894     5 IVVTSGKGGVGKTTTTANLGTALALLGKKVVLIDAD-IGlrNLDLVMGLENRI----VYDLvdvIEGECRLKQALIKDKR 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519253200 113 SENLWCIPAtidlagaeielvSMVRREyrlhDALS----STFIEE--AGFDFIFIDCPPSL--GLLtiNAMTAVNEVLI 183
Cdd:COG2894    80 FENLYLLPA------------SQTRDK----DALTpeqmKKLVEElkEEFDYILIDSPAGIeqGFK--NAIAGADEAIV 140
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 24-168 1.58e-15

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: 73.76  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  24 TRGAALTKPERTRRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDP-QGNASTALGAEHRAGtLSsyELLIGECT 102
Cdd:cd05387     8 TNLLFAGSDAGPKVIAVTSASPGEGKSTVAANLAVALAQSGKRVLLIDADLrRPSLHRLLGLPNEPG-LS--EVLSGQAS 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519253200 103 AEQAMQQSSaSENLWCIPA-TIDLAGAEielvsmVRREYRLHDalsstFIEEAG--FDFIFIDCPPSLG 168
Cdd:cd05387    85 LEDVIQSTN-IPNLDVLPAgTVPPNPSE------LLSSPRFAE-----LLEELKeqYDYVIIDTPPVLA 141
PRK10818 PRK10818
septum site-determining protein MinD;
36-286 2.44e-15

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 74.59  E-value: 2.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  36 RRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLD-PQGNASTALGAEHRAgTLSSYELLIGECTAEQAMQQSSASE 114
Cdd:PRK10818    3 RIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDiGLRNLDLIMGCERRV-VYDFVNVIQGDATLNQALIKDKRTE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 115 NLWCIPATidlagaeielvsmvrrEYRLHDALSSTFIE-------EAGFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQC 187
Cdd:PRK10818   82 NLYILPAS----------------QTRDKDALTREGVAkvlddlkAMDFEFIVCDSPAGIETGALMALYFADEAIITTNP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 188 EYYALEGVGQLL-----------NNIVMIRQHLnanlhisaiLLTMYD-ARTKLAEQVSEEVRGHFGDVVLRTKIPRSVK 255
Cdd:PRK10818  146 EVSSVRDSDRILgilasksrraeNGEEPIKEHL---------LLTRYNpGRVSRGDMLSMEDVLEILRIKLVGVIPEDQS 216

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1519253200 256 VSEAPGYGQTVLaYDPGSRGAMAYVDAAREL 286
Cdd:PRK10818  217 VLRASNQGEPVI-LDIEADAGKAYADTVDRL 246
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 25-291 3.80e-15

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: 75.15  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  25 RGAALTKPERTRRITVANQKGGVGKTTSSVNLAAGLAQN-GLKVLVVDLDPQ-GNASTALGAEHRAGTlssYELL----- 97
Cdd:COG4963    92 RLLDPGAARRGRVIAVVGAKGGVGATTLAVNLAWALAREsGRRVLLVDLDLQfGDVALYLDLEPRRGL---ADALrnpdr 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  98 IGECTAEQAMQQssASENLWCIPATIDLAGAEI-------ELVSMVRREyrlhdalsstfieeagFDFIFIDCPPSLGLL 170
Cdd:COG4963   169 LDETLLDRALTR--HSSGLSVLAAPADLERAEEvspeaveRLLDLLRRH----------------FDYVVVDLPRGLNPW 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 171 TINAMTAVNEVLIPIQCEYYALEGVGQLLNNIVMIRqHLNANLHisaILLTMYDARTKLAeqvSEEVRGHFGDVVLRTkI 250
Cdd:COG4963   231 TLAALEAADEVVLVTEPDLPSLRNAKRLLDLLRELG-LPDDKVR---LVLNRVPKRGEIS---AKDIEEALGLPVAAV-L 302

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1519253200 251 PRSVK-VSEAPGYGQTVLAYDPGSRGAMAYVDAARELSKRGD 291
Cdd:COG4963   303 PNDPKaVAEAANQGRPLAEVAPKSPLAKAIRKLAARLTGRPA 344
PHA02519 PHA02519
plasmid partition protein SopA; Reviewed
 38-264 6.45e-15

plasmid partition protein SopA; Reviewed


Pssm-ID: 107201 [Multi-domain]  Cd Length: 387  Bit Score: 74.66  E-value: 6.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  38 ITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVD-LDPQGNASTALGAE-----HRAGTLSSYELliGECTAEQAMQQSS 111
Cdd:PHA02519  109 LAVMSHKGGVYKTSSAVHTAQWLALQGHRVLLIEgNDPQGTASMYHGYVpdlhiHADDTLLPFYL--GERDNAEYAIKPT 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 112 ASENLWCIPATIDLAGAEIELvsmvrreYRLHDA---------LSSTFIEEA--GFDFIFIDCPPSLGLLTINAMTAVNE 180
Cdd:PHA02519  187 CWPGLDIIPSCLALHRIETDL-------MQYHDAgklphpphlMLRAAIESVwdNYDIIVIDSAPNLGTGTINVVCAADV 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 181 VLIPIQCEYYALEGVGQLLNNI--VMIRQHLNANLHISAILLTMYDARTKLAEQ-VSEEVRGHFGDVVLRtkipRSVKVS 257
Cdd:PHA02519  260 IVVATPAELFDYVSVLQFFTMLldLLATVDLGGFEPVVRLLLTKYSLTVGNQSRwMEEQIRNTWGSMVLR----QVVRVT 335


                  ....*..
gi 1519253200 258 EAPGYGQ 264
Cdd:PHA02519  336 DEVGKGQ 342
minD CHL00175
septum-site determining protein; Validated
 35-183 9.62e-15

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 73.27  E-value: 9.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  35 TRRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLD-PQGNASTALGAEHRAgTLSSYELLIGECTAEQAMQQSSAS 113
Cdd:CHL00175   15 SRIIVITSGKGGVGKTTTTANLGMSIARLGYRVALIDADiGLRNLDLLLGLENRV-LYTAMDVLEGECRLDQALIRDKRW 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519253200 114 ENLWCIPAtidlagaeielvSMVRREY-----RLHDALSStfIEEAGFDFIFIDCPPSLGLLTINAMTAVNEVLI 183
Cdd:CHL00175   94 KNLSLLAI------------SKNRQRYnvtrkNMNMLVDS--LKNRGYDYILIDCPAGIDVGFINAIAPAQEAIV 154
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 36-286 5.11e-14

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: 70.83  E-value: 5.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  36 RRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDpQG--NASTALGAEHRAgTLSSYELLIGECTAEQAMQQSSAS 113
Cdd:TIGR01968   2 RVIVITSGKGGVGKTTTTANLGTALARLGKKVVLIDAD-IGlrNLDLLLGLENRI-VYTLVDVVEGECRLQQALIKDKRL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 114 ENLWCIPAtidlagAEIELVSMVRREYRLhdALSSTFIEEagFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYYALE 193
Cdd:TIGR01968  80 KNLYLLPA------SQTRDKDAVTPEQMK--KLVNELKEE--FDYVIIDCPAGIESGFRNAVAPADEAIVVTTPEVSAVR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 194 G----VGQLLNNivMIRQHlnaNLHISAILLTMydarTKLAEQVS-EEVRGHFGdVVLRTKIPRSVKVSEAPGYGQTVlA 268
Cdd:TIGR01968 150 DadrvIGLLEAK--GIEKI---HLIVNRLRPEM----VKKGDMLSvDDVLEILS-IPLIGVIPEDEAIIVSTNKGEPV-V 218

                         250
                  ....*....|....*...
gi 1519253200 269 YDPGSRGAMAYVDAAREL 286
Cdd:TIGR01968 219 LNDKSRAGKAFENIARRI 236
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 36-183 1.29e-13

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: 69.14  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  36 RRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLD-PQGNASTALGAEHRAgTLSSYelLIGECTAEQAMQQSsaSE 114
Cdd:cd02038     1 RIIAVTSGKGGVGKTNVSANLALALSKLGKRVLLLDADlGLANLDILLGLAPKK-TLGDV--LKGRVSLEDIIVEG--PE 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519253200 115 NLWCIPATIDLAGAeIELVSMVRReyRLHDALSSTFIEeagFDFIFIDCPPSLGLLTINAMTAVNEVLI 183
Cdd:cd02038    76 GLDIIPGGSGMEEL-ANLDPEQKA--KLIEELSSLESN---YDYLLIDTGAGISRNVLDFLLAADEVIV 138
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 44-298 1.15e-12

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: 67.01  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  44 KGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALGAEHRAGTLSsyELLIGECTAEQAMQQS---SASENLWCI- 119
Cdd:cd02117     8 KGGIGKSTTASNLSAALAEGGKKVLHVGCDPKHDSTLLLTGGKVPPTID--EMLTEDGTAEELRREDllfSGFNGVDCVe 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 120 ----PATIDLAGAEIELVSMVRREYRLHDalsstfieeAGFDFIFIDCppsLGLLTINAMTA------VNEVLIPIQCEY 189
Cdd:cd02117    86 aggpEPGVGCGGRGIGTMLELLEEHGLLD---------DDYDVVIFDV---LGDVVCGGFAAplrrgfAQKVVIVVSEEL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 190 YALEGVgqllNNIV-MIRQHLNANLHISAILLTMYD-ARTKLAEQVSEEVrghfgdvvlRTKI----PRSVKVSEAPGYG 263
Cdd:cd02117   154 MSLYAA----NNIVkAVENYSKNGVRLAGLVANLRDpAGTEEIQAFAAAV---------GTKIlaviPRDPAVRRAELAR 220

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1519253200 264 QTVLAYDPGSRGAMAYVDAARELSKRGDFLPGQHS 298
Cdd:cd02117   221 VTVFEHDPVSPAASEFARLAAKIADAVPPVPGPRP 255
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 37-276 3.35e-12

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: 65.44  E-value: 3.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  37 RITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALGA--EHRAGtLSSYeLLIGECTAEqAMQQSSASE 114
Cdd:TIGR03371   3 VIAIVSVRGGVGKTTLTANLASALKLLGEPVLAIDLDPQNLLRLHFGMdwSVRDG-WARA-LLNGADWAA-AAYRSPDGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 115 NLwcIP-ATIDLAGAEIELVSMVRREYRLhdaLSStfIEEAGFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEyyale 193
Cdd:TIGR03371  80 LF--LPyGDLSADEREAYQAHDAGWLARL---LQQ--LDLAARDWVLIDLPRGPSPITRQALAAADLVLVVVNAD----- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 194 gvgqlLNNIVMIRQHLNANLHISA------ILLTMYDARTKLAEQVSEEVRGHFGDVVLRTKIPRSVKVSEAPGYGQTVL 267
Cdd:TIGR03371 148 -----AACYATLHQLALALFAGSGprdgprFLINQFDPARQLSRDVRAVLRQTLGSRLLPFVIHRDEAVSEALARGTPVL 222


                  ....*....
gi 1519253200 268 AYDPGSRGA 276
Cdd:TIGR03371 223 NYAPHSQAA 231
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 44-182 1.15e-10

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: 60.98  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  44 KGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALG--------------------------AEHRA---GTLSSY 94
Cdd:cd02035     8 KGGVGKTTIAAATAVRLAEQGKRVLLVSTDPAHSLSDAFGqklggetpvkgapnlwameidpeealEEYWEevkELLAQY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  95 ELLIGEctaEQAMQQSSASenlwcipatidLAGAEiELVSMvrreyrlhDALSStFIEEAGFDFIFIDCPP---SLGLLT 171
Cdd:cd02035    88 LRLPGL---DEVYAEELLS-----------LPGMD-EAAAF--------DELRE-YVESGEYDVIVFDTAPtghTLRLLS 143

                         170
                  ....*....|.
gi 1519253200 172 InAMTAVNEVL 182
Cdd:cd02035   144 L-PLEQVRELL 153
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 44-170 2.14e-10

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: 60.44  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  44 KGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALGAEhragtlssyelLIGECTAeqamqqssASENLWCIpaTI 123
Cdd:pfam02374   9 KGGVGKTTVSAATAVQLSELGKKVLLISTDPAHSLSDSFNQK-----------FGHEPTK--------VKENLSAM--EI 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519253200 124 DLAGAEIELVSMVRREYR-----------LHDALSST--------------FIEEAGFDFIFIDCPP---SLGLL 170
Cdd:pfam02374  68 DPNMELEEYWQEVQKYMNallglrmlegiLAEELASLpgideaasfdefkkYMDEGEYDVVVFDTAPtghTLRLL 142
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 35-73 1.00e-09

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: 57.85  E-value: 1.00e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1519253200  35 TRRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLD 73
Cdd:pfam10609   3 KHVIAVASGKGGVGKSTVAVNLALALARLGYKVGLLDAD 41
MipZ pfam09140
ATPase MipZ; MipZ is an ATPase that forms a complex with the chromosome partitioning protein ...
 36-185 1.12e-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: 58.23  E-value: 1.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  36 RRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQgNASTALGAEHRAGTL--SSYELLIGECTAEQAMQQSSAS 113
Cdd:pfam09140   1 HVIVVGNEKGGSGKSTTAVHVAVALLYKGARVAAIDLDLR-QRTFHRYFENRSATAdrTGLSLPTPEHLNLPDNDVAEVP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519253200 114 EnlwciPATIDLAGAEiELVSMVrreyrlhdalsstfieEAGFDFIFIDCPPSLGLLTINAMTAVNEVLIPI 185
Cdd:pfam09140  80 D-----GENIDDARLE-EAFADL----------------EARCDFIVIDTPGSDSPLSRLAHSRADTLVTPL 129
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 36-73 1.64e-09

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: 56.74  E-value: 1.64e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1519253200  36 RRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLD 73
Cdd:cd02037     1 HIIAVLSGKGGVGKSTVAVNLALALAKKGYKVGLLDAD 38
PRK13230 PRK13230
nitrogenase reductase-like protein; Reviewed
 44-288 1.74e-08

nitrogenase reductase-like protein; Reviewed


Pssm-ID: 183903  Cd Length: 279  Bit Score: 54.78  E-value: 1.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  44 KGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALGAEHRAGTLSSYElligectaEQAMQQSSASE-------NL 116
Cdd:PRK13230    9 KGGIGKSTTVCNIAAALAESGKKVLVVGCDPKADCTRNLVGEKIPTVLDVLR--------EKGIDNLGLEDiiyegfnGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 117 WCIPA-----TIDLAG-AEIELVSMVRReyrlhdalsSTFIEEAGFDFIFIDCppsLGLLTINA------MTAVNEVLIP 184
Cdd:PRK13230   81 YCVESggpepGYGCAGrGVITAIDLLKK---------LGVFEELGPDVVIYDI---LGDVVCGGfamplqKGLADDVYIV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 185 IQCEYYALEGVgqllNNIVM-IRQHlnANLHISAILLTMYDARTKL-AEQVSEEVRGHFGDVVLrTKIPRSVKVSEAPGY 262
Cdd:PRK13230  149 TTCDPMAIYAA----NNICKgIKRF--AKRGKSALGGIIYNGRSVIdAPDIVEEFAKKIGTNVI-GKIPMSNIITEAEIY 221

                         250       260
                  ....*....|....*....|....*.
gi 1519253200 263 GQTVLAYDPGSRGAMAYvdaaRELSK 288
Cdd:PRK13230  222 GKTVIEYAPDSEISNIF----RELAE 243
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 44-91 1.75e-08

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 54.40  E-value: 1.75e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1519253200  44 KGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALGAEHRAGTL 91
Cdd:COG3640     8 KGGVGKTTLSALLARYLAEKGKPVLAVDADPNANLAEALGLEVEADLI 55
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 36-73 2.04e-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: 51.66  E-value: 2.04e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1519253200  36 RRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLD 73
Cdd:cd01983     1 RVIAVTGGKGGVGKTTLAAALAVALAAKGYKVLLIDLD 38
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 36-284 2.91e-08

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: 53.44  E-value: 2.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  36 RRITVANQKGGVGKTTSSVNLAAGLAQ-NGLKVLVVDLD-PQGNASTALGAEHRAGTLSSYELL--IGECTAEQAMQQSS 111
Cdd:cd03111     1 RVVAVVGAKGGVGASTLAVNLAQELAQrAKDKVLLIDLDlPFGDLGLYLNLRPDYDLADVIQNLdrLDRTLLDSAVTRHS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 112 ASENLWCIPATI-DLAGAEIELVSmvrreyRLHDALSSTfieeagFDFIFIDCPPSLGLLTINAMTAVNEVLIPIQCEYY 190
Cdd:cd03111    81 SGLSLLPAPQELeDLEALGAEQVD------KLLQVLRAF------YDHIIVDLGHFLDEVTLAVLEAADEILLVTQQDLP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 191 ALEGVGQLLNnivMIRQHLNANLHISaILLTMYDARTKL-AEQVSEEVRGHFGDVvlrtkIP-RSVKVSEAPGYGQTVLA 268
Cdd:cd03111   149 SLRNARRLLD---SLRELEGSSDRLR-LVLNRYDKKSEIsPKDIEEALGLEVFAT-----LPnDYKAVSESANTGRPLVE 219

                         250
                  ....*....|....*.
gi 1519253200 269 YDPGSRGAMAYVDAAR 284
Cdd:cd03111   220 VAPRSALVRALQDLAA 235
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 36-171 1.43e-07

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: 51.28  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  36 RRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGnaSTALGA----EHRAGtLSsyELLIGECTAEQAMQQSS 111
Cdd:TIGR01007  18 KVLLITSVKPGEGKSTTSANIAIAFAQAGYKTLLIDGDMRN--SVMSGTfksqNKITG-LT--NFLSGTTDLSDAICDTN 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519253200 112 AsENLWCIPA-TIDLAGAEIelvsmvrreyrLHDALSSTFIEEAG--FDFIFIDCPPsLGLLT 171
Cdd:TIGR01007  93 I-ENLDVITAgPVPPNPTEL-----------LQSSNFKTLIETLRkrFDYIIIDTPP-IGTVT 142
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
44-186 4.82e-07

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 50.59  E-value: 4.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  44 KGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALG-------AEHRAGTLSSYELligecTAEQAMQQ------- 109
Cdd:COG0003    11 KGGVGKTTVAAATALALAERGKRTLLVSTDPAHSLGDVLGtelgnepTEVAVPNLYALEI-----DPEAELEEywervra 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 110 -------SSASENLwcipATIdLAGAEiELVSMvrreYRLHDalsstFIEEAGFDFIFIDCPPS---LGLLTI-NAMTAV 178
Cdd:COG0003    86 plrgllpSAGVDEL----AES-LPGTE-ELAAL----DELLE-----LLEEGEYDVIVVDTAPTghtLRLLSLpELLGWW 150


                  ....*...
gi 1519253200 179 NEVLIPIQ 186
Cdd:COG0003   151 LDRLLKLR 158
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
38-86 9.70e-07

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 49.66  E-value: 9.70e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1519253200  38 ITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQG-NASTALGAEH 86
Cdd:PRK11670  110 IAVSSGKGGVGKSSTAVNLALALAAEGAKVGILDADIYGpSIPTMLGAED 159
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 38-104 4.72e-06

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: 46.92  E-value: 4.72e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519253200  38 ITVANqKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALGAEHRAGTLSSYELLIGECTAE 104
Cdd:cd02034     3 IAVAG-KGGVGKTTIAALLIRYLAKKGGKVLAVDADPNSNLAETLGVEVEKLPLIKTIGDIRERTGA 68
NifH cd02040
nitrogenase component II NifH; NifH gene encodes component II (iron protein) of nitrogenase. ...
 44-82 7.75e-06

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: 46.74  E-value: 7.75e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1519253200  44 KGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNaSTAL 82
Cdd:cd02040     8 KGGIGKSTTASNLSAALAEMGKKVLHVGCDPKAD-STRL 45
PRK11519 PRK11519
tyrosine-protein kinase Wzc;
46-167 1.26e-05

tyrosine-protein kinase Wzc;


Pssm-ID: 183173 [Multi-domain]  Cd Length: 719  Bit Score: 46.68  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  46 GVGKTTSSVNLAAGLAQNGLKVLVVDLD-PQGNASTALGAEHRAGtLSsyELLIGECTAEQAMQQSSAsENLWCIPATid 124
Cdd:PRK11519  537 SIGKTFVCANLAAVISQTNKRVLLIDCDmRKGYTHELLGTNNVNG-LS--DILIGQGDITTAAKPTSI-ANFDLIPRG-- 610

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1519253200 125 lagaeieLVSMVRREYRLHDALSStFIEEAG--FDFIFIDCPPSL 167
Cdd:PRK11519  611 -------QVPPNPSELLMSERFAE-LVNWASknYDLVLIDTPPIL 647
Fer4_NifH pfam00142
4Fe-4S iron sulfur cluster binding proteins, NifH/frxC family;
44-82 2.40e-05

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


Pssm-ID: 395090  Cd Length: 271  Bit Score: 45.13  E-value: 2.40e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1519253200  44 KGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNaSTAL 82
Cdd:pfam00142   8 KGGIGKSTTSQNLSAALAEMGKKVLVVGCDPKAD-STRL 45
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 44-166 2.92e-05

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: 45.46  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  44 KGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALGAEHRAGTLSSyellIGECTAEQAMQQ---SSASENLwciP 120
Cdd:TIGR04291 329 KGGVGKTTVAAAIAVRLANKGLDVHLTTSDPAAHLSVTLTGSLNNLQVSR----IDPKQETERYRQevlATKGKEL---D 401

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1519253200 121 ATiDLAGAEIELVSMVRREYRLHDALSSTfIEEAGFDFIFIDCPPS 166
Cdd:TIGR04291 402 ED-GKAYLEEDLRSPCTEEIAVFQAFSRI-IREAGDRFVVMDTAPT 445
TadZ-like cd17869
pilus assembly protein TadZ; Pilus assembly protein TadZ is involved in the production of a ...
 35-207 5.07e-05

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: 43.68  E-value: 5.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  35 TRRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALGAEHRAgTLSSYELLIGECTAEQAMQQSS--- 111
Cdd:cd17869     3 TSVITFHSPCGGSGKSTVAAACAYTLAEKGKKTLYLNMERLQSTDVFFGASGRY-LMSDHLYTLKSRKANLADKLEScvk 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200 112 -ASENLWCIPATiDLAGAEIELvsmvrrEYRLHDALSSTFIEEAGFDFIFIDCPPSLGLLTINAMTAVNEVLIPIqceyy 190
Cdd:cd17869    82 qHESGVYYFSPF-KSALDILEI------KKDDILHMITKLVEAHAYDYIIMDLSFEFSSTVCKLLQASHNNVVIA----- 149

                         170
                  ....*....|....*..
gi 1519253200 191 aLEGVGQLLNNIVMIRQ 207
Cdd:cd17869   150 -LQDANSSYKLNKFLRA 165
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 44-77 1.21e-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: 43.54  E-value: 1.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1519253200  44 KGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGN 77
Cdd:TIGR04291  11 KGGVGKTSIACATAINLADQGKRVLLVSTDPASN 44
Bchl-like cd02032
L-subunit of protochlorophyllide reductase; This family of proteins contains BchL and ChlL. ...
 44-75 1.69e-04

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


Pssm-ID: 349752  Cd Length: 267  Bit Score: 42.67  E-value: 1.69e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1519253200  44 KGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQ 75
Cdd:cd02032     8 KGGIGKSTTSSNLSAAFAKRGKKVLQIGCDPK 39
chlL PRK13185
protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional
 44-75 2.05e-04

protochlorophyllide reductase iron-sulfur ATP-binding protein; Provisional


Pssm-ID: 237293  Cd Length: 270  Bit Score: 42.26  E-value: 2.05e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1519253200  44 KGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQ 75
Cdd:PRK13185   10 KGGIGKSTTSSNLSAAFAKLGKKVLQIGCDPK 41
chlL CHL00072
photochlorophyllide reductase subunit L
 44-82 4.25e-04

photochlorophyllide reductase subunit L


Pssm-ID: 177011  Cd Length: 290  Bit Score: 41.26  E-value: 4.25e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1519253200  44 KGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTAL 82
Cdd:CHL00072    8 KGGIGKSTTSCNISIALARRGKKVLQIGCDPKHDSTFTL 46
eps_transp_fam TIGR01005
exopolysaccharide transport protein family; The model describes the exopolysaccharide ...
 35-177 1.45e-03

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: 40.47  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519253200  35 TRRITVANQKGGVGKTTSSVNLAAGLAQNGLKVLVVDLD-PQGNASTALGAEHRAGTLssyELLIGECTAEQAMQQSSas 113
Cdd:TIGR01005 553 NNLIAIAGALPDEGKSFIAANFAALIAAGGKRTLLIDADiRKGGLHQMFGKAPKPGLL---DLLAGEASIEAGIHRDQ-- 627

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519253200 114 enlwcIPATIDLAGAEIELVSMVRREYRLHDALSStFIEEA--GFDFIFIDCPPSLGLLTINAMTA 177
Cdd:TIGR01005 628 -----RPGLAFIAAGGASHFPHNPNELLANPAMAE-LIDNArnAFDLVLVDLAALAAVADAAAFAA 687
CLP1_P pfam16575
mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of ...
 46-77 1.55e-03

mRNA cleavage and polyadenylation factor CLP1 P-loop; CLP1_P is the P-loop carrying domain of Clp1 mRNA cleavage and polyadenylation factor, Clp1, proteins in eukaryotes. Clp1 is essential for 3'-end processing of mRNAs. This region carries the P-loop suggesting it is the region that binds adenine or guanine nucleotide.


Pssm-ID: 406878  Cd Length: 187  Bit Score: 38.78  E-value: 1.55e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1519253200  46 GVGKTTSSVNLAAGLAQNGLKVLVVDLDP-QGN 77
Cdd:pfam16575   4 DSGKSTLCRILLNYAVRKGRKPVYVDLDVgQSE 36
ArsA_halo NF041417
arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical ...
 31-83 1.79e-03

arsenical pump-driving ATPase, halobacterial type; Members of this family of arsenical pump-driving ATPase (ArsA) occur typically in Halobacteria (a branch of the archaea), accompanied by homologs of ArsD and by HcsL and HcsS (halo-CC-Star proteins, long and short), two proteins that both end with Cys-Cys-COOH motifs indicative of interaction with heavy metal atoms.


Pssm-ID: 469308 [Multi-domain]  Cd Length: 617  Bit Score: 39.86  E-value: 1.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1519253200  31 KPERTRRITVANqKGGVGKTTSSVNLAAGLAQNGLKVLVVDLDPQGNASTALG 83
Cdd:NF041417    8 RGEDTEFVFFSG-KGGVGKSTVSCATAQWLARNGYDTLLVTTDPAPNLSDIFG 59
 
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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