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Conserved domains on  [gi|398364553|ref|NP_011424|]
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Fe-S cluster-binding ATPase [Saccharomyces cerevisiae S288C]

Protein Classification

Mrp/NBP35 family ATP-binding protein( domain architecture ID 10566257)

Mrp (multiple resistance and pH adaptation)/NBP35 (nucleotide-binding protein 35) family ATP-binding protein is an iron-sulfur (FeS) cluster protein that functions as a scaffold to assemble nascent FeS clusters for transfer to FeS-requiring enzymes

CATH:  3.40.50.300
Gene Ontology:  GO:0046872|GO:0005524|GO:0051536|GO:0140663|GO:0016226|GO:0016887
PubMed:  8921898

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 70-321 9.97e-136

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: 385.27  E-value: 9.97e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553   70 GIEHKILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGCIKETVHESNSGWTPVYVtDNLATMSI 149
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALAL-ARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  150 QYMLPEDDSAIIWRGSKKNLLIKKFLKDVDWDKLDYLVIDTPPGTSDEHISINKYMresGIDGALVVTTPQEVALLDVRK 229
Cdd:pfam10609  79 GFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL---PLTGAVIVTTPQDVALLDVRK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  230 EIDFCKKAGINILGLVENMSGFVCPNCKGESQIFKatTGGGEALCKELGIKFLGSVPLDPRIGKSCDMGESFLDNYPDSP 309
Cdd:pfam10609 156 AIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFG--KGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSP 233

                         250
                  ....*....|..
gi 398364553  310 ASSAVLNVVEAL 321
Cdd:pfam10609 234 AAKAFLKIADKV 245
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 70-321 9.97e-136

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: 385.27  E-value: 9.97e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553   70 GIEHKILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGCIKETVHESNSGWTPVYVtDNLATMSI 149
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALAL-ARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  150 QYMLPEDDSAIIWRGSKKNLLIKKFLKDVDWDKLDYLVIDTPPGTSDEHISINKYMresGIDGALVVTTPQEVALLDVRK 229
Cdd:pfam10609  79 GFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL---PLTGAVIVTTPQDVALLDVRK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  230 EIDFCKKAGINILGLVENMSGFVCPNCKGESQIFKatTGGGEALCKELGIKFLGSVPLDPRIGKSCDMGESFLDNYPDSP 309
Cdd:pfam10609 156 AIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFG--KGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSP 233

                         250
                  ....*....|..
gi 398364553  310 ASSAVLNVVEAL 321
Cdd:pfam10609 234 AAKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 73-293 4.04e-118

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: 339.09  E-value: 4.04e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  73 HKILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGCIKETVHESNSGWTPVYVtDNLATMSIQYM 152
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALAL-AKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 153 LPEDDsAIIWRGSKKNLLIKKFLKDVDWDKLDYLVIDTPPGTSDEHISINKYMresGIDGALVVTTPQEVALLDVRKEID 232
Cdd:cd02037   79 LPEDD-AVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398364553 233 FCKKAGINILGLVENMSGFVCPNCKGESQIFkaTTGGGEALCKELGIKFLGSVPLDPRIGK 293
Cdd:cd02037  155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
68-319 3.56e-110

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 324.85  E-value: 3.56e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  68 LSGIEHKILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGCIKETVHESNSGWTPVYVTDNLATM 147
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVAL-ARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 148 SIQYMLPEDDSAIIWRGSKKNLLIKKFLKDVDWDKLDYLVIDTPPGTSDEHISInkyMRESGIDGALVVTTPQEVALLDV 227
Cdd:NF041136  80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSV---AQLIPDAGAVIVTTPQELALADV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 228 RKEIDFCKKAGINILGLVENMSGFVCPNCKGESQIFKatTGGGEALCKELGIKFLGSVPLDPRIGKSCDMGESFLDNYPD 307
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234

                        250
                 ....*....|..
gi 398364553 308 SPASSAVLNVVE 319
Cdd:NF041136 235 SPAAKALEKIVD 246
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
70-308 4.57e-58

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 191.41  E-value: 4.57e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  70 GIEHKILVLSGKGGVGKSTFAAMLSWALSAdEDLQVGAMDLDICGPSLPHMLGCIKE-TVHESNSGWTPVyVTDNLATMS 148
Cdd:PRK11670 105 GVKNIIAVSSGKGGVGKSSTAVNLALALAA-EGAKVGILDADIYGPSIPTMLGAEDQrPTSPDGTHMAPI-MAHGLATNS 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 149 IQYMLpEDDSAIIWRGSKKNLLIKKFLKDVDWDKLDYLVIDTPPGTSDEHISINKYMResgIDGALVVTTPQEVALLDVR 228
Cdd:PRK11670 183 IGYLV-TDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDAK 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 229 KEIDFCKKAGINILGLVENMSGFVCPNCKGESQIFKatTGGGEALCKELGIKFLGSVPLDPRIGKSCDMGESFLDNYPDS 308
Cdd:PRK11670 259 KGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFG--TGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPES 336
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 63-255 1.76e-37

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: 135.31  E-value: 1.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  63 LITDNLSGIEHKILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGcIKETVHESN--SGWTPV-- 138
Cdd:COG0489   83 LLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALAL-AQSGKRVLLIDADLRGPSLHRMLG-LENRPGLSDvlAGEASLed 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 139 ----YVTDNLATMSIQyMLPEDDSAIIwrGSKKnllIKKFLKDVDwDKLDYLVIDTPPGTSDEHISI-NKYmresgIDGA 213
Cdd:COG0489  161 viqpTEVEGLDVLPAG-PLPPNPSELL--ASKR---LKQLLEELR-GRYDYVIIDTPPGLGVADATLlASL-----VDGV 228

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 398364553 214 LVVTTPQEVALLDVRKEIDFCKKAGINILGLVENMsgfVCPN 255
Cdd:COG0489  229 LLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 75-322 1.76e-07

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: 51.57  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553   75 ILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGCIKETVH------ESNSGWTPVYVTD----NL 144
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTAL-ARLGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  145 atmsiqYMLPEDDSAiiwrgSKKNLLIKKFLKDVDW--DKLDYLVIDTPPGtsdehisINKYMRE--SGIDGALVVTTPQ 220
Cdd:TIGR01968  83 ------YLLPASQTR-----DKDAVTPEQMKKLVNElkEEFDYVIIDCPAG-------IESGFRNavAPADEAIVVTTPE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  221 EVALLDVRKEIDFCKKAGINILGLVENMsgfVCPNckgesQIFKATTGGGEALCKELGIKFLGSVPLDPRIGKSCDMGES 300
Cdd:TIGR01968 145 VSAVRDADRVIGLLEAKGIEKIHLIVNR---LRPE-----MVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVSTNKGEP 216

                         250       260
                  ....*....|....*....|..
gi 398364553  301 FLDNyPDSPASSAVLNVVEALR 322
Cdd:TIGR01968 217 VVLN-DKSRAGKAFENIARRIL 237
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 70-321 9.97e-136

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: 385.27  E-value: 9.97e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553   70 GIEHKILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGCIKETVHESNSGWTPVYVtDNLATMSI 149
Cdd:pfam10609   1 GVKHVIAVASGKGGVGKSTVAVNLALAL-ARLGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  150 QYMLPEDDSAIIWRGSKKNLLIKKFLKDVDWDKLDYLVIDTPPGTSDEHISINKYMresGIDGALVVTTPQEVALLDVRK 229
Cdd:pfam10609  79 GFLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLL---PLTGAVIVTTPQDVALLDVRK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  230 EIDFCKKAGINILGLVENMSGFVCPNCKGESQIFKatTGGGEALCKELGIKFLGSVPLDPRIGKSCDMGESFLDNYPDSP 309
Cdd:pfam10609 156 AIDMFKKVNVPVLGVVENMSYFVCPHCGEETYIFG--KGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSP 233

                         250
                  ....*....|..
gi 398364553  310 ASSAVLNVVEAL 321
Cdd:pfam10609 234 AAKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 73-293 4.04e-118

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: 339.09  E-value: 4.04e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  73 HKILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGCIKETVHESNSGWTPVYVtDNLATMSIQYM 152
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALAL-AKKGYKVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 153 LPEDDsAIIWRGSKKNLLIKKFLKDVDWDKLDYLVIDTPPGTSDEHISINKYMresGIDGALVVTTPQEVALLDVRKEID 232
Cdd:cd02037   79 LPEDD-AVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398364553 233 FCKKAGINILGLVENMSGFVCPNCKGESQIFkaTTGGGEALCKELGIKFLGSVPLDPRIGK 293
Cdd:cd02037  155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
68-319 3.56e-110

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 324.85  E-value: 3.56e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  68 LSGIEHKILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGCIKETVHESNSGWTPVYVTDNLATM 147
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVAL-ARRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 148 SIQYMLPEDDSAIIWRGSKKNLLIKKFLKDVDWDKLDYLVIDTPPGTSDEHISInkyMRESGIDGALVVTTPQEVALLDV 227
Cdd:NF041136  80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSV---AQLIPDAGAVIVTTPQELALADV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 228 RKEIDFCKKAGINILGLVENMSGFVCPNCKGESQIFKatTGGGEALCKELGIKFLGSVPLDPRIGKSCDMGESFLDNYPD 307
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234

                        250
                 ....*....|..
gi 398364553 308 SPASSAVLNVVE 319
Cdd:NF041136 235 SPAAKALEKIVD 246
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
70-308 4.57e-58

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 191.41  E-value: 4.57e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  70 GIEHKILVLSGKGGVGKSTFAAMLSWALSAdEDLQVGAMDLDICGPSLPHMLGCIKE-TVHESNSGWTPVyVTDNLATMS 148
Cdd:PRK11670 105 GVKNIIAVSSGKGGVGKSSTAVNLALALAA-EGAKVGILDADIYGPSIPTMLGAEDQrPTSPDGTHMAPI-MAHGLATNS 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 149 IQYMLpEDDSAIIWRGSKKNLLIKKFLKDVDWDKLDYLVIDTPPGTSDEHISINKYMResgIDGALVVTTPQEVALLDVR 228
Cdd:PRK11670 183 IGYLV-TDDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDAK 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 229 KEIDFCKKAGINILGLVENMSGFVCPNCKGESQIFKatTGGGEALCKELGIKFLGSVPLDPRIGKSCDMGESFLDNYPDS 308
Cdd:PRK11670 259 KGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIFG--TGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPES 336
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 63-255 1.76e-37

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: 135.31  E-value: 1.76e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  63 LITDNLSGIEHKILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGcIKETVHESN--SGWTPV-- 138
Cdd:COG0489   83 LLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALAL-AQSGKRVLLIDADLRGPSLHRMLG-LENRPGLSDvlAGEASLed 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 139 ----YVTDNLATMSIQyMLPEDDSAIIwrGSKKnllIKKFLKDVDwDKLDYLVIDTPPGTSDEHISI-NKYmresgIDGA 213
Cdd:COG0489  161 viqpTEVEGLDVLPAG-PLPPNPSELL--ASKR---LKQLLEELR-GRYDYVIIDTPPGLGVADATLlASL-----VDGV 228

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 398364553 214 LVVTTPQEVALLDVRKEIDFCKKAGINILGLVENMsgfVCPN 255
Cdd:COG0489  229 LLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 75-311 9.66e-19

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: 83.39  E-value: 9.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  75 ILVLSGKGGVGKSTFAAMLSWALSaDEDLQVGAMDLDICGPSLPHMLGCI-KETVH-----ESNSGWTPVYVTDNLatms 148
Cdd:cd02038    3 IAVTSGKGGVGKTNVSANLALALS-KLGKRVLLLDADLGLANLDILLGLApKKTLGdvlkgRVSLEDIIVEGPEGL---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 149 iqYMLPED---DSAIIWRGSKKNLLIKKFLKDVDwdKLDYLVIDTPPGTSDEHISINkymreSGIDGALVVTTPQEVALL 225
Cdd:cd02038   78 --DIIPGGsgmEELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISRNVLDFL-----LAADEVIVVTTPEPTSIT 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 226 DVRKEIDFCKKAGINI-LGLVENMSgfvcpnckgesqifkATTGGGEALCKEL----------GIKFLGSVPLDPRIGKS 294
Cdd:cd02038  149 DAYALIKVLSRRGGKKnFRLIVNMA---------------RSPKEGRATFERLkkvakrfldiNLDFVGFIPYDQSVRRA 213

                        250
                 ....*....|....*..
gi 398364553 295 CDMGESFLDNYPDSPAS 311
Cdd:cd02038  214 VRSQKPFVLLFPNSKAS 230
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 88-324 1.12e-18

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: 83.40  E-value: 1.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  88 TFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGC---------------IKETVHESNSGwtpVYVtdnlatmsiqym 152
Cdd:COG0455    1 TVAVNLAAAL-ARLGKRVLLVDADLGLANLDVLLGLepkatladvlageadLEDAIVQGPGG---LDV------------ 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 153 LP-EDDSAIIWRGSKKNLLIKKFlKDVDwDKLDYLVIDTPPGTSDEHISInkyMRESgiDGALVVTTPQEVALLDVRKEI 231
Cdd:COG0455   65 LPgGSGPAELAELDPEERLIRVL-EELE-RFYDVVLVDTGAGISDSVLLF---LAAA--DEVVVVTTPEPTSITDAYALL 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 232 DFCKKA-GINILGLVENMsgfvCPNCKGESQIFKATTgggEALCKELGIK--FLGSVPLDPRIGKSCDMGESFLDNYPDS 308
Cdd:COG0455  138 KLLRRRlGVRRAGVVVNR----VRSEAEARDVFERLE---QVAERFLGVRlrVLGVIPEDPAVREAVRRGRPLVLAAPDS 210

                        250
                 ....*....|....*.
gi 398364553 309 PASSAVLNVVEALRDA 324
Cdd:COG0455  211 PAARAIRELAARLAGW 226
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 75-321 1.13e-16

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: 79.77  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  75 ILVLSGKGGVGKSTFAAMLSWALSADEDLQVGAMDLDICGPSLPHMLGC--------------------IKETVHESNSG 134
Cdd:COG4963  105 IAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFGDVALYLDLeprrgladalrnpdrldetlLDRALTRHSSG 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 135 wtpVYVTDNLATMSIQYMLPEDD-SAIIwrgskkNLLIKKFlkdvdwdklDYLVIDTPPGTSDEHISInkyMRESgiDGA 213
Cdd:COG4963  185 ---LSVLAAPADLERAEEVSPEAvERLL------DLLRRHF---------DYVVVDLPRGLNPWTLAA---LEAA--DEV 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 214 LVVTTPQEVALLDVRKEIDFCKKAGINI--LGLVENMSGfvcpnckgesqifKATTGGGEALCKELGIKFLGSVPLDPR- 290
Cdd:COG4963  242 VLVTEPDLPSLRNAKRLLDLLRELGLPDdkVRLVLNRVP-------------KRGEISAKDIEEALGLPVAAVLPNDPKa 308

                        250       260       270
                 ....*....|....*....|....*....|.
gi 398364553 291 IGKSCDMGESFLDNYPDSPASSAVLNVVEAL 321
Cdd:COG4963  309 VAEAANQGRPLAEVAPKSPLAKAIRKLAARL 339
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 75-321 2.07e-16

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: 77.24  E-value: 2.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  75 ILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGCiketvhESNSGWTPVYVTDNLATMSiQ---- 150
Cdd:cd02036    3 IVITSGKGGVGKTTTTANLGVAL-AKLGKKVLLIDADIGLRNLDLILGL------ENRIVYTLVDVLEGECRLE-Qalik 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 151 -------YMLPeddSAIIWrgSKKNLLIKKFLKDVDW--DKLDYLVIDTPPGT-SDEHISInkymreSGIDGALVVTTPQ 220
Cdd:cd02036   75 dkrwenlYLLP---ASQTR--DKDALTPEKLEELVKElkDSFDFILIDSPAGIeSGFINAI------APADEAIIVTNPE 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 221 EVALLDVRKEIDFCKKAGINILGLVENmsgfvcpnckgesQIFKATTGGGEALCKE-----LGIKFLGSVPLDPRIGKSC 295
Cdd:cd02036  144 ISSVRDADRVIGLLESKGIVNIGLIVN-------------RYRPEMVKSGDMLSVEdiqeiLGIPLLGVIPEDPEVIVAT 210

                        250       260
                 ....*....|....*....|....*.
gi 398364553 296 DMGESFLDNYPDSPASSAVLNVVEAL 321
Cdd:cd02036  211 NRGEPLVLYKPNSLAAKAFENIARRL 236
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 75-294 2.29e-16

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: 77.00  E-value: 2.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553   75 ILVLSGKGGVGKSTFAAMLSWALSADEdLQVGAMDLDICGPSLPHM--LGCIKETVHESNSGWT------PVYVTDNLAT 146
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRG-LRVLLIDLDPQSNNSSVEglEGDIAPALQALAEGLKgrvnldPILLKEKSDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  147 MSIQYM---LPEDDSAIIWRGSKKNLLIKKFLKDVDwDKLDYLVIDTPPGTSDEHISinkymRESGIDGALVVTTPQEVA 223
Cdd:pfam01656  80 GGLDLIpgnIDLEKFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGELLRN-----ALIAADYVIIPLEPEVIL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398364553  224 LLDVRKEIDFCKKAGINILGLVENMSGFVcPNCKGESQIFKATTgggEALCKEL-GIKFLGSVPLDPRIGKS 294
Cdd:pfam01656 154 VEDAKRLGGVIAALVGGYALLGLKIIGVV-LNKVDGDNHGKLLK---EALEELLrGLPVLGVIPRDEAVAEA 221
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 74-321 7.96e-14

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 70.20  E-value: 7.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  74 KILVlSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDIcGPSLPHMLGciketVHESNSGWTPV-----YVTDNLATMS 148
Cdd:COG3640    2 KIAV-AGKGGVGKTTLSALLARYL-AEKGKPVLAVDADP-NANLAEALG-----LEVEADLIKPLgemreLIKERTGAPG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 149 IQY--------MLPEDdsAIIWRGSKK------------------NLLIKKFLKDVDWDKLDYLVIDTPPGTsdEHISin 202
Cdd:COG3640   74 GGMfklnpkvdDIPEE--YLVEGDGVDllvmgtieeggsgcycpeNALLRALLNHLVLGNYEYVVVDMEAGI--EHLG-- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 203 kymR--ESGIDGALVVTTPQEVALLDVRKEIDFCKKAGINILGLVENmsgfvcpnckgesqifKATTGGGEA-LCKELGI 279
Cdd:COG3640  148 ---RgtAEGVDLLLVVSEPSRRSIETARRIKELAEELGIKKIYLVGN----------------KVREEEDEEfLRELLGL 208

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 398364553 280 KFLGSVPLDPRIGKScDMGESFLDNYPDSPASSAVLNVVEAL 321
Cdd:COG3640  209 ELLGFIPYDEEVREA-DLEGKPLLDLPDSPAVAAVEEIAEKL 249
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 75-321 5.63e-12

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: 64.88  E-value: 5.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  75 ILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGpSLPHMLGCIKETVHES-------NSGWTPVYVTDNLATM 147
Cdd:COG1192    4 IAVANQKGGVGKTTTAVNLAAAL-ARRGKRVLLIDLDPQG-NLTSGLGLDPDDLDPTlydllldDAPLEDAIVPTEIPGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 148 SIqymLPEDDS-----AIIWRGSKKNLLIKKFLKDVDwDKLDYLVIDTPPgtsdehiSINKYMReSGI---DGALVVTTP 219
Cdd:COG1192   82 DL---IPANIDlagaeIELVSRPGRELRLKRALAPLA-DDYDYILIDCPP-------SLGLLTL-NALaaaDSVLIPVQP 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 220 QEVAL----------LDVRKEIDfckkAGINILGLVENMsgfvcpnCKGESQIFKATTgggEALCKELGIKFLGS-VPLD 288
Cdd:COG1192  150 EYLSLeglaqlletiEEVREDLN----PKLEILGILLTM-------VDPRTRLSREVL---EELREEFGDKVLDTvIPRS 215

                        250       260       270
                 ....*....|....*....|....*....|...
gi 398364553 289 PRIGKSCDMGESFLDNYPDSPASSAVLNVVEAL 321
Cdd:COG1192  216 VALAEAPSAGKPVFEYDPKSKGAKAYRALAEEL 248
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 74-321 6.26e-11

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: 61.56  E-value: 6.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  74 KILVlSGKGGVGKSTFAAMLSWALS----------ADEDLQVG-AMDLDICGPSLPHMLGCIKETVHESNSGWTPVYVTD 142
Cdd:cd02034    2 KIAV-AGKGGVGKTTIAALLIRYLAkkggkvlavdADPNSNLAeTLGVEVEKLPLIKTIGDIRERTGAKKGEPPEGMSLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 143 NLATMSIQYMLPEDDS------AIIWRGSKK-----NLLIKKFLKDVDWDKLDYLVIDTPPGTsdEHISinkymR--ESG 209
Cdd:cd02034   81 PYVDDIIKEIIVEPDGidllvmGRPEGGGSGcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLS-----RgtIRA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 210 IDGALVVTTPQEVALLDVRKEIDFCKKAGINILGLVENmsgfvcpnckgesqifKATTGGGEALCKELGIKF--LGSVPL 287
Cdd:cd02034  154 VDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVN----------------KVRNEEEQELIEELLIKLklIGVIPY 217

                        250       260       270
                 ....*....|....*....|....*....|....
gi 398364553 288 DPRIGKSCDMGESFLDNypDSPASSAVLNVVEAL 321
Cdd:cd02034  218 DEEIMEADLKGKPLFDL--DSAAVKAIEKIVEKL 249
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 75-314 2.14e-10

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: 59.98  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  75 ILVLSGKGGVGKSTFAAMLSWALSADEDLQVGAMDLDICGPSLPHMLGCIKEtvhesnsgWTPVYVTDNLATMSIQYMlp 154
Cdd:cd03111    3 VAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPD--------YDLADVIQNLDRLDRTLL-- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 155 edDSAIIWRGSKKNLL-IKKFLKDV------DWDKL--------DYLVIDTPPGtsDEHISInKYMRESgiDGALVVTTP 219
Cdd:cd03111   73 --DSAVTRHSSGLSLLpAPQELEDLealgaeQVDKLlqvlrafyDHIIVDLGHF--LDEVTL-AVLEAA--DEILLVTQQ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 220 QEVALLDVRKEIDFCKKAGINI--LGLVENmsgfvcpnckgesqifKATTGGG---EALCKELGIKFLGSVPLDPR-IGK 293
Cdd:cd03111  146 DLPSLRNARRLLDSLRELEGSSdrLRLVLN----------------RYDKKSEispKDIEEALGLEVFATLPNDYKaVSE 209

                        250       260
                 ....*....|....*....|.
gi 398364553 294 SCDMGESFLDNYPDSPASSAV 314
Cdd:cd03111  210 SANTGRPLVEVAPRSALVRAL 230
PRK10818 PRK10818
septum site-determining protein MinD;
75-321 6.66e-08

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 53.02  E-value: 6.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  75 ILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGCIKETVHES----------NSGWTPVYVTDNL 144
Cdd:PRK10818   5 IVVTSGKGGVGKTTSSAAIATGL-AQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFvnviqgdatlNQALIKDKRTENL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 145 atmsiqYMLP----EDDSAIIWRGskknllIKKFLKDVDWDKLDYLVIDTPPGtsdehISINKYMRESGIDGALVVTTPQ 220
Cdd:PRK10818  84 ------YILPasqtRDKDALTREG------VAKVLDDLKAMDFEFIVCDSPAG-----IETGALMALYFADEAIITTNPE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 221 EVALLDVRKeidfckkaginILGLVENMSGFVcpnCKGESQIFK---------ATTGGGEALCKE-----LGIKFLGSVP 286
Cdd:PRK10818 147 VSSVRDSDR-----------ILGILASKSRRA---ENGEEPIKEhllltrynpGRVSRGDMLSMEdvleiLRIKLVGVIP 212

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 398364553 287 LDPRIGKSCDMGES-FLDNypDSPASSAVLNVVEAL 321
Cdd:PRK10818 213 EDQSVLRASNQGEPvILDI--EADAGKAYADTVDRL 246
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 75-322 1.76e-07

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: 51.57  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553   75 ILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGCIKETVH------ESNSGWTPVYVTD----NL 144
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTAL-ARLGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  145 atmsiqYMLPEDDSAiiwrgSKKNLLIKKFLKDVDW--DKLDYLVIDTPPGtsdehisINKYMRE--SGIDGALVVTTPQ 220
Cdd:TIGR01968  83 ------YLLPASQTR-----DKDAVTPEQMKKLVNElkEEFDYVIIDCPAG-------IESGFRNavAPADEAIVVTTPE 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  221 EVALLDVRKEIDFCKKAGINILGLVENMsgfVCPNckgesQIFKATTGGGEALCKELGIKFLGSVPLDPRIGKSCDMGES 300
Cdd:TIGR01968 145 VSAVRDADRVIGLLEAKGIEKIHLIVNR---LRPE-----MVKKGDMLSVDDVLEILSIPLIGVIPEDEAIIVSTNKGEP 216

                         250       260
                  ....*....|....*....|..
gi 398364553  301 FLDNyPDSPASSAVLNVVEALR 322
Cdd:TIGR01968 217 VVLN-DKSRAGKAFENIARRIL 237
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 74-286 1.92e-07

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


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 51.23  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  74 KILVLSGKGGVGKSTFAAMLSWALSadedlQVGAMDLDICGPSLPHMLGCIKETVHESNSGWTPVYVTDNLA-------- 145
Cdd:cd03110    1 IIAVLSGKGGTGKTTITANLAVLLY-----NVILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEKCIrcgncerv 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 146 ------------TMSIQYM-----------------LPEDDSAIIWRGSKKN--------------------LLIKKFLK 176
Cdd:cd03110   76 ckfgaileffqkLIVDESLcegcgacviicprgaiyLKDRDTGKIFISSSDGgplvhgrlnigeensgklvtELRKKALE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 177 DVDwdKLDYLVIDTPPGTsdeHISINKYMResGIDGALVVTTPQEVALLDVRKEIDFCKKAGINiLGLVENMSGfvcpnc 256
Cdd:cd03110  156 RSK--ECDLAIIDGPPGT---GCPVVASIT--GADAVLLVTEPTPSGLHDLKRAIELAKHFGIP-TGIVINRYD------ 221

                        250       260       270
                 ....*....|....*....|....*....|
gi 398364553 257 kgesqIFKATTGGGEALCKELGIKFLGSVP 286
Cdd:cd03110  222 -----INDEISEEIEDFADEEGIPLLGKIP 246
minD CHL00175
septum-site determining protein; Validated
 65-299 2.35e-06

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 48.23  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  65 TDNLSGIEHKILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGC---IKETVHESNSG---WTPV 138
Cdd:CHL00175   8 KEKSATMSRIIVITSGKGGVGKTTTTANLGMSI-ARLGYRVALIDADIGLRNLDLLLGLenrVLYTAMDVLEGecrLDQA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 139 YVTD----NLATMSIQYMLPEDDsaiIWRGSKKNLLikKFLKDVDWdklDYLVIDTPPGtsdehISINKYMRESGIDGAL 214
Cdd:CHL00175  87 LIRDkrwkNLSLLAISKNRQRYN---VTRKNMNMLV--DSLKNRGY---DYILIDCPAG-----IDVGFINAIAPAQEAI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 215 VVTTPQEVALLDVRKEIDFCKKAGINILGLVENmsgfvcpncKGESQIFKATTGGGEALCKE-LGIKFLGSVPLDPRIGK 293
Cdd:CHL00175 154 VVTTPEITAIRDADRVAGLLEANGIYNVKLLVN---------RVRPDMIQANDMMSVRDVQEmLGIPLLGAIPEDENVII 224


                 ....*.
gi 398364553 294 SCDMGE 299
Cdd:CHL00175 225 STNRGE 230
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 73-111 5.61e-06

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: 45.22  E-value: 5.61e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 398364553  73 HKILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLD 111
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAAL-ALRGKRVLLIDLD 38
eps_fam TIGR01007
capsular exopolysaccharide family; This model describes the capsular exopolysaccharide ...
 68-247 5.77e-06

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


Pssm-ID: 273392 [Multi-domain]  Cd Length: 204  Bit Score: 46.28  E-value: 5.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553   68 LSGIEHK-ILVLSGKGGVGKSTFAAMLSWALSadedlQVGAMDLDICGPSL-PHMLGCIKETvhESNSGWTPVY-----V 140
Cdd:TIGR01007  12 FSGAEIKvLLITSVKPGEGKSTTSANIAIAFA-----QAGYKTLLIDGDMRnSVMSGTFKSQ--NKITGLTNFLsgttdL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  141 TDNLATMSIQYM-------LPEDDSAIIwrGSKK-NLLIKKFLKdvdwdKLDYLVIDTPP-GT-SDEHIsinkYMREsgI 210
Cdd:TIGR01007  85 SDAICDTNIENLdvitagpVPPNPTELL--QSSNfKTLIETLRK-----RFDYIIIDTPPiGTvTDAAI----IARA--C 151

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 398364553  211 DGALVVTTPQEVALLDVRKEIDFCKKAGINILGLVEN 247
Cdd:TIGR01007 152 DASILVTDAGKIKKREVKKAKEQLEQAGSNFLGVVLN 188
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 74-111 9.07e-05

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: 41.26  E-value: 9.07e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 398364553  74 KILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLD 111
Cdd:cd01983    2 VIAVTGGKGGVGKTTLAAALAVAL-AAKGYKVLLIDLD 38
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 75-318 9.85e-05

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 43.12  E-value: 9.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  75 ILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDICGPSLPHMLGCIKETVHesnsgwTPVYV-------------- 140
Cdd:COG2894    5 IVVTSGKGGVGKTTTTANLGTAL-ALLGKKVVLIDADIGLRNLDLVMGLENRIVY------DLVDViegecrlkqalikd 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 141 --TDNLatmsiqYMLP----EDDSAIIWRGSKK--NLLIKKFlkdvdwdklDYLVIDTPPGtsdehIsinkymrESGI-- 210
Cdd:COG2894   78 krFENL------YLLPasqtRDKDALTPEQMKKlvEELKEEF---------DYILIDSPAG-----I-------EQGFkn 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 211 -----DGALVVTTPQEVALLDV-RkeidfckkaginILGLVENMSgfvcpncKGESQ-----IFKATTGGGEALCKE--- 276
Cdd:COG2894  131 aiagaDEAIVVTTPEVSSVRDAdR------------IIGLLEAKG-------IRKPHliinrYRPAMVKRGDMLSVEdvl 191

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 398364553 277 --LGIKFLGSVPLDPRIGKSCDMGE-SFLDnyPDSPASSAVLNVV 318
Cdd:COG2894  192 eiLAIPLLGVVPEDEEVIVSSNRGEpVVLD--EKSKAGQAYRNIA 234
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
74-192 5.93e-04

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 40.96  E-value: 5.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  74 KILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDIcGPSLPHMLGCiketvhESNSGWTPVYVtDNLATMSIQyml 153
Cdd:COG0003    4 RIIFFTGKGGVGKTTVAAATALAL-AERGKRTLLVSTDP-AHSLGDVLGT------ELGNEPTEVAV-PNLYALEID--- 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398364553 154 PEDDSAIIWRGSKKNL--------------------------LIKKFLKDVDWdklDYLVIDTPP 192
Cdd:COG0003   72 PEAELEEYWERVRAPLrgllpsagvdelaeslpgteelaaldELLELLEEGEY---DVIVVDTAP 133
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 74-247 6.16e-04

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: 40.57  E-value: 6.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  74 KILVLSGKGGVGKSTFAAMLSWALsADEDLQVGAMDLDIcGPSLPHMLGCiketvheSNSGWTPVYVTDNLATMSI---- 149
Cdd:cd02035    1 RIIFFGGKGGVGKTTIAAATAVRL-AEQGKRVLLVSTDP-AHSLSDAFGQ-------KLGGETPVKGAPNLWAMEIdpee 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553 150 ---QY---MLPEDDSAIIWRGSKKNLL-----------------IKKFLKDVDWdklDYLVIDTPPgtsDEHI------- 199
Cdd:cd02035   72 aleEYweeVKELLAQYLRLPGLDEVYAeellslpgmdeaaafdeLREYVESGEY---DVIVFDTAP---TGHTlrllslp 145

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 398364553 200 --SINKYMRESGIDGALVVTTPQEVALLDVRKEIDFCKKAGINILGLVEN 247
Cdd:cd02035  146 leQVRELLRDPERTTFVLVTIPEKLSIYETERLWGELQQYGIPVDGVVVN 195
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 50-99 8.86e-04

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 40.84  E-value: 8.86e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 398364553   50 CESLPKGP--DPDIP----LItDNLSGIEHKILVLSGKGGVGKSTFAAMLSWALSA 99
Cdd:TIGR04291 293 QLSLDITTpqVPDLPslsrLI-DEIAKSEKGLIMTMGKGGVGKTTVAAAIAVRLAN 347
cellulose_yhjQ TIGR03371
cellulose synthase operon protein YhjQ; Members of this family are the YhjQ protein, found ...
 73-312 2.32e-03

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


Pssm-ID: 274549 [Multi-domain]  Cd Length: 246  Bit Score: 38.87  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553   73 HKILVLSGKGGVGKSTFAAMLSWALSAdEDLQVGAMDLDICGpSLPHMLGcIKETV------HESNSG-WTPV---YVTD 142
Cdd:TIGR03371   2 KVIAIVSVRGGVGKTTLTANLASALKL-LGEPVLAIDLDPQN-LLRLHFG-MDWSVrdgwarALLNGAdWAAAayrSPDG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  143 NL----ATMSIQYMLPEDDSAIIWrgskknllIKKFLKDVDWDKLDYLVIDTPPGTSDehisinkYMRES--GIDGALVV 216
Cdd:TIGR03371  79 VLflpyGDLSADEREAYQAHDAGW--------LARLLQQLDLAARDWVLIDLPRGPSP-------ITRQAlaAADLVLVV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553  217 TTPQEVALLDVRKEIDFCKKAGINilglvENMSGFVCPNCKGESQ----IFKattgggeALCKELGIKFL-GSVPLDPRI 291
Cdd:TIGR03371 144 VNADAACYATLHQLALALFAGSGP-----RDGPRFLINQFDPARQlsrdVRA-------VLRQTLGSRLLpFVIHRDEAV 211

                         250       260
                  ....*....|....*....|.
gi 398364553  292 GKSCDMGESFLDNYPDSPASS 312
Cdd:TIGR03371 212 SEALARGTPVLNYAPHSQAAH 232
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 81-192 2.73e-03

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: 37.95  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364553   81 KGGVGKSTFAAMLSWALsADEDLQVGAMDLDICG--------------PSLPHML-------GCIKETVHEsnsgwtpvy 139
Cdd:pfam13614  10 KGGVGKTTTSVNLAAAL-AKKGKKVLLIDLDPQGnatsglgidknnveKTIYELLigecnieEAIIKTVIE--------- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 398364553  140 vtdNLATM--SIQYMLPEDDSAIIWrgsKKNLLIKKFLKDVDwDKLDYLVIDTPP 192
Cdd:pfam13614  80 ---NLDLIpsNIDLAGAEIELIGIE---NRENILKEALEPVK-DNYDYIIIDCPP 127
CBP_BcsQ pfam06564
Cellulose biosynthesis protein BcsQ; This is a family of bacterial proteins involved in ...
 74-135 3.80e-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: 38.13  E-value: 3.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398364553   74 KILVLSG-KGGVGKSTFAAMLSWALSADEDlQVGAMDLdicgpSLPHMLGCIKETVHESNSGW 135
Cdd:pfam06564   2 KILALQGvRGGVGTTSILAALAWALQRLGE-RVLLIDL-----SPDNLLRLHFNVPFEHRQGW 58
 
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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