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Conserved domains on  [gi|118572611|ref|NP_002475|]
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cytosolic Fe-S cluster assembly factor NUBP1 isoform 1 [Homo sapiens]

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 ...
 53-303 1.93e-147

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: 414.54  E-value: 1.93e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611   53 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVG 132
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  213 INFCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPLDPLIGKNCDKGQSFFIDAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 118572611  293 TLAYRSIIQRI 303
Cdd:pfam10609 235 AKAFLKIADKV 245
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 53-303 1.93e-147

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: 414.54  E-value: 1.93e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611   53 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVG 132
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  213 INFCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPLDPLIGKNCDKGQSFFIDAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 118572611  293 TLAYRSIIQRI 303
Cdd:pfam10609 235 AKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 55-275 1.44e-130

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: 370.29  E-value: 1.44e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVGFL 134
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGY-KVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLataHIDGAVIITTPQEVSLQDVRKEIN 214
Cdd:cd02037   79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118572611 215 FCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPLDPLIGK 275
Cdd:cd02037  155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
50-315 1.62e-126

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 366.06  E-value: 1.62e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  50 MKTVKHKILVLSGKGGVGKSTFSAHLAHGLAeDENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVEDNLGVM 129
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALA-RRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 130 SVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDV 209
Cdd:NF041136  80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIP---DAGAVIVTTPQELALADV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 210 RKEINFCRKVKLPIIGVVENMSGFICPKCKKESQIFPptTGGAELMCQDLEVPLLGRVPLDPLIGKNCDKGQSFFIDAPD 289
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234

                        250       260
                 ....*....|....*....|....*.
gi 118572611 290 SPATLAYRSIIQRIQefcNLHQSKEE 315
Cdd:NF041136 235 SPAAKALEKIVDPIL---ELLENKKS 257
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
51-303 1.77e-59

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 194.88  E-value: 1.77e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  51 KTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVEdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAA-EGAKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 210 RKEINFCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPLDPLIGKNCDKGQSFFIDAPD 289
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPE 335

                        250
                 ....*....|....
gi 118572611 290 SPATLAYRSIIQRI 303
Cdd:PRK11670 336 SEFTAIYRQLADRV 349
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 32-237 7.58e-45

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: 154.57  E-value: 7.58e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  32 ASGAGATPDTAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-- 109
Cdd:COG0489   70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPSLHRMLGLENRPgl 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 110 --VHQSGSGWSPV---YVEDNLGVMSVGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSVV 184
Cdd:COG0489  149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 118572611 185 rylaTAHIDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENMsgfICPK 237
Cdd:COG0489  222 ----ASLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 57-304 2.06e-12

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: 66.21  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611   57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 126
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALAR-LGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  127 GVMSVGflLSSPDDAVIWRGPKKngMIKQFLRDvdwgeVDYLIVDTPPGtsdehLSVVRYLATAHIDGAVIITTPQEVSL 206
Cdd:TIGR01968  83 YLLPAS--QTRDKDAVTPEQMKK--LVNELKEE-----FDYVIIDCPAG-----IESGFRNAVAPADEAIVVTTPEVSAV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  207 QDVRKeinfcrkvklpIIGVVENMSgfICPKCKKESQIFPPTTGGAELMCQD-----LEVPLLGRVPLDPLIGKNCDKGQ 281
Cdd:TIGR01968 149 RDADR-----------VIGLLEAKG--IEKIHLIVNRLRPEMVKKGDMLSVDdvleiLSIPLIGVIPEDEAIIVSTNKGE 215

                         250       260
                  ....*....|....*....|...
gi 118572611  282 SFFIDaPDSPATLAYRSIIQRIQ 304
Cdd:TIGR01968 216 PVVLN-DKSRAGKAFENIARRIL 237
ParA_partition NF041546
ParA family partition ATPase;
57-185 1.03e-06

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 48.32  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDIDicgpsiPKimglegeqvhQSGSGWSPVYvEDNLGVMSVGflLS 136
Cdd:NF041546   2 IAVLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD------PQ----------GSALDWAAAR-EDERPFPVVG--LA 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 118572611 137 SPDdaviwrgpkkngmIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSVVR 185
Cdd:NF041546  62 RPT-------------LHRELPSLA-RDYDFVVIDGPPRAEDLARSAIK 96
 
Name Accession Description Interval E-value
ParA pfam10609
NUBPL iron-transfer P-loop NTPase; This family contains ATPases involved in plasmid ...
 53-303 1.93e-147

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: 414.54  E-value: 1.93e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611   53 VKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVG 132
Cdd:pfam10609   2 VKHVIAVASGKGGVGKSTVAVNLALALAR-LGYKVGLLDADIYGPSIPRMLGLEGERPEQSDGGIIPVEA-HGIKVMSIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  133 FLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDVRKE 212
Cdd:pfam10609  80 FLLPDEDDAVIWRGPMKSGAIKQFLTDVDWGELDYLIIDLPPGTGDEQLTLAQLLP---LTGAVIVTTPQDVALLDVRKA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  213 INFCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPLDPLIGKNCDKGQSFFIDAPDSPA 292
Cdd:pfam10609 157 IDMFKKVNVPVLGVVENMSYFVCPHCGEETYIF--GKGGGEKLAEELGVPFLGEIPLDPDIREAGDEGKPFVLADPDSPA 234

                         250
                  ....*....|.
gi 118572611  293 TLAYRSIIQRI 303
Cdd:pfam10609 235 AKAFLKIADKV 245
Mrp_NBP35 cd02037
Mrp/NBP35 ATP-binding protein family; Mrp/NBP35 ATP-binding family protein are typically ...
 55-275 1.44e-130

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: 370.29  E-value: 1.44e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVeDNLGVMSVGFL 134
Cdd:cd02037    1 HIIAVLSGKGGVGKSTVAVNLALALAKKGY-KVGLLDADIYGPSIPRLLGVEGKPLHQSEEGIVPVEV-GGIKVMSIGFL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 135 LSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLataHIDGAVIITTPQEVSLQDVRKEIN 214
Cdd:cd02037   79 LP-EDDAVIWRGPMKSGAIKQFLKDVDWGELDYLIIDLPPGTGDEHLSLVQLI---PIDGAVVVTTPQEVSLIDVRKAID 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118572611 215 FCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPLDPLIGK 275
Cdd:cd02037  155 MCKKLNIPVLGIVENMSGFVCPHCGKKIYIF--GKGGGEKLAEELGVPFLGKIPLDPELAK 213
MrpORP NF041136
iron-sulfur cluster carrier protein MrpORP;
50-315 1.62e-126

iron-sulfur cluster carrier protein MrpORP;


Pssm-ID: 469059 [Multi-domain]  Cd Length: 365  Bit Score: 366.06  E-value: 1.62e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  50 MKTVKHKILVLSGKGGVGKSTFSAHLAHGLAeDENTQIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVEDNLGVM 129
Cdd:NF041136   1 LSRIKHKILVMSGKGGVGKSTVAANLAVALA-RRGYKVGLLDVDIHGPSIPKLLGLEGKRLGSEDEGILPVEYSDNLKVM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 130 SVGFLLSSPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDV 209
Cdd:NF041136  80 SIGFLLENRDDAVIWRGPVKMGVIKQFLSDVEWGDLDYLIIDSPPGTGDEPLSVAQLIP---DAGAVIVTTPQELALADV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 210 RKEINFCRKVKLPIIGVVENMSGFICPKCKKESQIFPptTGGAELMCQDLEVPLLGRVPLDPLIGKNCDKGQSFFIDAPD 289
Cdd:NF041136 157 RKSINFCRKLNIPILGIVENMSGFVCPHCGKEIDIFK--SGGGEKLAEEMGVPFLGRIPIDPEIVEAGDAGRPFVLDYAW 234

                        250       260
                 ....*....|....*....|....*.
gi 118572611 290 SPATLAYRSIIQRIQefcNLHQSKEE 315
Cdd:NF041136 235 SPAAKALEKIVDPIL---ELLENKKS 257
PRK11670 PRK11670
iron-sulfur cluster carrier protein ApbC;
51-303 1.77e-59

iron-sulfur cluster carrier protein ApbC;


Pssm-ID: 183270 [Multi-domain]  Cd Length: 369  Bit Score: 194.88  E-value: 1.77e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  51 KTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVYVEdNLGVM 129
Cdd:PRK11670 104 NGVKNIIAVSSGKGGVGKSSTAVNLALALAA-EGAKVGILDADIYGPSIPTMLGAEDQRpTSPDGTHMAPIMAH-GLATN 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 130 SVGFLLSsPDDAVIWRGPKKNGMIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVRYLAtahIDGAVIITTPQEVSLQDV 209
Cdd:PRK11670 182 SIGYLVT-DDNAMVWRGPMASKALMQMLQETLWPDLDYLVLDMPPGTGDIQLTLAQNIP---VTGAVVVTTPQDIALIDA 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 210 RKEINFCRKVKLPIIGVVENMSGFICPKCKKESQIFppTTGGAELMCQDLEVPLLGRVPLDPLIGKNCDKGQSFFIDAPD 289
Cdd:PRK11670 258 KKGIVMFEKVEVPVLGIVENMSMHICSNCGHHEPIF--GTGGAEKLAEKYHTQLLGQMPLHISLREDLDRGTPTVVSRPE 335

                        250
                 ....*....|....
gi 118572611 290 SPATLAYRSIIQRI 303
Cdd:PRK11670 336 SEFTAIYRQLADRV 349
Mrp COG0489
Fe-S cluster carrier ATPase, Mrp/ApbC/NBP35 family [Cell cycle control, cell division, ...
 32-237 7.58e-45

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: 154.57  E-value: 7.58e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  32 ASGAGATPDTAIEEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-- 109
Cdd:COG0489   70 LLLLLLALALLLLLLLLLLRLLLEVIAVTSGKGGEGKSTVAANLALALAQ-SGKRVLLIDADLRGPSLHRMLGLENRPgl 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 110 --VHQSGSGWSPV---YVEDNLGVMSVGFLLSSPDdaviwrGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSVV 184
Cdd:COG0489  149 sdVLAGEASLEDViqpTEVEGLDVLPAGPLPPNPS------ELLASKRLKQLLEELR-GRYDYVIIDTPPGLGVADATLL 221

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 118572611 185 rylaTAHIDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENMsgfICPK 237
Cdd:COG0489  222 ----ASLVDGVLLVVRPGKTALDDVRKALEMLEKAGVPVLGVVLNM---VCPK 267
CpaE COG4963
Flp pilus assembly ATPase CpaE/TadZ, contains N-terminal REC/TadZ_N domain [Intracellular ...
 57-303 1.16e-21

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: 93.64  E-value: 1.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTQIALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVEDNLGVMSVG 132
Cdd:COG4963  105 IAVVGAKGGVGATTLAVNLAWALARESGRRVLLVDLDLQFGDVALYLDLEPRRgladALRNPDRLDETLLDRALTRHSSG 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 133 F-LLSSPDDAVIWR--GPKKNGMIKQFLRDvdwgEVDYLIVDTPPGTSDEHLSVvryLATAHIdgaVIITTPQEV-SLQD 208
Cdd:COG4963  185 LsVLAAPADLERAEevSPEAVERLLDLLRR----HFDYVVVDLPRGLNPWTLAA---LEAADE---VVLVTEPDLpSLRN 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 209 VRKEINFCRKVKLPI--IGVVENmsgficpKCKKESQIfppttgGAELMCQDLEVPLLGRVPLDP-LIGKNCDKGQSFFI 285
Cdd:COG4963  255 AKRLLDLLRELGLPDdkVRLVLN-------RVPKRGEI------SAKDIEEALGLPVAAVLPNDPkAVAEAANQGRPLAE 321

                        250
                 ....*....|....*...
gi 118572611 286 DAPDSPATLAYRSIIQRI 303
Cdd:COG4963  322 VAPKSPLAKAIRKLAARL 339
CbiA pfam01656
CobQ/CobB/MinD/ParA nucleotide binding domain; This family consists of various cobyrinic acid ...
 57-283 1.51e-18

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: 82.78  E-value: 1.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611   57 ILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDIDIcGPSIPKIMGLEGE--QVHQS------GSGW-SPVYVEDNLG 127
Cdd:pfam01656   1 IAIAGTKGGVGKTTLAANLARALARRGL-RVLLIDLDP-QSNNSSVEGLEGDiaPALQAlaeglkGRVNlDPILLKEKSD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  128 VMSVGFLLSSPD---DAVIWRGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDehlSVVRYLATAhiDGAVIITTPQEV 204
Cdd:pfam01656  79 EGGLDLIPGNIDlekFEKELLGPRKEERLREALEALK-EDYDYVIIDGAPGLGE---LLRNALIAA--DYVIIPLEPEVI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  205 SLQDVRKEINFCRKVK-------LPIIGVVENMsgficpkckkesqiFPPTTGGAELMcQDLE-----VPLLGRVPLDPL 272
Cdd:pfam01656 153 LVEDAKRLGGVIAALVggyallgLKIIGVVLNK--------------VDGDNHGKLLK-EALEellrgLPVLGVIPRDEA 217

                         250
                  ....*....|.
gi 118572611  273 IGKNCDKGQSF 283
Cdd:pfam01656 218 VAEAPARGLPV 228
FlhG COG0455
MinD-like ATPase FlhG/YlxH, activator of the FlhF-type GTPase [Cell cycle control, cell ...
 70-303 4.63e-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: 81.47  E-value: 4.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  70 TFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQ-VHQSGSGWSPVY---VEDNLGVmsvgFLLSSPDDAVIWR 145
Cdd:COG0455    1 TVAVNLAAALAR-LGKRVLLVDADLGLANLDVLLGLEPKAtLADVLAGEADLEdaiVQGPGGL----DVLPGGSGPAELA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 146 GPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDehlSVVRYLATAhiDGAVIITTPQEVSLQDVRKEINFCR-KVKLPII 224
Cdd:COG0455   76 ELDPEERLIRVLEELE-RFYDVVLVDTGAGISD---SVLLFLAAA--DEVVVVTTPEPTSITDAYALLKLLRrRLGVRRA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 225 GVVENMSgficpkckKESQIFPPTTGGAELMCQ---DLEVPLLGRVPLDPLIGKNCDKGQSFFIDAPDSPATLAYRSIIQ 301
Cdd:COG0455  150 GVVVNRV--------RSEAEARDVFERLEQVAErflGVRLRVLGVIPEDPAVREAVRRGRPLVLAAPDSPAARAIRELAA 221


                 ..
gi 118572611 302 RI 303
Cdd:COG0455  222 RL 223
MinD cd02036
septum site-determining protein MinD; Septum site-determining protein MinD is part of the ...
 57-303 6.59e-17

septum site-determining protein MinD; Septum site-determining protein MinD is part of the operon MinCDE that determines the site of the formation of a septum at mid-cell, an important part of bacterial cell division. MinC is a nonspecific inhibitor of the septum protein FtsZ. MinE is the supressor of MinC. MinD plays a pivotal role, selecting the mid-cell over other sites through the activation and regulation of MinC and MinE. MinD is a membrane-associated ATPase, related to nitrogenase iron protein.


Pssm-ID: 349756 [Multi-domain]  Cd Length: 236  Bit Score: 78.40  E-value: 6.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEG----------------EQVHQSGSGWspv 120
Cdd:cd02036    3 IVITSGKGGVGKTTTTANLGVALAK-LGKKVLLIDADIGLRNLDLILGLENrivytlvdvlegecrlEQALIKDKRW--- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 121 yveDNLGVMSVGFllSSPDDAViwrGPKKngmIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSvvrylATAHIDGAVIITT 200
Cdd:cd02036   79 ---ENLYLLPASQ--TRDKDAL---TPEK---LEELVKELK-DSFDFILIDSPAGIESGFIN-----AIAPADEAIIVTN 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 201 PQEVSLQDVRKeinfcrkvklpIIGVVENMS----GFICPKCKKESqifppTTGGAELMCQD----LEVPLLGRVPLDPL 272
Cdd:cd02036  142 PEISSVRDADR-----------VIGLLESKGivniGLIVNRYRPEM-----VKSGDMLSVEDiqeiLGIPLLGVIPEDPE 205

                        250       260       270
                 ....*....|....*....|....*....|.
gi 118572611 273 IGKNCDKGQSFFIDAPDSPATLAYRSIIQRI 303
Cdd:cd02036  206 VIVATNRGEPLVLYKPNSLAAKAFENIARRL 236
FlhG-like cd02038
MinD-like ATPase FlhG; FlhG is a member of the SIMIBI superfamily. FlhG (also known as YlxH) ...
 57-293 7.26e-16

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: 75.30  E-value: 7.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLD-------IDIC-GPSIPKIMG--LEGEqvhqSGSGWSPVYVEDNL 126
Cdd:cd02038    3 IAVTSGKGGVGKTNVSANLALALSK-LGKRVLLLDadlglanLDILlGLAPKKTLGdvLKGR----VSLEDIIVEGPEGL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 127 GVMSVGfllSSPDDAVIWRGPKKNGMIKQFLRDVDwgEVDYLIVDTPPGTSDEhlsvVRYLATAhIDGAVIITTPQEVSL 206
Cdd:cd02038   78 DIIPGG---SGMEELANLDPEQKAKLIEELSSLES--NYDYLLIDTGAGISRN----VLDFLLA-ADEVIVVTTPEPTSI 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 207 QD---VRKEINfcRKVKLPIIGVVENMSgficpKCKKESQifpPTTGGAELMCQ---DLEVPLLGRVPLDPLIGKNCDKG 280
Cdd:cd02038  148 TDayaLIKVLS--RRGGKKNFRLIVNMA-----RSPKEGR---ATFERLKKVAKrflDINLDFVGFIPYDQSVRRAVRSQ 217

                        250
                 ....*....|...
gi 118572611 281 QSFFIDAPDSPAT 293
Cdd:cd02038  218 KPFVLLFPNSKAS 230
CooC COG3640
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ...
 56-303 2.98e-15

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


Pssm-ID: 442857 [Multi-domain]  Cd Length: 249  Bit Score: 74.05  E-value: 2.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  56 KILVlSGKGGVGKSTFSAHLAHGLAEDENTQIAL-LDIDicgPSIPKIMGLEGEQvhqsgSGWSPV-----YVEDNLGVM 129
Cdd:COG3640    2 KIAV-AGKGGVGKTTLSALLARYLAEKGKPVLAVdADPN---ANLAEALGLEVEA-----DLIKPLgemreLIKERTGAP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 130 SVGFLLSSP------DDAVIWRG---------PKK---------NGMIKQFLRDVDWGEVDYLIVDTPPGTsdEHLSvvR 185
Cdd:COG3640   73 GGGMFKLNPkvddipEEYLVEGDgvdllvmgtIEEggsgcycpeNALLRALLNHLVLGNYEYVVVDMEAGI--EHLG--R 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 186 YLATaHIDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENmsgficpKCKKESQIfppttggaELMCQDLEVPLLG 265
Cdd:COG3640  149 GTAE-GVDLLLVVSEPSRRSIETARRIKELAEELGIKKIYLVGN-------KVREEEDE--------EFLRELLGLELLG 212

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 118572611 266 RVPLDPLIGKNCDKGQSFFiDAPDSPATLAYRSIIQRI 303
Cdd:COG3640  213 FIPYDEEVREADLEGKPLL-DLPDSPAVAAVEEIAEKL 249
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 50-305 1.13e-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: 66.81  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  50 MKTvkhkILVLSGKGGVGKSTFSAHLAHGLAEDENtQIALLDIDICGpSIPKIMGLEGEQVHQS-------GSGWSPVYV 122
Cdd:COG1192    1 MKV----IAVANQKGGVGKTTTAVNLAAALARRGK-RVLLIDLDPQG-NLTSGLGLDPDDLDPTlydllldDAPLEDAIV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 123 EDNLGVMSVgfLLSSPD----DAVIWRGPKKNGMIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSVvryLATAhiDGAVII 198
Cdd:COG1192   75 PTEIPGLDL--IPANIDlagaEIELVSRPGRELRLKRALAPLA-DDYDYILIDCPPSLGLLTLNA---LAAA--DSVLIP 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 199 TTPQEVSL----------QDVRKEINfcrkVKLPIIGVVENMSGficPKCKKESQIfppttggAELMCQDLEVPLLG-RV 267
Cdd:COG1192  147 VQPEYLSLeglaqlletiEEVREDLN----PKLEILGILLTMVD---PRTRLSREV-------LEELREEFGDKVLDtVI 212

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 118572611 268 PLDPLIGKNCDKGQSFFIDAPDSPATLAYRSIIQRIQE 305
Cdd:COG1192  213 PRSVALAEAPSAGKPVFEYDPKSKGAKAYRALAEELLE 250
minD_bact TIGR01968
septum site-determining protein MinD; This model describes the bacterial and chloroplast form ...
 57-304 2.06e-12

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: 66.21  E-value: 2.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611   57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 126
Cdd:TIGR01968   4 IVITSGKGGVGKTTTTANLGTALAR-LGKKVVLIDADIGLRNLDLLLGLENRIVYtlvdvvEGECRLQQALIKDkrlkNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  127 GVMSVGflLSSPDDAVIWRGPKKngMIKQFLRDvdwgeVDYLIVDTPPGtsdehLSVVRYLATAHIDGAVIITTPQEVSL 206
Cdd:TIGR01968  83 YLLPAS--QTRDKDAVTPEQMKK--LVNELKEE-----FDYVIIDCPAG-----IESGFRNAVAPADEAIVVTTPEVSAV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  207 QDVRKeinfcrkvklpIIGVVENMSgfICPKCKKESQIFPPTTGGAELMCQD-----LEVPLLGRVPLDPLIGKNCDKGQ 281
Cdd:TIGR01968 149 RDADR-----------VIGLLEAKG--IEKIHLIVNRLRPEMVKKGDMLSVDdvleiLSIPLIGVIPEDEAIIVSTNKGE 215

                         250       260
                  ....*....|....*....|...
gi 118572611  282 SFFIDaPDSPATLAYRSIIQRIQ 304
Cdd:TIGR01968 216 PVVLN-DKSRAGKAFENIARRIL 237
PRK10818 PRK10818
septum site-determining protein MinD;
57-303 2.17e-12

septum site-determining protein MinD;


Pssm-ID: 182756 [Multi-domain]  Cd Length: 270  Bit Score: 66.12  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLEGEQVH------QSGSGWSPVYVED----NL 126
Cdd:PRK10818   5 IVVTSGKGGVGKTTSSAAIATGLAQ-KGKKTVVIDFDIGLRNLDLIMGCERRVVYdfvnviQGDATLNQALIKDkrteNL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 127 GVMSVGflLSSPDDAVIWRGpkkngmIKQFLRDVDWGEVDYLIVDTPPGTSDEHLSVVrYLAtahiDGAVIITTPQEVSL 206
Cdd:PRK10818  84 YILPAS--QTRDKDALTREG------VAKVLDDLKAMDFEFIVCDSPAGIETGALMAL-YFA----DEAIITTNPEVSSV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 207 QDVRKeinfcrkvklpIIGVVENmsgficpKCKKESQIFPP--------------TTGGAELMCQD----LEVPLLGRVP 268
Cdd:PRK10818 151 RDSDR-----------ILGILAS-------KSRRAENGEEPikehllltrynpgrVSRGDMLSMEDvleiLRIKLVGVIP 212

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 118572611 269 LDPLIGKNCDKGQSFFIDApDSPATLAYRSIIQRI 303
Cdd:PRK10818 213 EDQSVLRASNQGEPVILDI-EADAGKAYADTVDRL 246
CpaE-like cd03111
pilus assembly ATPase CpaE; This protein family consists of proteins similar to the cpaE ...
 57-299 3.07e-12

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: 64.99  E-value: 3.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTQIALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPVYVEDNLGVMSVG 132
Cdd:cd03111    3 VAVVGAKGGVGASTLAVNLAQELAQRAKDKVLLIDLDLPFGDLGLYLNLRPDYdladVIQNLDRLDRTLLDSAVTRHSSG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 133 F-LLSSP---DDAVIWRGPKKNGMIkQFLRdvdwGEVDYLIVDTPPGTSDEHLSVVRylataHIDGAVIITTPQEVSLQD 208
Cdd:cd03111   83 LsLLPAPqelEDLEALGAEQVDKLL-QVLR----AFYDHIIVDLGHFLDEVTLAVLE-----AADEILLVTQQDLPSLRN 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 209 VRKEINFCRKVKLPI--IGVVENmsgficpKCKKESQIFPPTTGGAelmcqdLEVPLLGRVPLDP-LIGKNCDKGQSFFI 285
Cdd:cd03111  153 ARRLLDSLRELEGSSdrLRLVLN-------RYDKKSEISPKDIEEA------LGLEVFATLPNDYkAVSESANTGRPLVE 219

                        250
                 ....*....|....
gi 118572611 286 DAPDSPATLAYRSI 299
Cdd:cd03111  220 VAPRSALVRALQDL 233
BY-kinase cd05387
bacterial tyrosine-kinase; Bacterial tyrosine (BY)-kinases catalyze the autophosphorylation on ...
 55-229 2.50e-11

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: 61.82  E-value: 2.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDIDICGPSIPKIMGLEGEQ----VHQSGSGWSPV---YVEDNLG 127
Cdd:cd05387   20 KVIAVTSASPGEGKSTVAANLAVALAQSGKR-VLLIDADLRRPSLHRLLGLPNEPglseVLSGQASLEDViqsTNIPNLD 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 128 VMSVGFLLSSPDDAViwRGPKKNGMIKQFLRdvdwgEVDYLIVDTPP--GTSDEHLsvvryLATaHIDGAVIITTPQEVS 205
Cdd:cd05387   99 VLPAGTVPPNPSELL--SSPRFAELLEELKE-----QYDYVIIDTPPvlAVADALI-----LAP-LVDGVLLVVRAGKTR 165

                        170       180
                 ....*....|....*....|....
gi 118572611 206 LQDVRKEINFCRKVKLPIIGVVEN 229
Cdd:cd05387  166 RREVKEALERLEQAGAKVLGVVLN 189
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 56-268 2.68e-10

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: 59.71  E-value: 2.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  56 KILVLSGKGGVGKSTFSAHLAHGLAEdentqIALLDIDICGPSIPKIMGLEGEQVHQSGSGWSPVYVED----------- 124
Cdd:cd03110    1 IIAVLSGKGGTGKTTITANLAVLLYN-----VILVDCDVDAPNLHLLLGPEPEEEEDFVGGKKAFIDQEkcircgncerv 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 125 -NLGVMSVGF----------------LLSSPDDAVIWRgPKKNGMIKQFLRD---------------------------- 159
Cdd:cd03110   76 cKFGAILEFFqklivdeslcegcgacVIICPRGAIYLK-DRDTGKIFISSSDggplvhgrlnigeensgklvtelrkkal 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 160 VDWGEVDYLIVDTPPGTsdeHLSVVRYLATAhiDGAVIITTPQEVSLQDVRKEINFCRKVKLPiIGVVENMSGficpkck 239
Cdd:cd03110  155 ERSKECDLAIIDGPPGT---GCPVVASITGA--DAVLLVTEPTPSGLHDLKRAIELAKHFGIP-TGIVINRYD------- 221

                        250       260
                 ....*....|....*....|....*....
gi 118572611 240 kesqIFPPTTGGAELMCQDLEVPLLGRVP 268
Cdd:cd03110  222 ----INDEISEEIEDFADEEGIPLLGKIP 246
MinD COG2894
Septum site-determining ATPase MinD [Cell cycle control, cell division, chromosome ...
 57-304 7.22e-10

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


Pssm-ID: 442139 [Multi-domain]  Cd Length: 258  Bit Score: 58.53  E-value: 7.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  57 ILVLSGKGGVGKSTFSAHLAHGLAEdENTQIALLDIDICGPSIPKIMGLE------------GE-QVHQSgsgwspvYVE 123
Cdd:COG2894    5 IVVTSGKGGVGKTTTTANLGTALAL-LGKKVVLIDADIGLRNLDLVMGLEnrivydlvdvieGEcRLKQA-------LIK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 124 D----NLgvmsvgFLL----SSPDDAViwrgpKKNGMIK--QFLRDvdwgEVDYLIVDTPPGTsdEHLSvvrYLATAHID 193
Cdd:COG2894   77 DkrfeNL------YLLpasqTRDKDAL-----TPEQMKKlvEELKE----EFDYILIDSPAGI--EQGF---KNAIAGAD 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 194 GAVIITTPQEVSLQDV-RkeinfcrkvklpIIGVVENMSgficpkcKKESQI----FPPT---TGG---AELMCQDLEVP 262
Cdd:COG2894  137 EAIVVTTPEVSSVRDAdR------------IIGLLEAKG-------IRKPHLiinrYRPAmvkRGDmlsVEDVLEILAIP 197

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 118572611 263 LLGRVPLDPLIGKNCDKGQSFFIDaPDSPATLAYRSIIQRIQ 304
Cdd:COG2894  198 LLGVVPEDEEVIVSSNRGEPVVLD-EKSKAGQAYRNIARRLL 238
CooC1 cd02034
accessory protein CooC1; The accessory protein CooC1, a nickel-binding ATPase, participates in ...
 56-303 5.11e-09

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: 55.78  E-value: 5.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  56 KILVlSGKGGVGKSTFSAHLAHGLAEDENTQIAlLDIDiCGPSIPKIMGLEGEQVHQSGSGWSpvyVEDNLG----VMSV 131
Cdd:cd02034    2 KIAV-AGKGGVGKTTIAALLIRYLAKKGGKVLA-VDAD-PNSNLAETLGVEVEKLPLIKTIGD---IRERTGakkgEPPE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 132 GFLLSSPDDAVIWRG--------------PKK---------NGMIKQFLRDVDWGEVDYLIVDTPPGTsdEHLS--VVRy 186
Cdd:cd02034   76 GMSLNPYVDDIIKEIivepdgidllvmgrPEGggsgcycpvNALLRELLRHLALKNYEYVVIDMEAGI--EHLSrgTIR- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 187 lataHIDGAVIITTPQEVSLQDVRKEINFCRKVKLPIIGVVENMSgficPKCKKESQIfppttggAELMCQDlevPLLGR 266
Cdd:cd02034  153 ----AVDLLIIVIEPSKRSIQTAKRIKELAEELGIKKIYLIVNKV----RNEEEQELI-------EELLIKL---KLIGV 214

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 118572611 267 VPLDPLIGKNCDKGQSFFIDapDSPATLAYRSIIQRI 303
Cdd:cd02034  215 IPYDEEIMEADLKGKPLFDL--DSAAVKAIEKIVEKL 249
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 55-230 1.73e-07

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: 49.46  E-value: 1.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  55 HKILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDIDicgpsipkimglegeqvHQSgsgwspvyvednlgvmsvgfl 134
Cdd:cd02042    1 KVIAVANQKGGVGKTTLAVNLAAALALRGKR-VLLIDLD-----------------PQG--------------------- 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 135 lsspdDAVIWRgpkkngmikqflrdvdwgeVDYLIVDTPPGTSDEHLSVvryLATAHIdgaVII-TTPQEVSLQDVRKEI 213
Cdd:cd02042   42 -----SLTSWL-------------------YDYILIDTPPSLGLLTRNA---LAAADL---VLIpVQPSPFDLDGLAKLL 91

                        170       180
                 ....*....|....*....|...
gi 118572611 214 NFCRKVK------LPIIGVVENM 230
Cdd:cd02042   92 DTLEELKkqlnppLLILGILLTR 114
minD CHL00175
septum-site determining protein; Validated
 44-306 4.76e-07

septum-site determining protein; Validated


Pssm-ID: 214385 [Multi-domain]  Cd Length: 281  Bit Score: 50.15  E-value: 4.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  44 EEIKEKMKTVKHKILVLSGKGGVGKSTFSAHLAHGLAEDEnTQIALLDIDICGPSIPKIMGLEGEQVHQSgsgwspvyve 123
Cdd:CHL00175   5 TEDKEKSATMSRIIVITSGKGGVGKTTTTANLGMSIARLG-YRVALIDADIGLRNLDLLLGLENRVLYTA---------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 124 dnLGVMSVGFLLsspDDAVI----WRG---------------PKKN-GMIKQFLRDVDWgevDYLIVDTPPGtsdehLSV 183
Cdd:CHL00175  74 --MDVLEGECRL---DQALIrdkrWKNlsllaisknrqrynvTRKNmNMLVDSLKNRGY---DYILIDCPAG-----IDV 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611 184 VRYLATAHIDGAVIITTPQEVSLQDVRK-----EINFCRKVKLPIIGVVENMsgficpkCKKESQIFPPTTGGAelmcqd 258
Cdd:CHL00175 141 GFINAIAPAQEAIVVTTPEITAIRDADRvagllEANGIYNVKLLVNRVRPDM-------IQANDMMSVRDVQEM------ 207

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118572611 259 LEVPLLGRVPLDPLIGKNCDKG--------------------------QSFFIDApDSPatlaYRSIIQRIQEF 306
Cdd:CHL00175 208 LGIPLLGAIPEDENVIISTNRGeplvlnkkltlsgiafenaarrlvgkQDYFIDL-DSP----SKGPLKRLQKF 276
ParA_partition NF041546
ParA family partition ATPase;
57-185 1.03e-06

ParA family partition ATPase;


Pssm-ID: 469431 [Multi-domain]  Cd Length: 202  Bit Score: 48.32  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  57 ILVLSGKGGVGKSTFSAHLAHGLAEDENTqIALLDIDicgpsiPKimglegeqvhQSGSGWSPVYvEDNLGVMSVGflLS 136
Cdd:NF041546   2 IAVLNQKGGVGKTTLATHLAAALARRGYR-VLLVDAD------PQ----------GSALDWAAAR-EDERPFPVVG--LA 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 118572611 137 SPDdaviwrgpkkngmIKQFLRDVDwGEVDYLIVDTPPGTSDEHLSVVR 185
Cdd:NF041546  62 RPT-------------LHRELPSLA-RDYDFVVIDGPPRAEDLARSAIK 96
SIMIBI cd01983
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ...
 56-93 3.05e-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: 42.42  E-value: 3.05e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 118572611  56 KILVLSGKGGVGKSTFSAHLAHGLAEDeNTQIALLDID 93
Cdd:cd01983    2 VIAVTGGKGGVGKTTLAAALAVALAAK-GYKVLLIDLD 38
ArsA_ATPase pfam02374
Anion-transporting ATPase; This Pfam family represents a conserved domain, which is sometimes ...
 55-174 5.99e-05

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: 43.88  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611   55 HKILVLSGKGGVGKSTFSAHLAHGLAE-------------------------------DENTQIALLDIDicgpsipkiM 103
Cdd:pfam02374   1 MRWIFFGGKGGVGKTTVSAATAVQLSElgkkvllistdpahslsdsfnqkfgheptkvKENLSAMEIDPN---------M 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572611  104 GLEGEqvhqsgsgWSPVYVEDNLGVMSVG-------FLLSSP--DDAVIWrgpkkngmiKQFLRDVDWGEVDYLIVDTPP 174
Cdd:pfam02374  72 ELEEY--------WQEVQKYMNALLGLRMlegilaeELASLPgiDEAASF---------DEFKKYMDEGEYDVVVFDTAP 134
ArsA COG0003
Anion-transporting ATPase, ArsA/GET3 family [Inorganic ion transport and metabolism];
56-82 1.26e-03

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


Pssm-ID: 439774  Cd Length: 299  Bit Score: 39.80  E-value: 1.26e-03
                         10        20
                 ....*....|....*....|....*..
gi 118572611  56 KILVLSGKGGVGKSTFSAHLAHGLAED 82
Cdd:COG0003    4 RIIFFTGKGGVGKTTVAAATALALAER 30
arsen_driv_ArsA TIGR04291
arsenical pump-driving ATPase; The broader family (TIGR00345) to which the current family ...
 43-81 1.67e-03

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


Pssm-ID: 275109 [Multi-domain]  Cd Length: 566  Bit Score: 40.07  E-value: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 118572611   43 IEEIKEKmktvKHKILVLSGKGGVGKSTFSAHLAHGLAE 81
Cdd:TIGR04291 313 IDEIAKS----EKGLIMTMGKGGVGKTTVAAAIAVRLAN 347
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
54-83 2.43e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 39.79  E-value: 2.43e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 118572611  54 KHKILVLSGKGGVGKSTFSAHLAHGLAEDE 83
Cdd:COG5635  179 KKKRLLILGEPGSGKTTLLRYLALELAERY 208
NifH-like cd02117
NifH family; This family contains the NifH (iron protein) of nitrogenase, L subunit (BchL/ChlL) ...
 56-81 2.44e-03

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: 38.89  E-value: 2.44e-03
                         10        20
                 ....*....|....*....|....*.
gi 118572611  56 KILVLSGKGGVGKSTFSAHLAHGLAE 81
Cdd:cd02117    1 ESIVVYGKGGIGKSTTASNLSAALAE 26
ArsA cd02035
Arsenical pump-driving ATPase ArsA; ArsA ATPase functions as an efflux pump located on the ...
 56-81 2.90e-03

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: 38.64  E-value: 2.90e-03
                         10        20
                 ....*....|....*....|....*.
gi 118572611  56 KILVLSGKGGVGKSTFSAHLAHGLAE 81
Cdd:cd02035    1 RIIFFGGKGGVGKTTIAAATAVRLAE 26
 
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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