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Conserved domains on  [gi|88759337|ref|NP_060536|]
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GPN-loop GTPase 2 [Homo sapiens]

Protein Classification

GPN-loop GTPase family protein( domain architecture ID 13027372)

GPN-loop GTPase family protein is characterized by a highly conserved motif consisting of the amino acids Gly-Pro-Asn such as Homo sapiens GPN-loop GTPase 2, a small GTPase which is required for proper nuclear import of RNA polymerase II (RNAPII), and may act at an RNAP assembly step prior to nuclear import

CATH:  3.40.50.300
EC:  3.6.5.-
Gene Ontology:  GO:0005525|GO:0003924
PubMed:  11916378

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GPN2 cd17871
GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization ...
 10-257 4.27e-131

GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). It forms heterodimers with GPN1 or GPN3.


:

Pssm-ID: 349780  Cd Length: 196  Bit Score: 370.71  E-value: 4.27e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  10 FGQAVIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYECAVDVGELVGLGDVMDALRLGPNGGLLYCMEYLE 89
Cdd:cd17871   1 FGQVVIGPPGSGKTTYCKGMQQFLSALGRKVAVVNLDPANEFLPYPCDVDIRELITVEDVMEELKLGPNGGLLYCMEYLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  90 ANLDWLRAKLDPLRGHYFLFDCPGQVELCTHHGALRSIFSQMAQWDLRLTAVHLVDSHYCTDPAKFISVLCTSLATMLHV 169
Cdd:cd17871  81 KNIDWLIDKLKKLKDSYLIFDCPGQVELYTHHNSLRNILDKLQKWLYRLVAVHLVDSHYCSDPSKFISALLLSLSTMLRL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337 170 ELPHINLLSKMDliehygklafnldyytevldlsylldhlasdpffrhyrqlneklvqliedysLVSFIPLNIQDKESIQ 249
Cdd:cd17871 161 ELPHVNVLSKID----------------------------------------------------LVSFIPLDVQDKESML 188


                ....*...
gi 88759337 250 RVLQAVDK 257
Cdd:cd17871 189 RLLKAIDK 196
 
Name Accession Description Interval E-value
GPN2 cd17871
GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization ...
 10-257 4.27e-131

GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). It forms heterodimers with GPN1 or GPN3.


Pssm-ID: 349780  Cd Length: 196  Bit Score: 370.71  E-value: 4.27e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  10 FGQAVIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYECAVDVGELVGLGDVMDALRLGPNGGLLYCMEYLE 89
Cdd:cd17871   1 FGQVVIGPPGSGKTTYCKGMQQFLSALGRKVAVVNLDPANEFLPYPCDVDIRELITVEDVMEELKLGPNGGLLYCMEYLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  90 ANLDWLRAKLDPLRGHYFLFDCPGQVELCTHHGALRSIFSQMAQWDLRLTAVHLVDSHYCTDPAKFISVLCTSLATMLHV 169
Cdd:cd17871  81 KNIDWLIDKLKKLKDSYLIFDCPGQVELYTHHNSLRNILDKLQKWLYRLVAVHLVDSHYCSDPSKFISALLLSLSTMLRL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337 170 ELPHINLLSKMDliehygklafnldyytevldlsylldhlasdpffrhyrqlneklvqliedysLVSFIPLNIQDKESIQ 249
Cdd:cd17871 161 ELPHVNVLSKID----------------------------------------------------LVSFIPLDVQDKESML 188


                ....*...
gi 88759337 250 RVLQAVDK 257
Cdd:cd17871 189 RLLKAIDK 196
ATP_bind_1 pfam03029
Conserved hypothetical ATP binding protein; Members of this family are found in a range of ...
 14-261 7.45e-88

Conserved hypothetical ATP binding protein; Members of this family are found in a range of archaea and eukaryotes and have hypothesized ATP binding activity.


Pssm-ID: 397252 [Multi-domain]  Cd Length: 238  Bit Score: 262.69  E-value: 7.45e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337    14 VIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYECAVDVGELVGLGDVMDALRLGPNGGLLYCMEYLEANLD 93
Cdd:pfam03029   1 VVGPAGSGKTTFVGALSEILPLRGRPVYVVNLDPAAENLPYPADIDIRELITVADVMEDYGLGPNGALTVAMDFGRITLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337    94 WLRAKLDpLRGHYFLFDCPGQVELCTHHGALRSIFSQMAQwDLRLTAVHLVDSHYCTDPAKFISVLCTSLATMLHVELPH 173
Cdd:pfam03029  81 WLDEELK-REDDYYLFDTPGQIELFTHWDSLAIIVEALES-RGALGAVYLVDTRRLTDPTDFFSGLLYALSIMLRLGLPF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337   174 INLLSKMDLIehygKLAFNLDYYTEVLDLSYLLDHLASdpffrHYRQLNEKLVQLIEDYSLV-SFIPLNIQDKESIQRVL 252
Cdd:pfam03029 159 VVALNKFDLL----SLEFALKWFTDPEDLQLLLELDDG-----KYRKLNEAIREALDLFYLVpVFLPDARERGESMEDLL 229


                  ....*....
gi 88759337   253 QAVDKANGY 261
Cdd:pfam03029 230 TLIDEALQY 238
PRK13768 PRK13768
GTPase; Provisional
 14-252 6.19e-40

GTPase; Provisional


Pssm-ID: 237498 [Multi-domain]  Cd Length: 253  Bit Score: 140.00  E-value: 6.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337   14 VIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYECAVDVGELVGLGDVMDALRLGPNGGLLYCMEYLEANLD 93
Cdd:PRK13768   7 FLGTAGSGKTTLTKALSDWLEEQGYDVAIVNLDPAVEYLPYTPDFDVRDYVTAREIMKKYGLGPNGALIASVDLLLTKAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337   94 WLRAKLDPLRGHYFLFDCPGQVELCTHHGALRSIFSQMAQwDLRLTAVHLVDSHYCTDPAKFISVLCTSLATMLHVELPH 173
Cdd:PRK13768  87 EIKEEIESLDADYVLVDTPGQMELFAFRESGRKLVERLSG-SSKSVVVFLIDAVLAKTPSDFVSLLLLALSVQLRLGLPQ 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  174 INLLSKMDLIEhygklAFNLDYYTEVL-DLSYLLDHLASDPFFrhYRQLNEKLVQLIEDYSLVS-FIPLNIQDKES---- 247
Cdd:PRK13768 166 IPVLNKADLLS-----EEELERILKWLeDPEYLLEELKLEKGL--QGLLSLELLRALEETGLPVrVIPVSAKTGEGfdel 238


                 ....*...
gi 88759337  248 ---IQRVL 252
Cdd:PRK13768 239 yaaIQEVF 246
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 19-119 5.57e-05

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: 43.69  E-value: 5.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  19 GSGKTTYCLGMSEFLRALGRRVAVVNLDP-AN--EGL---PYECAVDVGE-LVGLGDVMDALRLGPNGGlLYC------M 85
Cdd:COG1192  12 GVGKTTTAVNLAAALARRGKRVLLIDLDPqGNltSGLgldPDDLDPTLYDlLLDDAPLEDAIVPTEIPG-LDLipanidL 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 88759337  86 EYLEANL-------DWLRAKLDPLRGHY--FLFDCPGQVELCT 119
Cdd:COG1192  91 AGAEIELvsrpgreLRLKRALAPLADDYdyILIDCPPSLGLLT 133
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 13-75 4.28e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.97  E-value: 4.28e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88759337     13 AVIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYE-CAVDVGELVGLGDVMDALRL 75
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlLLIIVGGKKASGSGELRLRL 69
 
Name Accession Description Interval E-value
GPN2 cd17871
GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization ...
 10-257 4.27e-131

GPN-loop GTPase 2; GPN-loop GTPase 2 (GPN2) is a small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). It forms heterodimers with GPN1 or GPN3.


Pssm-ID: 349780  Cd Length: 196  Bit Score: 370.71  E-value: 4.27e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  10 FGQAVIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYECAVDVGELVGLGDVMDALRLGPNGGLLYCMEYLE 89
Cdd:cd17871   1 FGQVVIGPPGSGKTTYCKGMQQFLSALGRKVAVVNLDPANEFLPYPCDVDIRELITVEDVMEELKLGPNGGLLYCMEYLE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  90 ANLDWLRAKLDPLRGHYFLFDCPGQVELCTHHGALRSIFSQMAQWDLRLTAVHLVDSHYCTDPAKFISVLCTSLATMLHV 169
Cdd:cd17871  81 KNIDWLIDKLKKLKDSYLIFDCPGQVELYTHHNSLRNILDKLQKWLYRLVAVHLVDSHYCSDPSKFISALLLSLSTMLRL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337 170 ELPHINLLSKMDliehygklafnldyytevldlsylldhlasdpffrhyrqlneklvqliedysLVSFIPLNIQDKESIQ 249
Cdd:cd17871 161 ELPHVNVLSKID----------------------------------------------------LVSFIPLDVQDKESML 188


                ....*...
gi 88759337 250 RVLQAVDK 257
Cdd:cd17871 189 RLLKAIDK 196
GPN cd17868
GPN-loop GTPase; GPN-loop GTPases are deeply evolutionarily conserved family of three small ...
 10-257 4.53e-96

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


Pssm-ID: 349777 [Multi-domain]  Cd Length: 198  Bit Score: 281.90  E-value: 4.53e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  10 FGQAVIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYECAVDVGELVGLGDVMDALRLGPNGGLLYCMEYLE 89
Cdd:cd17868   1 YAILVIGPAGSGKTTFCKNMKEHLRARKRNPYVINLDPGNINEPLDYDIDIRDLIKYDDIMEELDLGPNGSIVYSLEYFE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  90 ANLDWLRAKLDPLR--GHYFLFDCPGQVELCTHHGALRSIFSQMAQWDLRLTAVHLVDSHYCTDPAKFISVLCTSLATML 167
Cdd:cd17868  81 KNFDWFEKKLENEDknPHYILFDCPGQIELFTHSDSLPKIIERFASWFISVVIVNLIDSQFLSDKSKFLSNLLIALSSMF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337 168 HVELPHINLLSKMDliehygklafnldyytevldlsylldhlasdpffrhyrqlneklvqliedysLVSFIPLNIQDKES 247
Cdd:cd17868 161 RLELPQINVISKMD----------------------------------------------------LLDFIPLNYSDEES 188

                       250
                ....*....|
gi 88759337 248 IQRVLQAVDK 257
Cdd:cd17868 189 IKLLLQNIDK 198
ATP_bind_1 pfam03029
Conserved hypothetical ATP binding protein; Members of this family are found in a range of ...
 14-261 7.45e-88

Conserved hypothetical ATP binding protein; Members of this family are found in a range of archaea and eukaryotes and have hypothesized ATP binding activity.


Pssm-ID: 397252 [Multi-domain]  Cd Length: 238  Bit Score: 262.69  E-value: 7.45e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337    14 VIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYECAVDVGELVGLGDVMDALRLGPNGGLLYCMEYLEANLD 93
Cdd:pfam03029   1 VVGPAGSGKTTFVGALSEILPLRGRPVYVVNLDPAAENLPYPADIDIRELITVADVMEDYGLGPNGALTVAMDFGRITLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337    94 WLRAKLDpLRGHYFLFDCPGQVELCTHHGALRSIFSQMAQwDLRLTAVHLVDSHYCTDPAKFISVLCTSLATMLHVELPH 173
Cdd:pfam03029  81 WLDEELK-REDDYYLFDTPGQIELFTHWDSLAIIVEALES-RGALGAVYLVDTRRLTDPTDFFSGLLYALSIMLRLGLPF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337   174 INLLSKMDLIehygKLAFNLDYYTEVLDLSYLLDHLASdpffrHYRQLNEKLVQLIEDYSLV-SFIPLNIQDKESIQRVL 252
Cdd:pfam03029 159 VVALNKFDLL----SLEFALKWFTDPEDLQLLLELDDG-----KYRKLNEAIREALDLFYLVpVFLPDARERGESMEDLL 229


                  ....*....
gi 88759337   253 QAVDKANGY 261
Cdd:pfam03029 230 TLIDEALQY 238
GPN3 cd17872
GPN-loop GTPase 3; GPN-loop GTPase 3 (GPN3) is a small GTPase that is required for nuclear ...
 10-256 5.72e-85

GPN-loop GTPase 3; GPN-loop GTPase 3 (GPN3) is a small GTPase that is required for nuclear targeting of RNA polymerase II. It forms heterodimers with GPN1.


Pssm-ID: 349781 [Multi-domain]  Cd Length: 196  Bit Score: 253.60  E-value: 5.72e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  10 FGQAVIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYECAVDVGELVGLGDVMDALRLGPNGGLLYCMEYLE 89
Cdd:cd17872   1 YAQLVMGPAGSGKSTYCSTLQEHCETLGRSVHVVNLDPAAEEFEYPVSIDIRDLISLEDVMEELGLGPNGGLVYCMEYLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  90 ANLDWLRAKLDPLRGHYFLFDCPGQVELCTHHGALRSIFSQMAQWDLRLTAVHLVDSHYCTDPAKFISVLCTSLATMLHV 169
Cdd:cd17872  81 ENLDWLEEQLGDYEDDYLIFDCPGQIELYTHLPVMKRLVDALQRWGFRLCAVYLLDSQFISDASKFISGVLSALSAMIQL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337 170 ELPHINLLSKMDliehygklafnldyytevldlsylldhlasdpffrhyrqlneklvqliedysLVSFIPLNIQDKESIQ 249
Cdd:cd17872 161 ELPHVNVLTKMD----------------------------------------------------LVSFLPLDITDEESIN 188


                ....*..
gi 88759337 250 RVLQAVD 256
Cdd:cd17872 189 NVLSQID 195
PRK13768 PRK13768
GTPase; Provisional
 14-252 6.19e-40

GTPase; Provisional


Pssm-ID: 237498 [Multi-domain]  Cd Length: 253  Bit Score: 140.00  E-value: 6.19e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337   14 VIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYECAVDVGELVGLGDVMDALRLGPNGGLLYCMEYLEANLD 93
Cdd:PRK13768   7 FLGTAGSGKTTLTKALSDWLEEQGYDVAIVNLDPAVEYLPYTPDFDVRDYVTAREIMKKYGLGPNGALIASVDLLLTKAD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337   94 WLRAKLDPLRGHYFLFDCPGQVELCTHHGALRSIFSQMAQwDLRLTAVHLVDSHYCTDPAKFISVLCTSLATMLHVELPH 173
Cdd:PRK13768  87 EIKEEIESLDADYVLVDTPGQMELFAFRESGRKLVERLSG-SSKSVVVFLIDAVLAKTPSDFVSLLLLALSVQLRLGLPQ 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  174 INLLSKMDLIEhygklAFNLDYYTEVL-DLSYLLDHLASDPFFrhYRQLNEKLVQLIEDYSLVS-FIPLNIQDKES---- 247
Cdd:PRK13768 166 IPVLNKADLLS-----EEELERILKWLeDPEYLLEELKLEKGL--QGLLSLELLRALEETGLPVrVIPVSAKTGEGfdel 238


                 ....*...
gi 88759337  248 ---IQRVL 252
Cdd:PRK13768 239 yaaIQEVF 246
GPN1 cd17870
GPN-loop GTPase 1; GPN-loop GTPase 1 (GPN1, also kown as MBD2-interacting protein or MBDin, ...
 14-257 2.37e-31

GPN-loop GTPase 1; GPN-loop GTPase 1 (GPN1, also kown as MBD2-interacting protein or MBDin, RNAPII-associated protein 4, and XPA-binding protein 1) is a GTPase is required for nuclear targeting of RNA polymerase II. It forms heterodimers with GPN3.


Pssm-ID: 349779 [Multi-domain]  Cd Length: 241  Bit Score: 117.28  E-value: 2.37e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  14 VIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYECAVDVGELVGLGDVMDALRLGPNGGLLYCMEYLEANLD 93
Cdd:cd17870   5 VVGMAGSGKTTFVQRLNAYLHDNKKPPYVINLDPAVKSLPYPPNIDIRDTVNYKEVMKQYGLGPNGAIVTSLNLFATKFD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  94 WLRAKLDPL--RGHYFLFDCPGQVELCTHHgALRSIFSQMAQWDLRLTAVHLVDSHYCTDPAKFISVLCTSLATMLHVEL 171
Cdd:cd17870  85 QVINLIEKRasELDYVIIDTPGQIEVFTWS-ASGSIITEALASSFPTVVVYVVDTPRCTSPITFMSNMLYACSILYKTKL 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337 172 PHINLLSKMDLIEHygklAFNLDYYTevlDLSYLLDHLASDPffRHYRQLNEKLVQLIED-YSLVSFIPLNIQDKESIQR 250
Cdd:cd17870 164 PFILVFNKTDVVSH----DFAIEWME---DFESFQDALKEDS--SYMSSLSRSMSLVLDEfYNNLRVVGVSAKTGEGFEE 234


                ....*..
gi 88759337 251 VLQAVDK 257
Cdd:cd17870 235 LLEAIDE 241
ParA COG1192
ParA-like ATPase involved in chromosome/plasmid partitioning or cellulose biosynthesis protein ...
 19-119 5.57e-05

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: 43.69  E-value: 5.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 88759337  19 GSGKTTYCLGMSEFLRALGRRVAVVNLDP-AN--EGL---PYECAVDVGE-LVGLGDVMDALRLGPNGGlLYC------M 85
Cdd:COG1192  12 GVGKTTTAVNLAAALARRGKRVLLIDLDPqGNltSGLgldPDDLDPTLYDlLLDDAPLEDAIVPTEIPG-LDLipanidL 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 88759337  86 EYLEANL-------DWLRAKLDPLRGHY--FLFDCPGQVELCT 119
Cdd:COG1192  91 AGAEIELvsrpgreLRLKRALAPLADDYdyILIDCPPSLGLLT 133
MMAA-like cd03114
methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB ...
 1-47 2.67e-04

methylmalonic aciduria associated protein; Methylmalonyl Co-A mutase-associated GTPase MeaB and its human homolog, methylmalonic aciduria associated protein (MMAA) are metallochaperones that function as a G-protein chaperone that assists AdoCbl cofactor delivery to the methylmalonyl-CoA mutase (MCM) and reactivation of the enzyme during catalysis. A member of the family, Escherichia coli ArgK, was previously thought to be a membrane ATPase which is required for transporting arginine, ornithine and lysine into the cells by the arginine and ornithine (AO system) and lysine, arginine and ornithine (LAO) transport systems.


Pssm-ID: 349768  Cd Length: 252  Bit Score: 41.79  E-value: 2.67e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 88759337   1 MAGAAPTTAFGQAVIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDP 47
Cdd:cd03114  38 ALLPQAGRAFRVGITGPPGAGKSTLIEALGRLLREQGHRVAVLAVDP 84
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 16-46 1.03e-03

Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK).


Pssm-ID: 238986 [Multi-domain]  Cd Length: 179  Bit Score: 39.21  E-value: 1.03e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 88759337  16 GPPGSGKTTYCLGMSEFLRALGRRVAVVNLD 46
Cdd:cd02028   6 GPSGSGKTTFAKKLSNQLRVNGIGPVVISLD 36
MeaB pfam03308
Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ...
 14-47 2.47e-03

Methylmalonyl Co-A mutase-associated GTPase MeaB; Family members were previously thought to be ArgK proteins acting as ATPase enzymes and kinases. They are now believed to be methylmalonyl Co-A mutase-associated GTPase MeaB. Structural studies of MeaB and the human ortholog (methylmalonyl associated protein A) MMAA, reveal alpha-helical domains at the N- and C-termini as well as a Ras-like GTPase domain. Mutational analysis of MeaB, show prohibited growth in Methylobacterium due to the inability to convert methylmalonyl-CoA to succinyl-CoA caused by an inactive form of methylmalonyl-CoA mutatase (mcm). In humans, mutations in (MMAA) are associated with the fatal disease methylmalonyl aciduria.


Pssm-ID: 281323 [Multi-domain]  Cd Length: 272  Bit Score: 38.96  E-value: 2.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 88759337    14 VIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDP 47
Cdd:pfam03308  38 VTGVPGAGKSTLIEALGMELRRRGHRVAVLAVDP 71
MobB cd03116
molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace ...
 13-43 3.08e-03

molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace element in the form of molybdenum cofactor (Moco) which is associated with the metabolism of nitrogen, carbon and sulfur by redox active enzymes. In Escherichia coli, the synthesis of Moco involves genes from several loci: moa, mob, mod, moe and mog. The mob locus contains mobA and mobB genes. MobB catalyzes the attachment of the guanine dinucleotide to molybdopterin.


Pssm-ID: 349770 [Multi-domain]  Cd Length: 157  Bit Score: 37.62  E-value: 3.08e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 88759337  13 AVIGPPGSGKTTYCLGMSEFLRALGRRVAVV 43
Cdd:cd03116   4 GVVGKSGSGKTTLIEKLIPELKARGLRVAVI 34
RecA-like_Thep1 cd19482
RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the ...
 13-40 3.17e-03

RecA-like domain of the nucleoside-triphosphatase THEP1 family; This family represents the THEP1 family ATPase domain. It includes nucleoside-triphosphatase THEP 1 from Aquifex aeolicus (aaTHEP1) a nucleoside-phosphatase, with activity towards ATP, GTP, CTP, TTP and UTP; and which may hydrolyze nucleoside diphosphates with lower efficiency. The catalytic function of aaTHEP1 remains unclear, it may be a DNA/RNA modifying enzyme. Human THEP1 (hsTHEP1) may have a general function in many human tissues, as it is widely expressed in most examined tissues (such as in brain, heart, lymph node, skin, pancreas); it is especially highly expressed in embryonic and various tumor tissues. This family belongs to the RecA-like NTPase superfamily which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410890 [Multi-domain]  Cd Length: 164  Bit Score: 37.58  E-value: 3.17e-03
                        10        20
                ....*....|....*....|....*...
gi 88759337  13 AVIGPPGSGKTTYCLGMSEFLRALGRRV 40
Cdd:cd19482   2 FITGPPGVGKTTLVLKVAELLKESGLKV 29
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 13-75 4.28e-03

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 36.97  E-value: 4.28e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 88759337     13 AVIGPPGSGKTTYCLGMSEFLRALGRRVAVVNLDPANEGLPYE-CAVDVGELVGLGDVMDALRL 75
Cdd:smart00382   6 LIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlLLIIVGGKKASGSGELRLRL 69
MobB COG1763
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ...
 13-43 4.90e-03

Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 441369 [Multi-domain]  Cd Length: 162  Bit Score: 37.08  E-value: 4.90e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 88759337  13 AVIGPPGSGKTTYCLGMSEFLRALGRRVAVV 43
Cdd:COG1763   5 GIVGYSGSGKTTLLEKLIPELKARGLRVGTI 35
DDXDc_reverse_gyrase cd17924
DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of ...
 13-43 5.19e-03

DDXD-box helicase domain of reverse gyrase; Reverse gyrase modifies the topological state of DNA by introducing positive supercoils in an ATP-dependent process. Reverse gyrase belongs to the type II DEAD box helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350682 [Multi-domain]  Cd Length: 189  Bit Score: 37.31  E-value: 5.19e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 88759337  13 AVIGPPGSGKTTYCLGMSEFLRALGRRVAVV 43
Cdd:cd17924  36 AIIAPTGVGKTTFGLATSLYLASKGKRSYLI 66
ParAB_family cd02042
partition proteins ParAB family; ParA and ParB of Caulobacter crescentus belong to a conserved ...
 19-47 6.46e-03

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: 36.36  E-value: 6.46e-03
                        10        20
                ....*....|....*....|....*....
gi 88759337  19 GSGKTTYCLGMSEFLRALGRRVAVVNLDP 47
Cdd:cd02042  11 GVGKTTLAVNLAAALALRGKRVLLIDLDP 39
COG4639 COG4639
Predicted kinase [General function prediction only];
15-46 7.31e-03

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 36.35  E-value: 7.31e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 88759337  15 IGPPGSGKTTyclgmseFLRALGRRVAVVNLD 46
Cdd:COG4639   8 IGLPGSGKST-------FARRLFAPTEVVSSD 32
THEP1 COG1618
Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];
13-41 7.88e-03

Nucleoside-triphosphatase THEP1 [Nucleotide transport and metabolism];


Pssm-ID: 441225 [Multi-domain]  Cd Length: 175  Bit Score: 36.42  E-value: 7.88e-03
                        10        20
                ....*....|....*....|....*....
gi 88759337  13 AVIGPPGSGKTTYCLGMSEFLRALGRRVA 41
Cdd:COG1618   4 FITGRPGVGKTTLLLKVVEELRDEGLRVG 32
AAA_31 pfam13614
AAA domain; This family includes a wide variety of AAA domains including some that have lost ...
 19-47 8.64e-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: 36.41  E-value: 8.64e-03
                          10        20
                  ....*....|....*....|....*....
gi 88759337    19 GSGKTTYCLGMSEFLRALGRRVAVVNLDP 47
Cdd:pfam13614  12 GVGKTTTSVNLAAALAKKGKKVLLIDLDP 40
 
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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