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Conserved domains on  [gi|24639713|ref|NP_525072|]
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partner of numb [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GBP_C super family cl46256
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 358-445 3.69e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


The actual alignment was detected with superfamily member cd16269:

Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.95  E-value: 3.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639713 358 RTLTEISEASEVEEDTEKLLEQDREAEviLEQEKILEQEMVSERERHLTREKQLKQEklLEREkhleREKLQEKLHEQLR 437
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLL--EEQQRELEQKLEDQERSYEEHLRQLKEK--MEEE----RENLLKEQERALE 262


                ....*...
gi 24639713 438 EKLQERAK 445
Cdd:cd16269 263 SKLKEQEA 270
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 270-443 1.19e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


The actual alignment was detected with superfamily member pfam17380:

Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.03  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639713   270 AISEESSMDIGKELDRYQLELENSINEaKLRKNGVLVD----RELPRNSLEVElPKNTKVSlvmetntQELMMQEVVTVD 345
Cdd:pfam17380 337 AEQERMAMERERELERIRQEERKRELE-RIRQEEIAMEisrmRELERLQMERQ-QKNERVR-------QELEAARKVKIL 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639713   346 TQVERRLVCTRRRTLTEI-SEASEVEEDTEKLLEQDREAEVileqEKILEQEMvsERERHLTREKQLKQEKLlEREKHLE 424
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIrAEQEEARQREVRRLEEERAREM----ERVRLEEQ--ERQQQVERLRQQEEERK-RKKLELE 480

                         170
                  ....*....|....*....
gi 24639713   425 REKLQEKLHEQLREKLQER 443
Cdd:pfam17380 481 KEKRDRKRAEEQRRKILEK 499
 
Name Accession Description Interval E-value
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 358-445 3.69e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.95  E-value: 3.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639713 358 RTLTEISEASEVEEDTEKLLEQDREAEviLEQEKILEQEMVSERERHLTREKQLKQEklLEREkhleREKLQEKLHEQLR 437
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLL--EEQQRELEQKLEDQERSYEEHLRQLKEK--MEEE----RENLLKEQERALE 262


                ....*...
gi 24639713 438 EKLQERAK 445
Cdd:cd16269 263 SKLKEQEA 270
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 270-443 1.19e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.03  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639713   270 AISEESSMDIGKELDRYQLELENSINEaKLRKNGVLVD----RELPRNSLEVElPKNTKVSlvmetntQELMMQEVVTVD 345
Cdd:pfam17380 337 AEQERMAMERERELERIRQEERKRELE-RIRQEEIAMEisrmRELERLQMERQ-QKNERVR-------QELEAARKVKIL 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639713   346 TQVERRLVCTRRRTLTEI-SEASEVEEDTEKLLEQDREAEVileqEKILEQEMvsERERHLTREKQLKQEKLlEREKHLE 424
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIrAEQEEARQREVRRLEEERAREM----ERVRLEEQ--ERQQQVERLRQQEEERK-RKKLELE 480

                         170
                  ....*....|....*....
gi 24639713   425 REKLQEKLHEQLREKLQER 443
Cdd:pfam17380 481 KEKRDRKRAEEQRRKILEK 499
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 356-446 2.40e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639713 356 RRRTLTEISEASEVEEDTEKLLEQDREAEVILEQEKILEQEMVSERERHLTREKQLKQEKLLEREKHLEREKLQEKLHEQ 435
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                        90
                ....*....|.
gi 24639713 436 LREKLQERAKH 446
Cdd:COG1196 409 EEALLERLERL 419
 
Name Accession Description Interval E-value
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 358-445 3.69e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.95  E-value: 3.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639713 358 RTLTEISEASEVEEDTEKLLEQDREAEviLEQEKILEQEMVSERERHLTREKQLKQEklLEREkhleREKLQEKLHEQLR 437
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLL--EEQQRELEQKLEDQERSYEEHLRQLKEK--MEEE----RENLLKEQERALE 262


                ....*...
gi 24639713 438 EKLQERAK 445
Cdd:cd16269 263 SKLKEQEA 270
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 270-443 1.19e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.03  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639713   270 AISEESSMDIGKELDRYQLELENSINEaKLRKNGVLVD----RELPRNSLEVElPKNTKVSlvmetntQELMMQEVVTVD 345
Cdd:pfam17380 337 AEQERMAMERERELERIRQEERKRELE-RIRQEEIAMEisrmRELERLQMERQ-QKNERVR-------QELEAARKVKIL 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639713   346 TQVERRLVCTRRRTLTEI-SEASEVEEDTEKLLEQDREAEVileqEKILEQEMvsERERHLTREKQLKQEKLlEREKHLE 424
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIrAEQEEARQREVRRLEEERAREM----ERVRLEEQ--ERQQQVERLRQQEEERK-RKKLELE 480

                         170
                  ....*....|....*....
gi 24639713   425 REKLQEKLHEQLREKLQER 443
Cdd:pfam17380 481 KEKRDRKRAEEQRRKILEK 499
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 356-446 2.40e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24639713 356 RRRTLTEISEASEVEEDTEKLLEQDREAEVILEQEKILEQEMVSERERHLTREKQLKQEKLLEREKHLEREKLQEKLHEQ 435
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                        90
                ....*....|.
gi 24639713 436 LREKLQERAKH 446
Cdd:COG1196 409 EEALLERLERL 419
 
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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