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Conserved domains on  [gi|1622831369|ref|XP_028687470|]
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guanylate-binding protein 2 isoform X2 [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
152-448 5.50e-161

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


:

Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 456.75  E-value: 5.50e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 152 GGIPVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVEKAIAHYEQQMGQKVQLPTETLQELLDLHRDSERE 231
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 232 AIEVFMKNSFKDVDQTFQRKLGAQLEARQDDFCKQNSKASSDCCMALLQDIFGPLEEDVKQGTFSKPGGYRLFIQKQQEL 311
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 312 KKKYYQVPRKGIQAEEVLKKYLESKEDVADALLQTDQSLSEKEKAIEVERIKAESAEAAKKMLEEIQKKNEQMMEQKEKS 391
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831369 392 YQEHVKQLTEKMERDRAQLMAEQEKTLALKLQEQERLLKEGFKNESQRLQKEIRDIQ 448
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP super family cl46410
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
1-150 5.11e-75

Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


The actual alignment was detected with superfamily member pfam02263:

Pssm-ID: 460516  Cd Length: 260  Bit Score: 235.73  E-value: 5.11e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369   1 MGTINQQAMDQLHYVTELTDRikanSSPGNNSVEDSADFVSFFPAFVWTLRDFTLELEVDGEPITADDYLELSLKLRQGT 80
Cdd:pfam02263 114 SQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFVWTVRDFSLPLEADGGPITGDEYLENRLKLSQGQ 189
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622831369  81 DKKSKSFNDPRLCIRKFFPNRKCFIFDWPAQKKYL-ARLEQLKEEELNPDFIEQVAEFCSYILSHSNVKTL 150
Cdd:pfam02263 190 HEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALnPQFEGLREDELDPEFQQQLREFCSYILSHSLVKTL 260
 
Name Accession Description Interval E-value
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
152-448 5.50e-161

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 456.75  E-value: 5.50e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 152 GGIPVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVEKAIAHYEQQMGQKVQLPTETLQELLDLHRDSERE 231
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 232 AIEVFMKNSFKDVDQTFQRKLGAQLEARQDDFCKQNSKASSDCCMALLQDIFGPLEEDVKQGTFSKPGGYRLFIQKQQEL 311
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 312 KKKYYQVPRKGIQAEEVLKKYLESKEDVADALLQTDQSLSEKEKAIEVERIKAESAEAAKKMLEEIQKKNEQMMEQKEKS 391
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831369 392 YQEHVKQLTEKMERDRAQLMAEQEKTLALKLQEQERLLKEGFKNESQRLQKEIRDIQ 448
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
158-448 1.87e-145

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: 416.98  E-value: 1.87e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 158 GPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVEKAIAHYEQQMGQKVQLPTETLQELLDLHRDSEREAIEVFM 237
Cdd:cd16269     1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 238 KNSFKDVDQTFQRKLGAQLEARQDDFCKQNSKASSDCCMALLQDIFGPLEEDVKQGTFSKPGGYRLFIQKQQELKKKYYQ 317
Cdd:cd16269    81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISQGSYSVPGGYQLYLEDREKLVEKYRQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 318 VPRKGIQAEEVLKKYLESKEDVADALLQTDQSLSEKEKAIEVERIKAESAEAAKKMLEEIQKKNEQMMEQKEKSYQEHVK 397
Cdd:cd16269   161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622831369 398 QLTEKMERDRAQLMAEQEKTLALKLQEQERLLKEGFKNESQRLQKEIRDIQ 448
Cdd:cd16269   241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
1-150 5.11e-75

Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460516  Cd Length: 260  Bit Score: 235.73  E-value: 5.11e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369   1 MGTINQQAMDQLHYVTELTDRikanSSPGNNSVEDSADFVSFFPAFVWTLRDFTLELEVDGEPITADDYLELSLKLRQGT 80
Cdd:pfam02263 114 SQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFVWTVRDFSLPLEADGGPITGDEYLENRLKLSQGQ 189
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622831369  81 DKKSKSFNDPRLCIRKFFPNRKCFIFDWPAQKKYL-ARLEQLKEEELNPDFIEQVAEFCSYILSHSNVKTL 150
Cdd:pfam02263 190 HEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALnPQFEGLREDELDPEFQQQLREFCSYILSHSLVKTL 260
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
2-143 1.83e-18

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that 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. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 83.91  E-value: 1.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369   2 GTINQQAMDQLHYVTELTDRikansspgNNSVEDSADFVSFFPAFVWTLRDFTLELEVDGEPITaddylelslklrQGTD 81
Cdd:cd01851   103 QTILGDDLDKLMGLLKTALE--------TLGLAGLHNFSKPKPLLLFVVRDFTGPTPLEGLDVT------------EKSE 162
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622831369  82 KKSKSFNDPRLCIRKFFPNRKCFIFDWPAQKKYLARLEqLKEEELNPDFIEQVAEFCSYILS 143
Cdd:cd01851   163 TLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQND-GRLKDLPPEFRKALKALRQRFFS 223
PTZ00121 PTZ00121
MAEBL; Provisional
227-443 6.46e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 6.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369  227 DSEREAIEVFMKNSFKDVDQTFQRKLGAQLEARQDDFCKQNSKASSDCCMALLQDIFGPLEEDVKQGTFSKPGGYRLfiQ 306
Cdd:PTZ00121  1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL--K 1626
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369  307 KQQELKKKYYQVPRKgiQAEEVlKKYLESKEDVADALLQTDQslsEKEKAIEVERikaeSAEAAKKMLEEIQKKNEQMM- 385
Cdd:PTZ00121  1627 KAEEEKKKVEQLKKK--EAEEK-KKAEELKKAEEENKIKAAE---EAKKAEEDKK----KAEEAKKAEEDEKKAAEALKk 1696
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622831369  386 EQKEKSYQEHVKQLTEKMERDRAQLMAEQE----KTLALKLQEQERLLK-------EGFKNESQRLQKE 443
Cdd:PTZ00121  1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEenkiKAEEAKKEAEEDKKKaeeakkdEEEKKKIAHLKKE 1765
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
306-448 5.26e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 306 QKQQELKKKYYQVPRKGIQAEEVLKKYLESKEDVADALLQTDQSLSEKEKAI-----EVERIKAESAEAAK--KMLEEIQ 378
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleeELEELEEELEEAEEelEEAEAEL 360
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 379 KKNEQMMEQKEKSYQEhvkQLTEKMERDRAQLMAEQEKTLALKLQEQERLLKEGFKNESQRLQKEIRDIQ 448
Cdd:COG1196   361 AEAEEALLEAEAELAE---AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
growth_prot_Scy NF041483
polarized growth protein Scy;
334-439 1.89e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.96  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369  334 ESKEDVADALLQTDQSLSEKEKaiEVERIKAESAEAAKKMLEEIQKKNEQMMEQKEK---SYQEHVKQLTEKMERDRAQL 410
Cdd:NF041483   925 EAERLTAEARAEAERLRDEARA--EAERVRADAAAQAEQLIAEATGEAERLRAEAAEtvgSAQQHAERIRTEAERVKAEA 1002
                           90       100
                   ....*....|....*....|....*....
gi 1622831369  411 MAEQEKTLALKLQEQERLLKEGFKNESQR 439
Cdd:NF041483  1003 AAEAERLRTEAREEADRTLDEARKDANKR 1031
 
Name Accession Description Interval E-value
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
152-448 5.50e-161

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 456.75  E-value: 5.50e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 152 GGIPVNGPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVEKAIAHYEQQMGQKVQLPTETLQELLDLHRDSERE 231
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 232 AIEVFMKNSFKDVDQTFQRKLGAQLEARQDDFCKQNSKASSDCCMALLQDIFGPLEEDVKQGTFSKPGGYRLFIQKQQEL 311
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 312 KKKYYQVPRKGIQAEEVLKKYLESKEDVADALLQTDQSLSEKEKAIEVERIKAESAEAAKKMLEEIQKKNEQMMEQKEKS 391
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622831369 392 YQEHVKQLTEKMERDRAQLMAEQEKTLALKLQEQERLLKEGFKNESQRLQKEIRDIQ 448
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
158-448 1.87e-145

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: 416.98  E-value: 1.87e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 158 GPRLESLVLTYVNAISSGDLPCMENAVLALAQIENSAAVEKAIAHYEQQMGQKVQLPTETLQELLDLHRDSEREAIEVFM 237
Cdd:cd16269     1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 238 KNSFKDVDQTFQRKLGAQLEARQDDFCKQNSKASSDCCMALLQDIFGPLEEDVKQGTFSKPGGYRLFIQKQQELKKKYYQ 317
Cdd:cd16269    81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISQGSYSVPGGYQLYLEDREKLVEKYRQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 318 VPRKGIQAEEVLKKYLESKEDVADALLQTDQSLSEKEKAIEVERIKAESAEAAKKMLEEIQKKNEQMMEQKEKSYQEHVK 397
Cdd:cd16269   161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622831369 398 QLTEKMERDRAQLMAEQEKTLALKLQEQERLLKEGFKNESQRLQKEIRDIQ 448
Cdd:cd16269   241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
1-150 5.11e-75

Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460516  Cd Length: 260  Bit Score: 235.73  E-value: 5.11e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369   1 MGTINQQAMDQLHYVTELTDRikanSSPGNNSVEDSADFVSFFPAFVWTLRDFTLELEVDGEPITADDYLELSLKLRQGT 80
Cdd:pfam02263 114 SQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFVWTVRDFSLPLEADGGPITGDEYLENRLKLSQGQ 189
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622831369  81 DKKSKSFNDPRLCIRKFFPNRKCFIFDWPAQKKYL-ARLEQLKEEELNPDFIEQVAEFCSYILSHSNVKTL 150
Cdd:pfam02263 190 HEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALnPQFEGLREDELDPEFQQQLREFCSYILSHSLVKTL 260
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
2-143 1.83e-18

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that 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. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 83.91  E-value: 1.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369   2 GTINQQAMDQLHYVTELTDRikansspgNNSVEDSADFVSFFPAFVWTLRDFTLELEVDGEPITaddylelslklrQGTD 81
Cdd:cd01851   103 QTILGDDLDKLMGLLKTALE--------TLGLAGLHNFSKPKPLLLFVVRDFTGPTPLEGLDVT------------EKSE 162
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622831369  82 KKSKSFNDPRLCIRKFFPNRKCFIFDWPAQKKYLARLEqLKEEELNPDFIEQVAEFCSYILS 143
Cdd:cd01851   163 TLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQND-GRLKDLPPEFRKALKALRQRFFS 223
PTZ00121 PTZ00121
MAEBL; Provisional
227-443 6.46e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 6.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369  227 DSEREAIEVFMKNSFKDVDQTFQRKLGAQLEARQDDFCKQNSKASSDCCMALLQDIFGPLEEDVKQGTFSKPGGYRLfiQ 306
Cdd:PTZ00121  1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL--K 1626
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369  307 KQQELKKKYYQVPRKgiQAEEVlKKYLESKEDVADALLQTDQslsEKEKAIEVERikaeSAEAAKKMLEEIQKKNEQMM- 385
Cdd:PTZ00121  1627 KAEEEKKKVEQLKKK--EAEEK-KKAEELKKAEEENKIKAAE---EAKKAEEDKK----KAEEAKKAEEDEKKAAEALKk 1696
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622831369  386 EQKEKSYQEHVKQLTEKMERDRAQLMAEQE----KTLALKLQEQERLLK-------EGFKNESQRLQKE 443
Cdd:PTZ00121  1697 EAEEAKKAEELKKKEAEEKKKAEELKKAEEenkiKAEEAKKEAEEDKKKaeeakkdEEEKKKIAHLKKE 1765
PTZ00121 PTZ00121
MAEBL; Provisional
305-450 2.64e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 2.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369  305 IQKQQELKKKYYQVPRKGIQAE--EVLKKYLESKEDVADALLQTDQSLSEKEKAIEVERIKAESAEAAKKmlEEIQKKNE 382
Cdd:PTZ00121  1436 AKKKAEEAKKADEAKKKAEEAKkaEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA--AEAKKKAD 1513
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622831369  383 QMMEQKEKSYQEHVKQLTEKMERDRAQLMAEQEKTLALKLQEQERLLKEGFKNESQRLQKEIRDIQMR 450
Cdd:PTZ00121  1514 EAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
PTZ00121 PTZ00121
MAEBL; Provisional
305-442 4.90e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 4.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369  305 IQKQQELKKKyyqvPRKGIQAEEVLKKYLESKEDvADALlqtDQSLSEKEKAIEVERIKAESAEAAKKMLEEIQKKNEQM 384
Cdd:PTZ00121  1301 KKKADEAKKK----AEEAKKADEAKKKAEEAKKK-ADAA---KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369  385 MEQKEKSYQEHVKQLTEKMERDRAQLMAEQEKTLA--LKLQEQERLLKEGFKNESQRLQK 442
Cdd:PTZ00121  1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAKKKAEEKKK 1432
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
303-447 1.90e-04

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 43.88  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 303 LFIQKQQELKK-KYYQVPRKGIQ--AEEVLKKYLESKEDvADALLQTDQSLSEKEKAIEVERIKAEsaeaaKKMLEEIQK 379
Cdd:pfam10168 566 LKLQKEQQLQElQSLEEERKSLSerAEKLAEKYEEIKDK-QEKLMRRCKKVLQRLNSQLPVLSDAE-----REMKKELET 639
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622831369 380 KNEQMmeqkeKSYQEHVKQLTEKMERDRAQLMAEQE--KTLALKL-QEQERLLKEGFKNESQ---RLQKEIRDI 447
Cdd:pfam10168 640 INEQL-----KHLANAIKQAKKKMNYQRYQIAKSQSirKKSSLSLsEKQRKTIKEILKQLGSeidELIKQVKDI 708
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
306-448 5.26e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 306 QKQQELKKKYYQVPRKGIQAEEVLKKYLESKEDVADALLQTDQSLSEKEKAI-----EVERIKAESAEAAK--KMLEEIQ 378
Cdd:COG1196   281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELeeleeELEELEEELEEAEEelEEAEAEL 360
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 379 KKNEQMMEQKEKSYQEhvkQLTEKMERDRAQLMAEQEKTLALKLQEQERLLKEGFKNESQRLQKEIRDIQ 448
Cdd:COG1196   361 AEAEEALLEAEAELAE---AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
PTZ00121 PTZ00121
MAEBL; Provisional
306-455 8.09e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 8.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369  306 QKQQELKKKYYQVPRKGI---QAEEVLKKYLESKEdvADALlqtDQSLSEKEKAIEVERiKAESAEAA---KKMLEEIQK 379
Cdd:PTZ00121  1398 KKAEEDKKKADELKKAAAakkKADEAKKKAEEKKK--ADEA---KKKAEEAKKADEAKK-KAEEAKKAeeaKKKAEEAKK 1471
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622831369  380 KNEQMMEQKEKSYQEHVKQLTEKMERDRAQL-MAEQEKTLA--LKLQEQERLLKEGFKNESQRLQKEIRDIQMRSKSQQ 455
Cdd:PTZ00121  1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAkKAAEAKKKAdeAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADE 1550
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
306-455 1.04e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 306 QKQQELKKKYYQVPRKGIQAEEVLKKYLESKEDVADALLQTDQSLSEKEKAIEvERIKAESAEAAKKM-----LEEIQKK 380
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA-EAEEELEELAEELLealraAAELAAQ 401
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622831369 381 NEQMMEQKEKSYQEHVKQLTEKMERDRAQLMAEQEKTLALKLQEQERLLKEGFKNESQRLQKEIRDIQMRSKSQQ 455
Cdd:COG1196   402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
PTZ00121 PTZ00121
MAEBL; Provisional
324-455 1.35e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369  324 QAEEVLKKYLESKEDVADALLQTDQSLSEKEKAIEVERiKAES----AEAAKKMLEEIQKKNEqMMEQKEKSYQEHVKQL 399
Cdd:PTZ00121  1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK-KAEEakkkADAAKKKAEEAKKAAE-AAKAEAEAAADEAEAA 1362
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1622831369  400 TEKMERDRAQLMAEQEKTLALKLQEQERLLKEGFKNESQRLQKEIRDIQMRSKSQQ 455
Cdd:PTZ00121  1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKK 1418
PTZ00121 PTZ00121
MAEBL; Provisional
306-442 1.38e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369  306 QKQQELKKKYYQVPRKgiqAEEVlKKYLESKEDVADALLQTDQSLSEKEKAIEVERIKA-ESAEAAKKMLEEIQKKNE-- 382
Cdd:PTZ00121  1322 KKAEEAKKKADAAKKK---AEEA-KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAkKKADAAKKKAEEKKKADEak 1397
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622831369  383 QMMEQKEKSYQEHVKQLTEKMERDRAQLMAEQ-EKTLALKLQEQERLLKEGFKNESQRLQK 442
Cdd:PTZ00121  1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEkKKADEAKKKAEEAKKADEAKKKAEEAKK 1458
PRK12704 PRK12704
phosphodiesterase; Provisional
363-453 1.63e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 363 KAESAEA-AKKMLEEIQKKNEQMMEQKEKSYQEHVKQLTEKMERD---RAQLMAEQEKTLalkLQEQERLlkegfKNESQ 438
Cdd:PRK12704   32 KIKEAEEeAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKElreRRNELQKLEKRL---LQKEENL-----DRKLE 103
                          90
                  ....*....|....*
gi 1622831369 439 RLQKEIRDIQMRSKS 453
Cdd:PRK12704  104 LLEKREEELEKKEKE 118
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
312-452 1.66e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 312 KKKYYQVPRK---GIQAEEVlKKYLESKEDVADALL-QTDQSLSEKEKaiEVERIKAESAEAAKKMLEEIQKKNEQMmeq 387
Cdd:COG2433   349 KNKFERVEKKvppDVDRDEV-KARVIRGLSIEEALEeLIEKELPEEEP--EAEREKEHEERELTEEEEEIRRLEEQV--- 422
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622831369 388 keKSYQEHVKQLTEKMERDRAQLMAEQEKTLALKLQEQERLLKE----GFKNESQRLQKEIRDIQMRSK 452
Cdd:COG2433   423 --ERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDreisRLDREIERLERELEEERERIE 489
growth_prot_Scy NF041483
polarized growth protein Scy;
334-439 1.89e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 40.96  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369  334 ESKEDVADALLQTDQSLSEKEKaiEVERIKAESAEAAKKMLEEIQKKNEQMMEQKEK---SYQEHVKQLTEKMERDRAQL 410
Cdd:NF041483   925 EAERLTAEARAEAERLRDEARA--EAERVRADAAAQAEQLIAEATGEAERLRAEAAEtvgSAQQHAERIRTEAERVKAEA 1002
                           90       100
                   ....*....|....*....|....*....
gi 1622831369  411 MAEQEKTLALKLQEQERLLKEGFKNESQR 439
Cdd:NF041483  1003 AAEAERLRTEAREEADRTLDEARKDANKR 1031
PTZ00121 PTZ00121
MAEBL; Provisional
306-443 3.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369  306 QKQQELKKKYYQVPRKgiqAEEVLKKYLESKEdvADALLQTDQSLSEKEKAIEVERIKAESAEAA--KKMLEEIQKKNE- 382
Cdd:PTZ00121  1483 KKADEAKKKAEEAKKK---ADEAKKAAEAKKK--ADEAKKAEEAKKADEAKKAEEAKKADEAKKAeeKKKADELKKAEEl 1557
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622831369  383 QMMEQKEKSYQEHVKQLTEKMERDRAQLMAEQEKTlalKLQEQERLLKEGFKNESQRLQKE 443
Cdd:PTZ00121  1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEA---RIEEVMKLYEEEKKMKAEEAKKA 1615
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
348-445 5.95e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.04  E-value: 5.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 348 QSLSEKEKAIEVERIKAESAeaakkmLEEIQKKNEQMMEQKEkSYQEHVKQLTEKMERDRAQLMAEQEKTLALKLQEQER 427
Cdd:PRK00409  523 ASLEELERELEQKAEEAEAL------LKEAEKLKEELEEKKE-KLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQ 595
                          90
                  ....*....|....*...
gi 1622831369 428 LLKEGFKNESQRLQKEIR 445
Cdd:PRK00409  596 LQKGGYASVKAHELIEAR 613
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
305-436 7.06e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.04  E-value: 7.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622831369 305 IQKQQELKKKYYQVPRKGIQAEEVLKKYLESKEDVADALlqtDQSLSEKEKAIEvERIKAESAEAAKKMLEEIQKKNEQM 384
Cdd:PRK00409  526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEE---DKLLEEAEKEAQ-QAIKEAKKEADEIIKELRQLQKGGY 601
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622831369 385 MEQKEKSYQEHVKQLTEKMERDRAQLMAEQEKTLALKLQEQERLLKEGFKNE 436
Cdd:PRK00409  602 ASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVGDEVKYLSLGQKGE 653
 
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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