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Conserved domains on  [gi|116812914|ref|NP_001034735|]
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guanylate-binding protein 10 [Mus musculus]

Protein Classification

guanylate-binding family protein( domain architecture ID 12033579)

guanylate-binding family protein such as guanylate-binding protein 1 (GBP1), which is induced by interferon and hydrolyzes GTP to GMP in 2 consecutive cleavage reactions, is a large GTPase of the dynamin superfamily involved in the regulation of membrane, cytoskeleton, and cell cycle progression dynamics

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 ...
 281-575 6.04e-149

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: 431.71  E-value: 6.04e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  281 EGIKVTGNKLGILVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKE 360
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  361 AMAVFMEHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENIS--TFFVPCGHKLYMDKREKI 438
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  439 EHDYWQVPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKS 518
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116812914  519 HKENIEQLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEGFKKKAEEMNKEIQQLR 575
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 16-279 1.10e-141

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: 411.77  E-value: 1.10e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914   16 NEQLSVNQEAIEILDKISQPVVVVAIVGWSRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914   96 TEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMITINHQALEQLHYVTELTELirakSSPNPAGIKNSTEFVSFFPDFV 175
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  176 WIVRDFMLELKLNGEDITSDDYLENALKLIPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKLDSITEDQL 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236

                         250       260
                  ....*....|....*....|....
gi 116812914  256 DPKFQEVTKAFVSYIFTYAKIKTL 279
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
 
Name Accession Description Interval E-value
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 281-575 6.04e-149

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: 431.71  E-value: 6.04e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  281 EGIKVTGNKLGILVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKE 360
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  361 AMAVFMEHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENIS--TFFVPCGHKLYMDKREKI 438
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  439 EHDYWQVPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKS 518
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116812914  519 HKENIEQLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEGFKKKAEEMNKEIQQLR 575
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 16-279 1.10e-141

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: 411.77  E-value: 1.10e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914   16 NEQLSVNQEAIEILDKISQPVVVVAIVGWSRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914   96 TEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMITINHQALEQLHYVTELTELirakSSPNPAGIKNSTEFVSFFPDFV 175
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  176 WIVRDFMLELKLNGEDITSDDYLENALKLIPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKLDSITEDQL 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236

                         250       260
                  ....*....|....*....|....
gi 116812914  256 DPKFQEVTKAFVSYIFTYAKIKTL 279
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 287-575 8.56e-139

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: 405.42  E-value: 8.56e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 287 GNKLGILVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKEAMAVFM 366
Cdd:cd16269    1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 367 EHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENIS--TFFVPCGHKLYMDKREKIEHDYWQ 444
Cdd:cd16269   81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 445 VPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENIE 524
Cdd:cd16269  161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 116812914 525 QLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEGFKKKAEEMNKEIQQLR 575
Cdd:cd16269  241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 31-272 3.52e-68

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: 221.04  E-value: 3.52e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  31 KISQPVVVVAIVGWSRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHP--TKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:cd01851    2 DVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEFE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 109 NDLWIFALSVLLSSTFIYNSMITINHQALEQLHYVTELTElirakSSPNPAGIKNsteFVSFFPDFVWIVRDFMLELKLN 188
Cdd:cd01851   82 NDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL-----ETLGLAGLHN---FSKPKPLLLFVVRDFTGPTPLE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 189 GEDITsddylenalkliPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKldSITEDQLDPKFQEVTKAFVS 268
Cdd:cd01851  154 GLDVT------------EKSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKALRQ 219


                 ....
gi 116812914 269 YIFT 272
Cdd:cd01851  220 RFFS 223
YeeP COG3596
Predicted GTPase [General function prediction only];
1-108 2.12e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 46.68  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914   1 MTQPQMAPICLVENHNEQLSVNQEAI-EILD--KISQPVVVVAIVGWSRTGKSYLMNCLAGQN-----HGFPlgstvqsQ 72
Cdd:COG3596    1 MSTEVSSLTERLEALKRLPQVLRELLaEALErlLVELPPPVIALVGKTGAGKSSLINALFGAEvaevgVGRP-------C 73

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 116812914  73 TKGIwmWCMPHPTKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:COG3596   74 TREI--QRYRLESDGLPGLVLLDTPGLGEVNERDRE 107
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 485-574 1.20e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.80  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 485 AEERAQKVAAEKEQDlLRQKQKEQQEYMEAQEKshKENIEQLRRKLMQEREQLIKDHnmmlKKQLKDQKAFLEEGFKKKA 564
Cdd:PRK09510  77 AEEQRKKKEQQQAEE-LQQKQAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALK----QKQAEEAAAKAAAAAKAKA 149

                         90
                 ....*....|
gi 116812914 565 EEMNKEIQQL 574
Cdd:PRK09510 150 EAEAKRAAAA 159
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 471-592 1.16e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 471 LQA-DTALTAGKKAIAEERAQKVAAEKEQDLLRQ---KQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQL-----IKDH 541
Cdd:COG1579   12 LQElDSELDRLEHRLKELPAELAELEDELAALEArleAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEY 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 116812914 542 NMMLKK--QLKDQKAFLEE---GFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:COG1579   92 EALQKEieSLKRRISDLEDeilELMERIEELEEELAELEAELAELEAELEEKKAEL 147
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 486-592 4.05e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  486 EERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQL--IKDHNMMLKKQLKDQKAFLEEgFKKK 563
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkkLNEEKKELEEKVKDLTKKISS-LKEK 525

                          90       100
                  ....*....|....*....|....*....
gi 116812914  564 AEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKDDFEL 554
 
Name Accession Description Interval E-value
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 281-575 6.04e-149

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: 431.71  E-value: 6.04e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  281 EGIKVTGNKLGILVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKE 360
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  361 AMAVFMEHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENIS--TFFVPCGHKLYMDKREKI 438
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  439 EHDYWQVPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKS 518
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 116812914  519 HKENIEQLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEGFKKKAEEMNKEIQQLR 575
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 16-279 1.10e-141

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: 411.77  E-value: 1.10e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914   16 NEQLSVNQEAIEILDKISQPVVVVAIVGWSRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHPTKPEHTLVLLD 95
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914   96 TEGLGDVEKGDPKNDLWIFALSVLLSSTFIYNSMITINHQALEQLHYVTELTELirakSSPNPAGIKNSTEFVSFFPDFV 175
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  176 WIVRDFMLELKLNGEDITSDDYLENALKLIPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKLDSITEDQL 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236

                         250       260
                  ....*....|....*....|....
gi 116812914  256 DPKFQEVTKAFVSYIFTYAKIKTL 279
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 287-575 8.56e-139

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: 405.42  E-value: 8.56e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 287 GNKLGILVTTYVDAINSGAVPCLDDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKEAMAVFM 366
Cdd:cd16269    1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 367 EHSFKDENQQFLKKLVELIGENKELFLSKNEEASNKYCQEELDRLSKDFMENIS--TFFVPCGHKLYMDKREKIEHDYWQ 444
Cdd:cd16269   81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 445 VPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENIE 524
Cdd:cd16269  161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 116812914 525 QLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEGFKKKAEEMNKEIQQLR 575
Cdd:cd16269  241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 31-272 3.52e-68

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: 221.04  E-value: 3.52e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  31 KISQPVVVVAIVGWSRTGKSYLMNCLAGQNHGFPLGSTVQSQTKGIWMWCMPHP--TKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:cd01851    2 DVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEFE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 109 NDLWIFALSVLLSSTFIYNSMITINHQALEQLHYVTELTElirakSSPNPAGIKNsteFVSFFPDFVWIVRDFMLELKLN 188
Cdd:cd01851   82 NDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL-----ETLGLAGLHN---FSKPKPLLLFVVRDFTGPTPLE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 189 GEDITsddylenalkliPGDKPRMQASNSCRECIRLFFPNRKCFVFDRPTHDKELLQKldSITEDQLDPKFQEVTKAFVS 268
Cdd:cd01851  154 GLDVT------------EKSETLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKALRQ 219


                 ....
gi 116812914 269 YIFT 272
Cdd:cd01851  220 RFFS 223
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 40-115 1.14e-06

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 48.61  E-value: 1.14e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116812914  40 AIVGWSRTGKSYLMNCLAGQNHGFPlgSTVQSQTKGIWMWCMPHPtKPEHTLVLLDTEGLGDVEKGDPKNDLWIFA 115
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEV--SDVPGTTRDPDVYVKELD-KGKVKLVLVDTPGLDEFGGLGREELARLLL 73
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 436-593 1.32e-06

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 51.76  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914   436 EKIEHDYW-----QVPRKGVKASEVFQSFLQSQAFIESSILQADTALTAGKKAiaEERAQKVAAEKEQDLLR---QKQKE 507
Cdd:pfam12128  588 KRIDVPEWaaseeELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASRE--ETFARTALKNARLDLRRlfdEKQSE 665

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914   508 QQEyMEAQEKSHKENIEQLRRKLMQEREQLIKDHnmmlkkqlkdqKAFLEEgFKKKAEEMNKEIQQ-LRDVIKDKKRNTD 586
Cdd:pfam12128  666 KDK-KNKALAERKDSANERLNSLEAQLKQLDKKH-----------QAWLEE-QKEQKREARTEKQAyWQVVEGALDAQLA 732


                   ....*..
gi 116812914   587 RIKDALL 593
Cdd:pfam12128  733 LLKAAIA 739
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 316-591 4.19e-06

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: 49.74  E-value: 4.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  316 LAQRENSVAVQKAADHYSEQMAQRLRLptetlqelldvhaacEKEAMAVFMEHSFKDEN-----QQFLKKLVELIGENKE 390
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQ---------------EKEEKAREVERRRKLEEaekarQAEMDRQAAIYAEQER 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  391 LFLSKNEEASNKYCQE---ELDRLSKDF----MENISTFfvpcgHKLYMDKREKIEH--DYWQVPRKGVKASEVFQSFLQ 461
Cdd:pfam17380 342 MAMERERELERIRQEErkrELERIRQEEiameISRMREL-----ERLQMERQQKNERvrQELEAARKVKILEEERQRKIQ 416

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  462 SQAFIESSI-LQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQ----------EKSHKENIEQLRRKL 530
Cdd:pfam17380 417 QQKVEMEQIrAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEErkrkklelekEKRDRKRAEEQRRKI 496

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116812914  531 ----MQEREQLI---KDHNMMLKKQLKD-QKAFLEEGFKKKAEEMNKEIQQlrdvIKDKKRNTDRIKDA 591
Cdd:pfam17380 497 lekeLEERKQAMieeERKRKLLEKEMEErQKAIYEEERRREAEEERRKQQE----MEERRRIQEQMRKA 561
YeeP COG3596
Predicted GTPase [General function prediction only];
1-108 2.12e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 46.68  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914   1 MTQPQMAPICLVENHNEQLSVNQEAI-EILD--KISQPVVVVAIVGWSRTGKSYLMNCLAGQN-----HGFPlgstvqsQ 72
Cdd:COG3596    1 MSTEVSSLTERLEALKRLPQVLRELLaEALErlLVELPPPVIALVGKTGAGKSSLINALFGAEvaevgVGRP-------C 73

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 116812914  73 TKGIwmWCMPHPTKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:COG3596   74 TREI--QRYRLESDGLPGLVLLDTPGLGEVNERDRE 107
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 485-574 1.20e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 44.80  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 485 AEERAQKVAAEKEQDlLRQKQKEQQEYMEAQEKshKENIEQLRRKLMQEREQLIKDHnmmlKKQLKDQKAFLEEGFKKKA 564
Cdd:PRK09510  77 AEEQRKKKEQQQAEE-LQQKQAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALK----QKQAEEAAAKAAAAAKAKA 149

                         90
                 ....*....|
gi 116812914 565 EEMNKEIQQL 574
Cdd:PRK09510 150 EAEAKRAAAA 159
PTZ00121 PTZ00121
MAEBL; Provisional
 482-591 6.40e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  482 KAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSH-KENIEQLRRKLMQER--EQLIKDHNMM-----LKKQLKDQK 553
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEeAKKADEAKKKAEEAKkaEEAKKKAEEAkkadeAKKKAEEAK 1483

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 116812914  554 AflEEGFKKKAEEMNKEIQQLRDVIKDKKRnTDRIKDA 591
Cdd:PTZ00121 1484 K--ADEAKKKAEEAKKKADEAKKAAEAKKK-ADEAKKA 1518
PTZ00121 PTZ00121
MAEBL; Provisional
 472-591 7.39e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  472 QADTALTAGKKAIAEE--RAQKVAAEKEQDLLRQKQKEQQEYMEAQEKShkENIEQLRRKLMQEREQLIKDHNMMLKKQL 549
Cdd:PTZ00121 1535 KADEAKKAEEKKKADElkKAEELKKAEEKKKAEEAKKAEEDKNMALRKA--EEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 116812914  550 KDQKaflEEGFK----KKAEEMNKEIQQLRDVIKDKKRNTDRIKDA 591
Cdd:PTZ00121 1613 KKAE---EAKIKaeelKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
PRK12704 PRK12704
phosphodiesterase; Provisional
 481-593 7.57e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 7.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 481 KKAIAEERAQKV--AAEKEQDLLRQKQKEQ--QEYMEAQEKSHKENIEqlRRKLMQEREQLIKDHNMMLKKQLkdqkafl 556
Cdd:PRK12704  32 KIKEAEEEAKRIleEAKKEAEAIKKEALLEakEEIHKLRNEFEKELRE--RRNELQKLEKRLLQKEENLDRKL------- 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 116812914 557 eEGFKKKAEEMNK---EIQQLRDVIKDKKRNTDRIKDALL 593
Cdd:PRK12704 103 -ELLEKREEELEKkekELEQKQQELEKKEEELEELIEEQL 141
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 485-572 8.83e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.10  E-value: 8.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 485 AEERAQKVAAEKEqdllRQKQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEGFKKKA 564
Cdd:PRK09510  89 AEELQQKQAAEQE----RLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA 164


                 ....*...
gi 116812914 565 EEMNKEIQ 572
Cdd:PRK09510 165 AEAKKKAE 172
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 471-592 1.16e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 471 LQA-DTALTAGKKAIAEERAQKVAAEKEQDLLRQ---KQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQL-----IKDH 541
Cdd:COG1579   12 LQElDSELDRLEHRLKELPAELAELEDELAALEArleAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrnNKEY 91

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 116812914 542 NMMLKK--QLKDQKAFLEE---GFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:COG1579   92 EALQKEieSLKRRISDLEDeilELMERIEELEEELAELEAELAELEAELEEKKAEL 147
PTZ00121 PTZ00121
MAEBL; Provisional
 451-593 1.45e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  451 KASEVFQSFLQSQAFIESSILQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKE-----NIEQ 525
Cdd:PTZ00121 1627 KAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeakKAEE 1706

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116812914  526 LRRKLMQER---EQLIK--DHNMMLKKQLKDQkaflEEGFKKKAEEMNKE------IQQLRDVIKDKKRNTDRIKDALL 593
Cdd:PTZ00121 1707 LKKKEAEEKkkaEELKKaeEENKIKAEEAKKE----AEEDKKKAEEAKKDeeekkkIAHLKKEEEKKAEEIRKEKEAVI 1781
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 486-575 1.45e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 39.64  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  486 EERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKEnIEQLRRKLMQEREQLikdhnMMLKKQLKDQKAFLEEGFKKKAE 565
Cdd:pfam05672   9 AEEAARILAEKRRQAREQREREEQERLEKEEEERLR-KEELRRRAEEERARR-----EEEARRLEEERRREEEERQRKAE 82

                          90
                  ....*....|
gi 116812914  566 EMNKEIQQLR 575
Cdd:pfam05672  83 EEAEEREQRE 92
iSH2_PIK3R2 cd12926
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
 509-593 1.51e-03

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 2, PIK3R2, also called p85beta; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. p85beta, also called PIK3R2, contains N-terminal SH3 and GAP domains. It is expressed ubiquitously but at lower levels than p85alpha. Its expression is increased in breast and colon cancer, correlates with tumor progression, and enhanced invasion. During viral infection, the viral nonstructural (NS1) protein binds p85beta specifically, which leads to PI3K activation and the promotion of viral replication. Mice deficient with PIK3R2 develop normally and exhibit moderate metabolic and immunological defects.


Pssm-ID: 214019 [Multi-domain]  Cd Length: 161  Bit Score: 39.68  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 509 QEYMEAQEKSHKENIEQLRRKLMQEREQLIKDHNMMLKK---QLKDQKAFLEEGFKKKAEEmNKEIQQLRDVIKDKKRNT 585
Cdd:cd12926   56 EEQGQTQEKCSKEYLERFRREGNEKEMQRILLNSERLKSriaEIHESRTKLEQDLRAQASD-NREIDKRMNSLKPDLMQL 134


                 ....*...
gi 116812914 586 DRIKDALL 593
Cdd:cd12926  135 RKIRDQYL 142
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
294-594 2.24e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 2.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 294 VTTYVDAINSGAVpcLDDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVhaacekeamavfmehSFKDE 373
Cdd:COG3206   83 LETQIEILKSRPV--LERVVDKLNLDEDPLGEEASREAAIERLRKNLTVEPVKGSNVIEI---------------SYTSP 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 374 NQQFLKKLVELIGEN--KELFLSKNEEASN--KYCQEELDRLskdfmenistffvpcghklymdkREKIEhdywqvprkg 449
Cdd:COG3206  146 DPELAAAVANALAEAylEQNLELRREEARKalEFLEEQLPEL-----------------------RKELE---------- 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 450 vKASEVFQSFLQSQAFIESS--ILQADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKS-----HKEN 522
Cdd:COG3206  193 -EAEAALEEFRQKNGLVDLSeeAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpviqqLRAQ 271

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116812914 523 IEQLRRKLMQEREQLIKDHNMM--LKKQLKDQKAFLEEGFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDALLN 594
Cdd:COG3206  272 LAELEAELAELSARYTPNHPDViaLRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
PRK11637 PRK11637
AmiB activator; Provisional
 472-583 2.40e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 40.83  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 472 QADTALTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQLIK-DHNmmlKKQLK 550
Cdd:PRK11637 170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSElRAN---ESRLR 246

                         90       100       110
                 ....*....|....*....|....*....|...
gi 116812914 551 DQKAFLEEGFKKKAEEMNKEIQQLRDVIKDKKR 583
Cdd:PRK11637 247 DSIARAEREAKARAEREAREAARVRDKQKQAKR 279
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 481-573 2.53e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  481 KKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQ-------------------EKSHKENIEQLRRKLMQEREQLIKDH 541
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQDEKAERdelraklyqeeqerkerqkEREEAEKKARQRQELQQAREEQIELK 248

                          90       100       110
                  ....*....|....*....|....*....|..
gi 116812914  542 NMMLKKQLKDQKAFLEEGFKKKAEEMNKEIQQ 573
Cdd:pfam13868 249 ERRLAEEAEREEEEFERMLRKQAEDEEIEQEE 280
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 486-592 4.05e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.39  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  486 EERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQL--IKDHNMMLKKQLKDQKAFLEEgFKKK 563
Cdd:TIGR04523 447 NQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELkkLNEEKKELEEKVKDLTKKISS-LKEK 525

                          90       100
                  ....*....|....*....|....*....
gi 116812914  564 AEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:TIGR04523 526 IEKLESEKKEKESKISDLEDELNKDDFEL 554
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 486-573 4.30e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.10  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  486 EERAQKVAAEkeqdllRQKQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEGFKKKAE 565
Cdd:pfam05672  46 EELRRRAEEE------RARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQKEEAEAKAREEAERQRQ 119


                  ....*...
gi 116812914  566 EMNKEIQQ 573
Cdd:pfam05672 120 EREKIMQQ 127
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 476-611 4.72e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 476 ALTAGKKAIAEERAQKvAAEKEQDLLRQKQKEQQEYMEAQEKSHKENIEQLR--RKLMQEREQLIKDhnmmLKKQLKDQK 553
Cdd:COG4942    8 ALLLALAAAAQADAAA-EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalERRIAALARRIRA----LEQELAALE 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116812914 554 AFLEEgFKKKAEEMNKEIQQLRDVIKD------KKRNTDRIKdALLNGFSTVLFHYLVRYLKHL 611
Cdd:COG4942   83 AELAE-LEKEIAELRAELEAQKEELAEllralyRLGRQPPLA-LLLSPEDFLDAVRRLQYLKYL 144
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 485-569 4.81e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.93  E-value: 4.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  485 AEERAQKVAAE---KEQDLLRQKQKEQQEYMEAQEKSHKENIEQL-----RRKLMQEREQLikdhNMMLKKQLKDQKAFL 556
Cdd:pfam15709 417 AQERARQQQEEfrrKLQELQRKKQQEEAERAEAEKQRQKELEMQLaeeqkRLMEMAEEERL----EYQRQKQEAEEKARL 492

                          90
                  ....*....|....
gi 116812914  557 E-EGFKKKAEEMNK 569
Cdd:pfam15709 493 EaEERRQKEEEAAR 506
PTZ00121 PTZ00121
MAEBL; Provisional
 481-590 5.27e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  481 KKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQEKSHKEN---IEQLRRKLMQER----------------EQLIKDH 541
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENkikAEEAKKEAEEDKkkaeeakkdeeekkkiAHLKKEE 1766

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 116812914  542 NMMLKKQLKDQKAFLEEGFKKKAEEMNKEIQQlrdVIKDKKRNTDRIKD 590
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK---KIKDIFDNFANIIE 1812
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 485-593 5.86e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.13  E-value: 5.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  485 AEERAQKVAAEKEQDL--LRQKQKEQQEYMEAQEKSHKENIEQLRRKLMQEREQLIKDHNMMLKKQLKDQKAFLEEgfKK 562
Cdd:pfam13868 100 REQMDEIVERIQEEDQaeAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAER--EE 177

                          90       100       110
                  ....*....|....*....|....*....|....
gi 116812914  563 KAEEMNKEIQQLRDV---IKDKKRNTDRIKDALL 593
Cdd:pfam13868 178 IEEEKEREIARLRAQqekAQDEKAERDELRAKLY 211
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 27-69 8.32e-03

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 37.92  E-value: 8.32e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 116812914  27 EILDKIS---QPVVVVAIVGWSRTGKSYLMNCLAGQNHGFPLGSTV 69
Cdd:cd03213   23 QLLKNVSgkaKPGELTAIMGPSGAGKSTLLNALAGRRTGLGVSGEV 68
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
477-592 8.83e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 8.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914  477 LTAGKKAIAEERAQKVAAEKEQDLLRQKQKEQQEYMEAQE-----KSHKENIEQLRrklmQEREQLIKDHNMM--LKKQL 549
Cdd:COG4913   619 LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWdeidvASAEREIAELE----AELERLDASSDDLaaLEEQL 694

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 116812914  550 KDQKAFLEEgFKKKAEEMNKEIQQLRDVIKDKKRNTDRIKDAL 592
Cdd:COG4913   695 EELEAELEE-LEEELDELKGEIGRLEKELEQAEEELDELQDRL 736
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 481-573 9.06e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.04  E-value: 9.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116812914 481 KKAIAEERAQKVAAEKEQ------DLLRQKQKEQQEYMEAQEKSHKEnIEQLRRKLMQEREQLIKDHNMMLKKQLKDQKA 554
Cdd:PRK00409 528 LERELEQKAEEAEALLKEaeklkeELEEKKEKLQEEEDKLLEEAEKE-AQQAIKEAKKEADEIIKELRQLQKGGYASVKA 606

                         90
                 ....*....|....*....
gi 116812914 555 fleegfkKKAEEMNKEIQQ 573
Cdd:PRK00409 607 -------HELIEARKRLNK 618
 
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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