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Conserved domains on  [gi|1242862639|ref|NP_001342332|]
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guanylate-binding protein 3 [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 pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
12-275 7.93e-162

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: 463.38  E-value: 7.93e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  12 KNQLTVNLEAIRILEQIAQPLVVVAIVGLYRTGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHPTKPTHTLVLLD 91
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  92 TEGLGDVEKGDPKNDSWIFALAVLLSSTFVYNSMSTINQQALEQLHFVTELTQLirakSSPREDKVKDSSEFVGFFPDFI 171
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 172 WAVRDFALELKLNGRPITEDEYLENALKLIQGDNLKVQQSNMTRECIRYFFPVRKCFVFDRPTSDKRLLLQIENVPENQL 251
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236
                         250       260
                  ....*....|....*....|....
gi 1242862639 252 ERNFQVESEKFCSYIFTNGKTKTL 275
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
277-573 7.43e-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: 462.14  E-value: 7.43e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 277 GGVIVTGNRLGTLVQTYVNAINSGTVPCLENAVTTLAQRENSIAVQKAADHYSEQMAQRMRLPTDTLQELLTVHAACEKE 356
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 357 AIAVFMEHSFKDDEQEFQKKLVVTIEERKEEFIRQNEAASIRHCQAELERLSESLRKSISCGAFSVPGGHSLYLEARKKI 436
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 437 ELGYQQVLRKGVKAKEVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAEKELELLRQRQKEQEQVMEAQERS 516
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1242862639 517 FRENIAKLQEKMESEKEMLLREQEKMLEHKLKVQEELLIEGFREKSDMLKNEISHLR 573
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
 
Name Accession Description Interval E-value
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
12-275 7.93e-162

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: 463.38  E-value: 7.93e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  12 KNQLTVNLEAIRILEQIAQPLVVVAIVGLYRTGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHPTKPTHTLVLLD 91
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  92 TEGLGDVEKGDPKNDSWIFALAVLLSSTFVYNSMSTINQQALEQLHFVTELTQLirakSSPREDKVKDSSEFVGFFPDFI 171
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 172 WAVRDFALELKLNGRPITEDEYLENALKLIQGDNLKVQQSNMTRECIRYFFPVRKCFVFDRPTSDKRLLLQIENVPENQL 251
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236
                         250       260
                  ....*....|....*....|....
gi 1242862639 252 ERNFQVESEKFCSYIFTNGKTKTL 275
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
277-573 7.43e-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: 462.14  E-value: 7.43e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 277 GGVIVTGNRLGTLVQTYVNAINSGTVPCLENAVTTLAQRENSIAVQKAADHYSEQMAQRMRLPTDTLQELLTVHAACEKE 356
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 357 AIAVFMEHSFKDDEQEFQKKLVVTIEERKEEFIRQNEAASIRHCQAELERLSESLRKSISCGAFSVPGGHSLYLEARKKI 436
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 437 ELGYQQVLRKGVKAKEVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAEKELELLRQRQKEQEQVMEAQERS 516
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1242862639 517 FRENIAKLQEKMESEKEMLLREQEKMLEHKLKVQEELLIEGFREKSDMLKNEISHLR 573
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
283-573 8.15e-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: 421.22  E-value: 8.15e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 283 GNRLGTLVQTYVNAINSGTVPCLENAVTTLAQRENSIAVQKAADHYSEQMAQRMRLPTDTLQELLTVHAACEKEAIAVFM 362
Cdd:cd16269     1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 363 EHSFKDDEQEFQKKLVVTIEERKEEFIRQNEAASIRHCQAELERLSESLRKSISCGAFSVPGGHSLYLEARKKIELGYQQ 442
Cdd:cd16269    81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISQGSYSVPGGYQLYLEDREKLVEKYRQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 443 VLRKGVKAKEVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAEKELELLRQRQKEQEQVMEAQERSFRENIA 522
Cdd:cd16269   161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1242862639 523 KLQEKMESEKEMLLREQEKMLEHKLKVQEELLIEGFREKSDMLKNEISHLR 573
Cdd:cd16269   241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
30-269 1.58e-64

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: 211.41  E-value: 1.58e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  30 QPLVVVAIVGLYRTGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHP--TKPTHTLVLLDTEGLGDVEKGDPKNDS 107
Cdd:cd01851     5 FPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEFENDA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 108 WIFALAVLLSSTFVYNSMSTINQQALEQLHFVTELTQLIRAKSspredkvkDSSEFVGFFPDFIWAVRDFALELKLNGRP 187
Cdd:cd01851    85 RLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTALETLGLA--------GLHNFSKPKPLLLFVVRDFTGPTPLEGLD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 188 ITEDEY-LENALKLIqgdnlkvqqsnmtRECIRYFFPVRKCFVFDRPTSDKrlLLQIENVPENQLERNFQVESEKFCSYI 266
Cdd:cd01851   157 VTEKSEtLIEELNKI-------------WSSIRKPFTPITCFVLPHPGLLH--KLLQNDGRLKDLPPEFRKALKALRQRF 221

                  ...
gi 1242862639 267 FTN 269
Cdd:cd01851   222 FSS 224
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
367-582 8.23e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 367 KDDEQEFQKKL-VVTIEERKEEfiRQNEAASIRHCQAELERLSESLRksiscgafsvpgghslylEARKKIELGYQQVLR 445
Cdd:COG1196   219 KEELKELEAELlLLKLRELEAE--LEELEAELEELEAELEELEAELA------------------ELEAELEELRLELEE 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 446 KGVKAKEVLKSFLQsqAIMEDSILQSDKALTDgERAIAAERTKKEVAEKELELLRQRQKEQEQVMEAQER--SFRENIAK 523
Cdd:COG1196   279 LELELEEAQAEEYE--LLAELARLEQDIARLE-ERRRELEERLEELEEELAELEEELEELEEELEELEEEleEAEEELEE 355
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1242862639 524 LQEKMESEKEMLLREQEKMLEhKLKVQEELLIEGFREKSDM--LKNEISHLREEMERTRRK 582
Cdd:COG1196   356 AEAELAEAEEALLEAEAELAE-AEEELEELAEELLEALRAAaeLAAQLEELEEAEEALLER 415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
450-582 2.06e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 2.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  450 AKEVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAEKELELLRQRQKEQEQVMEAQERSFREniakLQEKME 529
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE----LEEQLE 382
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1242862639  530 --SEKEMLLREQEKMLEHKLKVQEELLiEGFREKSDMLKNEISHLREEMERTRRK 582
Cdd:TIGR02168  383 tlRSKVAQLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEELLKKLEEAELK 436
PTZ00121 PTZ00121
MAEBL; Provisional
372-569 7.67e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 7.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  372 EFQKKLVVTIEERKEEFIRQNEAASIRhcqAELERLSESLRKSISCGAFSVPGGHSLYLEARKKIELGYQQVLRKGVKAK 451
Cdd:PTZ00121  1595 EEVMKLYEEEKKMKAEEAKKAEEAKIK---AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  452 EVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAE--KELELLRQRQKEQEQVMEAQERSFRENIAKLQE--K 527
Cdd:PTZ00121  1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEekKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEakK 1751
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1242862639  528 MESEK---EMLLREQEKMLEHKLKVQEELLIEGFREKSDMLKNEI 569
Cdd:PTZ00121  1752 DEEEKkkiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEV 1796
YeeP COG3596
Predicted GTPase [General function prediction only];
23-104 9.63e-04

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 41.68  E-value: 9.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  23 RILEQ--IAQPLVVVAIVGLYRTGKSYLMNRLAGRNhgFSLGSTVQSETKGIwmWCVPHPTKPTHTLVLLDTEGLGDVEK 100
Cdd:COG3596    28 EALERllVELPPPVIALVGKTGAGKSSLINALFGAE--VAEVGVGRPCTREI--QRYRLESDGLPGLVLLDTPGLGEVNE 103

                  ....
gi 1242862639 101 GDPK 104
Cdd:COG3596   104 RDRE 107
 
Name Accession Description Interval E-value
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
12-275 7.93e-162

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: 463.38  E-value: 7.93e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  12 KNQLTVNLEAIRILEQIAQPLVVVAIVGLYRTGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHPTKPTHTLVLLD 91
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  92 TEGLGDVEKGDPKNDSWIFALAVLLSSTFVYNSMSTINQQALEQLHFVTELTQLirakSSPREDKVKDSSEFVGFFPDFI 171
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 172 WAVRDFALELKLNGRPITEDEYLENALKLIQGDNLKVQQSNMTRECIRYFFPVRKCFVFDRPTSDKRLLLQIENVPENQL 251
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236
                         250       260
                  ....*....|....*....|....
gi 1242862639 252 ERNFQVESEKFCSYIFTNGKTKTL 275
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
277-573 7.43e-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: 462.14  E-value: 7.43e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 277 GGVIVTGNRLGTLVQTYVNAINSGTVPCLENAVTTLAQRENSIAVQKAADHYSEQMAQRMRLPTDTLQELLTVHAACEKE 356
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 357 AIAVFMEHSFKDDEQEFQKKLVVTIEERKEEFIRQNEAASIRHCQAELERLSESLRKSISCGAFSVPGGHSLYLEARKKI 436
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 437 ELGYQQVLRKGVKAKEVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAEKELELLRQRQKEQEQVMEAQERS 516
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1242862639 517 FRENIAKLQEKMESEKEMLLREQEKMLEHKLKVQEELLIEGFREKSDMLKNEISHLR 573
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
283-573 8.15e-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: 421.22  E-value: 8.15e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 283 GNRLGTLVQTYVNAINSGTVPCLENAVTTLAQRENSIAVQKAADHYSEQMAQRMRLPTDTLQELLTVHAACEKEAIAVFM 362
Cdd:cd16269     1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 363 EHSFKDDEQEFQKKLVVTIEERKEEFIRQNEAASIRHCQAELERLSESLRKSISCGAFSVPGGHSLYLEARKKIELGYQQ 442
Cdd:cd16269    81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISQGSYSVPGGYQLYLEDREKLVEKYRQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 443 VLRKGVKAKEVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAEKELELLRQRQKEQEQVMEAQERSFRENIA 522
Cdd:cd16269   161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1242862639 523 KLQEKMESEKEMLLREQEKMLEHKLKVQEELLIEGFREKSDMLKNEISHLR 573
Cdd:cd16269   241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
30-269 1.58e-64

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: 211.41  E-value: 1.58e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  30 QPLVVVAIVGLYRTGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHP--TKPTHTLVLLDTEGLGDVEKGDPKNDS 107
Cdd:cd01851     5 FPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEFENDA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 108 WIFALAVLLSSTFVYNSMSTINQQALEQLHFVTELTQLIRAKSspredkvkDSSEFVGFFPDFIWAVRDFALELKLNGRP 187
Cdd:cd01851    85 RLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTALETLGLA--------GLHNFSKPKPLLLFVVRDFTGPTPLEGLD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 188 ITEDEY-LENALKLIqgdnlkvqqsnmtRECIRYFFPVRKCFVFDRPTSDKrlLLQIENVPENQLERNFQVESEKFCSYI 266
Cdd:cd01851   157 VTEKSEtLIEELNKI-------------WSSIRKPFTPITCFVLPHPGLLH--KLLQNDGRLKDLPPEFRKALKALRQRF 221

                  ...
gi 1242862639 267 FTN 269
Cdd:cd01851   222 FSS 224
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
36-111 4.78e-08

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: 52.84  E-value: 4.78e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1242862639  36 AIVGLYRTGKSYLMNRLAGRNhgFSLGSTVQSETKGIWMWCVPHPtKPTHTLVLLDTEGLGDVEKGDPKNDSWIFA 111
Cdd:cd00882     1 VVVGRGGVGKSSLLNALLGGE--VGEVSDVPGTTRDPDVYVKELD-KGKVKLVLVDTPGLDEFGGLGREELARLLL 73
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
276-582 4.66e-07

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: 52.82  E-value: 4.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 276 RGGVIVTGNRLGTLVQTYVNAINSGTVPCLE--NAVTTLAQRENSIAVQKAADHYSEQMAQRMRLPTD----------TL 343
Cdd:pfam17380 239 RKESFNLAEDVTTMTPEYTVRYNGQTMTENEflNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEekareverrrKL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 344 QELLTV-HAACEKEAiAVFMEHS--FKDDEQEFQKklvVTIEERKEEF--IRQNEAASIRHCQAELERL-------SESL 411
Cdd:pfam17380 319 EEAEKArQAEMDRQA-AIYAEQErmAMERERELER---IRQEERKRELerIRQEEIAMEISRMRELERLqmerqqkNERV 394
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 412 RKSiscgafsvpgghslyLEARKKIELGYQQVLRKGVKAKEVLKSFLQSQaimeDSILQSDKALTDGERAIAAERTKKEV 491
Cdd:pfam17380 395 RQE---------------LEAARKVKILEEERQRKIQQQKVEMEQIRAEQ----EEARQREVRRLEEERAREMERVRLEE 455
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 492 AEKELELLRQRQKEQEQ-----VMEAQERSFREniAKLQEKMESEKEMLLREQeKMLEHKLKvqEELLIEGFREKSDMLK 566
Cdd:pfam17380 456 QERQQQVERLRQQEEERkrkklELEKEKRDRKR--AEEQRRKILEKELEERKQ-AMIEEERK--RKLLEKEMEERQKAIY 530
                         330
                  ....*....|....*.
gi 1242862639 567 NEisHLREEMERTRRK 582
Cdd:pfam17380 531 EE--ERRREAEEERRK 544
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
367-582 8.23e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 367 KDDEQEFQKKL-VVTIEERKEEfiRQNEAASIRHCQAELERLSESLRksiscgafsvpgghslylEARKKIELGYQQVLR 445
Cdd:COG1196   219 KEELKELEAELlLLKLRELEAE--LEELEAELEELEAELEELEAELA------------------ELEAELEELRLELEE 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 446 KGVKAKEVLKSFLQsqAIMEDSILQSDKALTDgERAIAAERTKKEVAEKELELLRQRQKEQEQVMEAQER--SFRENIAK 523
Cdd:COG1196   279 LELELEEAQAEEYE--LLAELARLEQDIARLE-ERRRELEERLEELEEELAELEEELEELEEELEELEEEleEAEEELEE 355
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1242862639 524 LQEKMESEKEMLLREQEKMLEhKLKVQEELLIEGFREKSDM--LKNEISHLREEMERTRRK 582
Cdd:COG1196   356 AEAELAEAEEALLEAEAELAE-AEEELEELAEELLEALRAAaeLAAQLEELEEAEEALLER 415
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
450-582 2.06e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 2.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  450 AKEVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAEKELELLRQRQKEQEQVMEAQERSFREniakLQEKME 529
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE----LEEQLE 382
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1242862639  530 --SEKEMLLREQEKMLEHKLKVQEELLiEGFREKSDMLKNEISHLREEMERTRRK 582
Cdd:TIGR02168  383 tlRSKVAQLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEELLKKLEEAELK 436
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
316-580 3.32e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 43.94  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 316 ENSIAVQKAadhyseqMAQRMRLPTDTLQELLTVHAACEKEAIAVFMEHSFKDDEQEfqkKLVVTIEE--RKEEFIRQNE 393
Cdd:pfam05483 306 QRSMSTQKA-------LEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFE---ATTCSLEEllRTEQQRLEKN 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 394 AASIRHCQAELERLSESLRKSIScgafsVPGGHSLYLEARKKIeLGYQQVLRKGVKAKEVLKSFLQSQAIMEDSILQS-D 472
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTK-----FKNNKEVELEELKKI-LAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQArE 449
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 473 KALTDGERAIAAERTK-----KEVAEKELELLRQRQKEQEQVMEAQERSFrENIAKLQEKmeSEKEMLLREQEKMLEHKL 547
Cdd:pfam05483 450 KEIHDLEIQLTAIKTSeehylKEVEDLKTELEKEKLKNIELTAHCDKLLL-ENKELTQEA--SDMTLELKKHQEDIINCK 526
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1242862639 548 KVQEELL--IEGFREKSDMLKNEISHLREEMERTR 580
Cdd:pfam05483 527 KQEERMLkqIENLEEKEMNLRDELESVREEFIQKG 561
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
473-582 4.59e-04

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: 42.22  E-value: 4.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 473 KALTDGERAIAAERTKKEVAEKELELLRQRQKEQeqvmEAQERSFRENIAKLQEKME---SEKEM--LLREQEkMLEHKL 547
Cdd:COG1579    31 AELAELEDELAALEARLEAAKTELEDLEKEIKRL----ELEIEEVEARIKKYEEQLGnvrNNKEYeaLQKEIE-SLKRRI 105
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1242862639 548 KVQEELLIEgFREKSDMLKNEISHLREEMERTRRK 582
Cdd:COG1579   106 SDLEDEILE-LMERIEELEEELAELEAELAELEAE 139
PTZ00121 PTZ00121
MAEBL; Provisional
372-569 7.67e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 7.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  372 EFQKKLVVTIEERKEEFIRQNEAASIRhcqAELERLSESLRKSISCGAFSVPGGHSLYLEARKKIELGYQQVLRKGVKAK 451
Cdd:PTZ00121  1595 EEVMKLYEEEKKMKAEEAKKAEEAKIK---AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  452 EVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAE--KELELLRQRQKEQEQVMEAQERSFRENIAKLQE--K 527
Cdd:PTZ00121  1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEekKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEakK 1751
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1242862639  528 MESEK---EMLLREQEKMLEHKLKVQEELLIEGFREKSDMLKNEI 569
Cdd:PTZ00121  1752 DEEEKkkiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEV 1796
YeeP COG3596
Predicted GTPase [General function prediction only];
23-104 9.63e-04

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 41.68  E-value: 9.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  23 RILEQ--IAQPLVVVAIVGLYRTGKSYLMNRLAGRNhgFSLGSTVQSETKGIwmWCVPHPTKPTHTLVLLDTEGLGDVEK 100
Cdd:COG3596    28 EALERllVELPPPVIALVGKTGAGKSSLINALFGAE--VAEVGVGRPCTREI--QRYRLESDGLPGLVLLDTPGLGEVNE 103

                  ....
gi 1242862639 101 GDPK 104
Cdd:COG3596   104 RDRE 107
PTZ00121 PTZ00121
MAEBL; Provisional
382-582 1.02e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  382 EERKEEFIRQNEAASirhcQAELERLSESLRKSiscgafsvpgghslyLEARKKIELGYQQVLRKGVKAK--EVLKSFLQ 459
Cdd:PTZ00121  1150 DAKRVEIARKAEDAR----KAEEARKAEDAKKA---------------EAARKAEEVRKAEELRKAEDARkaEAARKAEE 1210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  460 SQAIME----------DSILQSDKALTDGERAIAAERTKKEVAEKELELLRQRQKEQEQV-MEAQERSFRENIAKLQEKM 528
Cdd:PTZ00121  1211 ERKAEEarkaedakkaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaIKAEEARKADELKKAEEKK 1290
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1242862639  529 ESEKEMLLREQEKMLEHKLKVQEELLIEGFREKSDMLKNEISHLREEMERTRRK 582
Cdd:PTZ00121  1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
RHD3_GTPase pfam05879
Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of ...
43-114 1.19e-03

Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of several eukaryotic root hair defective 3 (RHD3) like GTP-binding proteins, including RHD3 from Arabidopsis and Sey1 from yeast, which are involved in homotypic membrane fusion of the endoplasmic reticulum. This domain binds GTP and forms dimers with other molecule for membrane tethering.


Pssm-ID: 461768  Cd Length: 243  Bit Score: 40.90  E-value: 1.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242862639  43 TGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHPTKPTHTLVLLDTEGLGDVEKG---DPKNDSWIFALAV 114
Cdd:pfam05879   6 TGKSTLLNHLFGTNFSVMDASGRQQTTKGIWLAKCKGIGNMEPNILVMDVEGTDGRERGedqDFERKSALFALAT 80
PTZ00121 PTZ00121
MAEBL; Provisional
382-578 1.46e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  382 EERKEEFIRQNEAASirhcQAELERLSESLRKSISCGAFSVPGGHSLYLEARKKIELGYQQVLRKGVK------AKEVLK 455
Cdd:PTZ00121  1573 EEDKNMALRKAEEAK----KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEqlkkkeAEEKKK 1648
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  456 SFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAEKelellrqRQKEQEQVMEAQERSFRENIAKLQEKMESEKEML 535
Cdd:PTZ00121  1649 AEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE-------KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1242862639  536 LREQE----KMLEHKLKVQEELLIEGFREKSDMLKNEISHLREEMER 578
Cdd:PTZ00121  1722 KKAEEenkiKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
441-582 1.53e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 441 QQVLRKGVKAKEVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAEKELELLRQRQKEQEQV------MEAQE 514
Cdd:PRK03918  168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeieeLEKEL 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 515 RSFRENIAKLQEKMESEKEML--LREQEKMLEHKLKVQEEL------------LIEGFREKSDMLKNEISHLREEMERTR 580
Cdd:PRK03918  248 ESLEGSKRKLEEKIRELEERIeeLKKEIEELEEKVKELKELkekaeeyiklseFYEEYLDELREIEKRLSRLEEEINGIE 327

                  ..
gi 1242862639 581 RK 582
Cdd:PRK03918  328 ER 329
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
430-578 1.72e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 430 LEARKKIELGYQQVLRKGVKAKEVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAEKELELLRQRQKEQEQV 509
Cdd:COG1196   627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1242862639 510 MEAQERS-FRENIAKLQEKMESEKEMLLREQEKMLEHKLKVQEELLIEGFREKSDM--LKNEISHLREEMER 578
Cdd:COG1196   707 RELAEAEeERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLeeLERELERLEREIEA 778
PTZ00121 PTZ00121
MAEBL; Provisional
354-581 1.92e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  354 EKEAIAVFMEHSFKDDEQEFQKklvvTIEERKEEFIRQNEAASIRH-------CQAELERLSESLRKSiscgafsvpggh 426
Cdd:PTZ00121  1223 AKKAEAVKKAEEAKKDAEEAKK----AEEERNNEEIRKFEEARMAHfarrqaaIKAEEARKADELKKA------------ 1286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  427 slyLEARKKIELGYQQVLRKGVKAK---EVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKK---EVAEKELELLR 500
Cdd:PTZ00121  1287 ---EEKKKADEAKKAEEKKKADEAKkkaEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKaeaEAAADEAEAAE 1363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  501 QRQKEQEQVMEAQERSFRENIAKLQEKMESEKemllrEQEKMLEHKLKVQEELLIEGFREKSDMLKNEISHLREEMERTR 580
Cdd:PTZ00121  1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKADE-----AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKK 1438

                   .
gi 1242862639  581 R 581
Cdd:PTZ00121  1439 K 1439
DUF4515 pfam14988
Domain of unknown function (DUF4515); This family of proteins is found in bacteria and ...
484-592 2.38e-03

Domain of unknown function (DUF4515); This family of proteins is found in bacteria and eukaryotes. Proteins in this family are typically between 198 and 469 amino acids in length. There are two completely conserved L residues that may be functionally important.


Pssm-ID: 405647 [Multi-domain]  Cd Length: 206  Bit Score: 39.75  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 484 AERTKKEVA---EKELELLRQR--QKEQEQVMEAQERSFRENIAKLQEKMESEKEMLLREQEKML-EHKLKVQeELLIEG 557
Cdd:pfam14988  34 IERRRQELAsryTQQTAELQTQllQKEKEQASLKKELQALRPFAKLKESQEREIQDLEEEKEKVRaETAEKDR-EAHLQF 112
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1242862639 558 FREKSDMLKN-EISHLREEMERTRRKPSLFGQILDT 592
Cdd:pfam14988 113 LKEKALLEKQlQELRILELGERATRELKRKAQALKL 148
PTZ00121 PTZ00121
MAEBL; Provisional
321-581 6.64e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 6.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  321 VQKAADHYSEQMAQRMRLPTDTLQELLTVHAACEKEAIAVfmEHSFKDDEQEFQKKLVVTIEERKEEFIRQNEAASIRhc 400
Cdd:PTZ00121  1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA--EEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK-- 1310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  401 qAELERLSESLRKSISCGAFSVPGGHSLYLEARKKIELGYQQVLRKGVKAKEVLKSFLQSQAIMEDSILQSDKALTDGER 480
Cdd:PTZ00121  1311 -AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEE 1389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639  481 AIAAERTKKEVAE--KELELLRQRQKEQEQVMEAQERSfrENIAKLQE-KMESEKEMLLREQEKMLEHKLKVQEELLIEG 557
Cdd:PTZ00121  1390 KKKADEAKKKAEEdkKKADELKKAAAAKKKADEAKKKA--EEKKKADEaKKKAEEAKKADEAKKKAEEAKKAEEAKKKAE 1467
                          250       260
                   ....*....|....*....|....
gi 1242862639  558 FREKSDMLKNEISHLREEMERTRR 581
Cdd:PTZ00121  1468 EAKKADEAKKKAEEAKKADEAKKK 1491
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
480-575 7.75e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 39.35  E-value: 7.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 480 RAIAAERTKKEVAEKELELLRQRQ---KEQEQVMEAQERSFREN----IAKLQEKMESEKEMLLREQEKMLEHKLKvqEE 552
Cdd:pfam09731 307 KKREEKHIERALEKQKEELDKLAEelsARLEEVRAADEAQLRLEfereREEIRESYEEKLRTELERQAEAHEEHLK--DV 384
                          90       100
                  ....*....|....*....|...
gi 1242862639 553 LLIEGFREKSDMLKNEISHLREE 575
Cdd:pfam09731 385 LVEQEIELQREFLQDIKEKVEEE 407
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
476-557 8.10e-03

Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil domain-containing protein 66 (CCDC) refers to a protein domain found in eukaryotes, and is approximately 160 amino acids in length. CCDC66 protein is detected mainly in the inner segments of photoreceptors in many vertebrates including mice and humans. It has been found in dogs, that a mutation in the CCDC66 gene causes generalized progressive retinal atrophy (gPRA). This shows that the protein encoded for by this gene is vital for healthy vision and guards against photoreceptor cell degeneration. The structure of CCDC66 proteins includes a heptad repeat pattern which contains at least one coiled-coil domain. There are at least two or more alpha-helices which form a cable-like structure.


Pssm-ID: 434558 [Multi-domain]  Cd Length: 154  Bit Score: 37.47  E-value: 8.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 476 TDGERAIAAERTKKEVAEKELELLRQRQKEQEQvmeaqersFRENIAKLQEKmeseKEMLLREQEKMLEHKLKVQEELLI 555
Cdd:pfam15236  68 KERQKKLEEERRRQEEQEEEERLRREREEEQKQ--------FEEERRKQKEK----EEAMTRKTQALLQAMQKAQELAQR 135

                  ..
gi 1242862639 556 EG 557
Cdd:pfam15236 136 LK 137
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
441-581 8.85e-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: 38.98  E-value: 8.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 441 QQVLRKGVKAKEVLKSFLQSQAIMEDSILQSDKALTDGERAIAAERTKKEVAEKELELLRQRQKEQEQVMEAQERSFREN 520
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242862639 521 IAKLQEKMESEKEMLLREQE---------KMLEHKLKVQEElLIEGFREKSDMLKNEISHLREEMERTRR 581
Cdd:COG4942   110 LRALYRLGRQPPLALLLSPEdfldavrrlQYLKYLAPARRE-QAEELRADLAELAALRAELEAERAELEA 178
 
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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