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Conserved domains on  [gi|765365472|ref|NP_001292190|]
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guanylate-binding protein 4 [Rattus norvegicus]

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 3.68e-159

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: 456.45  E-value: 3.68e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472   12 KEQLTVNLEAIGILEQIAQPLVVVAIVGLYRTGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHPTKPTHTLVLLD 91
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472   92 TEGLGDVEKGDPKNDSWIFALAVLLSSTFVYNSMSTINHQALEQLHYVTELTQLirakSDPREDKVEDSSEFVGFFPDFI 171
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  172 WAVRDFVLELKLDGRPITEDEYLENALKLIPENNPKGQKSNMTRECIRYFFPVRKCFVFDRPTNDKSLLFQIENVPENQL 251
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236

                         250       260
                  ....*....|....*....|....
gi 765365472  252 EWNFQVESENFCSYIFANGKTKTL 275
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 277-573 1.41e-158

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


:

Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 456.36  E-value: 1.41e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  277 GGVIVTGNRLGTLVQTYVDAINSGTVPCLENAVTALAQRENSAAVQKAAEHYAEQMAQRLRLPTDTLQELLEVHSACEKE 356
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  357 AIAVFMEHSFKDDEQEFQKRLVATIEKWKEEFMLRNEAASIRHCQAELEKLSESLKESISCGAFSVPGGHSLYLEARKKV 436
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  437 ELSYEQVPRKGVKAKEVLKSFLQSQATVENSILQSDKALTDGERAVAAERTKKEVAEKERELLKQRQKEQEQVMEAQERS 516
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 765365472  517 FQENIAKLQEKMERERVMLLREQEKMMEHKLKVQKELLVEGFRKKSDMLKNEISQLR 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 3.68e-159

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: 456.45  E-value: 3.68e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472   12 KEQLTVNLEAIGILEQIAQPLVVVAIVGLYRTGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHPTKPTHTLVLLD 91
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472   92 TEGLGDVEKGDPKNDSWIFALAVLLSSTFVYNSMSTINHQALEQLHYVTELTQLirakSDPREDKVEDSSEFVGFFPDFI 171
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  172 WAVRDFVLELKLDGRPITEDEYLENALKLIPENNPKGQKSNMTRECIRYFFPVRKCFVFDRPTNDKSLLFQIENVPENQL 251
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236

                         250       260
                  ....*....|....*....|....
gi 765365472  252 EWNFQVESENFCSYIFANGKTKTL 275
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 277-573 1.41e-158

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


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 456.36  E-value: 1.41e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  277 GGVIVTGNRLGTLVQTYVDAINSGTVPCLENAVTALAQRENSAAVQKAAEHYAEQMAQRLRLPTDTLQELLEVHSACEKE 356
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  357 AIAVFMEHSFKDDEQEFQKRLVATIEKWKEEFMLRNEAASIRHCQAELEKLSESLKESISCGAFSVPGGHSLYLEARKKV 436
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  437 ELSYEQVPRKGVKAKEVLKSFLQSQATVENSILQSDKALTDGERAVAAERTKKEVAEKERELLKQRQKEQEQVMEAQERS 516
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 765365472  517 FQENIAKLQEKMERERVMLLREQEKMMEHKLKVQKELLVEGFRKKSDMLKNEISQLR 573
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 283-573 5.99e-148

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: 429.30  E-value: 5.99e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 283 GNRLGTLVQTYVDAINSGTVPCLENAVTALAQRENSAAVQKAAEHYAEQMAQRLRLPTDTLQELLEVHSACEKEAIAVFM 362
Cdd:cd16269    1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 363 EHSFKDDEQEFQKRLVATIEKWKEEFMLRNEAASIRHCQAELEKLSESLKESISCGAFSVPGGHSLYLEARKKVELSYEQ 442
Cdd:cd16269   81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISQGSYSVPGGYQLYLEDREKLVEKYRQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 443 VPRKGVKAKEVLKSFLQSQATVENSILQSDKALTDGERAVAAERTKKEVAEKERELLKQRQKEQEQVMEAQERSFQENIA 522
Cdd:cd16269  161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 765365472 523 KLQEKMERERVMLLREQEKMMEHKLKVQKELLVEGFRKKSDMLKNEISQLR 573
Cdd:cd16269  241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 30-269 7.24e-67

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: 217.58  E-value: 7.24e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  30 QPLVVVAIVGLYRTGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHP--TKPTHTLVLLDTEGLGDVEKGDPKNDS 107
Cdd:cd01851    5 FPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEFENDA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 108 WIFALAVLLSSTFVYNSMSTINHQALEQLHYVTELTQLIRAKSDPREDKVedssefvgFFPDFIWAVRDFVLELKLDGRP 187
Cdd:cd01851   85 RLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTALETLGLAGLHNFSK--------PKPLLLFVVRDFTGPTPLEGLD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 188 ITEDEY-LENALKLIpennpkgqksnmtRECIRYFFPVRKCFVFDRPTNDKSLLFQieNVPENQLEWNFQVESENFCSYI 266
Cdd:cd01851  157 VTEKSEtLIEELNKI-------------WSSIRKPFTPITCFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKALRQRF 221


                 ...
gi 765365472 267 FAN 269
Cdd:cd01851  222 FSS 224
PTZ00121 PTZ00121
MAEBL; Provisional
 431-581 6.08e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  431 EARKKVELSYEQVPRKGVKAKEVLKsflqsqATVENSILQSDKALTDGERAVAAERTKKEvAEKERELLKQRQKEQEQVM 510
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKK------AEEENKIKAAEEAKKAEEDKKKAEEAKKA-EEDEKKAAEALKKEAEEAK 1702

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 765365472  511 EAQE--RSFQENIAKLQE--KMERERVMLLREQEKMMEHKLKVQKELLV-EGFRKKSDMLKNEISQLREEIERTRK 581
Cdd:PTZ00121 1703 KAEElkKKEAEEKKKAEElkKAEEENKIKAEEAKKEAEEDKKKAEEAKKdEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 431-582 7.52e-04

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: 42.06  E-value: 7.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 431 EARKKVELSYEQVPRKGVKAKEVLKSFLQSQATVENSILQSDKALTDGERAVAAERTKKEVAEKERELLKQRQKEQEQVM 510
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 511 EAQERSFQENIAKLQEKMERERVMLLREQE---------KMMEHKLKVQKELLvEGFRKKsdmlKNEISQLREEIERTRK 581
Cdd:COG4942  100 EAQKEELAELLRALYRLGRQPPLALLLSPEdfldavrrlQYLKYLAPARREQA-EELRAD----LAELAALRAELEAERA 174


                 .
gi 765365472 582 K 582
Cdd:COG4942  175 E 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 367-578 9.88e-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: 42.35  E-value: 9.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472   367 KDDEQEFQK-----RLVATIEKWKEEFMLRNEAASIRH-CQAELEKLSESLKESIScgafSVPGGHSLYLEARKKVELSY 440
Cdd:TIGR02168  219 KAELRELELallvlRLEELREELEELQEELKEAEEELEeLTAELQELEEKLEELRL----EVSELEEEIEELQKELYALA 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472   441 EQVPRKGVK---AKEVLKSFLQSQATVENSILQSDKALTDGERAVAAERTKKEVAEKERELLKQRQKEQEQVMEAQERSF 517
Cdd:TIGR02168  295 NEISRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 765365472   518 QEniakLQEKMERER--VMLLREQEKMmehklkvqkellvegfrkksdmLKNEISQLREEIER 578
Cdd:TIGR02168  375 EE----LEEQLETLRskVAQLELQIAS----------------------LNNEIERLEARLER 411
YeeP COG3596
Predicted GTPase [General function prediction only];
28-104 1.27e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 41.29  E-value: 1.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 765365472  28 IAQPLVVVAIVGLYRTGKSYLMNRLAGRNhgFSLGSTVQSETKGIwmWCVPHPTKPTHTLVLLDTEGLGDVEKGDPK 104
Cdd:COG3596   35 VELPPPVIALVGKTGAGKSSLINALFGAE--VAEVGVGRPCTREI--QRYRLESDGLPGLVLLDTPGLGEVNERDRE 107
 
Name Accession Description Interval E-value
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 12-275 3.68e-159

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: 456.45  E-value: 3.68e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472   12 KEQLTVNLEAIGILEQIAQPLVVVAIVGLYRTGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHPTKPTHTLVLLD 91
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472   92 TEGLGDVEKGDPKNDSWIFALAVLLSSTFVYNSMSTINHQALEQLHYVTELTQLirakSDPREDKVEDSSEFVGFFPDFI 171
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  172 WAVRDFVLELKLDGRPITEDEYLENALKLIPENNPKGQKSNMTRECIRYFFPVRKCFVFDRPTNDKSLLFQIENVPENQL 251
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236

                         250       260
                  ....*....|....*....|....
gi 765365472  252 EWNFQVESENFCSYIFANGKTKTL 275
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 277-573 1.41e-158

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


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 456.36  E-value: 1.41e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  277 GGVIVTGNRLGTLVQTYVDAINSGTVPCLENAVTALAQRENSAAVQKAAEHYAEQMAQRLRLPTDTLQELLEVHSACEKE 356
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  357 AIAVFMEHSFKDDEQEFQKRLVATIEKWKEEFMLRNEAASIRHCQAELEKLSESLKESISCGAFSVPGGHSLYLEARKKV 436
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISQGTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  437 ELSYEQVPRKGVKAKEVLKSFLQSQATVENSILQSDKALTDGERAVAAERTKKEVAEKERELLKQRQKEQEQVMEAQERS 516
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 765365472  517 FQENIAKLQEKMERERVMLLREQEKMMEHKLKVQKELLVEGFRKKSDMLKNEISQLR 573
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 283-573 5.99e-148

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: 429.30  E-value: 5.99e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 283 GNRLGTLVQTYVDAINSGTVPCLENAVTALAQRENSAAVQKAAEHYAEQMAQRLRLPTDTLQELLEVHSACEKEAIAVFM 362
Cdd:cd16269    1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 363 EHSFKDDEQEFQKRLVATIEKWKEEFMLRNEAASIRHCQAELEKLSESLKESISCGAFSVPGGHSLYLEARKKVELSYEQ 442
Cdd:cd16269   81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISQGSYSVPGGYQLYLEDREKLVEKYRQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 443 VPRKGVKAKEVLKSFLQSQATVENSILQSDKALTDGERAVAAERTKKEVAEKERELLKQRQKEQEQVMEAQERSFQENIA 522
Cdd:cd16269  161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 765365472 523 KLQEKMERERVMLLREQEKMMEHKLKVQKELLVEGFRKKSDMLKNEISQLR 573
Cdd:cd16269  241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 30-269 7.24e-67

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: 217.58  E-value: 7.24e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  30 QPLVVVAIVGLYRTGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHP--TKPTHTLVLLDTEGLGDVEKGDPKNDS 107
Cdd:cd01851    5 FPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEFENDA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 108 WIFALAVLLSSTFVYNSMSTINHQALEQLHYVTELTQLIRAKSDPREDKVedssefvgFFPDFIWAVRDFVLELKLDGRP 187
Cdd:cd01851   85 RLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTALETLGLAGLHNFSK--------PKPLLLFVVRDFTGPTPLEGLD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 188 ITEDEY-LENALKLIpennpkgqksnmtRECIRYFFPVRKCFVFDRPTNDKSLLFQieNVPENQLEWNFQVESENFCSYI 266
Cdd:cd01851  157 VTEKSEtLIEELNKI-------------WSSIRKPFTPITCFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKALRQRF 221


                 ...
gi 765365472 267 FAN 269
Cdd:cd01851  222 FSS 224
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 36-111 2.83e-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: 53.61  E-value: 2.83e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 765365472  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 ...
 313-582 1.21e-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: 51.66  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  313 AQRENSAAVQKAAEHYAEQmaQRLRLPTdtlqellevhsacEKEAIAVFMEHSFKDDEQEFQKRLVATIEKWKEefmlrn 392
Cdd:pfam17380 321 AEKARQAEMDRQAAIYAEQ--ERMAMER-------------ERELERIRQEERKRELERIRQEEIAMEISRMRE------ 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  393 eaasIRHCQAELEKLSESLKESiscgafsvpgghslyLEARKKVELSYEQVPRKgvkAKEVLKSFLQSQATVENSILQSD 472
Cdd:pfam17380 380 ----LERLQMERQQKNERVRQE---------------LEAARKVKILEEERQRK---IQQQKVEMEQIRAEQEEARQREV 437

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  473 KALTDgERAVAAERTKKEVAEKERELLKQRQKEQEQVMEAQERsfqeniaklqEKMERERVMLLREQEKMMEHKLKVQKE 552
Cdd:pfam17380 438 RRLEE-ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLEL----------EKEKRDRKRAEEQRRKILEKELEERKQ 506

                         250       260       270
                  ....*....|....*....|....*....|..
gi 765365472  553 LLVEGFRKKSdMLKNEISQLREEI--ERTRKK 582
Cdd:pfam17380 507 AMIEEERKRK-LLEKEMEERQKAIyeEERRRE 537
PTZ00121 PTZ00121
MAEBL; Provisional
 431-581 6.08e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 6.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  431 EARKKVELSYEQVPRKGVKAKEVLKsflqsqATVENSILQSDKALTDGERAVAAERTKKEvAEKERELLKQRQKEQEQVM 510
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKK------AEEENKIKAAEEAKKAEEDKKKAEEAKKA-EEDEKKAAEALKKEAEEAK 1702

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 765365472  511 EAQE--RSFQENIAKLQE--KMERERVMLLREQEKMMEHKLKVQKELLV-EGFRKKSDMLKNEISQLREEIERTRK 581
Cdd:PTZ00121 1703 KAEElkKKEAEEKKKAEElkKAEEENKIKAEEAKKEAEEDKKKAEEAKKdEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 405-556 9.00e-05

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 44.75  E-value: 9.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  405 EKLSESLKESISCGAFSVPGGHSLYL-EARKKVELSYEQVpRKGVKAKEVLKSFLQS-QATVENSILQSDKALTDGERAV 482
Cdd:pfam09787  24 EKLIASLKEGSGVEGLDSSTALTLELeELRQERDLLREEI-QKLRGQIQQLRTELQElEAQQQEEAESSREQLQELEEQL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  483 AAERTKKEVAEKERELLKQRQKEQEQVMEAQERSFQENIAKLQEKMERERVMLLRE-----QEKMMEHKLK------VQK 551
Cdd:pfam09787 103 ATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLTSKsqsssSQSELENRLHqltetlIQK 182


                  ....*
gi 765365472  552 ELLVE 556
Cdd:pfam09787 183 QTMLE 187
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 370-579 1.50e-04

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 44.85  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 370 EQEFQKRLVATIEKWKEEFMLR-NEAASIRHCQAELEKLSE-SLKESISCGAfsvPGGHSLYLEARKKVElsyEQVPRKG 447
Cdd:PLN03229 502 DQLMHPVLMEKIEKLKDEFNKRlSRAPNYLSLKYKLDMLNEfSRAKALSEKK---SKAEKLKAEINKKFK---EVMDRPE 575

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 448 VKAK-EVLKsflqsqATVENSILQSDKALTDGERAvAAERTKKEVAEKERELLKQ--------RQKEQEQVMEAQERSFQ 518
Cdd:PLN03229 576 IKEKmEALK------AEVASSGASSGDELDDDLKE-KVEKMKKEIELELAGVLKSmglevigvTKKNKDTAEQTPPPNLQ 648

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 765365472 519 ENIAKLQEKMER--ERVMLLREQEKMMEhKLKVQkelLVEGFRKKSDMLKNEISQLREEIERT 579
Cdd:PLN03229 649 EKIESLNEEINKkiERVIRSSDLKSKIE-LLKLE---VAKASKTPDVTEKEKIEALEQQIKQK 707
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 329-582 3.64e-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: 43.56  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  329 AEQMAQRLRLPTDTLQELLEV--HSACEKEAIAVFMEHSF---KDDEQEFQ--KRLVATIEKWKEEFMLRNEAASIRH-- 399
Cdd:pfam05483 270 ANQLEEKTKLQDENLKELIEKkdHLTKELEDIKMSLQRSMstqKALEEDLQiaTKTICQLTEEKEAQMEELNKAKAAHsf 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  400 CQAELEKLSESLKESISCgafsvpggHSLYLEARK-KVELSYEQVPRKGVKAKEVLKSFLQSQATVE--NSILQSDKALT 476
Cdd:pfam05483 350 VVTEFEATTCSLEELLRT--------EQQRLEKNEdQLKIITMELQKKSSELEEMTKFKNNKEVELEelKKILAEDEKLL 421

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  477 DGERAVaaERTKKEVAEKEREL---LKQRQKE------QEQVMEAQERSFQENIAKLQEKMERERV----------MLLR 537
Cdd:pfam05483 422 DEKKQF--EKIAEELKGKEQELiflLQAREKEihdleiQLTAIKTSEEHYLKEVEDLKTELEKEKLknieltahcdKLLL 499

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 765365472  538 EQEKM------MEHKLKVQKELLVEGFRKKSDMLKN------EISQLREEIERTRKK 582
Cdd:pfam05483 500 ENKELtqeasdMTLELKKHQEDIINCKKQEERMLKQienleeKEMNLRDELESVREE 556
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 468-581 3.77e-04

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: 43.57  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  468 ILQSDKALTDGERA-----VAAERTKKEVAEKERELLKQRQKEQEQVMEAQERSFQENIAKLQEK--MERERVM-LLREQ 539
Cdd:pfam17380 277 IVQHQKAVSERQQQekfekMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERmaMERERELeRIRQE 356

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 765365472  540 EKMMEHKLKVQKELLVEGFR-KKSDMLKNEISQ----LREEIERTRK 581
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRmRELERLQMERQQknerVRQELEAARK 403
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 431-582 7.52e-04

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: 42.06  E-value: 7.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 431 EARKKVELSYEQVPRKGVKAKEVLKSFLQSQATVENSILQSDKALTDGERAVAAERTKKEVAEKERELLKQRQKEQEQVM 510
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 511 EAQERSFQENIAKLQEKMERERVMLLREQE---------KMMEHKLKVQKELLvEGFRKKsdmlKNEISQLREEIERTRK 581
Cdd:COG4942  100 EAQKEELAELLRALYRLGRQPPLALLLSPEdfldavrrlQYLKYLAPARREQA-EELRAD----LAELAALRAELEAERA 174


                 .
gi 765365472 582 K 582
Cdd:COG4942  175 E 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 367-578 9.88e-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: 42.35  E-value: 9.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472   367 KDDEQEFQK-----RLVATIEKWKEEFMLRNEAASIRH-CQAELEKLSESLKESIScgafSVPGGHSLYLEARKKVELSY 440
Cdd:TIGR02168  219 KAELRELELallvlRLEELREELEELQEELKEAEEELEeLTAELQELEEKLEELRL----EVSELEEEIEELQKELYALA 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472   441 EQVPRKGVK---AKEVLKSFLQSQATVENSILQSDKALTDGERAVAAERTKKEVAEKERELLKQRQKEQEQVMEAQERSF 517
Cdd:TIGR02168  295 NEISRLEQQkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 765365472   518 QEniakLQEKMERER--VMLLREQEKMmehklkvqkellvegfrkksdmLKNEISQLREEIER 578
Cdd:TIGR02168  375 EE----LEEQLETLRskVAQLELQIAS----------------------LNNEIERLEARLER 411
PTZ00121 PTZ00121
MAEBL; Provisional
 431-582 1.03e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  431 EARKKVELSYEQVPRKGVKAKEVLKSFLQSQATV--ENSILQSDKALTDGERAVAAERTKKEVAEKER-ELLKQRQKEQ- 506
Cdd:PTZ00121 1567 EEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLyeEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKvEQLKKKEAEEk 1646

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  507 ---EQVMEAQE----RSFQENIAKLQEKMERERVMLLREQEKMMEHKLKVQKE--LLVEGFRKKSDMLKNEISQLREEIE 577
Cdd:PTZ00121 1647 kkaEELKKAEEenkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEeaKKAEELKKKEAEEKKKAEELKKAEE 1726


                  ....*
gi 765365472  578 RTRKK 582
Cdd:PTZ00121 1727 ENKIK 1731
RHD3_GTPase pfam05879
Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of ...
 43-114 1.04e-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: 41.28  E-value: 1.04e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 765365472   43 TGKSYLMNRLAGRNHGFSLGSTVQSETKGIWMWCVPHPTKPTHTLVLLDTEGLGDVEKG---DPKNDSWIFALAV 114
Cdd:pfam05879   6 TGKSTLLNHLFGTNFSVMDASGRQQTTKGIWLAKCKGIGNMEPNILVMDVEGTDGRERGedqDFERKSALFALAT 80
YeeP COG3596
Predicted GTPase [General function prediction only];
28-104 1.27e-03

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 41.29  E-value: 1.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 765365472  28 IAQPLVVVAIVGLYRTGKSYLMNRLAGRNhgFSLGSTVQSETKGIwmWCVPHPTKPTHTLVLLDTEGLGDVEKGDPK 104
Cdd:COG3596   35 VELPPPVIALVGKTGAGKSSLINALFGAE--VAEVGVGRPCTREI--QRYRLESDGLPGLVLLDTPGLGEVNERDRE 107
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 487-581 1.32e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 39.09  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  487 TKKEVAEKERELLKQRQKEqeqvMEAQERSFQENIAKLQE---KMERERVMLLREQEKmmEHKLKVQKELLVEGFRKKSD 563
Cdd:pfam13863  17 AKREEIERLEELLKQREEE----LEKKEQELKEDLIKFDKflkENDAKRRRALKKAEE--ETKLKKEKEKEIKKLTAQIE 90

                          90
                  ....*....|....*...
gi 765365472  564 MLKNEISQLREEIERTRK 581
Cdd:pfam13863  91 ELKSEISKLEEKLEEYKP 108
Caldesmon pfam02029
Caldesmon;
431-584 1.42e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 41.39  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  431 EARKKVELSYEQVPRKGVKAKEVLKSFLQSQATVENSILQSDKALTDGERAVAAERTKKEVAEKERELLKQRQKEQEQVM 510
Cdd:pfam02029 171 TENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKL 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  511 EAQERSFQEN----IAKLQEKmERERVMLLREQEKMMEHKLKVQKEllvEGFRKKSDMLKNEIS------QLREEIERTR 580
Cdd:pfam02029 251 EELRRRRQEKeseeFEKLRQK-QQEAELELEELKKKREERRKLLEE---EEQRRKQEEAERKLReeeekrRMKEEIERRR 326


                  ....
gi 765365472  581 KKPS 584
Cdd:pfam02029 327 AEAA 330
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
451-582 1.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 451 KEVLKSFLQSQATVENSILQSDKALTDGERAVAAERTKKEVAEKERELLKQRQKEQEQV------MEAQERSFQENIAKL 524
Cdd:PRK03918 178 IERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELkeeieeLEKELESLEGSKRKL 257

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 765365472 525 QEKME--RERVMLLREQEKMMEHKLKVQKEL------------LVEGFRKKSDMLKNEISQLREEIERTRKK 582
Cdd:PRK03918 258 EEKIRelEERIEELKKEIEELEEKVKELKELkekaeeyiklseFYEEYLDELREIEKRLSRLEEEINGIEER 329
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 316-580 2.70e-03

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: 40.86  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  316 ENSAAVQKAAEhyaeqmaQRLRLPTDTLQELLEVHSACEKEAIAVFMEHSFKDDEQEfqkRLVATIEKW--KEEFMLRNE 393
Cdd:pfam05483 306 QRSMSTQKALE-------EDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFE---ATTCSLEELlrTEQQRLEKN 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  394 AASIRHCQAELEKLSESLKESIScgafsVPGGHSLYLEARKKVeLSYEQVPRKGVKAKEVLKSFLQSQATVENSILQS-D 472
Cdd:pfam05483 376 EDQLKIITMELQKKSSELEEMTK-----FKNNKEVELEELKKI-LAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQArE 449

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  473 KALTDGERAVAAERTK-----KEVAEKERELLKQRQKEQEQVMEAQERSFqENIAKLQEKmeRERVMLLREQEKMMEHKL 547
Cdd:pfam05483 450 KEIHDLEIQLTAIKTSeehylKEVEDLKTELEKEKLKNIELTAHCDKLLL-ENKELTQEA--SDMTLELKKHQEDIINCK 526

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 765365472  548 KVQKELL--VEGFRKKSDMLKNEISQLREEIERTR 580
Cdd:pfam05483 527 KQEERMLkqIENLEEKEMNLRDELESVREEFIQKG 561
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 460-582 3.62e-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: 40.32  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  460 SQATVENsiLQSDKALTDGERAVAAERTKKEVAEKERELLKQRQKEQEQvmeaQERSfqeniaklqEKMERErvmLLREQ 539
Cdd:pfam15709 321 SKALLEK--REQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQ----LERA---------EKMREE---LELEQ 382

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 765365472  540 EKMMEhKLKVQKELLVEGFRKKSDMLKNEISQLREEIERTRKK 582
Cdd:pfam15709 383 QRRFE-EIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQ 424
PTZ00121 PTZ00121
MAEBL; Provisional
 431-581 3.89e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  431 EARKKVELSyeqvprkgvKAKEVLKSflqSQATVENSILQSDKALTDGERAVAAERTKK--EVAEKERELLKQR---QKE 505
Cdd:PTZ00121 1276 EARKADELK---------KAEEKKKA---DEAKKAEEKKKADEAKKKAEEAKKADEAKKkaEEAKKKADAAKKKaeeAKK 1343

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 765365472  506 QEQVMEAQERSFQENIAKLQEKMERERVMLLREQEKMMEHKLKVQKELLVEGFRKKSDMLKNEISQLREEIERTRK 581
Cdd:PTZ00121 1344 AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKK 1419
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 488-552 4.27e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 37.59  E-value: 4.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 765365472  488 KKEVAEKERELLKQRQKEQEQVMEAQERSfQENIAKLQEKMERERVMLLREQEKMMEHKLKVQKE 552
Cdd:pfam20492  42 ERRQAEEEAERLEQKRQEAEEEKERLEES-AEMEAEEKEQLEAELAEAQEEIARLEEEVERKEEE 105
DUF2058 pfam09831
Uncharacterized protein conserved in bacteria (DUF2058); This domain, found in various ...
 470-508 4.63e-03

Uncharacterized protein conserved in bacteria (DUF2058); This domain, found in various prokaryotic proteins, has no known function.


Pssm-ID: 430862 [Multi-domain]  Cd Length: 174  Bit Score: 38.33  E-value: 4.63e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 765365472  470 QSDKALTDGERAVAAERTKKEVAEKERELLKQRQKEQEQ 508
Cdd:pfam09831  30 QKRKKGAVDEAKAAAEEAKAEKAERDRELNRQRQAEAEQ 68
PTZ00121 PTZ00121
MAEBL; Provisional
 431-582 4.93e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 4.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  431 EARKKVELSYEQVPRKGVKAK--EVLKSflqsqatVENSILQSDKALTDGERAVAAERTKKEVAEKER-ELLKQRQKEQE 507
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRkaEEAKK-------AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKaEELKKAEEEKK 1633

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 765365472  508 QVMEAQERSFQENIAKLQEKMERERVMLLREQEKMMEHKLKVQKELLV---EGFRKKSDMLKNEISQLReEIERTRKK 582
Cdd:PTZ00121 1634 KVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKkaeEDEKKAAEALKKEAEEAK-KAEELKKK 1710
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 305-582 5.94e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 5.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 305 LENAVTALAQRENSAAVQKAAEHYAEQMAQRLRLPTDTLQELLEVHSACEKEAIAVFME-HSFKDDEQEFQKRLVATIEK 383
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARlEQDIARLEERRRELEERLEE 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 384 WKEEfmLRNEAASIRHCQAELEKLSESLKEsiscgafsvpgghslyLEARKKvelsyeqvprkgvKAKEVLKSFLQSQAT 463
Cdd:COG1196  321 LEEE--LAELEEELEELEEELEELEEELEE----------------AEEELE-------------EAEAELAEAEEALLE 369

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 464 VENSILQSDKALTDGERAVAAERTKKEVAEKERELLKQRQK--EQEQVM-EAQERSFQENIAKLQEKMERERVMLLREQE 540
Cdd:COG1196  370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEalLERLERlEEELEELEEALAELEEEEEEEEEALEEAAE 449

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 765365472 541 KMMEHK-LKVQKELLVEGFRKKSDMLKNEISQLREEIERTRKK 582
Cdd:COG1196  450 EEAELEeEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
RRP36 pfam06102
rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.
 485-582 7.42e-03

rRNA biogenesis protein RRP36; RRP36 is involved in the early processing steps of the pre-rRNA.


Pssm-ID: 461829 [Multi-domain]  Cd Length: 158  Bit Score: 37.54  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  485 ERTKKEVAEKERELLKQRQKEqeqvMEAQERSFQENIAKLQEKMERERvmllREQEKMMEHK----LK---VQKELLVEg 557
Cdd:pfam06102  67 KQLKKTKDPEEKEELKRTLQS----MESRLKAKKRKDREREVLKEHKK----EEKEKVKQGKkpfyLKkseKKKLLLKE- 137

                          90       100
                  ....*....|....*....|....*
gi 765365472  558 frKKSDMLKNeiSQLREEIERTRKK 582
Cdd:pfam06102 138 --KFEELKKS--GKLDKAIEKKRKK 158
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
449-578 7.43e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 7.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472 449 KAKEVLKSFLQSQATVENSILQSDKALTDGERAVAAERTKKEVAEKERELLKQRQKEQEQVMEAQERsfqenIAKLQEKM 528
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRER-----KRELEAEF 643

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 765365472 529 ERERVMLLREQEKMMEHKL-KVQKELlvEGFRKKSDMLKNEISQLREEIER 578
Cdd:PRK02224 644 DEARIEEAREDKERAEEYLeQVEEKL--DELREERDDLQAEIGAVENELEE 692
PTZ00121 PTZ00121
MAEBL; Provisional
 431-582 8.65e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 8.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  431 EARKKVELSYEQVPRKgvkAKEVLKSFLQSQATVENSILQSDKAlTDGERAVA---AERTKKEV-----AEKERELLKQR 502
Cdd:PTZ00121 1180 AARKAEEVRKAEELRK---AEDARKAEAARKAEEERKAEEARKA-EDAKKAEAvkkAEEAKKDAeeakkAEEERNNEEIR 1255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  503 QKEQ---------EQVMEAQERSFQENIAKLQEKMERERVMLLREQEKMMEHKLKVQKELLVEGFRKKSDMLKNEISQLR 573
Cdd:PTZ00121 1256 KFEEarmahfarrQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK 1335


                  ....*....
gi 765365472  574 EEIERTRKK 582
Cdd:PTZ00121 1336 KKAEEAKKA 1344
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 482-577 9.46e-03

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 37.73  E-value: 9.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472  482 VAAERTKKEVAEKERELLKQRQKEQEQVMEAQERS-----FQENIAKLQEKMERERVMLLREQEKMMEHKLKVQKEL--- 553
Cdd:pfam05010   8 AALEKARNEIEEKELEINELKAKYEELRRENLEMRkivaeFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQALADLnsv 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 765365472  554 ----------------LVEGFRKKSDMLKNEISQLREEIE 577
Cdd:pfam05010  88 eksfsdlfkryekqkeVISGYKKNEESLKKCAQDYLARIK 127
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 330-606 9.95e-03

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: 39.27  E-value: 9.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472   330 EQMAQRLRLPTDTLQELLEVHSACEKEAIAVFMEHSFKDDEQEFQKRLVATIEKWKEEFMLRNEAASIRHCQAELEKLSE 409
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472   410 SLKESISCGAFSVPGGHSLYLEAR-KKVELSYEQVPRKGVKAKEVLKSFLQSQATVENSILQSDKALTDGERAVAAERTK 488
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQiEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765365472   489 KEVAEKERELLKQRQKEQEQVMEAQER---SFQENIAKLQEKME--RERVMLLREQEKMMEHKLkvqKELlvegfRKKSD 563
Cdd:TIGR02168  847 IEELSEDIESLAAEIEELEELIEELESeleALLNERASLEEALAllRSELEELSEELRELESKR---SEL-----RRELE 918

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 765365472   564 MLKNEISQLREEIERTRKKpslFAHILDTVGNAFIMILPGAGK 606
Cdd:TIGR02168  919 ELREKLAQLELRLEGLEVR---IDNLQERLSEEYSLTLEEAEA 958
 
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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