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Conserved domains on  [gi|829496033|ref|NP_001034736|]
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guanylate binding protein 11 [Mus musculus]

Protein Classification

guanylate-binding family protein( domain architecture ID 12033579)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 281-575 2.49e-150

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: 435.56  E-value: 2.49e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  281 EGIKVTGNGLGILVTTYVDAINSGAVPCLHDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKE 360
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  361 AMAVFMEHSFKDENQQFLKKLVELISEKNGLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKI 438
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  439 EHDYWQVPRKGVKAIEVFQSFLQSQAIIESSILQADTALIAGQKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKR 518
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 829496033  519 NKENLEQLRRKLMQEREQLIKDHNMMLEKLMKEQKALLEEGYKKKAEEMRREIYRLR 575
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 16-279 5.86e-143

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: 415.23  E-value: 5.86e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033   16 NEQLLVNQEAIEILDKISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCVPHPTKPEHTLVLLD 95
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033   96 TEGLGDVEKGDPKNDLWIFALSVLLSSNFIYNSMNTISHDSLEKLHYVTELTELirakSSPNPHGIKNSTEFVSFFPDFV 175
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  176 WTVRDFTLKLKLNGEDITSDGYLENALKLIPDNNPRMQASNLARECIRRFFPNRKCFVFDRPTYDIELLQKLETISEDQL 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236

                         250       260
                  ....*....|....*....|....
gi 829496033  256 DPMFQKRTKAFVSYIFNYAKIKTL 279
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
 
Name Accession Description Interval E-value
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 281-575 2.49e-150

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: 435.56  E-value: 2.49e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  281 EGIKVTGNGLGILVTTYVDAINSGAVPCLHDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKE 360
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  361 AMAVFMEHSFKDENQQFLKKLVELISEKNGLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKI 438
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  439 EHDYWQVPRKGVKAIEVFQSFLQSQAIIESSILQADTALIAGQKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKR 518
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 829496033  519 NKENLEQLRRKLMQEREQLIKDHNMMLEKLMKEQKALLEEGYKKKAEEMRREIYRLR 575
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 16-279 5.86e-143

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: 415.23  E-value: 5.86e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033   16 NEQLLVNQEAIEILDKISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCVPHPTKPEHTLVLLD 95
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033   96 TEGLGDVEKGDPKNDLWIFALSVLLSSNFIYNSMNTISHDSLEKLHYVTELTELirakSSPNPHGIKNSTEFVSFFPDFV 175
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  176 WTVRDFTLKLKLNGEDITSDGYLENALKLIPDNNPRMQASNLARECIRRFFPNRKCFVFDRPTYDIELLQKLETISEDQL 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236

                         250       260
                  ....*....|....*....|....
gi 829496033  256 DPMFQKRTKAFVSYIFNYAKIKTL 279
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 287-575 8.55e-137

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: 400.80  E-value: 8.55e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 287 GNGLGILVTTYVDAINSGAVPCLHDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKEAMAVFM 366
Cdd:cd16269    1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 367 EHSFKDENQQFLKKLVELISEKNGLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQ 444
Cdd:cd16269   81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 445 VPRKGVKAIEVFQSFLQSQAIIESSILQADTALIAGQKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKRNKENLE 524
Cdd:cd16269  161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 829496033 525 QLRRKLMQEREQLIKDHNMMLEKLMKEQKALLEEGYKKKAEEMRREIYRLR 575
Cdd:cd16269  241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 31-271 4.17e-73

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: 234.14  E-value: 4.17e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  31 KISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCVPHP--TKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:cd01851    2 DVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEFE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 109 NDLWIFALSVLLSSNFIYNSMNTISHDSLEKLHYVTELTElirakSSPNPHGIKNsteFVSFFPDFVWTVRDFTLKLKLN 188
Cdd:cd01851   82 NDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL-----ETLGLAGLHN---FSKPKPLLLFVVRDFTGPTPLE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 189 GEDITSDGYlenalklipdnnPRMQASNLARECIRRFFPNRKCFVFDRPTYDIELLQKleTISEDQLDPMFQKRTKAFVS 268
Cdd:cd01851  154 GLDVTEKSE------------TLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKALRQ 219


                 ...
gi 829496033 269 YIF 271
Cdd:cd01851  220 RFF 222
PTZ00121 PTZ00121
MAEBL; Provisional
 481-586 1.07e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  481 QKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYME---AQEKRNKENLEQLRRKLMQER----------------EQLIKDH 541
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkKAEEENKIKAEEAKKEAEEDKkkaeeakkdeeekkkiAHLKKEE 1766

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 829496033  542 NMMLEKLMKEQKALLEEGYKKKAEEMRREIYRlrhNIKDMKQNSD 586
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK---KIKDIFDNFA 1808
YeeP COG3596
Predicted GTPase [General function prediction only];
23-108 3.93e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 45.91  E-value: 3.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  23 QEAIEILdKISQPVVVVAIVGLYRTGKSYLMNRLAGQN-----HGFPlgstvqsQTKGIwmWCVPHPTKPEHTLVLLDTE 97
Cdd:COG3596   27 AEALERL-LVELPPPVIALVGKTGAGKSSLINALFGAEvaevgVGRP-------CTREI--QRYRLESDGLPGLVLLDTP 96

                         90
                 ....*....|.
gi 829496033  98 GLGDVEKGDPK 108
Cdd:COG3596   97 GLGEVNERDRE 107
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 476-581 9.25e-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: 9.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 476 ALIAGQKAIAEKcTNKEAAEKEQDLLRQKQKEQQKYMEAQEKRNKENLEQLR--RKLMQEREQLIKDHNMMLEKLMKEQK 553
Cdd:COG4942    8 ALLLALAAAAQA-DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalERRIAALARRIRALEQELAALEAELA 86

                         90       100
                 ....*....|....*....|....*...
gi 829496033 554 ALleegyKKKAEEMRREIYRLRHNIKDM 581
Cdd:COG4942   87 EL-----EKEIAELRAELEAQKEELAEL 109
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 456-589 5.20e-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: 40.04  E-value: 5.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033   456 FQSFLQSQAIIESSILQADTALIAGQKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKRNK---ENLEQLRRKLMQ 532
Cdd:TIGR02168  311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleEQLETLRSKVAQ 390

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033   533 EREQL-------------IKDHNMMLEKLMKEQKALLEEGYKKKAEEMRREIYRLRHNIKDMKQNSDFFV 589
Cdd:TIGR02168  391 LELQIaslnneierlearLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
 
Name Accession Description Interval E-value
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 281-575 2.49e-150

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: 435.56  E-value: 2.49e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  281 EGIKVTGNGLGILVTTYVDAINSGAVPCLHDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKE 360
Cdd:pfam02841   1 GGITVTGPRLGSLVQTYVDAINSGAVPCLENAVLALAQIENSAAVQKAIAHYEQQMAQKVKLPTETLQELLDLHRDCEKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  361 AMAVFMEHSFKDENQQFLKKLVELISEKNGLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKI 438
Cdd:pfam02841  81 AIAVFMKRSFKDENQEFQKELVELLEAKKDDFLKQNEEASSKYCSALLQDLSEPLEEKISqgTFSKPGGYKLFLEERDKL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  439 EHDYWQVPRKGVKAIEVFQSFLQSQAIIESSILQADTALIAGQKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKR 518
Cdd:pfam02841 161 EAKYNQVPRKGVKAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERS 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 829496033  519 NKENLEQLRRKLMQEREQLIKDHNMMLEKLMKEQKALLEEGYKKKAEEMRREIYRLR 575
Cdd:pfam02841 241 YQEHVKQLIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQDLK 297
GBP pfam02263
Guanylate-binding protein, N-terminal domain; Transcription of the anti-viral ...
 16-279 5.86e-143

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: 415.23  E-value: 5.86e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033   16 NEQLLVNQEAIEILDKISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCVPHPTKPEHTLVLLD 95
Cdd:pfam02263   1 DHQLELNEEALEILSAITQPVVVVAIAGLYRTGKSFLMNFLAGKLTGFSLGGTVESETKGIWMWCVPHPNKPKHTLVLLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033   96 TEGLGDVEKGDPKNDLWIFALSVLLSSNFIYNSMNTISHDSLEKLHYVTELTELirakSSPNPHGIKNSTEFVSFFPDFV 175
Cdd:pfam02263  81 TEGLGDVEKSDNKNDAWIFALATLLSSTFVYNSSQTINQQALQQLHLVTELTEL----SSPRYGRVADSADFVSFFPDFV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  176 WTVRDFTLKLKLNGEDITSDGYLENALKLIPDNNPRMQASNLARECIRRFFPNRKCFVFDRPTYDIELLQKLETISEDQL 255
Cdd:pfam02263 157 WTVRDFSLPLEADGGPITGDEYLENRLKLSQGQHEELQNFNLPRLCIRSFFPKRKCFLFDRPGLKKALNPQFEGLREDEL 236

                         250       260
                  ....*....|....*....|....
gi 829496033  256 DPMFQKRTKAFVSYIFNYAKIKTL 279
Cdd:pfam02263 237 DPEFQQQLREFCSYILSHSLVKTL 260
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 287-575 8.55e-137

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: 400.80  E-value: 8.55e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 287 GNGLGILVTTYVDAINSGAVPCLHDAVTTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQELLDVHAACEKEAMAVFM 366
Cdd:cd16269    1 GRRLGTLVETYVDAINSGAVPCLENAVLALAQIENSAAVQKALAHYEEQMEQRVQLPTETLQELLDLHAACEKEALEVFM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 367 EHSFKDENQQFLKKLVELISEKNGLFLLKNEEASDKYCQEELDRLSKDLMDNIS--TFSVPGGHRLYMDMREKIEHDYWQ 444
Cdd:cd16269   81 KRSFKDEDQKFQKKLMEQLEEKKEEFCKQNEEASSKRCQALLQELSAPLEEKISqgSYSVPGGYQLYLEDREKLVEKYRQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 445 VPRKGVKAIEVFQSFLQSQAIIESSILQADTALIAGQKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKRNKENLE 524
Cdd:cd16269  161 VPRKGVKAEEVLQEFLQSKEAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLR 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 829496033 525 QLRRKLMQEREQLIKDHNMMLEKLMKEQKALLEEGYKKKAEEMRREIYRLR 575
Cdd:cd16269  241 QLKEKMEEERENLLKEQERALESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 31-271 4.17e-73

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: 234.14  E-value: 4.17e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  31 KISQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCVPHP--TKPEHTLVLLDTEGLGDVEKGDPK 108
Cdd:cd01851    2 DVGFPVVVVSVFGSQSSGKSFLLNHLFGTSDGFDVMDTSQQTTKGIWMWSDPFKdtDGKKHAVLLLDTEGTDGRERGEFE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 109 NDLWIFALSVLLSSNFIYNSMNTISHDSLEKLHYVTELTElirakSSPNPHGIKNsteFVSFFPDFVWTVRDFTLKLKLN 188
Cdd:cd01851   82 NDARLFALATLLSSVLIYNMWQTILGDDLDKLMGLLKTAL-----ETLGLAGLHN---FSKPKPLLLFVVRDFTGPTPLE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 189 GEDITSDGYlenalklipdnnPRMQASNLARECIRRFFPNRKCFVFDRPTYDIELLQKleTISEDQLDPMFQKRTKAFVS 268
Cdd:cd01851  154 GLDVTEKSE------------TLIEELNKIWSSIRKPFTPITCFVLPHPGLLHKLLQN--DGRLKDLPPEFRKALKALRQ 219


                 ...
gi 829496033 269 YIF 271
Cdd:cd01851  220 RFF 222
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 40-115 2.99e-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: 53.23  E-value: 2.99e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 829496033  40 AIVGLYRTGKSYLMNRLAGQNHGFPlgSTVQSQTKGIWMWCVPHPtKPEHTLVLLDTEGLGDVEKGDPKNDLWIFA 115
Cdd:cd00882    1 VVVGRGGVGKSSLLNALLGGEVGEV--SDVPGTTRDPDVYVKELD-KGKVKLVLVDTPGLDEFGGLGREELARLLL 73
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 492-570 1.84e-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: 54.36  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  492 EAAEKEQDL--LRQKQKEQ--QKYMEAQEKRNKENLEQLRRKL----MQEREQLI---KDHNMMLEKLMKE-QKALLEEG 559
Cdd:pfam17380 454 EEQERQQQVerLRQQEEERkrKKLELEKEKRDRKRAEEQRRKIlekeLEERKQAMieeERKRKLLEKEMEErQKAIYEEE 533

                          90
                  ....*....|.
gi 829496033  560 YKKKAEEMRRE 570
Cdd:pfam17380 534 RRREAEEERRK 544
PTZ00121 PTZ00121
MAEBL; Provisional
 481-586 1.07e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  481 QKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYME---AQEKRNKENLEQLRRKLMQER----------------EQLIKDH 541
Cdd:PTZ00121 1687 EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEelkKAEEENKIKAEEAKKEAEEDKkkaeeakkdeeekkkiAHLKKEE 1766

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 829496033  542 NMMLEKLMKEQKALLEEGYKKKAEEMRREIYRlrhNIKDMKQNSD 586
Cdd:PTZ00121 1767 EKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK---KIKDIFDNFA 1808
CCDC66 pfam15236
Coiled-coil domain-containing protein 66; This protein family, named Coiled-coil ...
 497-584 1.46e-05

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: 45.56  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  497 EQDLLRQKQKEQQKYMEAQ--EKRNKENLEQLRRKL--MQEREQLIKDHNMMLEKLMKEQKALL--EEGYKKKAEEMRRE 570
Cdd:pfam15236  46 ERERKRQKALEHQNAIKKQleEKERQKKLEEERRRQeeQEEEERLRREREEEQKQFEEERRKQKekEEAMTRKTQALLQA 125

                          90
                  ....*....|....
gi 829496033  571 IYRLRHNIKDMKQN 584
Cdd:pfam15236 126 MQKAQELAQRLKQE 139
YeeP COG3596
Predicted GTPase [General function prediction only];
23-108 3.93e-05

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 45.91  E-value: 3.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  23 QEAIEILdKISQPVVVVAIVGLYRTGKSYLMNRLAGQN-----HGFPlgstvqsQTKGIwmWCVPHPTKPEHTLVLLDTE 97
Cdd:COG3596   27 AEALERL-LVELPPPVIALVGKTGAGKSSLINALFGAEvaevgVGRP-------CTREI--QRYRLESDGLPGLVLLDTP 96

                         90
                 ....*....|.
gi 829496033  98 GLGDVEKGDPK 108
Cdd:COG3596   97 GLGEVNERDRE 107
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 314-553 9.09e-05

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 45.60  E-value: 9.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033   314 TTLAQRENSVAVQKAADHYSEQMAQRLRLPTETLQelldVHAACEKEAMAVFMEHSFKDENQQFLKKLVELISEKNGLFL 393
Cdd:pfam12128  462 LLLQLENFDERIERAREEQEAANAEVERLQSELRQ----ARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLL 537

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033   394 --LKNE-----EASDKYCQEELdRLSKDLMDNISTFSVPGGHRLY---MDMrEKIEHDYW-----QVPRKGVKAIEVFQS 458
Cdd:pfam12128  538 hfLRKEapdweQSIGKVISPEL-LHRTDLDPEVWDGSVGGELNLYgvkLDL-KRIDVPEWaaseeELRERLDKAEEALQS 615

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033   459 FLQSQAIIESSILQADTALIAGQKAIAE-KCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKRNKENLEQlRRKLMQEREQL 537
Cdd:pfam12128  616 AREKQAAAEEQLVQANGELEKASREETFaRTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANER-LNSLEAQLKQL 694

                          250
                   ....*....|....*.
gi 829496033   538 IKDHNMMLEKlMKEQK 553
Cdd:pfam12128  695 DKKHQAWLEE-QKEQK 709
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 495-583 1.19e-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: 45.11  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  495 EKEQDLLRQKQKEQQKYMEAQEKRNKENlEQLRRKLMQEREQ----LIKDHN-MMLEKLMKEQK-ALLEEGYKKK----- 563
Cdd:pfam17380 443 ERAREMERVRLEEQERQQQVERLRQQEE-ERKRKKLELEKEKrdrkRAEEQRrKILEKELEERKqAMIEEERKRKlleke 521

                          90       100
                  ....*....|....*....|....*....
gi 829496033  564 ---------AEEMRREIYRLRHNIKDMKQ 583
Cdd:pfam17380 522 meerqkaiyEEERRREAEEERRKQQEMEE 550
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 463-575 1.83e-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: 44.73  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  463 QAIIESSILQADTALIAGQKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEaqEKRNKENLEQLRRKLMQ-------ERE 535
Cdd:pfam17380 263 QTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVE--RRRKLEEAEKARQAEMDrqaaiyaEQE 340

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 829496033  536 QLIKDHNMMLEKLMKEQKAllEEGYKKKAEEMRREIYRLR 575
Cdd:pfam17380 341 RMAMERERELERIRQEERK--RELERIRQEEIAMEISRMR 378
PTZ00121 PTZ00121
MAEBL; Provisional
 481-570 2.95e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  481 QKAIAEKCTNKEAAEKEQDllrQKQKEQQKYMEAQEKRNKENLEQLRRKLMQEREQLIKDHNMmlEKLMKEQKALLEEGY 560
Cdd:PTZ00121 1668 KKAEEDKKKAEEAKKAEED---EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE--NKIKAEEAKKEAEED 1742

                          90
                  ....*....|
gi 829496033  561 KKKAEEMRRE 570
Cdd:PTZ00121 1743 KKKAEEAKKD 1752
DUF4175 pfam13779
Domain of unknown function (DUF4175);
472-567 5.65e-04

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 43.05  E-value: 5.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  472 QADTALIAGQKAIAEKCTNKeAAEKE-QDLLRQKQKEQQKYMEAQEKRNKENLEQLRRKLMQEREQLIKDHnmmLEKLMK 550
Cdd:pfam13779 486 DAERRLRAAQERLSEALERG-ASDEEiAKLMQELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEMTQQD---LQRMLD 561

                          90
                  ....*....|....*..
gi 829496033  551 EQKALLEEGYKKKAEEM 567
Cdd:pfam13779 562 RIEELARSGRRAEAQQM 578
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 485-566 7.22e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.10  E-value: 7.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 485 AEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKRNKENlEQLRRKLMQEREQLIKdhnmmlEKLMKEQKALLEEGYKKKA 564
Cdd:PRK09510  77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQ-EQKKQAEEAAKQAALK------QKQAEEAAAKAAAAAKAKA 149


                 ..
gi 829496033 565 EE 566
Cdd:PRK09510 150 EA 151
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
 498-583 7.45e-04

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: 39.47  E-value: 7.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  498 QDLLRQKQKEQQKYMEAQEKRnkenleqlrRKLMQEREQLIKDHNMMLEKLMKEQKALLEEGYKKKAEEMR------REI 571
Cdd:pfam13863  12 QLALDAKREEIERLEELLKQR---------EEELEKKEQELKEDLIKFDKFLKENDAKRRRALKKAEEETKlkkekeKEI 82

                          90
                  ....*....|..
gi 829496033  572 YRLRHNIKDMKQ 583
Cdd:pfam13863  83 KKLTAQIEELKS 94
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 494-570 8.41e-04

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


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 40.41  E-value: 8.41e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 829496033  494 AEKEQDLLRQKQKEQQKYMEaQEKRNKENLEQLRRKLMQEREQLikdhnMMLEKLMKEQKALLEEGYKKKAEEMRRE 570
Cdd:pfam05672  17 AEKRRQAREQREREEQERLE-KEEEERLRKEELRRRAEEERARR-----EEEARRLEEERRREEEERQRKAEEEAEE 87
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 481-570 9.14e-04

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 9.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  481 QKAIAEKCTNKEAAEKEQDLLR-------QKQKEQQKYMEAQEKRnkenlEQLRRKLMQEREQLIKDHNMMLEKLMKEQK 553
Cdd:pfam13868 186 IARLRAQQEKAQDEKAERDELRaklyqeeQERKERQKEREEAEKK-----ARQRQELQQAREEQIELKERRLAEEAEREE 260

                          90
                  ....*....|....*..
gi 829496033  554 ALLEEGYKKKAEEMRRE 570
Cdd:pfam13868 261 EEFERMLRKQAEDEEIE 277
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 476-581 9.25e-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: 9.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 476 ALIAGQKAIAEKcTNKEAAEKEQDLLRQKQKEQQKYMEAQEKRNKENLEQLR--RKLMQEREQLIKDHNMMLEKLMKEQK 553
Cdd:COG4942    8 ALLLALAAAAQA-DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAalERRIAALARRIRALEQELAALEAELA 86

                         90       100
                 ....*....|....*....|....*...
gi 829496033 554 ALleegyKKKAEEMRREIYRLRHNIKDM 581
Cdd:COG4942   87 EL-----EKEIAELRAELEAQKEELAEL 109
PRK12704 PRK12704
phosphodiesterase; Provisional
 491-569 1.08e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 1.08e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 829496033 491 KEAAEKEQDLLRQKQKEQQKymEAQEKRNKENLEQLRRKLMQEREQLIKdhnmmLEKLMKEQKALLEEGYKKKAEEMRR 569
Cdd:PRK12704  75 KELRERRNELQKLEKRLLQK--EENLDRKLELLEKREEELEKKEKELEQ-----KQQELEKKEEELEELIEEQLQELER 146
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 457-570 1.18e-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: 41.67  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 457 QSFLQSQ--AIIESSILQADTALIAG----QKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKRNKENLEQLRRKL 530
Cdd:COG4942  129 EDFLDAVrrLQYLKYLAPARREQAEElradLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 829496033 531 MQEREQlikdhnmmLEKLMKEQKALLEEGYKKKAEEMRRE 570
Cdd:COG4942  209 AELAAE--------LAELQQEAEELEALIARLEAEAAAAA 240
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 472-583 2.77e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.88  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  472 QADTALIAGQKAI-AEKctNKEAAEKEQDLLRQKQKEQQK-----------------------YMEAQEK--RNKENLEQ 525
Cdd:pfam17380 323 KARQAEMDRQAAIyAEQ--ERMAMERERELERIRQEERKRelerirqeeiameisrmrelerlQMERQQKneRVRQELEA 400

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  526 LRRK--LMQEREQLIKDHNMMLEKLMKEQKALLEEGYKKKAEEMRREIYRLRHNIKDMKQ 583
Cdd:pfam17380 401 ARKVkiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQ 460
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 481-570 3.01e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 3.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  481 QKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEK-RNKENLEQLRRKLMQEREQLIKDHNMMLEKLMKEQKALLEEG 559
Cdd:pfam13868 169 EEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDElRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELK 248

                          90
                  ....*....|.
gi 829496033  560 YKKKAEEMRRE 570
Cdd:pfam13868 249 ERRLAEEAERE 259
fliH PRK06669
flagellar assembly protein H; Validated
 445-570 3.59e-03

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 39.61  E-value: 3.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 445 VPRKGVKAIEVFQSFLQSQAIIESSILQADTALIAGQ--KAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKRNKen 522
Cdd:PRK06669  12 INKEKLKTHEIQKYRFKVLSIKEKERLREEEEEQVEQlrEEANDEAKEIIEEAEEDAFEIVEAAEEEAKEELLKKTDE-- 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 829496033 523 LEQLRRKLMQEREQLIKDHNMMLEKLMKEQKAlleEGYKKKAEEMRRE 570
Cdd:PRK06669  90 ASSIIEKLQMQIEREQEEWEEELERLIEEAKA---EGYEEGYEKGREE 134
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 491-570 3.74e-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: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  491 KEAAEKEQDLLRQKQKEQQKYMEAQEKRNKENLEQL---RRKLMQEREQlikdhnMMLEKLMKEQKAllEEGYKKKAEEM 567
Cdd:pfam15709 426 EEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQLaeeQKRLMEMAEE------ERLEYQRQKQEA--EEKARLEAEER 497


                  ...
gi 829496033  568 RRE 570
Cdd:pfam15709 498 RQK 500
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 481-570 4.16e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  481 QKAIAEKCTNKEAAEKEQDllRQKQKEQQKYMEAQEKRNKENLEQLRRKLMQEREQLIKDHNmmlEKLMKEQKALLEEGY 560
Cdd:pfam13868 244 QIELKERRLAEEAEREEEE--FERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEERE---EQRAAEREEELEEGE 318

                          90
                  ....*....|
gi 829496033  561 KKKAEEMRRE 570
Cdd:pfam13868 319 RLREEEAERR 328
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
 524-575 4.24e-03

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 37.93  E-value: 4.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 829496033  524 EQLRRKLMQEREQLIKDHNMMLEKLMKEQKALLEEGYKKKAEEMRREIYRLR 575
Cdd:pfam12474   6 EQQKDRFEQERQQLKKRYEKELEQLERQQKQQIEKLEQRQTQELRRLPKRIR 57
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 477-584 4.30e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 40.20  E-value: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 477 LIAG--QKAIAEKCTNKEAAEKEQDL--LRQKQKEQQKYMEAQEKRNKENLEQ----LRRKLMQEREQLIKDHNMMLEKL 548
Cdd:PRK00409 521 LIASleELERELEQKAEEAEALLKEAekLKEELEEKKEKLQEEEDKLLEEAEKeaqqAIKEAKKEADEIIKELRQLQKGG 600

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 829496033 549 MKEQKAlleegykKKAEEMRREIyRLRHNIKDMKQN 584
Cdd:PRK00409 601 YASVKA-------HELIEARKRL-NKANEKKEKKKK 628
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 456-589 5.20e-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: 40.04  E-value: 5.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033   456 FQSFLQSQAIIESSILQADTALIAGQKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKRNK---ENLEQLRRKLMQ 532
Cdd:TIGR02168  311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEeleEQLETLRSKVAQ 390

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033   533 EREQL-------------IKDHNMMLEKLMKEQKALLEEGYKKKAEEMRREIYRLRHNIKDMKQNSDFFV 589
Cdd:TIGR02168  391 LELQIaslnneierlearLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
478-586 5.27e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.84  E-value: 5.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 478 IAGQ--KAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKRNK-----ENLE----QLRRKLmQEREQLIKDHNMMLE 546
Cdd:COG2433  373 IRGLsiEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRleeqvERLEaeveELEAEL-EEKDERIERLERELS 451

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 829496033 547 KLMKEQKALLEEgyKKKAEEMRREIYRLRHNIKDMKQNSD 586
Cdd:COG2433  452 EARSEERREIRK--DREISRLDREIERLERELEEERERIE 489
RHD3_GTPase pfam05879
Root hair defective 3 GTP-binding protein (RHD3) GTPase domain; This is the GTPase domain of ...
 47-118 5.51e-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: 38.97  E-value: 5.51e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 829496033   47 TGKSYLMNRLAGQNHGFPLGSTVQSQTKGIWMWCVPHPTKPEHTLVLLDTEGLGDVEKG---DPKNDLWIFALSV 118
Cdd:pfam05879   6 TGKSTLLNHLFGTNFSVMDASGRQQTTKGIWLAKCKGIGNMEPNILVMDVEGTDGRERGedqDFERKSALFALAT 80
PRK11637 PRK11637
AmiB activator; Provisional
 479-583 5.85e-03

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 39.29  E-value: 5.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 479 AGQKAIAE-KCTNKE-AAEK---------EQDLLRQKQKEQQKYMEAQEKRNKeNLEQLRRKLMQEREQLIK-DHNmmlE 546
Cdd:PRK11637 167 ARQETIAElKQTREElAAQKaeleekqsqQKTLLYEQQAQQQKLEQARNERKK-TLTGLESSLQKDQQQLSElRAN---E 242

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 829496033 547 KLMKEQKALLEEGYKKKAEEMRREIYRLRHNIKDMKQ 583
Cdd:PRK11637 243 SRLRDSIARAEREAKARAEREAREAARVRDKQKQAKR 279
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 467-581 5.88e-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: 5.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 467 ESSILQADTALIAGQKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKRNKENLEQLRRKLMQEREQLIKDHNMMLE 546
Cdd:COG1196  667 RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEE 746

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 829496033 547 KLMKEQKALLEEGYKkkAEEMRREIYRLRHNIKDM 581
Cdd:COG1196  747 LLEEEALEELPEPPD--LEELERELERLEREIEAL 779
PTZ00121 PTZ00121
MAEBL; Provisional
 481-570 6.52e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 6.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  481 QKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKR----NKENLEQLRRKLMQER---EQLIKDHNmmlEKLMKEQK 553
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKkaeeDKKKAEEAKKAEEDEKkaaEALKKEAE---EAKKAEEL 1707

                          90
                  ....*....|....*..
gi 829496033  554 ALLEEGYKKKAEEMRRE 570
Cdd:PTZ00121 1708 KKKEAEEKKKAEELKKA 1724
Caldesmon pfam02029
Caldesmon;
479-569 7.17e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 39.47  E-value: 7.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  479 AGQKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKRNKEnleqlRRKLMQEREQLIKDHNmmleklmKEQKALLEE 558
Cdd:pfam02029 246 AEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREE-----RRKLLEEEEQRRKQEE-------AERKLREEE 313

                          90
                  ....*....|.
gi 829496033  559 GYKKKAEEMRR 569
Cdd:pfam02029 314 EKRRMKEEIER 324
PTZ00121 PTZ00121
MAEBL; Provisional
 472-586 7.66e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 7.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  472 QADTALIAGQKAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEKRNKENLEQLRRKLMQEREQLIKDHNMM-LEKLMK 550
Cdd:PTZ00121 1535 KADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkAEEAKK 1614

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 829496033  551 EQKALLEEGYKKKAEEMRREIYRLRHNIKDMKQNSD 586
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 456-554 8.79e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 8.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033 456 FQSFLQSQAIIeSSILQADTALIAGQKAIAEKCTNKEA--------AEKEQDLLRQKQKEQQKYMEAQEKRnKENLEQLR 527
Cdd:COG3883  114 FSDFLDRLSAL-SKIADADADLLEELKADKAELEAKKAeleaklaeLEALKAELEAAKAELEAQQAEQEAL-LAQLSAEE 191

                         90       100
                 ....*....|....*....|....*..
gi 829496033 528 RKLMQEREQLIKDHNMMLEKLMKEQKA 554
Cdd:COG3883  192 AAAEAQLAELEAELAAAEAAAAAAAAA 218
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
 462-583 8.95e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 38.12  E-value: 8.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  462 SQAIIESSILQADTALIAGQKAIAEKCTNKEAAEKE-QDLLRQKQKEQQKYMEAQEKRNkenlEQLRRKLMQEREQLiKD 540
Cdd:pfam04012  23 PEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRlEQQTEQAKKLEEKAQAALTKGN----EELAREALAEKKSL-EK 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 829496033  541 HNMMLEKLMKEQKALleegykkkAEEMRREIYRLRHNIKDMKQ 583
Cdd:pfam04012  98 QAEALETQLAQQRSA--------VEQLRKQLAALETKIQQLKA 132
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 491-583 8.99e-03

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


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 38.75  E-value: 8.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  491 KEAAEKEQDLLRQKQKEQQKYMEAQEKRNKENLEQLRRKLMQEREQLIKDHNMMLEKLMKEQKALLEEgyKKKAEEMRRE 570
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAER--EEIEEEKERE 185

                          90
                  ....*....|...
gi 829496033  571 IYRLRHNIKDMKQ 583
Cdd:pfam13868 186 IARLRAQQEKAQD 198
PTZ00121 PTZ00121
MAEBL; Provisional
 482-583 9.08e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  482 KAIAEKCTNKEAAEKEQDLLRQKQKEQQKYMEAQEK-RNKENLEQLRRKLMQER--EQLIK--DHNMMLEKLMK--EQKA 554
Cdd:PTZ00121 1404 KKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKaEEAKKADEAKKKAEEAKkaEEAKKkaEEAKKADEAKKkaEEAK 1483

                          90       100
                  ....*....|....*....|....*....
gi 829496033  555 LLEEGyKKKAEEMRREIYRLRHNIKDMKQ 583
Cdd:PTZ00121 1484 KADEA-KKKAEEAKKKADEAKKAAEAKKK 1511
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 491-575 9.86e-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: 36.43  E-value: 9.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829496033  491 KEAAEKEQDL----LRQKQKEQQKYMEAQEK--RNKENLEQLRRKLMQEREQLIKDHN---MMLEKLmKEQKALLEEGYK 561
Cdd:pfam20492   1 REEAEREKQEleerLKQYEEETKKAQEELEEseETAEELEEERRQAEEEAERLEQKRQeaeEEKERL-EESAEMEAEEKE 79

                          90
                  ....*....|....*..
gi 829496033  562 KKAEEMR---REIYRLR 575
Cdd:pfam20492  80 QLEAELAeaqEEIARLE 96
 
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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