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Conserved domains on  [gi|568914310|ref|XP_006498400|]
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formin-like protein 2 isoform X9 [Mus musculus]

Protein Classification

Drf_FH3 and FH2 domain-containing protein( domain architecture ID 10273080)

protein containing domains Drf_GBD, Drf_FH3, and FH2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 278-475 1.76e-57

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


:

Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 194.80  E-value: 1.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  278 GGHEIILSAFDNFKEVCGEKQRFEKLMEHFRN-EDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKL 356
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  357 KHTESDKLQVQIQAYLDNVF-DVGALLEDAETKNAALERVEELEEnisHLSEKLQDTENEAMsKIVELEKQLM--QRNKE 433
Cdd:pfam06367  81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPH-LLSILQHLLLirDDEEE 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568914310  434 LDVVREIYKDANTQVHTLRKMVKEKEeaiQRQSTLEKKIHEL 475
Cdd:pfam06367 157 LPSYWKLLEELVSQIVLHRTKPDPKF---DERKNLEIDINRL 195
FH2 super family cl19758
Formin Homology 2 Domain;
622-806 1.57e-49

Formin Homology 2 Domain;


The actual alignment was detected with superfamily member pfam02181:

Pssm-ID: 418645  Cd Length: 372  Bit Score: 179.00  E-value: 1.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  622 IKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPAIDLSSSKQKITqKASSKVTLLE 701
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSK-KKPKEVSLLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  702 ANRAKNLAITLRKAGKSADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERErkpLENLSDEDRFMMQFSKI 781
Cdd:pfam02181  80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156

                         170       180
                  ....*....|....*....|....*
gi 568914310  782 ERLLQKMTIMAFIGNFTESIQMLTP 806
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKP 181
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 23-275 3.68e-22

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


The actual alignment was detected with superfamily member pfam06371:

Pssm-ID: 461886  Cd Length: 188  Bit Score: 94.69  E-value: 3.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310   23 LPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQ-------ERFQVKNP--------PHTYIQKLKGyl 87
Cdd:pfam06371   1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310   88 DPAvtrkkfrrrvqeSTQVLRELEISLRTNHIGWVREFLNEEnkGLDVLVEYLSfaqyavtfdfesvestmestvdkskp 167
Cdd:pfam06371  79 DSI------------SSKQLESLRVALRTQPLSWVRRFIEAQ--GLGALLNVLS-------------------------- 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  168 wsrsiedlhrgsnlpspvgnsvsrsgrhsalryntlpsrrtLKNSRLVSKKDDV---HVCIMCLRAIMNYQYGFNMVMSH 244
Cdd:pfam06371 119 -----------------------------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGH 157

                         250       260       270
                  ....*....|....*....|....*....|.
gi 568914310  245 PHAVNEIALSLNNKNPRTKALVLELLAAVCL 275
Cdd:pfam06371 158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 278-475 1.76e-57

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 194.80  E-value: 1.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  278 GGHEIILSAFDNFKEVCGEKQRFEKLMEHFRN-EDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKL 356
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  357 KHTESDKLQVQIQAYLDNVF-DVGALLEDAETKNAALERVEELEEnisHLSEKLQDTENEAMsKIVELEKQLM--QRNKE 433
Cdd:pfam06367  81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPH-LLSILQHLLLirDDEEE 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568914310  434 LDVVREIYKDANTQVHTLRKMVKEKEeaiQRQSTLEKKIHEL 475
Cdd:pfam06367 157 LPSYWKLLEELVSQIVLHRTKPDPKF---DERKNLEIDINRL 195
FH2 pfam02181
Formin Homology 2 Domain;
622-806 1.57e-49

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 179.00  E-value: 1.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  622 IKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPAIDLSSSKQKITqKASSKVTLLE 701
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSK-KKPKEVSLLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  702 ANRAKNLAITLRKAGKSADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERErkpLENLSDEDRFMMQFSKI 781
Cdd:pfam02181  80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156

                         170       180
                  ....*....|....*....|....*
gi 568914310  782 ERLLQKMTIMAFIGNFTESIQMLTP 806
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKP 181
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
 623-806 3.75e-42

Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.


Pssm-ID: 214697 [Multi-domain]  Cd Length: 392  Bit Score: 158.67  E-value: 3.75e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310   623 KKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERileDLNVDEFEEIF--KTKAQGPAIDLSSSKQKITQKASSKVTLL 700
Cdd:smart00498   1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310   701 EANRAKNLAITLRKAGKSADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERkpLENLSDEDRFMMQFSK 780
Cdd:smart00498  78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155

                          170       180
                   ....*....|....*....|....*.
gi 568914310   781 IERLLQKMTIMAFIGNFTESIQMLTP 806
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKP 181
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 23-275 3.68e-22

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


Pssm-ID: 461886  Cd Length: 188  Bit Score: 94.69  E-value: 3.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310   23 LPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQ-------ERFQVKNP--------PHTYIQKLKGyl 87
Cdd:pfam06371   1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310   88 DPAvtrkkfrrrvqeSTQVLRELEISLRTNHIGWVREFLNEEnkGLDVLVEYLSfaqyavtfdfesvestmestvdkskp 167
Cdd:pfam06371  79 DSI------------SSKQLESLRVALRTQPLSWVRRFIEAQ--GLGALLNVLS-------------------------- 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  168 wsrsiedlhrgsnlpspvgnsvsrsgrhsalryntlpsrrtLKNSRLVSKKDDV---HVCIMCLRAIMNYQYGFNMVMSH 244
Cdd:pfam06371 119 -----------------------------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGH 157

                         250       260       270
                  ....*....|....*....|....*....|.
gi 568914310  245 PHAVNEIALSLNNKNPRTKALVLELLAAVCL 275
Cdd:pfam06371 158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 367-478 1.51e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 367 QIQAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEamskIVELEKQLMQRNKELD--------VV 437
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEAEIEerreelgeRA 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 438 REIYK------------------DANTQVHTLRKMV-----------KEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG3883   93 RALYRsggsvsyldvllgsesfsDFLDRLSALSKIAdadadlleelkADKAELEAKKAELEAKLAELEAL 162
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 377-486 2.47e-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: 41.58  E-value: 2.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310   377 DVGALLEDAETKNAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLrkmVK 456
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL---EQ 302

                           90       100       110
                   ....*....|....*....|....*....|
gi 568914310   457 EKEEAIQRQSTLEKKIHELEKQGTIKIQKK 486
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKL 332
PRK12704 PRK12704
phosphodiesterase; Provisional
 381-478 2.65e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 381 LLEDAETKNAALERVEELE--ENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEK 458
Cdd:PRK12704  43 ILEEAKKEAEAIKKEALLEakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122

                         90       100
                 ....*....|....*....|.
gi 568914310 459 EEAI-QRQSTLEKKIHELEKQ 478
Cdd:PRK12704 123 QQELeKKEEELEELIEEQLQE 143
 
Name Accession Description Interval E-value
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 278-475 1.76e-57

Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.


Pssm-ID: 461885 [Multi-domain]  Cd Length: 195  Bit Score: 194.80  E-value: 1.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  278 GGHEIILSAFDNFKEVCGEKQRFEKLMEHFRN-EDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKL 356
Cdd:pfam06367   1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  357 KHTESDKLQVQIQAYLDNVF-DVGALLEDAETKNAALERVEELEEnisHLSEKLQDTENEAMsKIVELEKQLM--QRNKE 433
Cdd:pfam06367  81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPH-LLSILQHLLLirDDEEE 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568914310  434 LDVVREIYKDANTQVHTLRKMVKEKEeaiQRQSTLEKKIHEL 475
Cdd:pfam06367 157 LPSYWKLLEELVSQIVLHRTKPDPKF---DERKNLEIDINRL 195
FH2 pfam02181
Formin Homology 2 Domain;
622-806 1.57e-49

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 179.00  E-value: 1.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  622 IKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPAIDLSSSKQKITqKASSKVTLLE 701
Cdd:pfam02181   1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSK-KKPKEVSLLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  702 ANRAKNLAITLRKAGKSADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERErkpLENLSDEDRFMMQFSKI 781
Cdd:pfam02181  80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156

                         170       180
                  ....*....|....*....|....*
gi 568914310  782 ERLLQKMTIMAFIGNFTESIQMLTP 806
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKP 181
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
 623-806 3.75e-42

Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, especially in the context of cytokinesis and cell polarisation. Members of this family have been found to interact with Rho-GTPases, profilin and other actin-assoziated proteins. These interactions are mediated by the proline-rich FH1 domain, usually located in front of FH2 (but not listed in SMART). Despite this cytosolic function, vertebrate formins have been assigned functions within the nucleus. A set of Formin-Binding Proteins (FBPs) has been shown to bind FH1 with their WW domain.


Pssm-ID: 214697 [Multi-domain]  Cd Length: 392  Bit Score: 158.67  E-value: 3.75e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310   623 KKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERileDLNVDEFEEIF--KTKAQGPAIDLSSSKQKITQKASSKVTLL 700
Cdd:smart00498   1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310   701 EANRAKNLAITLRKAGKSADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERkpLENLSDEDRFMMQFSK 780
Cdd:smart00498  78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155

                          170       180
                   ....*....|....*....|....*.
gi 568914310   781 IERLLQKMTIMAFIGNFTESIQMLTP 806
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKP 181
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 23-275 3.68e-22

Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, leading to activation of the Drf protein.


Pssm-ID: 461886  Cd Length: 188  Bit Score: 94.69  E-value: 3.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310   23 LPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQ-------ERFQVKNP--------PHTYIQKLKGyl 87
Cdd:pfam06371   1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310   88 DPAvtrkkfrrrvqeSTQVLRELEISLRTNHIGWVREFLNEEnkGLDVLVEYLSfaqyavtfdfesvestmestvdkskp 167
Cdd:pfam06371  79 DSI------------SSKQLESLRVALRTQPLSWVRRFIEAQ--GLGALLNVLS-------------------------- 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  168 wsrsiedlhrgsnlpspvgnsvsrsgrhsalryntlpsrrtLKNSRLVSKKDDV---HVCIMCLRAIMNYQYGFNMVMSH 244
Cdd:pfam06371 119 -----------------------------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGH 157

                         250       260       270
                  ....*....|....*....|....*....|.
gi 568914310  245 PHAVNEIALSLNNKNPRTKALVLELLAAVCL 275
Cdd:pfam06371 158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 367-478 1.51e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 44.82  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 367 QIQAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEamskIVELEKQLMQRNKELD--------VV 437
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEAEIEerreelgeRA 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 438 REIYK------------------DANTQVHTLRKMV-----------KEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG3883   93 RALYRsggsvsyldvllgsesfsDFLDRLSALSKIAdadadlleelkADKAELEAKKAELEAKLAELEAL 162
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 355-478 1.81e-04

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 43.35  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  355 KLKHTESD--KLQVQIQAYLDNVFDvgalledaetKNAAlERvEELEENISHLSEKLQDTENeamsKIVELEKQLMQRNK 432
Cdd:pfam15619  89 KLKEKEAEllRLRDQLKRLEKLSED----------KNLA-ER-EELQKKLEQLEAKLEDKDE----KIQDLERKLELENK 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568914310  433 ELDvvREIYKdANTQVHTLRKMVKEKEEAIQRqstLEKKIHELEKQ 478
Cdd:pfam15619 153 SFR--RQLAA-EKKKHKEAQEEVKILQEEIER---LQQKLKEKERE 192
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
349-478 5.32e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 5.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 349 LDEYLDKLKHTESDKLQVQIQAYLDNVF---------DVGALLEDAETKNAALERVEELEENI-SHLSEKLQD----TEN 414
Cdd:COG4717  349 LQELLREAEELEEELQLEELEQEIAALLaeagvedeeELRAALEQAEEYQELKEELEELEEQLeELLGELEELlealDEE 428

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568914310 415 EAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKmVKEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG4717  429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEE-DGELAELLQELEELKAELRELAEE 491
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
364-478 8.41e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 8.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  364 LQVQIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLQDTEnEAMSKIVELEKQLMQRNKELDVVREIYKD 443
Cdd:COG4913   615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEAELERLDASSDDLAALEEQ 693

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568914310  444 ANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG4913   694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 353-478 1.29e-03

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: 41.67  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  353 LDKLKHtESDKLQVQIQAYLDNVFDVGALLEDAETK-----NAALERVEELEENISHLSEKLQDTENEamskiVELEKQL 427
Cdd:pfam09787  49 LEELRQ-ERDLLREEIQKLRGQIQQLRTELQELEAQqqeeaESSREQLQELEEQLATERSARREAEAE-----LERLQEE 122

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568914310  428 MQRNKElDVVREI------YKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHEL-----EKQ 478
Cdd:pfam09787 123 LRYLEE-ELRRSKatlqsrIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQLtetliQKQ 183
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
354-485 1.31e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 354 DKLKHTESDKLQVQIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLqdtenEAMSKIVELEKQLMQRNKE 433
Cdd:COG4717   66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAE 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568914310 434 LDVVREIYKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQGTIKIQK 485
Cdd:COG4717  141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
349-496 1.79e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 349 LDEYLDKLKHTESDKLQvqiQAYLDNVFDVGALLEDAETKNAALE-RVEELEENISHLSEKLQDTENEAMSKIVELEKQL 427
Cdd:COG2433  378 IEEALEELIEKELPEEE---PEAEREKEHEERELTEEEEEIRRLEeQVERLEAEVEELEAELEEKDERIERLERELSEAR 454

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568914310 428 MQRNKELDVVREIYKDANTqVHTLRKMVKEKEEAIQRqstLEKKIHELEKqgTIKIQKKGDGdIAILPV 496
Cdd:COG2433  455 SEERREIRKDREISRLDRE-IERLERELEEERERIEE---LKRKLERLKE--LWKLEHSGEL-VPVKVV 516
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
385-478 2.13e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 385 AETKNAALERVEELEENISHLSEKLQDTENEamskIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEKEEAI-- 462
Cdd:COG4372   30 SEQLRKALFELDKLQEELEQLREELEQAREE----LEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELes 105

                         90
                 ....*....|....*...
gi 568914310 463 --QRQSTLEKKIHELEKQ 478
Cdd:COG4372  106 lqEEAEELQEELEELQKE 123
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 290-475 2.26e-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: 41.63  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  290 FKEVCGEKQRFEKLMEHFRNE--------DNNIDFMVASMQFINIVVHSVE-DMNFRVHLQYEFTKLGLDEYLDKL--KH 358
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREEtrqvymdlNNNIEKMILAFEELRVQAENARlEMHFKLKEDHEKIQHLEEEYKKEIndKE 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  359 TESDKLQVQIQAYLDNVFDVGALLEDAETKNAALERVEELE-ENISHLSEKlqdteNEAMSKIVELEKQLMQRNkeLDVV 437
Cdd:pfam05483 240 KQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQdENLKELIEK-----KDHLTKELEDIKMSLQRS--MSTQ 312

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568914310  438 REIYKDANTQVHTLRKMVKEKEEAIQrQSTLEKKIHEL 475
Cdd:pfam05483 313 KALEEDLQIATKTICQLTEEKEAQME-ELNKAKAAHSF 349
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 377-486 2.47e-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: 41.58  E-value: 2.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310   377 DVGALLEDAETKNAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLrkmVK 456
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL---EQ 302

                           90       100       110
                   ....*....|....*....|....*....|
gi 568914310   457 EKEEAIQRQSTLEKKIHELEKQGTIKIQKK 486
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKL 332
PRK12704 PRK12704
phosphodiesterase; Provisional
 381-478 2.65e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 2.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 381 LLEDAETKNAALERVEELE--ENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEK 458
Cdd:PRK12704  43 ILEEAKKEAEAIKKEALLEakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122

                         90       100
                 ....*....|....*....|.
gi 568914310 459 EEAI-QRQSTLEKKIHELEKQ 478
Cdd:PRK12704 123 QQELeKKEEELEELIEEQLQE 143
PRK11281 PRK11281
mechanosensitive channel MscK;
353-452 3.05e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 41.44  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  353 LDKLK----HTESDKLQVQI----QAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEAMSK--IV 421
Cdd:PRK11281   45 LDALNkqklLEAEDKLVQQDleqtLALLDKIDRQKEETEQLKQQlAQAPAKLRQAQAELEALKDDNDEETRETLSTlsLR 124

                          90       100       110
                  ....*....|....*....|....*....|.
gi 568914310  422 ELEKQLMQRNKELDVVREIYKDANTQVHTLR 452
Cdd:PRK11281  125 QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQ 155
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 378-478 4.20e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.18  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  378 VGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLmQRNKELDVVREIYKDANTQVHTLRKMVK 456
Cdd:pfam15905 175 VMAKQEGMEGKlQVTQKNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLL-EYITELSCVSEQVEKYKLDIAQLEELLK 253

                          90       100
                  ....*....|....*....|...
gi 568914310  457 EKEEAIQR-QSTLEKKIHELEKQ 478
Cdd:pfam15905 254 EKNDEIESlKQSLEEKEQELSKQ 276
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 380-478 4.32e-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: 40.13  E-value: 4.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 380 ALLEDAETKNAALERVEELEENISHLSEKLQDTEneamSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRkmvKEKE 459
Cdd:COG4942   14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALARRIRALEQELAALE---AELA 86

                         90
                 ....*....|....*....
gi 568914310 460 EAIQRQSTLEKKIHELEKQ 478
Cdd:COG4942   87 ELEKEIAELRAELEAQKEE 105
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 349-478 5.16e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.52  E-value: 5.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 349 LDEYLDKLKHtESDKLQVQIQAYLDNVFDVGALLEDAETknaaleRVEELEENISHLSEKLQDTEneamSKIVELEKQLM 428
Cdd:COG1579   15 LDSELDRLEH-RLKELPAELAELEDELAALEARLEAAKT------ELEDLEKEIKRLELEIEEVE----ARIKKYEEQLG 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568914310 429 Q--RNKELDVV-REI-------------YKDANTQVHTLRKMVKEKEEAI-QRQSTLEKKIHELEKQ 478
Cdd:COG1579   84 NvrNNKEYEALqKEIeslkrrisdledeILELMERIEELEEELAELEAELaELEAELEEKKAELDEE 150
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 384-478 7.15e-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: 7.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310   384 DAETKNAALERVEELEENISHLsEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEKEEAIQ 463
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKI-EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743

                           90
                   ....*....|....*....
gi 568914310   464 ----RQSTLEKKIHELEKQ 478
Cdd:TIGR02168  744 qleeRIAQLSKELTELEAE 762
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 357-478 7.84e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 7.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310  357 KHTESDKLQVQIQayldnvfdvgallEDAETKNAALERVEELEENISHLSEKLQDTENEamskIVELEKQLMQRNKELDV 436
Cdd:TIGR04523 122 LEVELNKLEKQKK-------------ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ----KEELENELNLLEKEKLN 184

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 568914310  437 VREIYKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:TIGR04523 185 IQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQ 226
DUF2312 pfam10073
Uncharacterized protein conserved in bacteria (DUF2312); Members of this family of ...
 393-444 8.03e-03

Uncharacterized protein conserved in bacteria (DUF2312); Members of this family of hypothetical bacterial proteins have no known function. Structural modelling suggests this domain may bind nucleic acids.


Pssm-ID: 431032  Cd Length: 72  Bit Score: 35.62  E-value: 8.03e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568914310  393 ERVEELEENISHLSEKLQDTENEA---------MSKIVELEKQLMQRNKELDVVREIYKDA 444
Cdd:pfam10073  10 ERIERLEEEKKAIAEDIKDVYAEAkgrgfdtkvMRKIVKLRKMDKDERQEQEALLELYKAA 70
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
367-478 9.26e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 9.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 367 QIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLqdTEN-----EAMSKIVELEKQLMQRNKE-LDVVREI 440
Cdd:COG3206  244 ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARY--TPNhpdviALRAQIAALRAQLQQEAQRiLASLEAE 321

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 568914310 441 YKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG3206  322 LEALQAREASLQAQLAQLEARLAELPELEAELRRLERE 359
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 386-462 9.41e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.68  E-value: 9.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914310 386 ETKNAALERVEELEENISHLSEKLQD------TENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEK- 458
Cdd:COG0542  433 EQDEASFERLAELRDELAELEEELEAlkarweAEKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEv 512


                 ....*
gi 568914310 459 -EEAI 462
Cdd:COG0542  513 tEEDI 517
 
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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