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Conserved domains on  [gi|2217325272|ref|XP_047299070|]
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formin-like protein 2 isoform X11 [Homo sapiens]

Protein Classification

formin homology family protein( domain architecture ID 10273102)

formin homology family protein is a cytoskeletal remodeling protein that may be involved a diverse array of cellular functions including the regulation of actin dynamics as well as the stability and organization of microtubules

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
565-916 4.92e-119

Formin Homology 2 Domain;


:

Pssm-ID: 396655  Cd Length: 372  Bit Score: 369.68  E-value: 4.92e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  565 IKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPaIDLSSSKQKIPQKGSNKVTLLE 644
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTK-KNKKSEDKSSSKKKPKEVSLLD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  645 ANRAKNLAITLRKAGKTADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERErkpLENLSDEDRFMMQFSKI 724
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  725 ERLMQKMTIMAFIGNFAESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 803
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  804 KSTDRKQTLLHYISNVVKEKYHQVSLFYNELHYVEKAAAVSLENVLLDVKELQRGMDLTKREYTMHDHN--------TLL 875
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfrEVL 316

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2217325272  876 KEFILNNEGKLKKLQDDAKIAQDAFDDVVKYFGENPKTTPP 916
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSP 357
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 227-424 4.94e-56

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: 192.49  E-value: 4.94e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  227 GGHEIILSAFDNFKEVCGEKQRFEKLMEHFRN-EDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKL 305
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  306 KHTESDKLQVQIQAYLDNVF-DVGALLEDAETKNAALERVEELEEnisHLSEKLQDTENEAMsKIVELEKQLM--QRNKE 382
Cdd:pfam06367   81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPH-LLSILQHLLLirDDEEE 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2217325272  383 LDVVREIYKDANTQVHTLRKMVKEKEeaiQRQSTLEKKIHEL 424
Cdd:pfam06367  157 LPSYWKLLEELVSQIVLHRTKPDPKF---DERKNLEIDINRL 195
Drf_GBD super family cl05720
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 23-224 5.45e-28

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: 111.64  E-value: 5.45e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   23 LPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQ-------ERFQVKNP--------PHTYIQKLKGyl 87
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   88 DPAvtrkkfrrrvqeSTQVLRELEISLRTNHIGWVREFLNEEnkGLDVLVEYLSfaqyavtyntlpsrrtLKNSRLVSKK 167
Cdd:pfam06371   79 DSI------------SSKQLESLRVALRTQPLSWVRRFIEAQ--GLGALLNVLS----------------KINRKKSQEE 128

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  168 DDV---HVCIMCLRAIMNYQYGFNMVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCL 224
Cdd:pfam06371  129 EDLdreYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
565-916 4.92e-119

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 369.68  E-value: 4.92e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  565 IKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPaIDLSSSKQKIPQKGSNKVTLLE 644
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTK-KNKKSEDKSSSKKKPKEVSLLD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  645 ANRAKNLAITLRKAGKTADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERErkpLENLSDEDRFMMQFSKI 724
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  725 ERLMQKMTIMAFIGNFAESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 803
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  804 KSTDRKQTLLHYISNVVKEKYHQVSLFYNELHYVEKAAAVSLENVLLDVKELQRGMDLTKREYTMHDHN--------TLL 875
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfrEVL 316

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2217325272  876 KEFILNNEGKLKKLQDDAKIAQDAFDDVVKYFGENPKTTPP 916
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSP 357
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
 566-989 2.87e-88

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: 288.86  E-value: 2.87e-88
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   566 KKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERileDLNVDEFEEIF--KTKAQGPAIDLSSSKQKIPQKGSNKVTLL 643
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   644 EANRAKNLAITLRKAGKTADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERkpLENLSDEDRFMMQFSK 723
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   724 IERLMQKMTIMAFIGNFAESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 802
Cdd:smart00498  156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   803 TKSTDRKQTLLHYISNVVKEKY--------HQVSLFYNELHYVEKAAAVSLENVLLDVKELQRGmdltkreytmhdhntl 874
Cdd:smart00498  236 VKSADNKTTLLHFLVKIIRKKYlgglsdpeNLDDKFIEVMKPFLKAAKEKYDKLQKDLSDLKTR---------------- 299

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   875 lkefilnnegklkklqddakiaqdaFDDVVKYFGENPKTTPPSVFFPVFVRFVKAYKQAEEENELRKKQEQALMEKLLEQ 954
Cdd:smart00498  300 -------------------------FEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEEERRKKLVKE 354

                           410       420       430
                    ....*....|....*....|....*....|....*
gi 2217325272   955 EALMEQQDPKspsHKSKRQQQELIAELRRRQVKDN 989
Cdd:smart00498  355 TTEYEQSSSR---QKERNPSMDFEVERDFLGVLDS 386
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 227-424 4.94e-56

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: 192.49  E-value: 4.94e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  227 GGHEIILSAFDNFKEVCGEKQRFEKLMEHFRN-EDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKL 305
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  306 KHTESDKLQVQIQAYLDNVF-DVGALLEDAETKNAALERVEELEEnisHLSEKLQDTENEAMsKIVELEKQLM--QRNKE 382
Cdd:pfam06367   81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPH-LLSILQHLLLirDDEEE 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2217325272  383 LDVVREIYKDANTQVHTLRKMVKEKEeaiQRQSTLEKKIHEL 424
Cdd:pfam06367  157 LPSYWKLLEELVSQIVLHRTKPDPKF---DERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 23-224 5.45e-28

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: 111.64  E-value: 5.45e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   23 LPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQ-------ERFQVKNP--------PHTYIQKLKGyl 87
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   88 DPAvtrkkfrrrvqeSTQVLRELEISLRTNHIGWVREFLNEEnkGLDVLVEYLSfaqyavtyntlpsrrtLKNSRLVSKK 167
Cdd:pfam06371   79 DSI------------SSKQLESLRVALRTQPLSWVRRFIEAQ--GLGALLNVLS----------------KINRKKSQEE 128

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  168 DDV---HVCIMCLRAIMNYQYGFNMVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCL 224
Cdd:pfam06371  129 EDLdreYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 316-427 1.46e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  316 QIQAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEamskIVELEKQLMQRNKELD--------VV 386
Cdd:COG3883     17 QIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEAEIEerreelgeRA 92

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  387 REIYK------------------DANTQVHTLRKMV-----------KEKEEAIQRQSTLEKKIHELEKQ 427
Cdd:COG3883     93 RALYRsggsvsyldvllgsesfsDFLDRLSALSKIAdadadlleelkADKAELEAKKAELEAKLAELEAL 162
PRK11281 PRK11281
mechanosensitive channel MscK;
302-401 5.58e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.67  E-value: 5.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  302 LDKLK----HTESDKLQVQI----QAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEAMSK--IV 370
Cdd:PRK11281    45 LDALNkqklLEAEDKLVQQDleqtLALLDKIDRQKEETEQLKQQlAQAPAKLRQAQAELEALKDDNDEETRETLSTlsLR 124

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2217325272  371 ELEKQLMQRNKELDVVREIYKDANTQVHTLR 401
Cdd:PRK11281   125 QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQ 155
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 326-435 6.29e-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: 40.81  E-value: 6.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  326 DVGALLEDAETKNAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLrkmVK 405
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL---EQ 302

                           90       100       110
                   ....*....|....*....|....*....|
gi 2217325272  406 EKEEAIQRQSTLEKKIHELEKQGTIKIQKK 435
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKL 332
 
Name Accession Description Interval E-value
FH2 pfam02181
Formin Homology 2 Domain;
565-916 4.92e-119

Formin Homology 2 Domain;


Pssm-ID: 396655  Cd Length: 372  Bit Score: 369.68  E-value: 4.92e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  565 IKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPaIDLSSSKQKIPQKGSNKVTLLE 644
Cdd:pfam02181    1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTK-KNKKSEDKSSSKKKPKEVSLLD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  645 ANRAKNLAITLRKAGKTADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERErkpLENLSDEDRFMMQFSKI 724
Cdd:pfam02181   80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  725 ERLMQKMTIMAFIGNFAESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 803
Cdd:pfam02181  157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  804 KSTDRKQTLLHYISNVVKEKYHQVSLFYNELHYVEKAAAVSLENVLLDVKELQRGMDLTKREYTMHDHN--------TLL 875
Cdd:pfam02181  237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfrEVL 316

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 2217325272  876 KEFILNNEGKLKKLQDDAKIAQDAFDDVVKYFGENPKTTPP 916
Cdd:pfam02181  317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSP 357
FH2 smart00498
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ...
 566-989 2.87e-88

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: 288.86  E-value: 2.87e-88
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   566 KKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERileDLNVDEFEEIF--KTKAQGPAIDLSSSKQKIPQKGSNKVTLL 643
Cdd:smart00498    1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   644 EANRAKNLAITLRKAGKTADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERkpLENLSDEDRFMMQFSK 723
Cdd:smart00498   78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   724 IERLMQKMTIMAFIGNFAESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 802
Cdd:smart00498  156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   803 TKSTDRKQTLLHYISNVVKEKY--------HQVSLFYNELHYVEKAAAVSLENVLLDVKELQRGmdltkreytmhdhntl 874
Cdd:smart00498  236 VKSADNKTTLLHFLVKIIRKKYlgglsdpeNLDDKFIEVMKPFLKAAKEKYDKLQKDLSDLKTR---------------- 299

                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   875 lkefilnnegklkklqddakiaqdaFDDVVKYFGENPKTTPPSVFFPVFVRFVKAYKQAEEENELRKKQEQALMEKLLEQ 954
Cdd:smart00498  300 -------------------------FEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEEERRKKLVKE 354

                           410       420       430
                    ....*....|....*....|....*....|....*
gi 2217325272   955 EALMEQQDPKspsHKSKRQQQELIAELRRRQVKDN 989
Cdd:smart00498  355 TTEYEQSSSR---QKERNPSMDFEVERDFLGVLDS 386
Drf_FH3 pfam06367
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins.
 227-424 4.94e-56

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: 192.49  E-value: 4.94e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  227 GGHEIILSAFDNFKEVCGEKQRFEKLMEHFRN-EDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKL 305
Cdd:pfam06367    1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  306 KHTESDKLQVQIQAYLDNVF-DVGALLEDAETKNAALERVEELEEnisHLSEKLQDTENEAMsKIVELEKQLM--QRNKE 382
Cdd:pfam06367   81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPH-LLSILQHLLLirDDEEE 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2217325272  383 LDVVREIYKDANTQVHTLRKMVKEKEeaiQRQSTLEKKIHEL 424
Cdd:pfam06367  157 LPSYWKLLEELVSQIVLHRTKPDPKF---DERKNLEIDINRL 195
Drf_GBD pfam06371
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ...
 23-224 5.45e-28

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: 111.64  E-value: 5.45e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   23 LPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQ-------ERFQVKNP--------PHTYIQKLKGyl 87
Cdd:pfam06371    1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD-- 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272   88 DPAvtrkkfrrrvqeSTQVLRELEISLRTNHIGWVREFLNEEnkGLDVLVEYLSfaqyavtyntlpsrrtLKNSRLVSKK 167
Cdd:pfam06371   79 DSI------------SSKQLESLRVALRTQPLSWVRRFIEAQ--GLGALLNVLS----------------KINRKKSQEE 128

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  168 DDV---HVCIMCLRAIMNYQYGFNMVMSHPHAVNEIALSLNNKNPRTKALVLELLAAVCL 224
Cdd:pfam06371  129 EDLdreYEILKCLKALMNNKFGLDHVLGHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 316-427 1.46e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  316 QIQAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEamskIVELEKQLMQRNKELD--------VV 386
Cdd:COG3883     17 QIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEAEIEerreelgeRA 92

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  387 REIYK------------------DANTQVHTLRKMV-----------KEKEEAIQRQSTLEKKIHELEKQ 427
Cdd:COG3883     93 RALYRsggsvsyldvllgsesfsDFLDRLSALSKIAdadadlleelkADKAELEAKKAELEAKLAELEAL 162
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
313-427 1.54e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  313 LQVQIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLQDTEnEAMSKIVELEKQLMQRNKELDVVREIYKD 392
Cdd:COG4913    615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEAELERLDASSDDLAALEEQ 693

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 2217325272  393 ANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQ 427
Cdd:COG4913    694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
298-427 2.74e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  298 LDEYLDKLKHTESDKLQVQIQAYLDNVF---------DVGALLEDAETKNAALERVEELEENI-SHLSEKLQD----TEN 363
Cdd:COG4717    349 LQELLREAEELEEELQLEELEQEIAALLaeagvedeeELRAALEQAEEYQELKEELEELEEQLeELLGELEELlealDEE 428

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217325272  364 EAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKmVKEKEEAIQRQSTLEKKIHELEKQ 427
Cdd:COG4717    429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEE-DGELAELLQELEELKAELRELAEE 491
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 304-427 3.02e-03

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: 39.89  E-value: 3.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  304 KLKHTESD--KLQVQIQAYLDNVFDvgalledaetKNAAlERvEELEENISHLSEKLQDTENeamsKIVELEKQLMQRNK 381
Cdd:pfam15619   89 KLKEKEAEllRLRDQLKRLEKLSED----------KNLA-ER-EELQKKLEQLEAKLEDKDE----KIQDLERKLELENK 152

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 2217325272  382 ELDvvREIYKdANTQVHTLRKMVKEKEEAIQRqstLEKKIHELEKQ 427
Cdd:pfam15619  153 SFR--RQLAA-EKKKHKEAQEEVKILQEEIER---LQQKLKEKERE 192
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
298-445 3.07e-03

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.38  E-value: 3.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  298 LDEYLDKLKHTESDKLQvqiQAYLDNVFDVGALLEDAETKNAALE-RVEELEENISHLSEKLQDTENEAMSKIVELEKQL 376
Cdd:COG2433    378 IEEALEELIEKELPEEE---PEAEREKEHEERELTEEEEEIRRLEeQVERLEAEVEELEAELEEKDERIERLERELSEAR 454

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217325272  377 MQRNKELDVVREIYKDANTqVHTLRKMVKEKEEAIQRqstLEKKIHELEKqgTIKIQKKGDGdIAILPV 445
Cdd:COG2433    455 SEERREIRKDREISRLDRE-IERLERELEEERERIEE---LKRKLERLKE--LWKLEHSGEL-VPVKVV 516
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 302-424 3.77e-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: 40.51  E-value: 3.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  302 LDKLKHtESDKLQVQIQAYLDNVFDVGALLEDAETK-----NAALERVEELEENISHLSEKLQDTENEamskiVELEKQL 376
Cdd:pfam09787   49 LEELRQ-ERDLLREEIQKLRGQIQQLRTELQELEAQqqeeaESSREQLQELEEQLATERSARREAEAE-----LERLQEE 122

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2217325272  377 MQRNKElDVVREI------YKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHEL 424
Cdd:pfam09787  123 LRYLEE-ELRRSKatlqsrIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQL 175
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
303-434 4.39e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 4.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  303 DKLKHTESDKLQVQIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLqdtenEAMSKIVELEKQLMQRNKE 382
Cdd:COG4717     66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAE 140

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2217325272  383 LDVVREIYKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQGTIKIQK 434
Cdd:COG4717    141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
PRK11281 PRK11281
mechanosensitive channel MscK;
302-401 5.58e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.67  E-value: 5.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  302 LDKLK----HTESDKLQVQI----QAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEAMSK--IV 370
Cdd:PRK11281    45 LDALNkqklLEAEDKLVQQDleqtLALLDKIDRQKEETEQLKQQlAQAPAKLRQAQAELEALKDDNDEETRETLSTlsLR 124

                           90       100       110
                   ....*....|....*....|....*....|.
gi 2217325272  371 ELEKQLMQRNKELDVVREIYKDANTQVHTLR 401
Cdd:PRK11281   125 QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQ 155
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 326-435 6.29e-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: 40.81  E-value: 6.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  326 DVGALLEDAETKNAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLrkmVK 405
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL---EQ 302

                           90       100       110
                   ....*....|....*....|....*....|
gi 2217325272  406 EKEEAIQRQSTLEKKIHELEKQGTIKIQKK 435
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKL 332
PRK12704 PRK12704
phosphodiesterase; Provisional
 330-427 6.31e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 6.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217325272  330 LLEDAETKNAALERVEELE--ENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEK 407
Cdd:PRK12704    43 ILEEAKKEAEAIKKEALLEakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122

                           90       100
                   ....*....|....*....|.
gi 2217325272  408 EEAI-QRQSTLEKKIHELEKQ 427
Cdd:PRK12704   123 QQELeKKEEELEELIEEQLQE 143
 
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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