|
Name |
Accession |
Description |
Interval |
E-value |
| FH2 |
pfam02181 |
Formin Homology 2 Domain; |
623-974 |
1.11e-119 |
|
Formin Homology 2 Domain;
Pssm-ID: 396655 Cd Length: 372 Bit Score: 373.14 E-value: 1.11e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 623 IKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPaIDLSSSKQKIPQKGSNKVTLLE 702
Cdd:pfam02181 1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTK-KNKKSEDKSSSKKKPKEVSLLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 703 ANRAKNLAITLRKAGKTADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERErkpLENLSDEDRFMMQFSKI 782
Cdd:pfam02181 80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 783 ERLMQKMTIMAFIGNFAESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 861
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 862 KSTDRKQTLLHYISNVVKEKYHQVSLFYNELHYVEKAAAVSLENVLLDVKELQRGMDLTKREYTMHDHN--------TLL 933
Cdd:pfam02181 237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfrEVL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767916463 934 KEFILNNEGKLKKLQDDAKIAQDAFDDVVKYFGENPKTTPP 974
Cdd:pfam02181 317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSP 357
|
|
| FH2 |
smart00498 |
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ... |
624-1047 |
6.67e-89 |
|
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: 291.56 E-value: 6.67e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 624 KKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERileDLNVDEFEEIF--KTKAQGPAIDLSSSKQKIPQKGSNKVTLL 701
Cdd:smart00498 1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 702 EANRAKNLAITLRKAGKTADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERkpLENLSDEDRFMMQFSK 781
Cdd:smart00498 78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 782 IERLMQKMTIMAFIGNFAESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 860
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 861 TKSTDRKQTLLHYISNVVKEKY--------HQVSLFYNELHYVEKAAAVSLENVLLDVKELQRGmdltkreytmhdhntl 932
Cdd:smart00498 236 VKSADNKTTLLHFLVKIIRKKYlgglsdpeNLDDKFIEVMKPFLKAAKEKYDKLQKDLSDLKTR---------------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 933 lkefilnnegklkklqddakiaqdaFDDVVKYFGENPKTTPPSVFFPVFVRFVKAYKQAEEENELRKKQEQALMEKLLEQ 1012
Cdd:smart00498 300 -------------------------FEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEEERRKKLVKE 354
|
410 420 430
....*....|....*....|....*....|....*
gi 767916463 1013 EALMEQQDPKspsHKSKRQQQELIAELRRRQVKDN 1047
Cdd:smart00498 355 TTEYEQSSSR---QKERNPSMDFEVERDFLGVLDS 386
|
|
| Drf_FH3 |
pfam06367 |
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins. |
278-475 |
2.41e-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: 193.26 E-value: 2.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 278 GGHEIILSAFDNFKEVCGEKQRFEKLMEHFRN-EDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKL 356
Cdd:pfam06367 1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 357 KHTESDKLQVQIQAYLDNVF-DVGALLEDAETKNAALERVEELEEnisHLSEKLQDTENEAMsKIVELEKQLM--QRNKE 433
Cdd:pfam06367 81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPH-LLSILQHLLLirDDEEE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767916463 434 LDVVREIYKDANTQVHTLRKMVKEKEeaiQRQSTLEKKIHEL 475
Cdd:pfam06367 157 LPSYWKLLEELVSQIVLHRTKPDPKF---DERKNLEIDINRL 195
|
|
| Drf_GBD |
pfam06371 |
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ... |
23-275 |
1.29e-21 |
|
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: 93.54 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 23 LPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQ-------ERFQVKNP--------PHTYIQKLKGyl 87
Cdd:pfam06371 1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 88 DPAvtrkkfrrrvqeSTQVLRELEISLRTNHIGWVREFLNEEnkGLDVLVEYLSfaqyavtfdfesvestvessvdkskp 167
Cdd:pfam06371 79 DSI------------SSKQLESLRVALRTQPLSWVRRFIEAQ--GLGALLNVLS-------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 168 wsrsiedlhrgsnlpspvgnsvsrsgrhsalryntlpsrrtLKNSRLVSKKDDV---HVCIMCLRAIMNYQYGFNMVMSH 244
Cdd:pfam06371 119 -----------------------------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGH 157
|
250 260 270
....*....|....*....|....*....|.
gi 767916463 245 PHAVNEIALSLNNKNPRTKALVLELLAAVCL 275
Cdd:pfam06371 158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
367-478 |
1.49e-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: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 367 QIQAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEamskIVELEKQLMQRNKELD--------VV 437
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEAEIEerreelgeRA 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 438 REIYK------------------DANTQVHTLRKMV-----------KEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG3883 93 RALYRsggsvsyldvllgsesfsDFLDRLSALSKIAdadadlleelkADKAELEAKKAELEAKLAELEAL 162
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
381-478 |
5.20e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 381 LLEDAETKNAALERVEELE--ENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEK 458
Cdd:PRK12704 43 ILEEAKKEAEAIKKEALLEakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
|
90 100
....*....|....*....|.
gi 767916463 459 EEAI-QRQSTLEKKIHELEKQ 478
Cdd:PRK12704 123 QQELeKKEEELEELIEEQLQE 143
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
377-486 |
5.81e-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: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 377 DVGALLEDAETKNAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLrkmVK 456
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL---EQ 302
|
90 100 110
....*....|....*....|....*....|
gi 767916463 457 EKEEAIQRQSTLEKKIHELEKQGTIKIQKK 486
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKL 332
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FH2 |
pfam02181 |
Formin Homology 2 Domain; |
623-974 |
1.11e-119 |
|
Formin Homology 2 Domain;
Pssm-ID: 396655 Cd Length: 372 Bit Score: 373.14 E-value: 1.11e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 623 IKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPaIDLSSSKQKIPQKGSNKVTLLE 702
Cdd:pfam02181 1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTK-KNKKSEDKSSSKKKPKEVSLLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 703 ANRAKNLAITLRKAGKTADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERErkpLENLSDEDRFMMQFSKI 782
Cdd:pfam02181 80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 783 ERLMQKMTIMAFIGNFAESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 861
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 862 KSTDRKQTLLHYISNVVKEKYHQVSLFYNELHYVEKAAAVSLENVLLDVKELQRGMDLTKREYTMHDHN--------TLL 933
Cdd:pfam02181 237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfrEVL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 767916463 934 KEFILNNEGKLKKLQDDAKIAQDAFDDVVKYFGENPKTTPP 974
Cdd:pfam02181 317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSP 357
|
|
| FH2 |
smart00498 |
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ... |
624-1047 |
6.67e-89 |
|
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: 291.56 E-value: 6.67e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 624 KKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERileDLNVDEFEEIF--KTKAQGPAIDLSSSKQKIPQKGSNKVTLL 701
Cdd:smart00498 1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 702 EANRAKNLAITLRKAGKTADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERkpLENLSDEDRFMMQFSK 781
Cdd:smart00498 78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 782 IERLMQKMTIMAFIGNFAESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 860
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 861 TKSTDRKQTLLHYISNVVKEKY--------HQVSLFYNELHYVEKAAAVSLENVLLDVKELQRGmdltkreytmhdhntl 932
Cdd:smart00498 236 VKSADNKTTLLHFLVKIIRKKYlgglsdpeNLDDKFIEVMKPFLKAAKEKYDKLQKDLSDLKTR---------------- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 933 lkefilnnegklkklqddakiaqdaFDDVVKYFGENPKTTPPSVFFPVFVRFVKAYKQAEEENELRKKQEQALMEKLLEQ 1012
Cdd:smart00498 300 -------------------------FEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEEERRKKLVKE 354
|
410 420 430
....*....|....*....|....*....|....*
gi 767916463 1013 EALMEQQDPKspsHKSKRQQQELIAELRRRQVKDN 1047
Cdd:smart00498 355 TTEYEQSSSR---QKERNPSMDFEVERDFLGVLDS 386
|
|
| Drf_FH3 |
pfam06367 |
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins. |
278-475 |
2.41e-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: 193.26 E-value: 2.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 278 GGHEIILSAFDNFKEVCGEKQRFEKLMEHFRN-EDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKL 356
Cdd:pfam06367 1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 357 KHTESDKLQVQIQAYLDNVF-DVGALLEDAETKNAALERVEELEEnisHLSEKLQDTENEAMsKIVELEKQLM--QRNKE 433
Cdd:pfam06367 81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPH-LLSILQHLLLirDDEEE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767916463 434 LDVVREIYKDANTQVHTLRKMVKEKEeaiQRQSTLEKKIHEL 475
Cdd:pfam06367 157 LPSYWKLLEELVSQIVLHRTKPDPKF---DERKNLEIDINRL 195
|
|
| Drf_GBD |
pfam06371 |
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ... |
23-275 |
1.29e-21 |
|
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: 93.54 E-value: 1.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 23 LPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQ-------ERFQVKNP--------PHTYIQKLKGyl 87
Cdd:pfam06371 1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 88 DPAvtrkkfrrrvqeSTQVLRELEISLRTNHIGWVREFLNEEnkGLDVLVEYLSfaqyavtfdfesvestvessvdkskp 167
Cdd:pfam06371 79 DSI------------SSKQLESLRVALRTQPLSWVRRFIEAQ--GLGALLNVLS-------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 168 wsrsiedlhrgsnlpspvgnsvsrsgrhsalryntlpsrrtLKNSRLVSKKDDV---HVCIMCLRAIMNYQYGFNMVMSH 244
Cdd:pfam06371 119 -----------------------------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGH 157
|
250 260 270
....*....|....*....|....*....|.
gi 767916463 245 PHAVNEIALSLNNKNPRTKALVLELLAAVCL 275
Cdd:pfam06371 158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
367-478 |
1.49e-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: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 367 QIQAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEamskIVELEKQLMQRNKELD--------VV 437
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEAEIEerreelgeRA 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 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 |
1.60e-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: 41.04 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 355 KLKHTESD--KLQVQIQAYLDNVFDvgalledaetKNAAlERvEELEENISHLSEKLQDTENeamsKIVELEKQLMQRNK 432
Cdd:pfam15619 89 KLKEKEAEllRLRDQLKRLEKLSED----------KNLA-ER-EELQKKLEQLEAKLEDKDE----KIQDLERKLELENK 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 767916463 433 ELDvvREIYKdANTQVHTLRKMVKEKEEAIQRqstLEKKIHELEKQ 478
Cdd:pfam15619 153 SFR--RQLAA-EKKKHKEAQEEVKILQEEIER---LQQKLKEKERE 192
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-478 |
1.95e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 364 LQVQIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLQDTEnEAMSKIVELEKQLMQRNKELDVVREIYKD 443
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEAELERLDASSDDLAALEEQ 693
|
90 100 110
....*....|....*....|....*....|....*
gi 767916463 444 ANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
349-478 |
2.10e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 349 LDEYLDKLKHTESDKLQVQIQAYLDNVF---------DVGALLEDAETKNAALERVEELEENI-SHLSEKLQD----TEN 414
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAALLaeagvedeeELRAALEQAEEYQELKEELEELEEQLeELLGELEELlealDEE 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767916463 415 EAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKmVKEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEE-DGELAELLQELEELKAELRELAEE 491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
354-485 |
3.68e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 354 DKLKHTESDKLQVQIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLqdtenEAMSKIVELEKQLMQRNKE 433
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAE 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 767916463 434 LDVVREIYKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQGTIKIQK 485
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
353-475 |
4.02e-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: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 353 LDKLKHtESDKLQVQIQAYLDNVFDVGALLEDAETK-----NAALERVEELEENISHLSEKLQDTENEamskiVELEKQL 427
Cdd:pfam09787 49 LEELRQ-ERDLLREEIQKLRGQIQQLRTELQELEAQqqeeaESSREQLQELEEQLATERSARREAEAE-----LERLQEE 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 767916463 428 MQRNKElDVVREI------YKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHEL 475
Cdd:pfam09787 123 LRYLEE-ELRRSKatlqsrIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQL 175
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
349-496 |
4.30e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 349 LDEYLDKLKHTESDKLQvqiQAYLDNVFDVGALLEDAETKNAALE-RVEELEENISHLSEKLQDTENEAMSKIVELEKQL 427
Cdd:COG2433 378 IEEALEELIEKELPEEE---PEAEREKEHEERELTEEEEEIRRLEeQVERLEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767916463 428 MQRNKELDVVREIYKDANTqVHTLRKMVKEKEEAIQRqstLEKKIHELEKqgTIKIQKKGDGdIAILPV 496
Cdd:COG2433 455 SEERREIRKDREISRLDRE-IERLERELEEERERIEE---LKRKLERLKE--LWKLEHSGEL-VPVKVV 516
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
381-478 |
5.20e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 381 LLEDAETKNAALERVEELE--ENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEK 458
Cdd:PRK12704 43 ILEEAKKEAEAIKKEALLEakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
|
90 100
....*....|....*....|.
gi 767916463 459 EEAI-QRQSTLEKKIHELEKQ 478
Cdd:PRK12704 123 QQELeKKEEELEELIEEQLQE 143
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
353-452 |
5.61e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 353 LDKLK----HTESDKLQVQI----QAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEAMSK--IV 421
Cdd:PRK11281 45 LDALNkqklLEAEDKLVQQDleqtLALLDKIDRQKEETEQLKQQlAQAPAKLRQAQAELEALKDDNDEETRETLSTlsLR 124
|
90 100 110
....*....|....*....|....*....|.
gi 767916463 422 ELEKQLMQRNKELDVVREIYKDANTQVHTLR 452
Cdd:PRK11281 125 QLESRLAQTLDQLQNAQNDLAEYNSQLVSLQ 155
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
377-486 |
5.81e-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: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 377 DVGALLEDAETKNAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLrkmVK 456
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL---EQ 302
|
90 100 110
....*....|....*....|....*....|
gi 767916463 457 EKEEAIQRQSTLEKKIHELEKQGTIKIQKK 486
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKL 332
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
290-475 |
9.87e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.09 E-value: 9.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 290 FKEVCGEKQRFEKLMEHFRNE--------DNNIDFMVASMQFINIVVHSVE-DMNFRVHLQYEFTKLGLDEYLDKL--KH 358
Cdd:pfam05483 160 LKETCARSAEKTKKYEYEREEtrqvymdlNNNIEKMILAFEELRVQAENARlEMHFKLKEDHEKIQHLEEEYKKEIndKE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767916463 359 TESDKLQVQIQAYLDNVFDVGALLEDAETKnaalerVEELEENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVR 438
Cdd:pfam05483 240 KQVSLLLIQITEKENKMKDLTFLLEESRDK------ANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQK 313
|
170 180 190
....*....|....*....|....*....|....*..
gi 767916463 439 EIYKDANTQVHTLRKMVKEKEEAIQrQSTLEKKIHEL 475
Cdd:pfam05483 314 ALEEDLQIATKTICQLTEEKEAQME-ELNKAKAAHSF 349
|
|
| |
