|
Name |
Accession |
Description |
Interval |
E-value |
| FH2 |
pfam02181 |
Formin Homology 2 Domain; |
622-973 |
1.26e-116 |
|
Formin Homology 2 Domain;
Pssm-ID: 396655 Cd Length: 372 Bit Score: 364.67 E-value: 1.26e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 622 IKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPAIDLSSSKQKITqKASSKVTLLE 701
Cdd:pfam02181 1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSK-KKPKEVSLLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 702 ANRAKNLAITLRKAGKSADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERErkpLENLSDEDRFMMQFSKI 781
Cdd:pfam02181 80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 782 ERLLQKMTIMAFIGNFTESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 860
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 861 KSTDRKQTLLHYISNVVKEKYQQVTLFYNELHYVEKAAAVSLENVLLDVKELQRGMDLTKREYTMHDHN--------TLL 932
Cdd:pfam02181 237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfrEVL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568914300 933 KEFLLHNEGKLKKLQEDAKIAQDAFDDVVKYFGENPKTTPP 973
Cdd:pfam02181 317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSP 357
|
|
| FH2 |
smart00498 |
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ... |
623-1046 |
2.64e-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: 289.64 E-value: 2.64e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 623 KKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERileDLNVDEFEEIF--KTKAQGPAIDLSSSKQKITQKASSKVTLL 700
Cdd:smart00498 1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 701 EANRAKNLAITLRKAGKSADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERkpLENLSDEDRFMMQFSK 780
Cdd:smart00498 78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 781 IERLLQKMTIMAFIGNFTESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 859
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 860 TKSTDRKQTLLHYISNVVKEKYQQVtlFYNELHYVEKAAAVslenvlldvkelqrgmdltkreytmhdhntlLKEFLLHN 939
Cdd:smart00498 236 VKSADNKTTLLHFLVKIIRKKYLGG--LSDPENLDDKFIEV-------------------------------MKPFLKAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 940 EGKLKKLQEDAKIAQDAFDDVVKYFGENPKTTPPSVFFPVFVRFVKAYKQAEEENELRKKQEQALMEKLLEQEALMEQQD 1019
Cdd:smart00498 283 KEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEEERRKKLVKETTEYEQSS 362
|
410 420
....*....|....*....|....*..
gi 568914300 1020 AKspsHKSKRQQQELIAELRRRQVKDN 1046
Cdd:smart00498 363 SR---QKERNPSMDFEVERDFLGVLDS 386
|
|
| Drf_FH3 |
pfam06367 |
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins. |
278-475 |
2.11e-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: 193.64 E-value: 2.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 278 GGHEIILSAFDNFKEVCGEKQRFEKLMEHFRN-EDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKL 356
Cdd:pfam06367 1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 357 KHTESDKLQVQIQAYLDNVF-DVGALLEDAETKNAALERVEELEEnisHLSEKLQDTENEAMsKIVELEKQLM--QRNKE 433
Cdd:pfam06367 81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPH-LLSILQHLLLirDDEEE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568914300 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 |
1.88e-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: 93.15 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 23 LPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQ-------ERFQVKNP--------PHTYIQKLKGyl 87
Cdd:pfam06371 1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 88 DPAvtrkkfrrrvqeSTQVLRELEISLRTNHIGWVREFLNEEnkGLDVLVEYLSfaqyavtfdfesvestmestvdkskp 167
Cdd:pfam06371 79 DSI------------SSKQLESLRVALRTQPLSWVRRFIEAQ--GLGALLNVLS-------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 168 wsrsiedlhrgsnlpspvgnsvsrsgrhsalryntlpsrrtLKNSRLVSKKDDV---HVCIMCLRAIMNYQYGFNMVMSH 244
Cdd:pfam06371 119 -----------------------------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGH 157
|
250 260 270
....*....|....*....|....*....|.
gi 568914300 245 PHAVNEIALSLNNKNPRTKALVLELLAAVCL 275
Cdd:pfam06371 158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
367-478 |
1.66e-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: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 367 QIQAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEamskIVELEKQLMQRNKELD--------VV 437
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEAEIEerreelgeRA 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 438 REIYK------------------DANTQVHTLRKMV-----------KEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG3883 93 RALYRsggsvsyldvllgsesfsDFLDRLSALSKIAdadadlleelkADKAELEAKKAELEAKLAELEAL 162
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
381-478 |
5.63e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 381 LLEDAETKNAALERVEELE--ENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEK 458
Cdd:PRK12704 43 ILEEAKKEAEAIKKEALLEakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
|
90 100
....*....|....*....|.
gi 568914300 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 |
6.22e-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: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 377 DVGALLEDAETKNAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLrkmVK 456
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL---EQ 302
|
90 100 110
....*....|....*....|....*....|
gi 568914300 457 EKEEAIQRQSTLEKKIHELEKQGTIKIQKK 486
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKL 332
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FH2 |
pfam02181 |
Formin Homology 2 Domain; |
622-973 |
1.26e-116 |
|
Formin Homology 2 Domain;
Pssm-ID: 396655 Cd Length: 372 Bit Score: 364.67 E-value: 1.26e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 622 IKKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERILEDLNVDEFEEIFKTKAQGPAIDLSSSKQKITqKASSKVTLLE 701
Cdd:pfam02181 1 PKKTPKPKKKLKPLHWDKVRPSQDRGTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSK-KKPKEVSLLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 702 ANRAKNLAITLRKAGKSADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERErkpLENLSDEDRFMMQFSKI 781
Cdd:pfam02181 80 PKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGD---PSELGRAEQFLLELSKI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 782 ERLLQKMTIMAFIGNFTESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNS-SKRGAVYGFKLQSLDLLLDT 860
Cdd:pfam02181 157 PRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDgTRRGQAKGFKLSSLLKLSDT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 861 KSTDRKQTLLHYISNVVKEKYQQVTLFYNELHYVEKAAAVSLENVLLDVKELQRGMDLTKREYTMHDHN--------TLL 932
Cdd:pfam02181 237 KSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDehpddkfrEVL 316
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 568914300 933 KEFLLHNEGKLKKLQEDAKIAQDAFDDVVKYFGENPKTTPP 973
Cdd:pfam02181 317 KEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSP 357
|
|
| FH2 |
smart00498 |
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ... |
623-1046 |
2.64e-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: 289.64 E-value: 2.64e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 623 KKPIKTKFRMPVFNWVALKPNQINGTVFNEIDDERileDLNVDEFEEIF--KTKAQGPAIDLSSSKQKITQKASSKVTLL 700
Cdd:smart00498 1 KKEPKPKKKLKPLHWDKLNPSDLSGTVWDKIDEES---EGDLDELEELFsaKEKTKSASKDVSEKKSILKKKASQEFKIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 701 EANRAKNLAITLRKAGKSADEICKAIHVFDLKTLPVDFVECLMRFLPTENEVKVLRLYERERkpLENLSDEDRFMMQFSK 780
Cdd:smart00498 78 DPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEED--PEELARAEQFLLLISN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 781 IERLLQKMTIMAFIGNFTESIQMLTPQLHAIIAASVSIKSSQKLKKILEIILALGNYMNS-SKRGAVYGFKLQSLDLLLD 859
Cdd:smart00498 156 IPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGgSRRGQAYGFKLSSLLKLSD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 860 TKSTDRKQTLLHYISNVVKEKYQQVtlFYNELHYVEKAAAVslenvlldvkelqrgmdltkreytmhdhntlLKEFLLHN 939
Cdd:smart00498 236 VKSADNKTTLLHFLVKIIRKKYLGG--LSDPENLDDKFIEV-------------------------------MKPFLKAA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 940 EGKLKKLQEDAKIAQDAFDDVVKYFGENPKTTPPSVFFPVFVRFVKAYKQAEEENELRKKQEQALMEKLLEQEALMEQQD 1019
Cdd:smart00498 283 KEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEEEEEERRKKLVKETTEYEQSS 362
|
410 420
....*....|....*....|....*..
gi 568914300 1020 AKspsHKSKRQQQELIAELRRRQVKDN 1046
Cdd:smart00498 363 SR---QKERNPSMDFEVERDFLGVLDS 386
|
|
| Drf_FH3 |
pfam06367 |
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins. |
278-475 |
2.11e-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: 193.64 E-value: 2.11e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 278 GGHEIILSAFDNFKEVCGEKQRFEKLMEHFRN-EDNNIDFMVASMQFINIVVHSVEDMNFRVHLQYEFTKLGLDEYLDKL 356
Cdd:pfam06367 1 GGHEKVLEATLNFKEVCRERGRFQSLVGALDSsENDNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 357 KHTESDKLQVQIQAYLDNVF-DVGALLEDAETKNAALERVEELEEnisHLSEKLQDTENEAMsKIVELEKQLM--QRNKE 433
Cdd:pfam06367 81 RELENDELDDQLQAFEENREeDVEELLERFDDVNVDLDDPSELFE---LLWNKLKDTEAEPH-LLSILQHLLLirDDEEE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 568914300 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 |
1.88e-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: 93.15 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 23 LPMPEPGELEERFAIVLNAMNLPPDKARLLRQYDNEKKWELICDQ-------ERFQVKNP--------PHTYIQKLKGyl 87
Cdd:pfam06371 1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYkstnfqkEGGGSKSDsesnetgsPEYYVKKLKD-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 88 DPAvtrkkfrrrvqeSTQVLRELEISLRTNHIGWVREFLNEEnkGLDVLVEYLSfaqyavtfdfesvestmestvdkskp 167
Cdd:pfam06371 79 DSI------------SSKQLESLRVALRTQPLSWVRRFIEAQ--GLGALLNVLS-------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 168 wsrsiedlhrgsnlpspvgnsvsrsgrhsalryntlpsrrtLKNSRLVSKKDDV---HVCIMCLRAIMNYQYGFNMVMSH 244
Cdd:pfam06371 119 -----------------------------------------KINRKKSQEEEDLdreYEILKCLKALMNNKFGLDHVLGH 157
|
250 260 270
....*....|....*....|....*....|.
gi 568914300 245 PHAVNEIALSLNNKNPRTKALVLELLAAVCL 275
Cdd:pfam06371 158 PSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
367-478 |
1.66e-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: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 367 QIQAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEamskIVELEKQLMQRNKELD--------VV 437
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAElDALQAELEELNEEYNELQAELEALQAE----IDKLQAEIAEAEAEIEerreelgeRA 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 438 REIYK------------------DANTQVHTLRKMV-----------KEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG3883 93 RALYRsggsvsyldvllgsesfsDFLDRLSALSKIAdadadlleelkADKAELEAKKAELEAKLAELEAL 162
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
364-478 |
1.84e-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: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 364 LQVQIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLQDTEnEAMSKIVELEKQLMQRNKELDVVREIYKD 443
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA-SAEREIAELEAELERLDASSDDLAALEEQ 693
|
90 100 110
....*....|....*....|....*....|....*
gi 568914300 444 ANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG4913 694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEE 728
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
355-478 |
2.10e-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: 40.66 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 355 KLKHTESD--KLQVQIQAYLDNVFDvgalledaetKNAAlERvEELEENISHLSEKLQDTENeamsKIVELEKQLMQRNK 432
Cdd:pfam15619 89 KLKEKEAEllRLRDQLKRLEKLSED----------KNLA-ER-EELQKKLEQLEAKLEDKDE----KIQDLERKLELENK 152
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 568914300 433 ELDvvREIYKdANTQVHTLRKMVKEKEEAIQRqstLEKKIHELEKQ 478
Cdd:pfam15619 153 SFR--RQLAA-EKKKHKEAQEEVKILQEEIER---LQQKLKEKERE 192
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
349-478 |
2.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 349 LDEYLDKLKHTESDKLQVQIQAYLDNVF---------DVGALLEDAETKNAALERVEELEENI-SHLSEKLQD----TEN 414
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAALLaeagvedeeELRAALEQAEEYQELKEELEELEEQLeELLGELEELlealDEE 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568914300 415 EAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKmVKEKEEAIQRQSTLEKKIHELEKQ 478
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEE-DGELAELLQELEELKAELRELAEE 491
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
349-496 |
3.36e-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: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 349 LDEYLDKLKHTESDKLQvqiQAYLDNVFDVGALLEDAETKNAALE-RVEELEENISHLSEKLQDTENEAMSKIVELEKQL 427
Cdd:COG2433 378 IEEALEELIEKELPEEE---PEAEREKEHEERELTEEEEEIRRLEeQVERLEAEVEELEAELEEKDERIERLERELSEAR 454
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568914300 428 MQRNKELDVVREIYKDANTqVHTLRKMVKEKEEAIQRqstLEKKIHELEKqgTIKIQKKGDGdIAILPV 496
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 ... |
353-475 |
4.35e-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: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 353 LDKLKHtESDKLQVQIQAYLDNVFDVGALLEDAETK-----NAALERVEELEENISHLSEKLQDTENEamskiVELEKQL 427
Cdd:pfam09787 49 LEELRQ-ERDLLREEIQKLRGQIQQLRTELQELEAQqqeeaESSREQLQELEEQLATERSARREAEAE-----LERLQEE 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 568914300 428 MQRNKElDVVREI------YKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHEL 475
Cdd:pfam09787 123 LRYLEE-ELRRSKatlqsrIKDREAEIEKLRNQLTSKSQSSSSQSELENRLHQL 175
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
354-485 |
4.64e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 354 DKLKHTESDKLQVQIQAYLDNVFDVGALLEDAETKNAALERVEELEENISHLSEKLqdtenEAMSKIVELEKQLMQRNKE 433
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAE 140
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 568914300 434 LDVVREIYKDANTQVHTLRKMVKEKEEAIQRQSTLEKKIHELEKQGTIKIQK 485
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
381-478 |
5.63e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 381 LLEDAETKNAALERVEELE--ENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLRKMVKEK 458
Cdd:PRK12704 43 ILEEAKKEAEAIKKEALLEakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQK 122
|
90 100
....*....|....*....|.
gi 568914300 459 EEAI-QRQSTLEKKIHELEKQ 478
Cdd:PRK12704 123 QQELeKKEEELEELIEEQLQE 143
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
353-452 |
5.66e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.05 E-value: 5.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 353 LDKLK----HTESDKLQVQI----QAYLDNVFDVGALLEDAETK-NAALERVEELEENISHLSEKLQDTENEAMSK--IV 421
Cdd:PRK11281 45 LDALNkqklLEAEDKLVQQDleqtLALLDKIDRQKEETEQLKQQlAQAPAKLRQAQAELEALKDDNDEETRETLSTlsLR 124
|
90 100 110
....*....|....*....|....*....|.
gi 568914300 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 |
6.22e-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: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914300 377 DVGALLEDAETKNAALERVEELEENISHLSEKLQDTENEAMSKIVELEKQLMQRNKELDVVREIYKDANTQVHTLrkmVK 456
Cdd:TIGR02168 226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRL---EQ 302
|
90 100 110
....*....|....*....|....*....|
gi 568914300 457 EKEEAIQRQSTLEKKIHELEKQGTIKIQKK 486
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKL 332
|
|
| |
