|
Name |
Accession |
Description |
Interval |
E-value |
| FH2 |
pfam02181 |
Formin Homology 2 Domain; |
741-1117 |
3.86e-131 |
|
Formin Homology 2 Domain;
Pssm-ID: 396655 Cd Length: 372 Bit Score: 406.27 E-value: 3.86e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 741 PKKLYKPEVQLRRPNWSKLVAEDLSqDCFWTKVKEDRFENNELFAKLTLTFSAQTKTSKAKKDQEGGEEKKSVQKKKVKe 820
Cdd:pfam02181 1 PKKTPKPKKKLKPLHWDKVRPSQDR-GTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVSLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 821 lkvlDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKDEYDDLAESEQFGVVMG 900
Cdd:pfam02181 79 ----DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 901 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSESFSSLLEITLLVGNYMNAGSRNAGAFGFNISFLCKLR 980
Cdd:pfam02181 155 KIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 981 DTKSTDQKMTLLHFLAELCENDYPDVLKFPDELAHVEKASRVSAENLQKNLDQMKKQISDVERDVQNFPAATDEKDKFVE 1060
Cdd:pfam02181 235 DTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFRE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622947471 1061 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFLFDPKKLSVEEFFMDLHNFRNMF 1117
Cdd:pfam02181 315 VLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
|
|
| FH2 |
smart00498 |
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ... |
742-1179 |
3.30e-129 |
|
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: 401.73 E-value: 3.30e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 742 KKLYKPEVQLRRPNWSKLVAEDLSqDCFWTKVKEdrfENNELFAKLTLTFSAQTKTSKAKKDQEggEEKKSVQKKKVKEL 821
Cdd:smart00498 1 KKEPKPKKKLKPLHWDKLNPSDLS-GTVWDKIDE---ESEGDLDELEELFSAKEKTKSASKDVS--EKKSILKKKASQEF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 822 KVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKDE-YDDLAESEQFGVVMG 900
Cdd:smart00498 75 KILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLIS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 901 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSESFSSLLEITLLVGNYMNAGSRNAGAFGFNISFLCKLR 980
Cdd:smart00498 155 NIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 981 DTKSTDQKMTLLHFLAELCENDYpdvlkfpdelahvekasrvsaenlqknldqmkkqisdverdVQNFPAATDEKDKFVE 1060
Cdd:smart00498 235 DVKSADNKTTLLHFLVKIIRKKY-----------------------------------------LGGLSDPENLDDKFIE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 1061 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFLFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRREtEEKMRRAKLA 1140
Cdd:smart00498 274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEE-EEEERRKKLV 352
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1622947471 1141 KEKAEKERL-EKQQKREQLIDMNAEGDETGVMDSLLEALQ 1179
Cdd:smart00498 353 KETTEYEQSsSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
|
|
| Drf_FH3 |
pfam06367 |
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins. |
265-455 |
1.37e-62 |
|
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: 211.36 E-value: 1.37e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 265 DMNERVLEAMTERAEMD-EVERFQPLLDGLKSGT--TIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQDL 341
Cdd:pfam06367 1 GGHEKVLEATLNFKEVCrERGRFQSLVGALDSSEndNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 342 REIENEDMRVQLNVFDEQGEEDSYDLKGRLDDIRMEMDDFNEVFQILLNTVKDSKAEPHFLSILQHLLLVRNDYEARPQY 421
Cdd:pfam06367 81 RELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1622947471 422 YKLIEECISQIVLHKNGADPDFKCR-HLQIEIEGL 455
Cdd:pfam06367 161 WKLLEELVSQIVLHRTKPDPKFDERkNLEIDINRL 195
|
|
| Drf_GBD |
pfam06371 |
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ... |
75-259 |
5.08e-41 |
|
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: 149.39 E-value: 5.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 75 LQDVSDEQVLVLFEQMLLDMNLNEEKQQPLREKDIIIKREMVSQYLYT--SKAGMSQKESSK-----SAMMYIQELRSGL 147
Cdd:pfam06371 1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTnfQKEGGGSKSDSEsnetgSPEYYVKKLKDDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 148 RDmplLSCLESLRVSLNNNPVSWVQTF-GAEGLASLLDILKRLHDEKEEtaGSYDSRNKHEIIRCLKAFMNNKFGIKTML 226
Cdd:pfam06371 81 IS---SKQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQ--EEEDLDREYEILKCLKALMNNKFGLDHVL 155
|
170 180 190
....*....|....*....|....*....|...
gi 1622947471 227 ETEEGILLLVRAMDPAVPNMMIDAAKLLSALCI 259
Cdd:pfam06371 156 GHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
420-561 |
1.41e-05 |
|
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: 49.67 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 420 QYYKLIEECISQIVLHKngadpdFKCRHLQIEIEGLIDQM--------IDKTKVEKSEAKAAELEKQLDS---ELTARHE 488
Cdd:TIGR02168 292 ALANEISRLEQQKQILR------ERLANLERQLEELEAQLeeleskldELAEELAELEEKLEELKEELESleaELEELEA 365
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622947471 489 LQVEMKKLESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAAI 561
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
488-597 |
1.76e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 488 ELQVEMKKLESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAAITVAPSV 567
Cdd:COG3883 140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
90 100 110
....*....|....*....|....*....|
gi 1622947471 568 PSSAAAPPAPPLPGDSGTIIRPPPAPGDST 597
Cdd:COG3883 220 AAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
466-557 |
1.72e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 41.93 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 466 EKSEAKAAELEKQLDSELTARHELQVEMkklesdFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLtgeVAKLTKE 545
Cdd:pfam04849 141 SETESSCSTPLRRNESFSSLHGCVQLDA------LQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQL---MSDCVEQ 211
|
90
....*....|..
gi 1622947471 546 LEDAKKEMASLS 557
Cdd:pfam04849 212 LSEANQQMAELS 223
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
464-557 |
2.74e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 464 KVEKSEAKAAELEKQLDSELTARHELQVEM----------KKLESDFEQKLQDLQGEKDalhsEKQQIATEKQDLEAEVS 533
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTAIDELEEIMdefneqskklLELKNKISTNKQSLITLVD----KAKKVKAAIEELQAEFV 375
|
90 100
....*....|....*....|....
gi 1622947471 534 QLTGEVAKLTKELEDAKKEMASLS 557
Cdd:PHA02562 376 DNAEELAKLQDELDKIVKTKSELV 399
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
442-556 |
3.89e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 442 DFKCRHLQIEIEGL---IDQM-IDKTKVEKSEAKAAELEKQL-DSELTARHELQvEMKKLESDFEQKLQ-DLQGEKDALH 515
Cdd:smart00787 136 EWRMKLLEGLKEGLdenLEGLkEDYKLLMKELELLNSIKPKLrDRKDALEEELR-QLKQLEDELEDCDPtELDRAKEKLK 214
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622947471 516 SEKQQIATEKQ---DLEAEVSQLTGEVAKLTKELEDAKKEMASL 556
Cdd:smart00787 215 KLLQEIMIKVKkleELEEELQELESKIEDLTNKKSELNTEIAEA 258
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
307-554 |
4.20e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 307 QLINALITPAEELDFRVHIRSELMRLgLHQVLQDLREIENE--DMRVQLNVFDEQGEEDSYDLKGRLDDIRMEMDDFNEV 384
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQ-LSKELTELEAEIEEleERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 385 FQILLNTVKDSKAEphflsiLQHLLLVRNDYEARpqyyklIEECISQIV-LHKNGADpdfkcrhLQIEIEGLIDQMidkt 463
Cdd:TIGR02168 805 LDELRAELTLLNEE------AANLRERLESLERR------IAATERRLEdLEEQIEE-------LSEDIESLAAEI---- 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 464 kvEKSEAKAAELEKQLDSELTARHELQVEMKKLESDF----------EQKLQDLQGEKDALHSEKQQIATEKQDLEAEVS 533
Cdd:TIGR02168 862 --EELEELIEELESELEALLNERASLEEALALLRSELeelseelrelESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
250 260
....*....|....*....|..
gi 1622947471 534 QLTGEVAKLTK-ELEDAKKEMA 554
Cdd:TIGR02168 940 NLQERLSEEYSlTLEEAEALEN 961
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
320-561 |
7.89e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.80 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 320 DFRVHIRSELMRLglHQVLQDLREIENE---DMRVQLN-----VFDEQGEEDSYDLKGRLDDIRMEMddFNEVFQIllnt 391
Cdd:PTZ00108 901 DYKEFLESETLKE--KDVIVDYRDYSTAntvHFTVKLNdgvleQWEEEGIEKVFKLKSTISTTNMVL--FDENGKI---- 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 392 VKDSKAEPhflsILQHLLLVRND-YEARPQYykLIEECISQIVLHKNgadpdfKCRHLQIEIEGLIDqmIDKtkvekseA 470
Cdd:PTZ00108 973 KKYSDALD----ILKEFYLVRLDlYKKRKEY--LLGKLERELARLSN------KVRFIKHVINGELV--ITN-------A 1031
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 471 KAAELEKQLDSELTARHElQVEMKKLESDFEQKLQDLQGEKDALHSEKQQIATEKQD----LEAEVSQLTGE-VAKLTKE 545
Cdd:PTZ00108 1032 KKKDLVKELKKLGYVRFK-DIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSydylLSMPIWSLTKEkVEKLNAE 1110
|
250
....*....|....*.
gi 1622947471 546 LEDAKKEMASLSAAAI 561
Cdd:PTZ00108 1111 LEKKEKELEKLKNTTP 1126
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FH2 |
pfam02181 |
Formin Homology 2 Domain; |
741-1117 |
3.86e-131 |
|
Formin Homology 2 Domain;
Pssm-ID: 396655 Cd Length: 372 Bit Score: 406.27 E-value: 3.86e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 741 PKKLYKPEVQLRRPNWSKLVAEDLSqDCFWTKVKEDRFENNELFAKLTLTFSAQTKTSKAKKDQEGGEEKKSVQKKKVKe 820
Cdd:pfam02181 1 PKKTPKPKKKLKPLHWDKVRPSQDR-GTVWDKLDDESFELDGDLSELEELFSAKAKTKKNKKSEDKSSSKKKPKEVSLL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 821 lkvlDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKDEYDDLAESEQFGVVMG 900
Cdd:pfam02181 79 ----DPKRAQNIAILLRKLKLPPEEIIQAILEGDEDALDLELLENLLKMAPTKEELKKLKEYKGDPSELGRAEQFLLELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 901 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSESFSSLLEITLLVGNYMNAGSRNAGAFGFNISFLCKLR 980
Cdd:pfam02181 155 KIPRLEARLRALLFKSTFEEEIEELKPSLEALEAASEELRNSRKFKKLLELILALGNYMNDGTRRGQAKGFKLSSLLKLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 981 DTKSTDQKMTLLHFLAELCENDYPDVLKFPDELAHVEKASRVSAENLQKNLDQMKKQISDVERDVQNFPAATDEKDKFVE 1060
Cdd:pfam02181 235 DTKSTDNKTTLLHYLVKIIREKFPEVLDFSSELSHVKKAAKVNLEQLEKDVKQLERGLKKLERELELSALDEHPDDKFRE 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622947471 1061 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFLFDPKKLSVEEFFMDLHNFRNMF 1117
Cdd:pfam02181 315 VLKEFLKSAEEKLDKLESLLREALELFKELVEYFGEDPKETSPEEFFKILRDFLKEF 371
|
|
| FH2 |
smart00498 |
Formin Homology 2 Domain; FH proteins control rearrangements of the actin cytoskeleton, ... |
742-1179 |
3.30e-129 |
|
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: 401.73 E-value: 3.30e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 742 KKLYKPEVQLRRPNWSKLVAEDLSqDCFWTKVKEdrfENNELFAKLTLTFSAQTKTSKAKKDQEggEEKKSVQKKKVKEL 821
Cdd:smart00498 1 KKEPKPKKKLKPLHWDKLNPSDLS-GTVWDKIDE---ESEGDLDELEELFSAKEKTKSASKDVS--EKKSILKKKASQEF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 822 KVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKDE-YDDLAESEQFGVVMG 900
Cdd:smart00498 75 KILDPKRSQNLAILLRKLHMSYEEIKEAILEGDEDVLSVDLLEQLLKYAPTKEELKKLREYKEEdPEELARAEQFLLLIS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 901 TVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSESFSSLLEITLLVGNYMNAGSRNAGAFGFNISFLCKLR 980
Cdd:smart00498 155 NIPYLEERLNALLFKANFEEEVEDLKPQIEKVEAACEELRESKKFRKLLELILAIGNYMNGGSRRGQAYGFKLSSLLKLS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 981 DTKSTDQKMTLLHFLAELCENDYpdvlkfpdelahvekasrvsaenlqknldqmkkqisdverdVQNFPAATDEKDKFVE 1060
Cdd:smart00498 235 DVKSADNKTTLLHFLVKIIRKKY-----------------------------------------LGGLSDPENLDDKFIE 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 1061 KMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFLFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRREtEEKMRRAKLA 1140
Cdd:smart00498 274 VMKPFLKAAKEKYDKLQKDLSDLKTRFEKLVEYYGEDPKDTSPEEFFKDFNEFLKEFSKAAEENIKKEE-EEEERRKKLV 352
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1622947471 1141 KEKAEKERL-EKQQKREQLIDMNAEGDETGVMDSLLEALQ 1179
Cdd:smart00498 353 KETTEYEQSsSRQKERNPSMDFEVERDFLGVLDSLLEELG 392
|
|
| Drf_FH3 |
pfam06367 |
Diaphanous FH3 Domain; This region is found in the Formin-like and and diaphanous proteins. |
265-455 |
1.37e-62 |
|
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: 211.36 E-value: 1.37e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 265 DMNERVLEAMTERAEMD-EVERFQPLLDGLKSGT--TIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQDL 341
Cdd:pfam06367 1 GGHEKVLEATLNFKEVCrERGRFQSLVGALDSSEndNVEYKVATMQFINALVNSPEDLQFRLHLRSEFTALGLDRILDKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 342 REIENEDMRVQLNVFDEQGEEDSYDLKGRLDDIRMEMDDFNEVFQILLNTVKDSKAEPHFLSILQHLLLVRNDYEARPQY 421
Cdd:pfam06367 81 RELENDELDDQLQAFEENREEDVEELLERFDDVNVDLDDPSELFELLWNKLKDTEAEPHLLSILQHLLLIRDDEEELPSY 160
|
170 180 190
....*....|....*....|....*....|....*
gi 1622947471 422 YKLIEECISQIVLHKNGADPDFKCR-HLQIEIEGL 455
Cdd:pfam06367 161 WKLLEELVSQIVLHRTKPDPKFDERkNLEIDINRL 195
|
|
| Drf_GBD |
pfam06371 |
Diaphanous GTPase-binding Domain; This domain is bound to by GTP-attached Rho proteins, ... |
75-259 |
5.08e-41 |
|
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: 149.39 E-value: 5.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 75 LQDVSDEQVLVLFEQMLLDMNLNEEKQQPLREKDIIIKREMVSQYLYT--SKAGMSQKESSK-----SAMMYIQELRSGL 147
Cdd:pfam06371 1 LPKPDENEIDELFDELMEEMNLPEEKRRPMLAKPIEKKWQLIVQYKSTnfQKEGGGSKSDSEsnetgSPEYYVKKLKDDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 148 RDmplLSCLESLRVSLNNNPVSWVQTF-GAEGLASLLDILKRLHDEKEEtaGSYDSRNKHEIIRCLKAFMNNKFGIKTML 226
Cdd:pfam06371 81 IS---SKQLESLRVALRTQPLSWVRRFiEAQGLGALLNVLSKINRKKSQ--EEEDLDREYEILKCLKALMNNKFGLDHVL 155
|
170 180 190
....*....|....*....|....*....|...
gi 1622947471 227 ETEEGILLLVRAMDPAVPNMMIDAAKLLSALCI 259
Cdd:pfam06371 156 GHPSSIDLLVQSLDSERLKTRKLVLELLTALCL 188
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
420-561 |
1.41e-05 |
|
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: 49.67 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 420 QYYKLIEECISQIVLHKngadpdFKCRHLQIEIEGLIDQM--------IDKTKVEKSEAKAAELEKQLDS---ELTARHE 488
Cdd:TIGR02168 292 ALANEISRLEQQKQILR------ERLANLERQLEELEAQLeeleskldELAEELAELEEKLEELKEELESleaELEELEA 365
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622947471 489 LQVEMKKLESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAAI 561
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
488-597 |
1.76e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 488 ELQVEMKKLESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAAITVAPSV 567
Cdd:COG3883 140 ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
90 100 110
....*....|....*....|....*....|
gi 1622947471 568 PSSAAAPPAPPLPGDSGTIIRPPPAPGDST 597
Cdd:COG3883 220 AAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
464-559 |
1.81e-04 |
|
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: 44.53 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 464 KVEKSEAKAAELEKQLDSELTARHELQVEMKKLESDFEQK-------------------LQDLQGEKDALHSEKQQIATE 524
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearikkyeeqlgnvrnnkeYEALQKEIESLKRRISDLEDE 111
|
90 100 110
....*....|....*....|....*....|....*
gi 1622947471 525 KQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAA 559
Cdd:COG1579 112 ILELMERIEELEEELAELEAELAELEAELEEKKAE 146
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
446-558 |
2.76e-04 |
|
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: 45.43 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 446 RHLQIEIEGL-IDQMIDK-TKVEKSEAKAAELEKQLDSELTARH----ELQVEMKKLESDFEQ---KLQDLQGEKDALHS 516
Cdd:TIGR02168 223 RELELALLVLrLEELREElEELQEELKEAEEELEELTAELQELEekleELRLEVSELEEEIEElqkELYALANEISRLEQ 302
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1622947471 517 EKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSA 558
Cdd:TIGR02168 303 QKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE 344
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
480-560 |
2.88e-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: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 480 DSELTARHELQVEMKKLESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAA 559
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
.
gi 1622947471 560 A 560
Cdd:COG3883 95 L 95
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
492-560 |
3.77e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 3.77e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622947471 492 EMKKLESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAA 560
Cdd:COG3883 137 ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
473-561 |
3.80e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 473 AELEKQLDS-----ELTARH-ELQVEMKKLES--------DFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGE 538
Cdd:COG1196 196 GELERQLEPlerqaEKAERYrELKEELKELEAellllklrELEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100
....*....|....*....|...
gi 1622947471 539 VAKLTKELEDAKKEMASLSAAAI 561
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELA 298
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
466-560 |
7.32e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 466 EKSEAKAAELEkQLDSELTARHELQVEMKKLESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKE 545
Cdd:COG4942 20 DAAAEAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90
....*....|....*
gi 1622947471 546 LEDAKKEMASLSAAA 560
Cdd:COG4942 99 LEAQKEELAELLRAL 113
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
463-560 |
9.24e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 463 TKVEKSEAKAAELEKQLDSELTARHELQVEMKKLESDFEQ----------KLQDLQGEKDALHSEKQQIATEKQDLEAEV 532
Cdd:COG1196 260 AELAELEAELEELRLELEELELELEEAQAEEYELLAELARleqdiarleeRRRELEERLEELEEELAELEEELEELEEEL 339
|
90 100
....*....|....*....|....*...
gi 1622947471 533 SQLTGEVAKLTKELEDAKKEMASLSAAA 560
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEAL 367
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
462-559 |
1.38e-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: 41.83 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 462 KTKVEKSEAKAAELEKQLDSELTAR--HELQVEMKKLE---SDFEQKLQDLQGEKDALhseKQQIATEKQDLEAEVSQLT 536
Cdd:COG1579 65 ELEIEEVEARIKKYEEQLGNVRNNKeyEALQKEIESLKrriSDLEDEILELMERIEEL---EEELAELEAELAELEAELE 141
|
90 100
....*....|....*....|...
gi 1622947471 537 GEVAKLTKELEDAKKEMASLSAA 559
Cdd:COG1579 142 EKKAELDEELAELEAELEELEAE 164
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
466-557 |
1.72e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 41.93 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 466 EKSEAKAAELEKQLDSELTARHELQVEMkklesdFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLtgeVAKLTKE 545
Cdd:pfam04849 141 SETESSCSTPLRRNESFSSLHGCVQLDA------LQEKLRGLEEENLKLRSEASHLKTETDTYEEKEQQL---MSDCVEQ 211
|
90
....*....|..
gi 1622947471 546 LEDAKKEMASLS 557
Cdd:pfam04849 212 LSEANQQMAELS 223
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
462-561 |
1.91e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 462 KTKVEKSEAKAAELEKQLDSELTARHELQVEMKKLESDF---EQKLQDLQGEKDALHSEKQQI-------ATEKQDLEAE 531
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELeelELELEEAQAEEYELLAELARLeqdiarlEERRRELEER 317
|
90 100 110
....*....|....*....|....*....|
gi 1622947471 532 VSQLTGEVAKLTKELEDAKKEMASLSAAAI 561
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELE 347
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
446-560 |
2.16e-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: 42.06 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 446 RHLQIEIEGLIDQMidKTKVEKSEAKAAELEKQLDSELTARHELQVEMKKLESDFEQKLQDLQgekdALHSEKQQIATEK 525
Cdd:COG4942 142 KYLAPARREQAEEL--RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA----RLEKELAELAAEL 215
|
90 100 110
....*....|....*....|....*....|....*
gi 1622947471 526 QDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAA 560
Cdd:COG4942 216 AELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
464-558 |
2.39e-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: 42.35 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 464 KVEKSEAKAAELEKQLDSELTARHELQVEMKKLES---DFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVA 540
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKeleELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIE 764
|
90
....*....|....*...
gi 1622947471 541 KLTKELEDAKKEMASLSA 558
Cdd:TIGR02168 765 ELEERLEEAEEELAEAEA 782
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
462-558 |
2.63e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 462 KTKVEKSEAKAAELEKQLDSELTARHELQVEMKKLE---SDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGE 538
Cdd:COG4372 72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
90 100
....*....|....*....|
gi 1622947471 539 VAKLTKELEDAKKEMASLSA 558
Cdd:COG4372 152 LKELEEQLESLQEELAALEQ 171
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
464-557 |
2.74e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 464 KVEKSEAKAAELEKQLDSELTARHELQVEM----------KKLESDFEQKLQDLQGEKDalhsEKQQIATEKQDLEAEVS 533
Cdd:PHA02562 300 RITKIKDKLKELQHSLEKLDTAIDELEEIMdefneqskklLELKNKISTNKQSLITLVD----KAKKVKAAIEELQAEFV 375
|
90 100
....*....|....*....|....
gi 1622947471 534 QLTGEVAKLTKELEDAKKEMASLS 557
Cdd:PHA02562 376 DNAEELAKLQDELDKIVKTKSELV 399
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
442-556 |
3.89e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 442 DFKCRHLQIEIEGL---IDQM-IDKTKVEKSEAKAAELEKQL-DSELTARHELQvEMKKLESDFEQKLQ-DLQGEKDALH 515
Cdd:smart00787 136 EWRMKLLEGLKEGLdenLEGLkEDYKLLMKELELLNSIKPKLrDRKDALEEELR-QLKQLEDELEDCDPtELDRAKEKLK 214
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1622947471 516 SEKQQIATEKQ---DLEAEVSQLTGEVAKLTKELEDAKKEMASL 556
Cdd:smart00787 215 KLLQEIMIKVKkleELEEELQELESKIEDLTNKKSELNTEIAEA 258
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
307-554 |
4.20e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 307 QLINALITPAEELDFRVHIRSELMRLgLHQVLQDLREIENE--DMRVQLNVFDEQGEEDSYDLKGRLDDIRMEMDDFNEV 384
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQ-LSKELTELEAEIEEleERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA 804
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 385 FQILLNTVKDSKAEphflsiLQHLLLVRNDYEARpqyyklIEECISQIV-LHKNGADpdfkcrhLQIEIEGLIDQMidkt 463
Cdd:TIGR02168 805 LDELRAELTLLNEE------AANLRERLESLERR------IAATERRLEdLEEQIEE-------LSEDIESLAAEI---- 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 464 kvEKSEAKAAELEKQLDSELTARHELQVEMKKLESDF----------EQKLQDLQGEKDALHSEKQQIATEKQDLEAEVS 533
Cdd:TIGR02168 862 --EELEELIEELESELEALLNERASLEEALALLRSELeelseelrelESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
250 260
....*....|....*....|..
gi 1622947471 534 QLTGEVAKLTK-ELEDAKKEMA 554
Cdd:TIGR02168 940 NLQERLSEEYSlTLEEAEALEN 961
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
443-558 |
5.89e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 443 FKCRHLQIEIEGLIDQMIDKTK-VEKSEAKAAELEKQLDS---ELTARHELQVEMKKLESDFEQKLQDLQGEKDALHSEK 518
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREeLEQLEEELEQARSELEQleeELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL 117
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1622947471 519 QQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSA 558
Cdd:COG4372 118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
448-558 |
6.97e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.20 E-value: 6.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 448 LQIEIEGLIDQMID-KTKVEKSEAKAAELEKQLDSELTARHELQVEMKK------------------LES----DF---- 500
Cdd:COG3883 42 LQAELEELNEEYNElQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraralyrsggsvsyldvlLGSesfsDFldrl 121
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622947471 501 ----------EQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSA 558
Cdd:COG3883 122 salskiadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
320-561 |
7.89e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 40.80 E-value: 7.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 320 DFRVHIRSELMRLglHQVLQDLREIENE---DMRVQLN-----VFDEQGEEDSYDLKGRLDDIRMEMddFNEVFQIllnt 391
Cdd:PTZ00108 901 DYKEFLESETLKE--KDVIVDYRDYSTAntvHFTVKLNdgvleQWEEEGIEKVFKLKSTISTTNMVL--FDENGKI---- 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 392 VKDSKAEPhflsILQHLLLVRND-YEARPQYykLIEECISQIVLHKNgadpdfKCRHLQIEIEGLIDqmIDKtkvekseA 470
Cdd:PTZ00108 973 KKYSDALD----ILKEFYLVRLDlYKKRKEY--LLGKLERELARLSN------KVRFIKHVINGELV--ITN-------A 1031
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 471 KAAELEKQLDSELTARHElQVEMKKLESDFEQKLQDLQGEKDALHSEKQQIATEKQD----LEAEVSQLTGE-VAKLTKE 545
Cdd:PTZ00108 1032 KKKDLVKELKKLGYVRFK-DIIKKKSEKITAEEEEGAEEDDEADDEDDEEELGAAVSydylLSMPIWSLTKEkVEKLNAE 1110
|
250
....*....|....*.
gi 1622947471 546 LEDAKKEMASLSAAAI 561
Cdd:PTZ00108 1111 LEKKEKELEKLKNTTP 1126
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
446-549 |
8.07e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 446 RHLQIEIEGLIDQMIDktkVEKSEAKAAELEKQLDSELTARHELqvemKKLEsdfeQKLQDLQGEKDALHSEKQQIATEK 525
Cdd:COG4913 647 REALQRLAEYSWDEID---VASAEREIAELEAELERLDASSDDL----AALE----EQLEELEAELEELEEELDELKGEI 715
|
90 100
....*....|....*....|....
gi 1622947471 526 QDLEAEVSQLTGEVAKLTKELEDA 549
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRLEAA 739
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
446-552 |
8.60e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 446 RHLQIEIEGLIDQMID-KTKVEKSEAKAAELEKQLDSELTARHELQVEMKKLESDFEQKLQDLQGEKDALHSEKQQIATE 524
Cdd:COG4717 135 EALEAELAELPERLEElEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
90 100
....*....|....*....|....*...
gi 1622947471 525 KQDLEAEVSQLTGEVAKLTKELEDAKKE 552
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALE 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
446-556 |
8.70e-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: 40.43 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622947471 446 RHLQIEIEGLIDQMidKTKVEKSEAKAAELEKQLDSELTARHELQVEMKKLESDF----------EQKLQDLQGEKDALH 515
Cdd:TIGR02168 718 RKELEELSRQISAL--RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLeeaeeelaeaEAEIEELEAQIEQLK 795
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1622947471 516 SEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASL 556
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
|
| |
