|
Name |
Accession |
Description |
Interval |
E-value |
| GCP6_N |
pfam19340 |
Gamma-tubulin complex component 6 N-terminus; This family represents the N-terminal ... |
28-341 |
1.38e-180 |
|
Gamma-tubulin complex component 6 N-terminus; This family represents the N-terminal alpha-helical region of Gamma-tubulin complex component 6 (GCP6), a protein indispensable for assembly of the gamma-tubulin complex and for microtubule nucleation. It is located at the centrioles and the pericentriolar material, being required for centriole formation and reduplication. It has been shown that the N-terminal domains define the functional identity of gamma-tubulin complex proteins. GCP6 carries a large internal insertion phosphorylated by Plk4 and contains a domain of interaction with keratins.
Pssm-ID: 466048 Cd Length: 315 Bit Score: 545.12 E-value: 1.38e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 28 VNRKKAKLSLKRVAYNALFANLFQEDTHQRQPD-SKLPVKNKVLMLSFDLRVGGLGPEADRLEELVEKLETAPDCPFVEV 106
Cdd:pfam19340 1 VSRPRFKRALKKAAYGALFEKLFQEETAKWPSElAKTPVRNKLLMLSFDLRVAGLGDEADRLEELVEKLEAGPSSPLAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 107 GSVLDLLVQLAGSGPPQVLRRKRDYFFNNKHAGRNIPYSGYDCYDLSVFEMDVRSLISGEENLCHNMVQEALQVMEAAPG 186
Cdd:pfam19340 81 EAVLDLLVQLAGSGPPQPLSFKRDYFRREKHVLRRVPLLGYDSYDLRVLEADAWSLVCREEWLFLHYIQYTLQLMEAAPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 187 TGLTTVGLFSTGDSCGDRFERDTRVSLFGALVHSRTYDMDVRLDLPPVPDSADFSGLAIKVPQIVDQWEDEGFQSASNLT 266
Cdd:pfam19340 161 TGLPTLGLFSLQLEAEDRFEKETRVSLFGALVHSRTYDMDVRLDLPPVPSNADLSGLAIKVPQSLDQSEDEGFQSASNLT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937933965 267 PDSQSEPSMTPDLDLWEAVLTYEASKRRCWERIGCPPGHREEPYLTEAGRDAFDRFCRLCHGELQALSGGLLQTP 341
Cdd:pfam19340 241 PDSQSEPSMTPDIDVWEAALTYEPSKRRCWERVGCPPGKREEPYLTEAGREAFDQLYRLREGELQVLSSPLLQLP 315
|
|
| GCP_C_terminal |
pfam04130 |
Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components ... |
1460-1760 |
2.83e-66 |
|
Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains.
Pssm-ID: 461187 Cd Length: 297 Bit Score: 226.74 E-value: 2.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 1460 HFEALRHFLLMEDGEFAQSLSDLLFEKLGagqTPGELLNPLVLNSILSKALQyslhgdTPHATNLSFA-LKYLPEVFAPN 1538
Cdd:pfam04130 4 HLRALKRYLLLGQGDFISRLMDALFDELW---KPASSLLRHNLTGLLEEAIR------SSNAQRDLPDvLRRLDARLDPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 1539 APDVLSCLELRYKVDWPLNIVITESCLNKYSGIFSFLLQLKLMMWTLKDIcfHLKRTALVSHtagSVQFRQLQLFKHEMQ 1618
Cdd:pfam04130 75 SLGGWDFLTLEYKVPWPLSLVLTPEALTKYQRLFRFLLRLKRVEFVLSSL--WRRRQMSGSR---SVLWHRARLLRQEMI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 1619 HFVKVIQGYIANQILHVSWCEFRARLAV-VGDLEEIQRAHAEYLHRAVFRGLLTEKAAPVMNIIHSIFSLVLKFRSQLIS 1697
Cdd:pfam04130 150 HFVSQLQYYVMFEVIEPSWREFEEKLQKaASDLDDLIEAHEDFLDRILKKCFLTSPQQPLLKLLEEILSLILDFAEALDG 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937933965 1698 QNWGPATGPRGAEHPNFPLMQQS-----YSTFKYYSHFLFKVVTKLVNRGYQPHLEDFLLRINFNNYY 1760
Cdd:pfam04130 230 LYLSVSESARAEAEDELPELERErlrrlEKQFRKKVSLLLKVLRGLKSHPDESHLRQLLLRLDFNGYY 297
|
|
| GCP_N_terminal |
pfam17681 |
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ... |
352-631 |
1.62e-30 |
|
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Functional studies have shown that the N-terminal domain defines the functional identity of GCPs, suggesting that all GCPs are incorporated into the helix of gamma-tubulin small complexes (gTURCs) via lateral interactions between their N-terminal domains. Thereby, they define the direct neighbors and position the GCPs within the helical wall of gTuRC. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains. In addition to the conserved sequences, the N-terminal domains carry specific insertions of various sizes depending on the GCP, i.e. internal insertions or N-terminal extensions. These insertions may equally contribute to the function of individual GCPs as they have been implied in specific interactions with regulatory or structural proteins. For instance, GCP6 carries a large internal insertion phosphorylated by Plk4 and containing a domain of interaction with keratins, whereas the N-terminal extension of GCP3 interacts with the recruitment protein MOZART1.
Pssm-ID: 465456 Cd Length: 298 Bit Score: 123.55 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 352 VKDSLNVLLGVVSATFSLCQPTQAFVVEpgVHVSGASPESISSILSEVAEYGTCYTRLSHFSLQPvvgSLCSRGLVFQAF 431
Cdd:pfam17681 1 LRDLLFALQGISGSYIRFDESDSRIVDD--IRIPGILPPSLRSLLSRLLELGLLYRRLRKFVESS---SSFEYGLVLQAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 432 TSGLRRYLQ-YYRACV-------LSTPPTLSLLTIGFLFKKLGRQLRYLAELcgVGTVSLATSGepravfptGVKLLSYL 503
Cdd:pfam17681 76 CAALQEELTeYYRLIAqlesqllEASDSILTLLRLVVWLQPPLLLLRVLSNL--VEAVEKQNLK--------GGALLSLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 504 YQEALdNCSNEHYPVLLSLLKTSCEPYTRFIHDWVYSGVFRDVYGEFMIQVNHE--YLSFRDKFYWTHGYVLiskeVEDC 581
Cdd:pfam17681 146 HEATS-HGDPFVRELLSRLLQRVSRPYLEMLERWIYEGELDDPYNEFFVEENPSvaKESLTSDDLWEDKYTL----RPEM 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937933965 582 VPVFL-KHIAHDVYVCGKTINLLKLCCPRHY--------LCWSDVPVPRISVIFSLEEL 631
Cdd:pfam17681 221 LPSFLsPDLAEKILLTGKSLNFLRECCGDSWriedtaseLEYGDDLSESSIFSLSLEEL 279
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
628-811 |
2.64e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 61.09 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 628 LEELKEIEKDcavyvgRMERVARYSSISKEE--KELRMEIAKQELIVHAREAASRVLSElsdrQMSEQIALDTRKREQFQ 705
Cdd:pfam13868 28 IAEKKRIKAE------EKEEERRLDEMMEEEreRALEEEEEKEEERKEERKRYRQELEE----QIEEREQKRQEEYEEKL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 706 RLKEQFVKDQER----------RLAARQEELGDDFSYAHELRareKRLKALEEELERKARQALVDHYSKLSAEAARREQK 775
Cdd:pfam13868 98 QEREQMDEIVERiqeedqaeaeEKLEKQRQLREEIDEFNEEQ---AEWKELEKEEEREEDERILEYLKEKAEREEEREAE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1937933965 776 ALWRIRRHRLESARLRFLLE---DQKCIQEMLRD---MEAHQ 811
Cdd:pfam13868 175 REEIEEEKEREIARLRAQQEkaqDEKAERDELRAklyQEEQE 216
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
657-773 |
3.23e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 58.25 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 657 EEKELRMEIAKQELIVHAREAASRVLSELsDRQMSEqialdtrKREQFQRL------KEQFVKDQERRLAARQEELGDDf 730
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIHKLRNEF-EKELRE-------RRNELQKLekrllqKEENLDRKLELLEKREEELEKK- 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1937933965 731 syAHELRAREKRLKALEEELERKARQAL--VDHYSKLSAEAARRE 773
Cdd:PRK12704 116 --EKELEQKQQELEKKEEELEELIEEQLqeLERISGLTAEEAKEI 158
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
629-819 |
7.85e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 629 EELKEIEKDCAVYVGRMERVARysSISKEEKELRMEIAKQELIVHAREAASRVLSELSDRQMSEQIALDTRKREQFQRLK 708
Cdd:COG1196 323 EELAELEEELEELEEELEELEE--ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 709 -----EQFVKDQERRLAARQEELGDDfsYAHELRAREKRLKALEEELERKARQALVDhysKLSAEAARREQKALWRIRRH 783
Cdd:COG1196 401 qleelEEAEEALLERLERLEEELEEL--EEALAELEEEEEEEEEALEEAAEEEAELE---EEEEALLELLAELLEEAALL 475
|
170 180 190
....*....|....*....|....*....|....*.
gi 1937933965 784 RLESARLRFLLEDQKCIQEMLRDMEAHQPQEPLSVL 819
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
629-814 |
7.97e-06 |
|
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: 51.21 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 629 EELKEIEKdcAVYVGRMER-VARYSSISKEEKELRMEIAKQELIVHAREAASRVLsELSDRQMSEQIA------------ 695
Cdd:TIGR02168 220 AELRELEL--ALLVLRLEElREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELEEEIEelqkelyalane 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 696 ---LDTRKREQFQRLK----------EQFVKDQERR------LAARQEELGDDFSYAHELRAREKRLKALEEELERKARQ 756
Cdd:TIGR02168 297 isrLEQQKQILRERLAnlerqleeleAQLEELESKLdelaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937933965 757 ALVDHYSKLSAEAARREQKALWRIRRHRLES------ARLRFLLEDqkcIQEMLRDMEAHQPQE 814
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEArlerleDRRERLQQE---IEELLKKLEEAELKE 437
|
|
| DUF4573 |
pfam15140 |
Domain of unknown function (DUF4573); This family of proteins is found in eukaryotes. Proteins ... |
1044-1199 |
1.57e-05 |
|
Domain of unknown function (DUF4573); This family of proteins is found in eukaryotes. Proteins in this family are typically approximately 360 amino acids in length.
Pssm-ID: 434493 [Multi-domain] Cd Length: 176 Bit Score: 47.13 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 1044 NIKVGDYMSDVALPRPRWNIHGHVSEANIGVGENVSDVAPSRPRWNVHGHVSDASIKVGENVSDVAPSRPRWNVHGHVSD 1123
Cdd:pfam15140 10 EIQPLKGVREIEPPQPGGKDDPLGAEEKKKDLRAVTEVEPLKGVAEIEPLGPVSEIQPLRAVSERDPLGAVEEIEPPQAA 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937933965 1124 ASIKVGENVSEVAPSRPRWNVHGHvsdasikvgENVSDVAPSRPRWNVHGHVSDASIKVGENVSDVAPSRPRWNVH 1199
Cdd:pfam15140 90 SEMKPLGTAENILPLEAAREIHPL---------EAVGKIEPLQLVETIPKENESPEIHPLEGSQEIEPLEPVQLIE 156
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
658-789 |
3.59e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.59 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 658 EKELRmeiakqelivHAREAASRVLSELSDRQMSEQIALDTRKREQFQRLkeqfvkDQErrLAARQE----ELGDDFSYA 733
Cdd:NF041483 93 ERELR----------DARAQTQRILQEHAEHQARLQAELHTEAVQRRQQL------DQE--LAERRQtvesHVNENVAWA 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937933965 734 HELRAR-EKRLKALEEELERKARQALvdhySKLSAEAARREQKAlwrirRHRL----ESAR 789
Cdd:NF041483 155 EQLRARtESQARRLLDESRAEAEQAL----AAARAEAERLAEEA-----RQRLgseaESAR 206
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
674-809 |
6.26e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.82 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 674 AREAASRVLSElSDRQMSEQIALDTRKREQFQRLKEQFVKDQERRLAARQEELGDDFSYAHElrAREKRLKALEEELeRK 753
Cdd:NF041483 522 AEETLERTRAE-AERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHT--EAEERLTAAEEAL-AD 597
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937933965 754 ARqalvdhysklsAEAARREQKALWRIRRHRLESA-RLRFLLEDQKCIQEMLRDMEA 809
Cdd:NF041483 598 AR-----------AEAERIRREAAEETERLRTEAAeRIRTLQAQAEQEAERLRTEAA 643
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GCP6_N |
pfam19340 |
Gamma-tubulin complex component 6 N-terminus; This family represents the N-terminal ... |
28-341 |
1.38e-180 |
|
Gamma-tubulin complex component 6 N-terminus; This family represents the N-terminal alpha-helical region of Gamma-tubulin complex component 6 (GCP6), a protein indispensable for assembly of the gamma-tubulin complex and for microtubule nucleation. It is located at the centrioles and the pericentriolar material, being required for centriole formation and reduplication. It has been shown that the N-terminal domains define the functional identity of gamma-tubulin complex proteins. GCP6 carries a large internal insertion phosphorylated by Plk4 and contains a domain of interaction with keratins.
Pssm-ID: 466048 Cd Length: 315 Bit Score: 545.12 E-value: 1.38e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 28 VNRKKAKLSLKRVAYNALFANLFQEDTHQRQPD-SKLPVKNKVLMLSFDLRVGGLGPEADRLEELVEKLETAPDCPFVEV 106
Cdd:pfam19340 1 VSRPRFKRALKKAAYGALFEKLFQEETAKWPSElAKTPVRNKLLMLSFDLRVAGLGDEADRLEELVEKLEAGPSSPLAEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 107 GSVLDLLVQLAGSGPPQVLRRKRDYFFNNKHAGRNIPYSGYDCYDLSVFEMDVRSLISGEENLCHNMVQEALQVMEAAPG 186
Cdd:pfam19340 81 EAVLDLLVQLAGSGPPQPLSFKRDYFRREKHVLRRVPLLGYDSYDLRVLEADAWSLVCREEWLFLHYIQYTLQLMEAAPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 187 TGLTTVGLFSTGDSCGDRFERDTRVSLFGALVHSRTYDMDVRLDLPPVPDSADFSGLAIKVPQIVDQWEDEGFQSASNLT 266
Cdd:pfam19340 161 TGLPTLGLFSLQLEAEDRFEKETRVSLFGALVHSRTYDMDVRLDLPPVPSNADLSGLAIKVPQSLDQSEDEGFQSASNLT 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937933965 267 PDSQSEPSMTPDLDLWEAVLTYEASKRRCWERIGCPPGHREEPYLTEAGRDAFDRFCRLCHGELQALSGGLLQTP 341
Cdd:pfam19340 241 PDSQSEPSMTPDIDVWEAALTYEPSKRRCWERVGCPPGKREEPYLTEAGREAFDQLYRLREGELQVLSSPLLQLP 315
|
|
| GCP_C_terminal |
pfam04130 |
Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components ... |
1460-1760 |
2.83e-66 |
|
Gamma tubulin complex component C-terminal; This is the C-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Structure-based sequence analysis revealed the existence of an exposed surface area conserved in all human GCPs and in GCP4 orthologs. This area is located in the C-terminal domain of GCP4, which was confirmed in vitro to bind directly to gamma-tubulin. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains.
Pssm-ID: 461187 Cd Length: 297 Bit Score: 226.74 E-value: 2.83e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 1460 HFEALRHFLLMEDGEFAQSLSDLLFEKLGagqTPGELLNPLVLNSILSKALQyslhgdTPHATNLSFA-LKYLPEVFAPN 1538
Cdd:pfam04130 4 HLRALKRYLLLGQGDFISRLMDALFDELW---KPASSLLRHNLTGLLEEAIR------SSNAQRDLPDvLRRLDARLDPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 1539 APDVLSCLELRYKVDWPLNIVITESCLNKYSGIFSFLLQLKLMMWTLKDIcfHLKRTALVSHtagSVQFRQLQLFKHEMQ 1618
Cdd:pfam04130 75 SLGGWDFLTLEYKVPWPLSLVLTPEALTKYQRLFRFLLRLKRVEFVLSSL--WRRRQMSGSR---SVLWHRARLLRQEMI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 1619 HFVKVIQGYIANQILHVSWCEFRARLAV-VGDLEEIQRAHAEYLHRAVFRGLLTEKAAPVMNIIHSIFSLVLKFRSQLIS 1697
Cdd:pfam04130 150 HFVSQLQYYVMFEVIEPSWREFEEKLQKaASDLDDLIEAHEDFLDRILKKCFLTSPQQPLLKLLEEILSLILDFAEALDG 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937933965 1698 QNWGPATGPRGAEHPNFPLMQQS-----YSTFKYYSHFLFKVVTKLVNRGYQPHLEDFLLRINFNNYY 1760
Cdd:pfam04130 230 LYLSVSESARAEAEDELPELERErlrrlEKQFRKKVSLLLKVLRGLKSHPDESHLRQLLLRLDFNGYY 297
|
|
| GCP_N_terminal |
pfam17681 |
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components ... |
352-631 |
1.62e-30 |
|
Gamma tubulin complex component N-terminal; This is the N-terminal domain found in components of the gamma-tubulin complex proteins (GCPs). Family members include spindle pole body (SBP) components such as Spc97 and Spc98 which function as the microtubule-organizing center in yeast. Furthermore, family members such as human GCP4 (Gamma-tubulin complex component 4) have been structurally elucidated. Functional studies have shown that the N-terminal domain defines the functional identity of GCPs, suggesting that all GCPs are incorporated into the helix of gamma-tubulin small complexes (gTURCs) via lateral interactions between their N-terminal domains. Thereby, they define the direct neighbors and position the GCPs within the helical wall of gTuRC. Sequence alignment of human GCPs based on the GCP4 structure helped delineate conserved regions in the N- and C-terminal domains. In addition to the conserved sequences, the N-terminal domains carry specific insertions of various sizes depending on the GCP, i.e. internal insertions or N-terminal extensions. These insertions may equally contribute to the function of individual GCPs as they have been implied in specific interactions with regulatory or structural proteins. For instance, GCP6 carries a large internal insertion phosphorylated by Plk4 and containing a domain of interaction with keratins, whereas the N-terminal extension of GCP3 interacts with the recruitment protein MOZART1.
Pssm-ID: 465456 Cd Length: 298 Bit Score: 123.55 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 352 VKDSLNVLLGVVSATFSLCQPTQAFVVEpgVHVSGASPESISSILSEVAEYGTCYTRLSHFSLQPvvgSLCSRGLVFQAF 431
Cdd:pfam17681 1 LRDLLFALQGISGSYIRFDESDSRIVDD--IRIPGILPPSLRSLLSRLLELGLLYRRLRKFVESS---SSFEYGLVLQAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 432 TSGLRRYLQ-YYRACV-------LSTPPTLSLLTIGFLFKKLGRQLRYLAELcgVGTVSLATSGepravfptGVKLLSYL 503
Cdd:pfam17681 76 CAALQEELTeYYRLIAqlesqllEASDSILTLLRLVVWLQPPLLLLRVLSNL--VEAVEKQNLK--------GGALLSLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 504 YQEALdNCSNEHYPVLLSLLKTSCEPYTRFIHDWVYSGVFRDVYGEFMIQVNHE--YLSFRDKFYWTHGYVLiskeVEDC 581
Cdd:pfam17681 146 HEATS-HGDPFVRELLSRLLQRVSRPYLEMLERWIYEGELDDPYNEFFVEENPSvaKESLTSDDLWEDKYTL----RPEM 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937933965 582 VPVFL-KHIAHDVYVCGKTINLLKLCCPRHY--------LCWSDVPVPRISVIFSLEEL 631
Cdd:pfam17681 221 LPSFLsPDLAEKILLTGKSLNFLRECCGDSWriedtaseLEYGDDLSESSIFSLSLEEL 279
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
628-811 |
2.64e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 61.09 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 628 LEELKEIEKDcavyvgRMERVARYSSISKEE--KELRMEIAKQELIVHAREAASRVLSElsdrQMSEQIALDTRKREQFQ 705
Cdd:pfam13868 28 IAEKKRIKAE------EKEEERRLDEMMEEEreRALEEEEEKEEERKEERKRYRQELEE----QIEEREQKRQEEYEEKL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 706 RLKEQFVKDQER----------RLAARQEELGDDFSYAHELRareKRLKALEEELERKARQALVDHYSKLSAEAARREQK 775
Cdd:pfam13868 98 QEREQMDEIVERiqeedqaeaeEKLEKQRQLREEIDEFNEEQ---AEWKELEKEEEREEDERILEYLKEKAEREEEREAE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1937933965 776 ALWRIRRHRLESARLRFLLE---DQKCIQEMLRD---MEAHQ 811
Cdd:pfam13868 175 REEIEEEKEREIARLRAQQEkaqDEKAERDELRAklyQEEQE 216
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
656-814 |
4.15e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 60.32 E-value: 4.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 656 KEEKELRMEIAKQELIVHAREAAS-----RVLSELSDRQMSEQIALDTRKREQFQRLKEQFVKDQER---RLAARQEELG 727
Cdd:pfam13868 118 AEEKLEKQRQLREEIDEFNEEQAEwkeleKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEReiaRLRAQQEKAQ 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 728 DdfsyahELRAREK-RLKALEEELERKARQALvdhysklsAEAARREQKALWRIRRHRLESARLRflledqkciqEMLRD 806
Cdd:pfam13868 198 D------EKAERDElRAKLYQEEQERKERQKE--------REEAEKKARQRQELQQAREEQIELK----------ERRLA 253
|
....*...
gi 1937933965 807 MEAHQPQE 814
Cdd:pfam13868 254 EEAEREEE 261
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
628-861 |
6.34e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.91 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 628 LEELKEIEKDCAVYVGRMERV------ARYSSISKEEKELRMEIAKQELIV------HAREAASRVLSELSDRQMsEQIA 695
Cdd:pfam17380 374 ISRMRELERLQMERQQKNERVrqeleaARKVKILEEERQRKIQQQKVEMEQiraeqeEARQREVRRLEEERAREM-ERVR 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 696 LDTRKRE-QFQRLKEQ--------FVKDQERRLAARQEELGDDFsYAHELRAR-------EKRLKALEEELERKaRQALV 759
Cdd:pfam17380 453 LEEQERQqQVERLRQQeeerkrkkLELEKEKRDRKRAEEQRRKI-LEKELEERkqamieeERKRKLLEKEMEER-QKAIY 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 760 DHYSKLSAEAARREQKAL---WRIRRHRLESARLRFLLEDQKCIQEMLRDMEAHQPQEplSVLPSTcSQVTSLGPEHE-- 834
Cdd:pfam17380 531 EEERRREAEEERRKQQEMeerRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR--AEYEAT-TPITTIKPIYRpr 607
|
250 260
....*....|....*....|....*...
gi 1937933965 835 -GEGHSCDLESTELRCdCSNQPCASTPS 861
Cdd:pfam17380 608 iSEYQPPDVESHMIRF-TTQSPEWATPS 634
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
633-811 |
7.14e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.91 E-value: 7.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 633 EIEKDCAVYVGR----MERVARYSSISKEEKELRMEIAKQELIvhAREAASrvLSELSDRQMSEQiALDTRKREQFQRLK 708
Cdd:pfam17380 328 EMDRQAAIYAEQermaMERERELERIRQEERKRELERIRQEEI--AMEISR--MRELERLQMERQ-QKNERVRQELEAAR 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 709 EQFVKDQERRLAARQEELGDDFSYAHELRAREKRLKALEEELERK---------ARQALVDHY---------SKLSAEAA 770
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREmervrleeqERQQQVERLrqqeeerkrKKLELEKE 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1937933965 771 RREQKALWRIRRHRLE---SARLRFLLEDQKCIQEMLRDMEAHQ 811
Cdd:pfam17380 483 KRDRKRAEEQRRKILEkelEERKQAMIEEERKRKLLEKEMEERQ 526
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
677-814 |
2.21e-08 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 56.64 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 677 AASRVLSELSDRQMSE-------QIALDT---RKREQfqRLKEQFVKDQERRlaARQEElgddfsyaHELRAREKRLKaL 746
Cdd:pfam13904 31 SSSQSSSLTYARKLEGlklerqpLEAYENwlaAKQRQ--RQKELQAQKEERE--KEEQE--------AELRKRLAKEK-Y 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937933965 747 EEELERKARQALVDHYSKLSAEAARREQKALWRIRRHRL-ESARLRF-------LLEDQKCIQEMLRDMEAHQPQE 814
Cdd:pfam13904 98 QEWLQRKARQQTKKREESHKQKAAESASKSLAKPERKVSqEEAKEVLqewerkkLEQQQRKREEEQREQLKKEEEE 173
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
629-811 |
3.02e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 57.62 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 629 EELKEIEKDCAVYVG-RMERVARYssiskEEKELRMEIAKQELIVHAREAASRVLSE-------LSDRQMSEQ------- 693
Cdd:pfam13868 148 EEEREEDERILEYLKeKAEREEER-----EAEREEIEEEKEREIARLRAQQEKAQDEkaerdelRAKLYQEEQerkerqk 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 694 -IALDTRKREQFQRLKEQFVKDQERRLAARQEELGDDFSYAHELRAREKRLKALEEELERKARQALVDHysklsaeaaRR 772
Cdd:pfam13868 223 eREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEH---------RR 293
|
170 180 190
....*....|....*....|....*....|....*....
gi 1937933965 773 EQKALWRIRRHRLESARLRFLLEdqkciQEMLRDMEAHQ 811
Cdd:pfam13868 294 ELEKQIEEREEQRAAEREEELEE-----GERLREEEAER 327
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
657-773 |
3.23e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 58.25 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 657 EEKELRMEIAKQELIVHAREAASRVLSELsDRQMSEqialdtrKREQFQRL------KEQFVKDQERRLAARQEELGDDf 730
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKEEIHKLRNEF-EKELRE-------RRNELQKLekrllqKEENLDRKLELLEKREEELEKK- 115
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1937933965 731 syAHELRAREKRLKALEEELERKARQAL--VDHYSKLSAEAARRE 773
Cdd:PRK12704 116 --EKELEQKQQELEKKEEELEELIEEQLqeLERISGLTAEEAKEI 158
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
629-819 |
7.85e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 629 EELKEIEKDCAVYVGRMERVARysSISKEEKELRMEIAKQELIVHAREAASRVLSELSDRQMSEQIALDTRKREQFQRLK 708
Cdd:COG1196 323 EELAELEEELEELEEELEELEE--ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 709 -----EQFVKDQERRLAARQEELGDDfsYAHELRAREKRLKALEEELERKARQALVDhysKLSAEAARREQKALWRIRRH 783
Cdd:COG1196 401 qleelEEAEEALLERLERLEEELEEL--EEALAELEEEEEEEEEALEEAAEEEAELE---EEEEALLELLAELLEEAALL 475
|
170 180 190
....*....|....*....|....*....|....*.
gi 1937933965 784 RLESARLRFLLEDQKCIQEMLRDMEAHQPQEPLSVL 819
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
629-811 |
1.22e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 629 EELKEIEKdcAVYVGRMERV-ARYSSISKEEKELRMEIAKQEL--------IVHAREAASRVLSELSDRQMSEQIAL--- 696
Cdd:COG1196 220 EELKELEA--ELLLLKLRELeAELEELEAELEELEAELEELEAelaeleaeLEELRLELEELELELEEAQAEEYELLael 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 697 -DTRKREQFQRLKEQFVKDQERRLAARQEELGDDfsyAHELRAREKRLKALEEELERKARQALVDHYSKLSAEAARREQK 775
Cdd:COG1196 298 aRLEQDIARLEERRRELEERLEELEEELAELEEE---LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
|
170 180 190
....*....|....*....|....*....|....*.
gi 1937933965 776 ALWRIRRHRLESARLRFLLEDQKCIQEMLRDMEAHQ 811
Cdd:COG1196 375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
676-815 |
1.43e-06 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 49.65 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 676 EAASRVLSElSDRQMSEQIALDTRKREQFQRLKEQFVKDQERRLA---ARQEElgddfsyahELRAREKRLKALEEELER 752
Cdd:pfam05672 10 EEAARILAE-KRRQAREQREREEQERLEKEEEERLRKEELRRRAEeerARREE---------EARRLEEERRREEEERQR 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937933965 753 KARQAlvdhysklSAEAARREQKALWRIRRHRLES-ARLRfllEDQKciqEMLRDMEAHQPQEP 815
Cdd:pfam05672 80 KAEEE--------AEEREQREQEEQERLQKQKEEAeAKAR---EEAE---RQRQEREKIMQQEE 129
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
623-816 |
3.65e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 623 SVIFSLE----ELKEIEKDCAVYVGRMERVArySSISKEEKEL-----RMEIAKQELiVHAREAASRVLSELSDRQmsEQ 693
Cdd:COG4372 35 KALFELDklqeELEQLREELEQAREELEQLE--EELEQARSELeqleeELEELNEQL-QAAQAELAQAQEELESLQ--EE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 694 IaldTRKREQFQRLKEQ--FVKDQERRLAARQEELgddfsyAHELRAREKRLKALEEELERKARQ--ALVDHYSKLSAEA 769
Cdd:COG4372 110 A---EELQEELEELQKErqDLEQQRKQLEAQIAEL------QSEIAEREEELKELEEQLESLQEElaALEQELQALSEAE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1937933965 770 ArreQKALWRIRRHRLESARLRFLLEDQKCIQEMLRDMEAHQPQEPL 816
Cdd:COG4372 181 A---EQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
629-814 |
7.97e-06 |
|
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: 51.21 E-value: 7.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 629 EELKEIEKdcAVYVGRMER-VARYSSISKEEKELRMEIAKQELIVHAREAASRVLsELSDRQMSEQIA------------ 695
Cdd:TIGR02168 220 AELRELEL--ALLVLRLEElREELEELQEELKEAEEELEELTAELQELEEKLEEL-RLEVSELEEEIEelqkelyalane 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 696 ---LDTRKREQFQRLK----------EQFVKDQERR------LAARQEELGDDFSYAHELRAREKRLKALEEELERKARQ 756
Cdd:TIGR02168 297 isrLEQQKQILRERLAnlerqleeleAQLEELESKLdelaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937933965 757 ALVDHYSKLSAEAARREQKALWRIRRHRLES------ARLRFLLEDqkcIQEMLRDMEAHQPQE 814
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEArlerleDRRERLQQE---IEELLKKLEEAELKE 437
|
|
| DUF4573 |
pfam15140 |
Domain of unknown function (DUF4573); This family of proteins is found in eukaryotes. Proteins ... |
1044-1199 |
1.57e-05 |
|
Domain of unknown function (DUF4573); This family of proteins is found in eukaryotes. Proteins in this family are typically approximately 360 amino acids in length.
Pssm-ID: 434493 [Multi-domain] Cd Length: 176 Bit Score: 47.13 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 1044 NIKVGDYMSDVALPRPRWNIHGHVSEANIGVGENVSDVAPSRPRWNVHGHVSDASIKVGENVSDVAPSRPRWNVHGHVSD 1123
Cdd:pfam15140 10 EIQPLKGVREIEPPQPGGKDDPLGAEEKKKDLRAVTEVEPLKGVAEIEPLGPVSEIQPLRAVSERDPLGAVEEIEPPQAA 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937933965 1124 ASIKVGENVSEVAPSRPRWNVHGHvsdasikvgENVSDVAPSRPRWNVHGHVSDASIKVGENVSDVAPSRPRWNVH 1199
Cdd:pfam15140 90 SEMKPLGTAENILPLEAAREIHPL---------EAVGKIEPLQLVETIPKENESPEIHPLEGSQEIEPLEPVQLIE 156
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
629-808 |
3.26e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 629 EELKEIEKDCAVYVGRMERVARYSSISKEEKELRMEIAKQELIVHAREAASRVLSELSDRQMSEQI-ALDTRKREQFQRL 707
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIkAEELKKAEEEKKK 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 708 KEQF-------------VKDQERRLAARQEELG----DDFSYAHELRAREKRLKALEEELERKARQAL-VDHYSKLSAEA 769
Cdd:PTZ00121 1635 VEQLkkkeaeekkkaeeLKKAEEENKIKAAEEAkkaeEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkAEELKKKEAEE 1714
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1937933965 770 ARR--EQKALWRIRRHRLESARlRFLLEDQKCIQEMLRDME 808
Cdd:PTZ00121 1715 KKKaeELKKAEEENKIKAEEAK-KEAEEDKKKAEEAKKDEE 1754
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
629-784 |
5.31e-05 |
|
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: 46.46 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 629 EELKEIEKDCAVYVGRMERV-ARYSSIS--KEEKELRMEIAKQElivhareaasRVLSELSDRQMSEQIALDTrKREQFQ 705
Cdd:COG1579 59 KEIKRLELEIEEVEARIKKYeEQLGNVRnnKEYEALQKEIESLK----------RRISDLEDEILELMERIEE-LEEELA 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937933965 706 RLKEQfVKDQERRLAARQEELGDDFSyahELRAREKRLKALEEELERKARQALVDHYSKLsaeAARREQKALWRIRRHR 784
Cdd:COG1579 128 ELEAE-LAELEAELEEKKAELDEELA---ELEAELEELEAEREELAAKIPPELLALYERI---RKRKNGLAVVPVEGGA 199
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
629-806 |
6.69e-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: 48.13 E-value: 6.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 629 EELKEIEKDCAVYVGRMErvarysSISKEEKELRMEIAKQELIVHAREAASRVLSELSDrQMSEQIALdtrKREQFQRLK 708
Cdd:TIGR02168 337 EELAELEEKLEELKEELE------SLEAELEELEAELEELESRLEELEEQLETLRSKVA-QLELQIAS---LNNEIERLE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 709 EQfVKDQERRLAARQEELGDDFSYAHELRARE--KRLKALEEELErKARQALVDHYSKLSAEAARREQkALWRIRRHRLE 786
Cdd:TIGR02168 407 AR-LERLEDRRERLQQEIEELLKKLEEAELKElqAELEELEEELE-ELQEELERLEEALEELREELEE-AEQALDAAERE 483
|
170 180
....*....|....*....|
gi 1937933965 787 SARLRFLLEDQKCIQEMLRD 806
Cdd:TIGR02168 484 LAQLQARLDSLERLQENLEG 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
656-811 |
8.26e-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: 47.74 E-value: 8.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 656 KEEKELRMEiakqelivHAREAASRV---LSELsDRQMsEQIALDTRKREQFQRLKEQF-----------VKDQERRLAA 721
Cdd:TIGR02168 174 RKETERKLE--------RTRENLDRLediLNEL-ERQL-KSLERQAEKAERYKELKAELrelelallvlrLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 722 RQEELGDdfsYAHELRAREKRLKALEEELE--RKARQAL---VDHYSK----LSAEAARREQkalwRIRRHRlesARLRF 792
Cdd:TIGR02168 244 LQEELKE---AEEELEELTAELQELEEKLEelRLEVSELeeeIEELQKelyaLANEISRLEQ----QKQILR---ERLAN 313
|
170
....*....|....*....
gi 1937933965 793 LLEDQKCIQEMLRDMEAHQ 811
Cdd:TIGR02168 314 LERQLEELEAQLEELESKL 332
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
628-817 |
9.95e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 628 LEELKEIEKDCAVYvgrMERVARYSSISKEEKELRMEIakqelivharEAASRVLSELsdRQMSEQIALDTRKREQFQRL 707
Cdd:COG4717 70 LKELKELEEELKEA---EEKEEEYAELQEELEELEEEL----------EELEAELEEL--REELEKLEKLLQLLPLYQEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 708 KEQfvkdqERRLAARQEELGDDFSYAHELRAREKRLKALEEELERkARQALVDHYSKLSAEAARREQKALWRIRRHRLES 787
Cdd:COG4717 135 EAL-----EAELAELPERLEELEERLEELRELEEELEELEAELAE-LQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190
....*....|....*....|....*....|....*...
gi 1937933965 788 ARLRFLLED--------QKCIQEMLRDMEAHQPQEPLS 817
Cdd:COG4717 209 AELEEELEEaqeeleelEEELEQLENELEAAALEERLK 246
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
668-796 |
1.07e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.78 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 668 QELIVHAREAASRVLSELSDRqmseqiaLDTRKREQFQRLKEqfvKDQERrlAARQEELGddfsyahelRAREKRLKALE 747
Cdd:pfam02029 236 REEEAEVFLEAEQKLEELRRR-------RQEKESEEFEKLRQ---KQQEA--ELELEELK---------KKREERRKLLE 294
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1937933965 748 EElERKARQAlvDHYSKLSAEAARREQKAlwRIRRHRLESARLR-FLLED 796
Cdd:pfam02029 295 EE-EQRRKQE--EAERKLREEEEKRRMKE--EIERRRAEAAEKRqKLPED 339
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
655-814 |
1.29e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 655 SKEEKELRmeiAKQELIVHAREAASRVLSELSDRQMSEQIALDTRKR--EQFQRLKEQFVKDQERR--LAARQEELGDdf 730
Cdd:pfam01576 1 TRQEEEMQ---AKEEELQKVKERQQKAESELKELEKKHQQLCEEKNAlqEQLQAETELCAEAEEMRarLAARKQELEE-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 731 sYAHELRARekrlkaLEEELER---------KARQALVDHYSKLSAEAARREQKALWRI----RRHRLESARLrfLLEDQ 797
Cdd:pfam01576 76 -ILHELESR------LEEEEERsqqlqnekkKMQQHIQDLEEQLDEEEAARQKLQLEKVtteaKIKKLEEDIL--LLEDQ 146
|
170 180
....*....|....*....|....*
gi 1937933965 798 --------KCIQEMLRDMEAHQPQE 814
Cdd:pfam01576 147 nsklskerKLLEERISEFTSNLAEE 171
|
|
| FliJ |
COG2882 |
Flagellar biosynthesis chaperone FliJ [Cell motility]; |
644-777 |
1.50e-04 |
|
Flagellar biosynthesis chaperone FliJ [Cell motility];
Pssm-ID: 442129 [Multi-domain] Cd Length: 142 Bit Score: 43.74 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 644 RMERVARYssisKEEKElrmEIAKQEL--IVHAREAASRVLSELSD--RQMSEQI---------ALDTRKREQF-QRLKE 709
Cdd:COG2882 6 RLQTLLDL----AEKEE---DEAARELgqAQQALEQAEEQLEQLEQyrEEYEQRLqqklqqglsAAQLRNYQQFiARLDE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937933965 710 ------QFVKDQERRLAARQEELgddfsyahelRAREKRLKALEEELERKARQALVdhysklsaEAARREQKAL 777
Cdd:COG2882 79 aieqqqQQVAQAEQQVEQARQAW----------LEARQERKALEKLKERRREEERQ--------EENRREQKEL 134
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
646-805 |
1.72e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 45.80 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 646 ERVARYSSISKEEKELRMEIAKQELIvhaREAASRVLSELSDRQMSEQIAL-----DTRKREQFQRLKE-----QFVKDQ 715
Cdd:pfam15558 66 EKEQRKARLGREERRRADRREKQVIE---KESRWREQAEDQENQRQEKLERarqeaEQRKQCQEQRLKEkeeelQALREQ 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 716 ERRLAARQEELGDDFSYAHELRA-REKRLKALEEELERKARQALVDHYSKlSAEAARR---EQKALWRIRRH-RLESARL 790
Cdd:pfam15558 143 NSLQLQERLEEACHKRQLKEREEqKKVQENNLSELLNHQARKVLVDCQAK-AEELLRRlslEQSLQRSQENYeQLVEERH 221
|
170
....*....|....*
gi 1937933965 791 RFLLEDQKCIQEMLR 805
Cdd:pfam15558 222 RELREKAQKEEEQFQ 236
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
663-798 |
1.93e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 663 MEIAKQELIVHAREAASRVLSELSDRQMSEQIALDTRKREQFQRLKEQfVKDQERRLAARQEELgddFSYAHELRAREKR 742
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREE-LEQAREELEQLEEEL---EQARSELEQLEEE 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937933965 743 LKALEEELErKARQALVDHYSKLsaEAARREQKALWRiRRHRLESARLRflLEDQK 798
Cdd:COG4372 82 LEELNEQLQ-AAQAELAQAQEEL--ESLQEEAEELQE-ELEELQKERQD--LEQQR 131
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
658-789 |
3.59e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 45.59 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 658 EKELRmeiakqelivHAREAASRVLSELSDRQMSEQIALDTRKREQFQRLkeqfvkDQErrLAARQE----ELGDDFSYA 733
Cdd:NF041483 93 ERELR----------DARAQTQRILQEHAEHQARLQAELHTEAVQRRQQL------DQE--LAERRQtvesHVNENVAWA 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937933965 734 HELRAR-EKRLKALEEELERKARQALvdhySKLSAEAARREQKAlwrirRHRL----ESAR 789
Cdd:NF041483 155 EQLRARtESQARRLLDESRAEAEQAL----AAARAEAERLAEEA-----RQRLgseaESAR 206
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
700-809 |
3.64e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 43.90 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 700 KREQFQRLKEQFVKDQERRLAARQEELGDDFSYAHELRAREKRLKALEEELERKARQALVDHYSKLSAEAARREQKALWR 779
Cdd:pfam04012 19 KAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEELAREALAEKKSLEKQ 98
|
90 100 110
....*....|....*....|....*....|
gi 1937933965 780 IRRHRLESARLRFLLEDqkcIQEMLRDMEA 809
Cdd:pfam04012 99 AEALETQLAQQRSAVEQ---LRKQLAALET 125
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
630-811 |
3.97e-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: 3.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 630 ELKEIEKDCAVYVGRMERVA-RYSSISKEEKELRMEIAKQELIVH----AREAASRVLSELSDR--QMSEQIALDTR--- 699
Cdd:TIGR02168 727 QISALRKDLARLEAEVEQLEeRIAQLSKELTELEAEIEELEERLEeaeeELAEAEAEIEELEAQieQLKEELKALREald 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 700 -KREQFQRLKEQF------VKDQERRLAARQEELGDdfsYAHELRAREKRLKALEEELE------RKARQALVDHY-SKL 765
Cdd:TIGR02168 807 eLRAELTLLNEEAanlrerLESLERRIAATERRLED---LEEQIEELSEDIESLAAEIEeleeliEELESELEALLnERA 883
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937933965 766 SAEAARREQKALWRIRRHRLESARLRFLLEDQKCI--QEMLRDMEAHQ 811
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEelREKLAQLELRL 931
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
629-813 |
4.73e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 629 EELKEIEKDCAvyvgRMERVARYSSISKEEKELRMEIAK-----QELI--VHAREAASRVLSELSDR---QMSEQIAL-- 696
Cdd:pfam13868 36 AEEKEEERRLD----EMMEEERERALEEEEEKEEERKEErkryrQELEeqIEEREQKRQEEYEEKLQereQMDEIVERiq 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 697 --DTRKREQFQRLKEQFVKD--------QERRLAARQEELGDD---FSYAHELRAREKRLKALEEELERKA---RQALVD 760
Cdd:pfam13868 112 eeDQAEAEEKLEKQRQLREEidefneeqAEWKELEKEEEREEDeriLEYLKEKAEREEEREAEREEIEEEKereIARLRA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1937933965 761 HYSKLSAEAARREQKALWRIRRHRLESARLRFLLEDQKCIQEMLRDMEAHQPQ 813
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQ 244
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
688-775 |
4.79e-04 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 41.78 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 688 RQMSE-QIALDTrKREQFQRLKEQFvKDQERRLAARQEELGDD------FSYAHELRAREKRLKALEEELERKARQA--- 757
Cdd:pfam13863 6 REMFLvQLALDA-KREEIERLEELL-KQREEELEKKEQELKEDlikfdkFLKENDAKRRRALKKAEEETKLKKEKEKeik 83
|
90
....*....|....*....
gi 1937933965 758 -LVDHYSKLSAEAARREQK 775
Cdd:pfam13863 84 kLTAQIEELKSEISKLEEK 102
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
665-806 |
4.85e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 665 IAKQELIVHAREAASRVLSELSDR--QMSEQIALDTRKREQFQRLKEQF-----VKDQERRLAARQEEL------GDDFS 731
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERleALEAELDALQERREALQRLAEYSwdeidVASAEREIAELEAELerldasSDDLA 688
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937933965 732 YA-HELRAREKRLKALEEELERKARQAlvdhySKLSAE--AARREQKALwrirRHRLESARLRFLLEDQKCIQEMLRD 806
Cdd:COG4913 689 ALeEQLEELEAELEELEEELDELKGEI-----GRLEKEleQAEEELDEL----QDRLEAAEDLARLELRALLEERFAA 757
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
627-808 |
5.34e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 627 SLEELKEIEKdcavyvgRMERVARYSSiSKEEKELRMEIAKQELivharEAASRVLSELSD--RQMSEQIALDTRKREQF 704
Cdd:PRK03918 167 LGEVIKEIKR-------RIERLEKFIK-RTENIEELIKEKEKEL-----EEVLREINEISSelPELREELEKLEKEVKEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 705 QRLKEQFVKdQERRLAARQEELGddfSYAHELRAREKRLKALE---EELERKAR-----QALVDHYSKLSAEAARREQKa 776
Cdd:PRK03918 234 EELKEEIEE-LEKELESLEGSKR---KLEEKIRELEERIEELKkeiEELEEKVKelkelKEKAEEYIKLSEFYEEYLDE- 308
|
170 180 190
....*....|....*....|....*....|..
gi 1937933965 777 lwrIRRHRLESARLRFLLEDqkcIQEMLRDME 808
Cdd:PRK03918 309 ---LREIEKRLSRLEEEING---IEERIKELE 334
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
646-758 |
5.50e-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: 5.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 646 ERVARYSSISKEEKELRMEIAKQELIVHAREAASRVLSELSDRQMSEQIALDTRKREQFQRLKEQFVKDQERRLAARQEE 725
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
90 100 110
....*....|....*....|....*....|....*
gi 1937933965 726 LGDDFSYAHELRAREKRLKALEEELER--KARQAL 758
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERleREIEAL 779
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
654-803 |
6.19e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 44.56 E-value: 6.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 654 ISKEEKE------LRMEIAKQELIVHAR-----EAASRVLSELSDR--QMSEQIALDTRKREQFQRLKEQFVKDQERrla 720
Cdd:pfam15709 325 LEKREQEkasrdrLRAERAEMRRLEVERkrreqEEQRRLQQEQLERaeKMREELELEQQRRFEEIRLRKQRLEEERQ--- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 721 aRQEElgddfsyahelrarEKRLKALEEELER-KARQALVDHYSKLSAEAARREQKALWRI-----RRHRLESArlrfLL 794
Cdd:pfam15709 402 -RQEE--------------EERKQRLQLQAAQeRARQQQEEFRRKLQELQRKKQQEEAERAeaekqRQKELEMQ----LA 462
|
....*....
gi 1937933965 795 EDQKCIQEM 803
Cdd:pfam15709 463 EEQKRLMEM 471
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
674-809 |
6.26e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.82 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 674 AREAASRVLSElSDRQMSEQIALDTRKREQFQRLKEQFVKDQERRLAARQEELGDDFSYAHElrAREKRLKALEEELeRK 753
Cdd:NF041483 522 AEETLERTRAE-AERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHT--EAEERLTAAEEAL-AD 597
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937933965 754 ARqalvdhysklsAEAARREQKALWRIRRHRLESA-RLRFLLEDQKCIQEMLRDMEA 809
Cdd:NF041483 598 AR-----------AEAERIRREAAEETERLRTEAAeRIRTLQAQAEQEAERLRTEAA 643
|
|
| DUF4573 |
pfam15140 |
Domain of unknown function (DUF4573); This family of proteins is found in eukaryotes. Proteins ... |
1057-1235 |
7.04e-04 |
|
Domain of unknown function (DUF4573); This family of proteins is found in eukaryotes. Proteins in this family are typically approximately 360 amino acids in length.
Pssm-ID: 434493 [Multi-domain] Cd Length: 176 Bit Score: 42.50 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 1057 PRPRWNIHGhvseanigvGENVSDVAPSRPRWNVHGHVSDASIKVGENVSDVAPSRPRWNVHGHVSDASIKVGENVSEVA 1136
Cdd:pfam15140 5 SRPTSEIQP---------LKGVREIEPPQPGGKDDPLGAEEKKKDLRAVTEVEPLKGVAEIEPLGPVSEIQPLRAVSERD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 1137 PSRPRWNVHGHVSDASIKVGENVSDVAPSRPRWNVHGHvsdasikvgENVSDVAPSRPRWNVHGHVSEASIRIGENVSDV 1216
Cdd:pfam15140 76 PLGAVEEIEPPQAASEMKPLGTAENILPLEAAREIHPL---------EAVGKIEPLQLVETIPKENESPEIHPLEGSQEI 146
|
170 180
....*....|....*....|
gi 1937933965 1217 D-LQPHGHVQPPLILEEPFP 1235
Cdd:pfam15140 147 EpLEPVQLIEPLGEVEQIQP 166
|
|
| Lon |
COG0466 |
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ... |
648-770 |
7.74e-04 |
|
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440234 [Multi-domain] Cd Length: 785 Bit Score: 44.24 E-value: 7.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 648 VARYSSISKEEKelrmeiakQEL--IVHAREAASRVLSELSDR----QMSEQIALDTRKR-EQFQR---LKEQfvkdqer 717
Cdd:COG0466 172 IASHLPLKIEEK--------QELleTLDVKERLEKLLELLEKEievlELEKKIRSRVKEQmEKSQReyyLREQ------- 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937933965 718 rLAARQEELGDDFSYAHELRAREKRLKALE--EELERKARQALvDHYSKL---SAEAA 770
Cdd:COG0466 237 -LKAIQKELGEKDDGEDEIEELREKIEKAKlpEEVKEKAEKEL-KKLERMppmSAEAT 292
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
618-811 |
9.00e-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: 44.28 E-value: 9.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 618 PVPRISVIFSLE-ELKEIEKDCAvyvgRMErvARYSSISKEEKELRmeiAKQELIVHAREAASRVLSELSDRQMSEQIAL 696
Cdd:TIGR02168 665 SAKTNSSILERRrEIEELEEKIE----ELE--EKIAELEKALAELR---KELEELEEELEQLRKELEELSRQISALRKDL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 697 DTRKREQFQRLKEQFVKDQER-RLAARQEELGDDFSYAH-ELRAREKRLKALEEELER--KARQALVDHYSKLSAEAAR- 771
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELtELEAEIEELEERLEEAEeELAEAEAEIEELEAQIEQlkEELKALREALDELRAELTLl 815
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1937933965 772 --REQKALWRIRRHRLESARLRFLLEDqkcIQEMLRDMEAHQ 811
Cdd:TIGR02168 816 neEAANLRERLESLERRIAATERRLED---LEEQIEELSEDI 854
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
674-787 |
1.35e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.80 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 674 AREAASRVLSElsdrqmSEQIAlDTRKRE-------QFQRLKEQFVKD-QERRlaarqeelgddfsyaHELRAREKRLKA 745
Cdd:pfam12072 32 AEELAKRIIEE------AKKEA-ETKKKEalleakeEIHKLRAEAERElKERR---------------NELQRQERRLLQ 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1937933965 746 LEEELERK------ARQALVDHYSKLSAEAARREQK-----ALWRIRRHRLES 787
Cdd:pfam12072 90 KEETLDRKdeslekKEESLEKKEKELEAQQQQLEEKeeeleELIEEQRQELER 142
|
|
| FliJ |
pfam02050 |
Flagellar FliJ protein; |
657-777 |
1.40e-03 |
|
Flagellar FliJ protein;
Pssm-ID: 426581 [Multi-domain] Cd Length: 123 Bit Score: 40.34 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 657 EEKELRMEIAKQEL--IVHAREAASRVLSELSDRQMSEQIALDTRKREQFQRLKEQF----------VKDQERRLAARQE 724
Cdd:pfam02050 1 DEAARELAEAQRELqqAEEKLEELQQYRAEYQQQLSGAGQGISAAELRNYQAFISQLdeaiaqqqqeLAQAEAQVEKARE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1937933965 725 ELgddfsyaHELRAREKRLKALEEELERKARQALvdhysklsaeaARREQKAL 777
Cdd:pfam02050 81 EW-------QEARQERKSLEKLREREKKEERKEQ-----------NRREQKQL 115
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
619-757 |
1.80e-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: 42.83 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 619 VPRISVIFSLEELKEIEKDcAVYvgrMERVARYssISKEEKELRMEIAKQELIVHAREAASRVLSELSDRQMSEQIALDT 698
Cdd:COG4942 119 QPPLALLLSPEDFLDAVRR-LQY---LKYLAPA--RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937933965 699 RKREQfqrlkEQFVKDQERRLAARQEELGddfsyahELRAREKRLKALEEELERKARQA 757
Cdd:COG4942 193 LKAER-----QKLLARLEKELAELAAELA-------ELQQEAEELEALIARLEAEAAAA 239
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
656-811 |
1.98e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 42.72 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 656 KEEKELRMEIAKQELIVHAR--EAASRVLSELSDRQMS-EQIALdtRKREQFQRLKEQfvKDQERRLAARQEELgddfsy 732
Cdd:pfam15558 164 EEQKKVQENNLSELLNHQARkvLVDCQAKAEELLRRLSlEQSLQ--RSQENYEQLVEE--RHRELREKAQKEEE------ 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 733 aHELRARE----------KRLKALEEELERKARQALvDHYSKLSAEAARR--EQKALwRIRRHRL--------ESARLRF 792
Cdd:pfam15558 234 -QFQRAKWraeekeeerqEHKEALAELADRKIQQAR-QVAHKTVQDKAQRarELNLE-REKNHHIlklkvekeEKCHREG 310
|
170 180
....*....|....*....|....
gi 1937933965 793 LLE-----DQKcIQEMLRDMEAHQ 811
Cdd:pfam15558 311 IKEaikkkEQR-SEQISREKEATL 333
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
629-772 |
2.34e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 42.54 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 629 EELKEIEKdcavyvgRMERVARYSSiskEEKELRMEIAKQELIVHAREAasrvlsELSDRQMSEQIALdtRKREQFQRLK 708
Cdd:COG2433 410 EEEEEIRR-------LEEQVERLEA---EVEELEAELEEKDERIERLER------ELSEARSEERREI--RKDREISRLD 471
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937933965 709 EQfVKDQERRLAARQEELgddfsyaHELRAREKRLKALeEELERKARQALVDHYSKLSAEAARR 772
Cdd:COG2433 472 RE-IERLERELEEERERI-------EELKRKLERLKEL-WKLEHSGELVPVKVVEKFTKEAIRR 526
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
614-795 |
2.83e-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: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 614 WSDVPVPRISVIFSLEELKEIEKDCAVYVGRmERVARYSSISKEEKELRMEIAKQELIVHAREAASRVLSELSDRQMSEQ 693
Cdd:COG1196 610 EADARYYVLGDTLLGRTLVAARLEAALRRAV-TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERL 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 694 IALDTRKREQFQRLKEQFVKDQERRLAARQEELGDDFSYAHELRAREKRLKALEEELERKARQALVDHYSKLSAEAARRE 773
Cdd:COG1196 689 AEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
170 180 190
....*....|....*....|....*....|....*
gi 1937933965 774 QKALwRIRRHRLE-------------SARLRFLLE 795
Cdd:COG1196 769 LERL-EREIEALGpvnllaieeyeelEERYDFLSE 802
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
630-756 |
3.48e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 630 ELKEIEKdcavyvgRMERVARYSSISKEEKELRMEiAKQELIVHAREAASRVLselsdRQMSEQIALDT-------RKRE 702
Cdd:pfam13868 223 EREEAEK-------KARQRQELQQAREEQIELKER-RLAEEAEREEEEFERML-----RKQAEDEEIEQeeaekrrMKRL 289
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1937933965 703 QFQRLKEQFVKDQER-RLAARQEELgDDFsyAHELRAREKRLKALEEELERKARQ 756
Cdd:pfam13868 290 EHRRELEKQIEEREEqRAAEREEEL-EEG--ERLREEEAERRERIEEERQKKLKE 341
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
699-809 |
3.82e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 699 RKREQFQRLKEQFVKDQERRLAARQEELGDDFSYAHELRAREKRLKALEEELE--RKARQALVDHYSKLSAEAARREQKA 776
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEelEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110
....*....|....*....|....*....|....*
gi 1937933965 777 LWRIRRHRLES--ARLRFLLEDQKCIQEMLRDMEA 809
Cdd:COG4717 133 ELEALEAELAElpERLEELEERLEELRELEEELEE 167
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
628-758 |
4.12e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 628 LEELKEIEKDCAVYvgrMERVARYSSISKEEKELRMEIakQELivhAREAasrvlSELSDrQMSEQIaldtRKREQFQR- 706
Cdd:COG1340 149 LEKAKKALEKNEKL---KELRAELKELRKEAEEIHKKI--KEL---AEEA-----QELHE-EMIELY----KEADELRKe 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937933965 707 ---LKEQFVKDQER------RLAARQEELGDdfsYAHELRAREKRLKAL-----EEELERKARQAL 758
Cdd:COG1340 211 adeLHKEIVEAQEKadelheEIIELQKELRE---LRKELKKLRKKQRALkrekeKEELEEKAEEIF 273
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
625-777 |
4.70e-03 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 39.22 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 625 IFSLE---ELKEIEKDcavyvgrmERVARYSSISKEEKELRMEIakQELIVHAREAASRVLSElsdrQMSEQIALDTRKR 701
Cdd:TIGR02473 1 EFRLQkllDLREKEEE--------QAKLELAKAQAEFERLETQL--QQLIKYREEYEQQALEK----VGAGTSALELSNY 66
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937933965 702 EQFQRLKEQFVKDQERRLAARQEELGDdfsyAHE-LRAREKRLKALEEELERKARQALvdhysklsAEAARREQKAL 777
Cdd:TIGR02473 67 QRFIRQLDQRIQQQQQELALLQQEVEA----KRErLLEARRELKALEKLKEKKQKEYR--------AEEAKREQKEM 131
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
643-798 |
5.12e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 41.62 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 643 GRMERVARYSSISKEEKELRMEIAKQElIVHAREAASRVLSELSDRQMSEQIALDTRKREQFQRLkeqfvkdqERRLAAR 722
Cdd:PRK12705 19 GVLVVLLKKRQRLAKEAERILQEAQKE-AEEKLEAALLEAKELLLRERNQQRQEARREREELQRE--------EERLVQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937933965 723 QEELGddfsyahelrAREKRLKALEEELErKARQALVDHYSKLSAEAARREQKaLWRIRRHRLESAR------LRFLLED 796
Cdd:PRK12705 90 EEQLD----------ARAEKLDNLENQLE-EREKALSARELELEELEKQLDNE-LYRVAGLTPEQARklllklLDAELEE 157
|
..
gi 1937933965 797 QK 798
Cdd:PRK12705 158 EK 159
|
|
| |
