|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
564-891 |
0e+00 |
|
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276817 [Multi-domain] Cd Length: 329 Bit Score: 539.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 564 KGNIRVLCRVRPVCAGEAdaADTKNLVTFDPEDDAVLYLSNKG-KLMTFELDKVFTTQATQEEVFQEVQSLVTSCIDGFN 642
Cdd:cd01366 1 KGNIRVFCRVRPLLPSEE--NEDTSHITFPDEDGQTIELTSIGaKQKEFSFDKVFDPEASQEDVFEEVSPLVQSALDGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 643 VCIFAYGQTGSGKTYTMEGIPEDPGINQRALRLLFSEVSE-KKPDWDYKITVSMVEIYNETLRNLLGDN--PNEKLDIKM 719
Cdd:cd01366 79 VCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKElKEKGWSYTIKASMLEIYNETIRDLLAPGnaPQKKLEIRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 720 CPDgSGQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITVAGFNSSTGHRTSGKLNLVDLAGS 799
Cdd:cd01366 159 DSE-KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVGKLNLVDLAGS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 800 ERIAKSGAEGSRLREAQCINKSLSALGDVINSLRSKHSHVPFRNSRLTYLLQDSLSGDSKTLMMVQVSPLESNISESVCS 879
Cdd:cd01366 238 ERLNKSGATGDRLKETQAINKSLSALGDVISALRQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNLNETLNS 317
|
330
....*....|..
gi 688598103 880 LKFAQRVRTVEI 891
Cdd:cd01366 318 LRFASKVNSCEL 329
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
566-895 |
1.79e-150 |
|
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play important roles in intracellular transport of organelles and in cell division.
Pssm-ID: 214526 [Multi-domain] Cd Length: 335 Bit Score: 448.94 E-value: 1.79e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 566 NIRVLCRVRPVCAGEADAaDTKNLVTFDPEDDA---VLYLSNKGKLMTFELDKVFTTQATQEEVFQEV-QSLVTSCIDGF 641
Cdd:smart00129 1 NIRVVVRVRPLNKREKSR-KSPSVVPFPDKVGKtltVRSPKNRQGEKKFTFDKVFDATASQEDVFEETaAPLVDSVLEGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 642 NVCIFAYGQTGSGKTYTMEGIPEDPGINQRALRLLFSEVSEKKPDWDYKITVSMVEIYNETLRNLLGDNPNeKLDIKMcp 721
Cdd:smart00129 80 NATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGWQFSVKVSYLEIYNEKIRDLLNPSSK-KLEIRE-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 722 DGSGQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITV--AGFNSSTGHRTSGKLNLVDLAGS 799
Cdd:smart00129 157 DEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVeqKIKNSSSGSGKASKLNLVDLAGS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 800 ERIAKSGAEGSRLREAQCINKSLSALGDVINSLR--SKHSHVPFRNSRLTYLLQDSLSGDSKTLMMVQVSPLESNISESV 877
Cdd:smart00129 237 ERAKKTGAEGDRLKEAGNINKSLSALGNVINALAqhSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSNLEETL 316
|
330
....*....|....*...
gi 688598103 878 CSLKFAQRVRTVEIGPSS 895
Cdd:smart00129 317 STLRFASRAKEIKNKPIV 334
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
572-889 |
8.64e-139 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 418.13 E-value: 8.64e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 572 RVRPVCAGEADAADTKNLVTFDPEDDAVLY--LSNKGKLMTFELDKVFTTQATQEEVFQE-VQSLVTSCIDGFNVCIFAY 648
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVESshLTNKNRTKTFTFDKVFDPEATQEDVYEEtAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 649 GQTGSGKTYTMEGIPEDPGINQRALRLLFSEVSEKKPDWDYKITVSMVEIYNETLRNLLGDNPNEKLDIKMCPDGSGQLY 728
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIREDPKKGVY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 729 VPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITVAGFNSSTG---HRTSGKLNLVDLAGSERIAKS 805
Cdd:pfam00225 161 VKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGgeeSVKTGKLNLVDLAGSERASKT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 806 G-AEGSRLREAQCINKSLSALGDVINSLRSKHS-HVPFRNSRLTYLLQDSLSGDSKTLMMVQVSPLESNISESVCSLKFA 883
Cdd:pfam00225 241 GaAGGQRLKEAANINKSLSALGNVISALADKKSkHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEETLSTLRFA 320
|
....*.
gi 688598103 884 QRVRTV 889
Cdd:pfam00225 321 SRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
566-887 |
3.84e-122 |
|
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276812 [Multi-domain] Cd Length: 326 Bit Score: 375.05 E-value: 3.84e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 566 NIRVLCRVRPvcAGEADAADTKNLVTFDPEDDAVLYLSNKGKLM--TFELDKVFTTQATQEEVFQEV-QSLVTSCIDGFN 642
Cdd:cd00106 1 NVRVAVRVRP--LNGREARSAKSVISVDGGKSVVLDPPKNRVAPpkTFAFDAVFDSTSTQEEVYEGTaKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 643 VCIFAYGQTGSGKTYTMEGI-PEDPGINQRALRLLFSEVSE-KKPDWDYKITVSMVEIYNETLRNLLGDNPNEKLDIKMc 720
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKrKETKSSFSVSASYLEIYNEKIYDLLSPVPKKPLSLRE- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 721 pDGSGQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITVAGFNSST--GHRTSGKLNLVDLAG 798
Cdd:cd00106 158 -DPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKsgESVTSSKLNLVDLAG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 799 SERIAKSGAEGSRLREAQCINKSLSALGDVINSLRSKHS-HVPFRNSRLTYLLQDSLSGDSKTLMMVQVSPLESNISESV 877
Cdd:cd00106 237 SERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNkHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSENFEETL 316
|
330
....*....|
gi 688598103 878 CSLKFAQRVR 887
Cdd:cd00106 317 STLRFASRAK 326
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
567-890 |
4.24e-99 |
|
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members of this group seem to perform a variety of functions, and have been implicated in neuronal organelle transport and chromosome segregation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276823 [Multi-domain] Cd Length: 341 Bit Score: 315.04 E-value: 4.24e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 567 IRVLCRVRPVCAGEADAADtKNLVTFDPEDDAVLYLSNKgklmTFELDKVFTTQATQEEVFQE-VQSLVTSCIDGFNVCI 645
Cdd:cd01372 3 VRVAVRVRPLLPKEIIEGC-RICVSFVPGEPQVTVGTDK----SFTFDYVFDPSTEQEEVYNTcVAPLVDGLFEGYNATV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 646 FAYGQTGSGKTYTMEG-----IPEDP-GINQRALRLLFSEVSEKKPDWDYKITVSMVEIYNETLRNLLGDNPNEKLDIKM 719
Cdd:cd01372 78 LAYGQTGSGKTYTMGTaytaeEDEEQvGIIPRAIQHIFKKIEKKKDTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTISI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 720 CPDGSGQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITV--------AGFNSSTGHR--TSG 789
Cdd:cd01372 158 REDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLeqtkkngpIAPMSADDKNstFTS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 790 KLNLVDLAGSERIAKSGAEGSRLREAQCINKSLSALGDVINSL---RSKHSHVPFRNSRLTYLLQDSLSGDSKTLMMVQV 866
Cdd:cd01372 238 KFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALgdeSKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACV 317
|
330 340
....*....|....*....|....
gi 688598103 867 SPLESNISESVCSLKFAQRVRTVE 890
Cdd:cd01372 318 SPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
566-889 |
4.56e-98 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 311.70 E-value: 4.56e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 566 NIRVLCRVRPVCAGEAdAADTKNLVTFDPEDDAVLYLSNKGKL----MTFELDKVFTTQATQEEVFQE-VQSLVTSCIDG 640
Cdd:cd01371 2 NVKVVVRCRPLNGKEK-AAGALQIVDVDEKRGQVSVRNPKATAneppKTFTFDAVFDPNSKQLDVYDEtARPLVDSVLEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 641 FNVCIFAYGQTGSGKTYTMEGIPEDP---GINQRALRLLFSEVSEKKPDWDYKITVSMVEIYNETLRNLLGDNPNEKLDI 717
Cdd:cd01371 81 YNGTIFAYGQTGTGKTYTMEGKREDPelrGIIPNSFAHIFGHIARSQNNQQFLVRVSYLEIYNEEIRDLLGKDQTKRLEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 718 KMCPDgSGqLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITVAG---FNSSTGHRTSGKLNLV 794
Cdd:cd01371 161 KERPD-TG-VYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECsekGEDGENHIRVGKLNLV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 795 DLAGSERIAKSGAEGSRLREAQCINKSLSALGDVINSL-RSKHSHVPFRNSRLTYLLQDSLSGDSKTLMMVQVSPLESNI 873
Cdd:cd01371 239 DLAGSERQSKTGATGERLKEATKINLSLSALGNVISALvDGKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADYNY 318
|
330
....*....|....*.
gi 688598103 874 SESVCSLKFAQRVRTV 889
Cdd:cd01371 319 DETLSTLRYANRAKNI 334
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
566-889 |
2.20e-95 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 304.25 E-value: 2.20e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 566 NIRVLCRVRPVCAGEADAADtKNLVTFDPEDDAVLYLSNKGKlmTFELDKVFTTQATQEEVFQE-VQSLVTSCIDGFNVC 644
Cdd:cd01369 3 NIKVVCRFRPLNELEVLQGS-KSIVKFDPEDTVVIATSETGK--TFSFDRVFDPNTTQEDVYNFaAKPIVDDVLNGYNGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 645 IFAYGQTGSGKTYTMEGIPEDP---GINQRALRLLFSEVSEKKPDWDYKITVSMVEIYNETLRNLLgDNPNEKLDIKmcP 721
Cdd:cd01369 80 IFAYGQTSSGKTYTMEGKLGDPesmGIIPRIVQDIFETIYSMDENLEFHVKVSYFEIYMEKIRDLL-DVSKTNLSVH--E 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 722 DGSGQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITVAGFNSSTGHRTSGKLNLVDLAGSER 801
Cdd:cd01369 157 DKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKKSGKLYLVDLAGSEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 802 IAKSGAEGSRLREAQCINKSLSALGDVINSL-RSKHSHVPFRNSRLTYLLQDSLSGDSKTLMMVQVSPLESNISESVCSL 880
Cdd:cd01369 237 VSKTGAEGAVLDEAKKINKSLSALGNVINALtDGKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLSTL 316
|
....*....
gi 688598103 881 KFAQRVRTV 889
Cdd:cd01369 317 RFGQRAKTI 325
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
566-885 |
1.27e-89 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 289.63 E-value: 1.27e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 566 NIRVLCRVRPVCAGEADAADTK-------NLVTFDPEDDAVLYL----------SNKGKLMTFELDKVFTTQATQEEVFQ 628
Cdd:cd01370 1 SLTVAVRVRPFSEKEKNEGFRRivkvmdnHMLVFDPKDEEDGFFhggsnnrdrrKRRNKELKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 629 E-VQSLVTSCIDGFNVCIFAYGQTGSGKTYTMEGIPEDPGINQRALRLLFSEVSEKKPDWDYKITVSMVEIYNETLRNLL 707
Cdd:cd01370 81 EtTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESLKDEKEFEVSMSYLEIYNETIRDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 708 gDNPNEKLDIkmCPDGSGQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITV------AGFNS 781
Cdd:cd01370 161 -NPSSGPLEL--REDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVrqqdktASINQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 782 STghrTSGKLNLVDLAGSERIAKSGAEGSRLREAQCINKSLSALGDVINSLRSKHS---HVPFRNSRLTYLLQDSLSGDS 858
Cdd:cd01370 238 QV---RQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKknkHIPYRDSKLTRLLKDSLGGNC 314
|
330 340
....*....|....*....|....*..
gi 688598103 859 KTLMMVQVSPLESNISESVCSLKFAQR 885
Cdd:cd01370 315 RTVMIANISPSSSSYEETHNTLKYANR 341
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
566-889 |
2.11e-87 |
|
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276825 [Multi-domain] Cd Length: 321 Bit Score: 283.07 E-value: 2.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 566 NIRVLCRVRPVCAGEADAADTKNLVTfdpEDDAVLYLSNKGKLMTFelDKVFTTQATQEEVFQEV-QSLVTSCIDGFNVC 644
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQVAWEI---DNDTIYLVEPPSTSFTF--DHVFGGDSTNREVYELIaKPVVKSALEGYNGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 645 IFAYGQTGSGKTYTMEGIPEDPGINQRALRLLFSEVsEKKPDWDYKITVSMVEIYNETLRNLLgdNPNEKlDIKMCPDGS 724
Cdd:cd01374 76 IFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKI-QDTPDREFLLRVSYLEIYNEKINDLL--SPTSQ-NLKIRDDVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 725 GQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITV---AGFNSSTGHRTSGKLNLVDLAGSER 801
Cdd:cd01374 152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIessERGELEEGTVRVSTLNLIDLAGSER 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 802 IAKSGAEGSRLREAQCINKSLSALGDVINSLRSKHS--HVPFRNSRLTYLLQDSLSGDSKTLMMVQVSPLESNISESVCS 879
Cdd:cd01374 232 AAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVggHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNT 311
|
330
....*....|
gi 688598103 880 LKFAQRVRTV 889
Cdd:cd01374 312 LKFASRAKKI 321
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
565-887 |
4.24e-86 |
|
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.
Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 280.78 E-value: 4.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 565 GNIRVLCRVRPVCAGEAdAADTKNLVTFDPEDDAVLYLSN--------KGKLMTFELDKVF-------TTQATQEEVFQE 629
Cdd:cd01365 1 ANVKVAVRVRPFNSREK-ERNSKCIVQMSGKETTLKNPKQadknnkatREVPKSFSFDYSYwshdsedPNYASQEQVYED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 630 V-QSLVTSCIDGFNVCIFAYGQTGSGKTYTMEGIPEDPGINQRALRLLFSEV-SEKKPDWDYKITVSMVEIYNETLRNLL 707
Cdd:cd01365 80 LgEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIaDTTNQNMSYSVEVSYMEIYNEKVRDLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 708 G-DNPNEKLDIKMCPDGSGQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHAL--LIITVAGFNSSTG 784
Cdd:cd01365 160 NpKPKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVftIVLTQKRHDAETN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 785 HRT--SGKLNLVDLAGSERIAKSGAEGSRLREAQCINKSLSALGDVINSL--------RSKHSHVPFRNSRLTYLLQDSL 854
Cdd:cd01365 240 LTTekVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmssgksKKKSSFIPYRDSVLTWLLKENL 319
|
330 340 350
....*....|....*....|....*....|...
gi 688598103 855 SGDSKTLMMVQVSPLESNISESVCSLKFAQRVR 887
Cdd:cd01365 320 GGNSKTAMIAAISPADINYEETLSTLRYADRAK 352
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
551-910 |
6.89e-82 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 276.23 E-value: 6.89e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 551 NLRKKCHNELVRLKGNIRVLCRVRPvcageadaadTKNLVTFDPEDDAVLYLSNKGKLMTFELDKVFTTQATQEEVFQE- 629
Cdd:COG5059 8 PLKSRLSSRNEKSVSDIKSTIRIIP----------GELGERLINTSKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEEt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 630 VQSLVTSCIDGFNVCIFAYGQTGSGKTYTMEGIPEDPGINQRALRLLFSEVSEKKPDWDYKITVSMVEIYNETLRNLLGD 709
Cdd:COG5059 78 IKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEDLSMTKDFAVSISYLEIYNEKIYDLLSP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 710 NPNEKLdikMCPDGSGQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITVAGFNSSTGHRTSG 789
Cdd:COG5059 158 NEESLN---IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTSETS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 790 KLNLVDLAGSERIAKSGAEGSRLREAQCINKSLSALGDVINSLR--SKHSHVPFRNSRLTYLLQDSLSGDSKTLMMVQVS 867
Cdd:COG5059 235 KLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGdkKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTIS 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 688598103 868 PLESNISESVCSLKFAQRVR----TVEIGPSSSSSRRQAENSSTSSS 910
Cdd:COG5059 315 PSSNSFEETINTLKFASRAKsiknKIQVNSSSDSSREIEEIKFDLSE 361
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
566-885 |
2.00e-80 |
|
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle pole proteins, participate in spindle assembly and chromosome segregation during cell division. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276815 [Multi-domain] Cd Length: 353 Bit Score: 265.34 E-value: 2.00e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 566 NIRVLCRVRPVCAGEADAADTKNLVTFDPEDDAVL---YLSNKGKLMTFELDKVFTTQATQEEVFQEVQS-LVTSCIDGF 641
Cdd:cd01364 3 NIQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtgGLADKSSTKTYTFDMVFGPEAKQIDVYRSVVCpILDEVLMGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 642 NVCIFAYGQTGSGKTYTMEG-----------IPEDPGINQRALRLLFSEVSEKKPDwdYKITVSMVEIYNETLRNLLGDN 710
Cdd:cd01364 83 NCTIFAYGQTGTGKTYTMEGdrspneeytweLDPLAGIIPRTLHQLFEKLEDNGTE--YSVKVSYLEIYNEELFDLLSPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 711 --PNEKLDIKMCPDGSGQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITVAGFNSSTGHRT- 787
Cdd:cd01364 161 sdVSERLRMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEEl 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 788 --SGKLNLVDLAGSERIAKSGAEGSRLREAQCINKSLSALGDVINSLRSKHSHVPFRNSRLTYLLQDSLSGDSKTLMMVQ 865
Cdd:cd01364 241 vkIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPHVPYRESKLTRLLQDSLGGRTKTSIIAT 320
|
330 340
....*....|....*....|
gi 688598103 866 VSPLESNISESVCSLKFAQR 885
Cdd:cd01364 321 ISPASVNLEETLSTLEYAHR 340
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
566-887 |
1.68e-75 |
|
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members of this subgroup seem to play a role in mitosis and meiosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276824 [Multi-domain] Cd Length: 347 Bit Score: 251.66 E-value: 1.68e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 566 NIRVLCRVRPVCAGEADAADTKNLVTFDPedDAVLYLSNKGKLMTFelDKVFTTQATQEEVFQEV-QSLVTSCIDGFNVC 644
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSS--DTLVLHSKPPKTFTF--DHVADSNTNQESVFQSVgKPIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 645 IFAYGQTGSGKTYTMEGIPEDP--------GINQRALRLLFSEVSEKKPD----WDYKITVSMVEIYNETLRNLLgDNPN 712
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQREKEKagegKSFLCKCSFLEIYNEQIYDLL-DPAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 713 EKLDIKmcPDGSGQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITV------AGFNSStghR 786
Cdd:cd01373 157 RNLKLR--EDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIeswekkACFVNI---R 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 787 TSgKLNLVDLAGSERIAKSGAEGSRLREAQCINKSLSALGDVINSL----RSKHSHVPFRNSRLTYLLQDSLSGDSKTLM 862
Cdd:cd01373 232 TS-RLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALvdvaHGKQRHVCYRDSKLTFLLRDSLGGNAKTAI 310
|
330 340
....*....|....*....|....*
gi 688598103 863 MVQVSPLESNISESVCSLKFAQRVR 887
Cdd:cd01373 311 IANVHPSSKCFGETLSTLRFAQRAK 335
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
566-887 |
3.19e-70 |
|
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276827 [Multi-domain] Cd Length: 319 Bit Score: 236.25 E-value: 3.19e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 566 NIRVLCRVRPVCAGEADAADTKNLVTFDPEDDAVLYLSNKGKLMTFELDKVFTTQATQEEVF-QEVQSLVTSCIDGFNVC 644
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPRNHGETLKYQFDAFYGEESTQEDIYaREVQPIVPHLLEGQNAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 645 IFAYGQTGSGKTYTMEGIPEDPGINQRALRLLFsEVSEKKPdWDYKITVSMVEIYNETLRNLLgDNPNEKLDIKMCPDGs 724
Cdd:cd01376 81 VFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-QMTRKEA-WALSFTMSYLEIYQEKILDLL-EPASKELVIREDKDG- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 725 gQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITVAGFNSSTGHR-TSGKLNLVDLAGSERIA 803
Cdd:cd01376 157 -NILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRqRTGKLNLIDLAGSEDNR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 804 KSGAEGSRLREAQCINKSLSALGDVINSLRSKHSHVPFRNSRLTYLLQDSLSGDSKTLMMVQVSPLESNISESVCSLKFA 883
Cdd:cd01376 236 RTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQDTLSTLNFA 315
|
....
gi 688598103 884 QRVR 887
Cdd:cd01376 316 ARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
567-887 |
9.16e-69 |
|
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play a role in cell shape remodeling. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276826 [Multi-domain] Cd Length: 334 Bit Score: 232.86 E-value: 9.16e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 567 IRVLCRVRPVCAGEAD----AADTKNLVTFDPEDDAVLYLSNKGKLMTFELDKVFTtQATQEEVFQEV-QSLVTSCIDGF 641
Cdd:cd01375 2 VQAFVRVRPTDDFAHEmikyGEDGKSISIHLKKDLRRGVVNNQQEDWSFKFDGVLH-NASQELVYETVaKDVVSSALAGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 642 NVCIFAYGQTGSGKTYTMEGIPE---DPGINQRALRLLFSEVsEKKPDWDYKITVSMVEIYNETLRNLLGDNPNEKLD-- 716
Cdd:cd01375 81 NGTIFAYGQTGAGKTFTMTGGTEnykHRGIIPRALQQVFRMI-EERPTKAYTVHVSYLEIYNEQLYDLLSTLPYVGPSvt 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 717 -IKMCPDGSGQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITVAGFNSSTGHRT--SGKLNL 793
Cdd:cd01375 160 pMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLSSEKyiTSKLNL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 794 VDLAGSERIAKSGAEGSRLREAQCINKSLSALGDVINSLRSKH-SHVPFRNSRLTYLLQDSLSGDSKTLMMVQVSPLESN 872
Cdd:cd01375 240 VDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDKDrTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQ 319
|
330
....*....|....*
gi 688598103 873 ISESVCSLKFAQRVR 887
Cdd:cd01375 320 LEETLSTLRFASRVK 334
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
567-883 |
1.26e-67 |
|
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members of this group may play a role in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276819 [Multi-domain] Cd Length: 345 Bit Score: 229.97 E-value: 1.26e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 567 IRVLCRVRPVCAGEADAAD-------TKNLVTFDPEDDAVLYLSNKG---KLMTFELDKVFTTQATQEEVFQEV-QSLVT 635
Cdd:cd01368 3 VKVYLRVRPLSKDELESEDegcieviNSTTVVLHPPKGSAANKSERNggqKETKFSFSKVFGPNTTQKEFFQGTaLPLVQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 636 SCIDGFNVCIFAYGQTGSGKTYTMEGIPEDPGINQRALRLLFSEVSekkpdwDYKITVSMVEIYNETLRNLLGDNPNEKL 715
Cdd:cd01368 83 DLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIG------GYSVFVSYIEIYNEYIYDLLEPSPSSPT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 716 D----IKMCPDGSGQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITV-----AGFNSSTGHR 786
Cdd:cd01368 157 KkrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLvqapgDSDGDVDQDK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 787 ---TSGKLNLVDLAGSERIAKSGAEGSRLREAQCINKSLSALGDVINSLRS-----KHSHVPFRNSRLTYLLQDSLSGDS 858
Cdd:cd01368 237 dqiTVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLREnqlqgTNKMVPFRDSKLTHLFQNYFDGEG 316
|
330 340
....*....|....*....|....*
gi 688598103 859 KTLMMVQVSPLESNISESVCSLKFA 883
Cdd:cd01368 317 KASMIVNVNPCASDYDETLHVMKFS 341
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
566-886 |
6.55e-65 |
|
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276818 [Multi-domain] Cd Length: 328 Bit Score: 221.79 E-value: 6.55e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 566 NIRVLCRVRPvCAGEADAADTKNLVTFDPEDDAVLY-------LSNKGKLMTFELDKVFTTQATQEEVFQE-VQSLVTSC 637
Cdd:cd01367 1 KIKVCVRKRP-LNKKEVAKKEIDVVSVPSKLTLIVHepklkvdLTKYIENHTFRFDYVFDESSSNETVYRStVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 638 IDGFNVCIFAYGQTGSGKTYTMEG----IPEDPGINQRALRLLFSEVSEKKPDWDYKITVSMVEIYNETLRNLLgdnpNE 713
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGdfsgQEESKGIYALAARDVFRLLNKLPYKDNLGVTVSFFEIYGGKVFDLL----NR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 714 KLDIKMCPDGSGQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITvagFNSSTGHRTSGKLNL 793
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQII---LRDRGTNKLHGKLSF 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 794 VDLAGSERIA-KSGAEGSRLREAQCINKSLSALGDVINSLRSKHSHVPFRNSRLTYLLQDSLSGD-SKTLMMVQVSPLES 871
Cdd:cd01367 233 VDLAGSERGAdTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHIPFRGSKLTQVLKDSFIGEnSKTCMIATISPGAS 312
|
330
....*....|....*
gi 688598103 872 NISESVCSLKFAQRV 886
Cdd:cd01367 313 SCEHTLNTLRYADRV 327
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
567-890 |
3.41e-53 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 202.86 E-value: 3.41e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 567 IRVLCRVRPVCAGEADAADTKNLvtfdpEDDAvlyLSNKGKlmTFELDKVFTTQATQEEVFQEVQS-LVTSCIDGFNVCI 645
Cdd:PLN03188 100 VKVIVRMKPLNKGEEGEMIVQKM-----SNDS---LTINGQ--TFTFDSIADPESTQEDIFQLVGApLVENCLAGFNSSV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 646 FAYGQTGSGKTYTMEGIP----------EDPGINQRALRLLFSEVSEKK-----PDWDYKITVSMVEIYNETLRNLLgdN 710
Cdd:PLN03188 170 FAYGQTGSGKTYTMWGPAnglleehlsgDQQGLTPRVFERLFARINEEQikhadRQLKYQCRCSFLEIYNEQITDLL--D 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 711 PNEKlDIKMCPDGSGQLYVPGLSEFTVESVEDINKVFDLGHMNRATACTNLNEHSSRSHALLIITVAGFNSSTGHRTSG- 789
Cdd:PLN03188 248 PSQK-NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSf 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 790 ---KLNLVDLAGSERIAKSGAEGSRLREAQCINKSLSALGDVIN-----SLRSKHSHVPFRNSRLTYLLQDSLSGDSKTL 861
Cdd:PLN03188 327 ktsRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINilaeiSQTGKQRHIPYRDSRLTFLLQESLGGNAKLA 406
|
330 340
....*....|....*....|....*....
gi 688598103 862 MMVQVSPLESNISESVCSLKFAQRVRTVE 890
Cdd:PLN03188 407 MVCAISPSQSCKSETFSTLRFAQRAKAIK 435
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
546-707 |
5.46e-41 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 147.37 E-value: 5.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 546 YKREMNLRKKCHNELVRLKGNIRVLCRVRPvcageadAADTKNLVTFDPEDDAVLYLSNKGKlmTFELDKVFTTQATQEE 625
Cdd:pfam16796 1 LEEEETLRRKLENSIQELKGNIRVFARVRP-------ELLSEAQIDYPDETSSDGKIGSKNK--SFSFDRVFPPESEQED 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 626 VFQEVQSLVTSCIDGFNVCIFAYGQTGSGktytmegipEDPGINQRALRLLFSEVSEKKPDWDYKITVSMVEIYNETLRN 705
Cdd:pfam16796 72 VFQEISQLVQSCLDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGWKYTIELQFVEIYNESSQD 142
|
..
gi 688598103 706 LL 707
Cdd:pfam16796 143 LL 144
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
614-833 |
9.49e-25 |
|
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.
Pssm-ID: 276814 [Multi-domain] Cd Length: 170 Bit Score: 101.65 E-value: 9.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 614 DKVFTTQATQEEVFQEVQSLVTSCIDGFNV-CIFAYGQTGSGKTYTMEGIpedpgInQRALRLLFSEVSEKKPDWDYKIT 692
Cdd:cd01363 23 YRGFRRSESQPHVFAIADPAYQSMLDGYNNqSIFAYGESGAGKTETMKGV-----I-PYLASVAFNGINKGETEGWVYLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 693 VSMVEIYNEtlrnllgdnpnekldikmcpdgsgqlyvpglseftvesVEDINkvfDLGHMNRaTACTNLNEHSSRSHALL 772
Cdd:cd01363 97 EITVTLEDQ--------------------------------------ILQAN---PILEAFG-NAKTTRNENSSRFGKFI 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688598103 773 IItvagfnsstghrtsgklnLVDLAGSERiaksgaegsrlreaqcINKSLSALGDVINSLR 833
Cdd:cd01363 135 EI------------------LLDIAGFEI----------------INESLNTLMNVLRATR 161
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
183-528 |
2.98e-14 |
|
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: 77.40 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 183 AVITGLRTQVKELEEKLVDQTQEVERLRSELgaTDLEKQLEVLESENQRLKQELKTSHTQTscSAARcphsQDVEVLRGE 262
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKAL--AELRKELEELEEELEQLRKELEELSRQI--SALR----KDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 263 LCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQLnTRLCDDEDTLRRHTT 342
Cdd:TIGR02168 742 VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL-DELRAELTLLNEEAA 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 343 VPQVKYvtktvevesAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLrtdrarlygllskavg 422
Cdd:TIGR02168 821 NLRERL---------ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEL---------------- 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 423 ggnTEVTLRLSKILMYEGEMERAQGQLEAEMQSLEEEKNRvIEEAFIRAESEMKAVHENLAGVRMNLLTLQPALRTltcD 502
Cdd:TIGR02168 876 ---EALLNERASLEEALALLRSELEELSEELRELESKRSE-LRRELEELREKLAQLELRLEGLEVRIDNLQERLSE---E 948
|
330 340
....*....|....*....|....*.
gi 688598103 503 YNCLKRQVQDFPYMLEKAIAEAKQEI 528
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRL 974
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
172-416 |
1.60e-13 |
|
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: 75.09 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 172 ERLQKVEGEqlavITGLRTQVKELEEKLVDQTQEVERLRSELgaTDLEKQLEVLESENQRLKQELKTSHTQTSCSAARCP 251
Cdd:TIGR02168 260 AELQELEEK----LEELRLEVSELEEEIEELQKELYALANEI--SRLEQQKQILRERLANLERQLEELEAQLEELESKLD 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 252 HSQ---------------DVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEAS 316
Cdd:TIGR02168 334 ELAeelaeleekleelkeELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLE 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 317 GHRSLNDEQLNTRLCDDEDTLRrhttvpqvkyvtKTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLhdsq 396
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAEL------------KELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL---- 477
|
250 260
....*....|....*....|
gi 688598103 397 rtsSQLRQQLRTDRARLYGL 416
Cdd:TIGR02168 478 ---DAAERELAQLQARLDSL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
172-478 |
5.02e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.43 E-value: 5.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 172 ERLQKVEGE-QLAVITGLRTQVKELEEKLVDQTQEVERLRSELGAtdLEKQLEVLESENQRLKQELKTSHTQTSCSAARc 250
Cdd:COG1196 220 EELKELEAElLLLKLRELEAELEELEAELEELEAELEELEAELAE--LEAELEELRLELEELELELEEAQAEEYELLAE- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 251 phsqdVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQLntrl 330
Cdd:COG1196 297 -----LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL---- 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 331 cddedtlrrhttvpqvkyvtKTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDR 410
Cdd:COG1196 368 --------------------LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688598103 411 ARLYGLLSKAVgggntEVTLRLSKILMYEGEMERAQGQLEAEMQSLEEEKNRVIEEAFIRAESEMKAV 478
Cdd:COG1196 428 EALAELEEEEE-----EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
548-835 |
7.21e-12 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 69.00 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 548 REMNLRKKCHNELVRLKgNIRVLCRVRPVcagEADAADTKNLVTFDPEDDAVL-------YLSNKGKLMTFELDKVFTTQ 620
Cdd:COG5059 289 RESKLTRLLQDSLGGNC-NTRVICTISPS---SNSFEETINTLKFASRAKSIKnkiqvnsSSDSSREIEEIKFDLSEDRS 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 621 ATQEEVFQEVQSLVTSCIDGfnvcIFAYGQTGSGKTYTMegIPEDPGINQRALRLLFSEV-SEKKPDWDYKITVSMVEIY 699
Cdd:COG5059 365 EIEILVFREQSQLSQSSLSG----IFAYMQSLKKETETL--KSRIDLIMKSIISGTFERKkLLKEEGWKYKSTLQFLRIE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 700 -------NETLRNLLGDNPNEKLDIKMcpdgsgqlyvPGLSEFTVESVEDINKVFDLGH-MNRATACTNLNEHSSRSHAL 771
Cdd:COG5059 439 idrllllREEELSKKKTKIHKLNKLRH----------DLSSLLSSIPEETSDRVESEKAsKLRSSASTKLNLRSSRSHSK 508
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688598103 772 LIITVAGFNSSTGhrtSGKLNLVDLAGSERIAKSgAEGSRLREAQCINKSLSALGDVINSLRSK 835
Cdd:COG5059 509 FRDHLNGSNSSTK---ELSLNQVDLAGSERKVSQ-SVGELLRETQSLNKSLSSLGDVIHALGSK 568
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
86-404 |
6.08e-10 |
|
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: 63.54 E-value: 6.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 86 ARLRSEDAAKRLLLQRLQTHDHQLNQDNHQNQEYSPLYQEPQEQLRLQAGQLNQAASPTGVRSSTALTQRPVDFPsALQV 165
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE-ELAE 779
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 166 SKVHSPERLQKVEGEQLAV------ITGLRTQVKELEEKLVDQTQEVERLRSELGATdlEKQLEVLESENQRLKQEL-KT 238
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELkalreaLDELRAELTLLNEEAANLRERLESLERRIAAT--ERRLEDLEEQIEELSEDIeSL 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 239 SHTQTSCSAARCPHSQDVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGH 318
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 319 RSLNDEQLNTRLCDDEDtlrrhttVPQVKYVTKTVEVESAQCKQALMEAQARN------TALQEqLSVQRQLLRELEQQL 392
Cdd:TIGR02168 938 IDNLQERLSEEYSLTLE-------EAEALENKIEDDEEEARRRLKRLENKIKElgpvnlAAIEE-YEELKERYDFLTAQK 1009
|
330
....*....|..
gi 688598103 393 HDSQRTSSQLRQ 404
Cdd:TIGR02168 1010 EDLTEAKETLEE 1021
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
180-555 |
9.06e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 180 EQLAVITGLRTQVKELEEKLvDQTQE----VERLRSELgatdlEKQLEVLE--SENQRLKQELKtshtqtscsaarcphs 253
Cdd:COG1196 162 EEAAGISKYKERKEEAERKL-EATEEnlerLEDILGEL-----ERQLEPLErqAEKAERYRELK---------------- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 254 qdvevlrgelcrkdEQWRERERRLAALEmqLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQLNtrlcdd 333
Cdd:COG1196 220 --------------EELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE------ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 334 edtlrrhttvpqvkyvTKTVEVESAQckQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDRARL 413
Cdd:COG1196 278 ----------------ELELELEEAQ--AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 414 ygllskavgggnTEVTLRLSKILMYEGEMERAQGQLEAEMQSLEEEKNRVIEEAFIRAESEMKAVHEnLAGVRMNLLTLQ 493
Cdd:COG1196 340 ------------EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELE 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688598103 494 PALRTLTCDYNCLKRQVQDfpymLEKAIAEAKQEICQVIGEVSSANQELLRKYKREMNLRKK 555
Cdd:COG1196 407 EAEEALLERLERLEEELEE----LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
265-471 |
1.14e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 265 RKDEQWRERER---------RLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQLNTRLCDDE- 334
Cdd:COG4913 591 EKDDRRRIRSRyvlgfdnraKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREi 670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 335 DTLRRHttvpqvkyvtktvevesaqcKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQL---RQQLRTDRA 411
Cdd:COG4913 671 AELEAE--------------------LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLekeLEQAEEELD 730
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688598103 412 RLYGLLSKAVGGGNTEVTLRLSKilMYEGEMERAQG-----QLEAEMQSLEEEKNRvIEEAFIRA 471
Cdd:COG4913 731 ELQDRLEAAEDLARLELRALLEE--RFAAALGDAVErelreNLEERIDALRARLNR-AEEELERA 792
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
98-412 |
1.33e-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: 62.06 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 98 LLQRLQTHDHQLNQDNHQNQEYSPLYQEPQEQLR--------LQAGQLNQAASPTgvRSSTALTQRPVDFPSALQVSKVH 169
Cdd:pfam17380 277 IVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAReverrrklEEAEKARQAEMDR--QAAIYAEQERMAMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 170 SPER---LQKVEGEQLAVITglrTQVKELEEKLVDQTQEVERLRSELGATdleKQLEVLESENQRLKQELKTSHTQTscs 246
Cdd:pfam17380 355 QEERkreLERIRQEEIAMEI---SRMRELERLQMERQQKNERVRQELEAA---RKVKILEEERQRKIQQQKVEMEQI--- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 247 aarcpHSQDVEVLRGELCRKDEqwrERERRLAALEMQLQDRSAVVEELQQQleEAAQRRHELQEQLEEASGHRSlndEQL 326
Cdd:pfam17380 426 -----RAEQEEARQREVRRLEE---ERAREMERVRLEEQERQQQVERLRQQ--EEERKRKKLELEKEKRDRKRA---EEQ 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 327 NTRLCDDEDTLRRHTTVPQvKYVTKTVEVESAQCKQALMEAQARNTA---------LQEQLSVQRQLLRELEQ--QLHDS 395
Cdd:pfam17380 493 RRKILEKELEERKQAMIEE-ERKRKLLEKEMEERQKAIYEEERRREAeeerrkqqeMEERRRIQEQMRKATEErsRLEAM 571
|
330
....*....|....*..
gi 688598103 396 QRTSSQLRQQLRTDRAR 412
Cdd:pfam17380 572 EREREMMRQIVESEKAR 588
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
281-567 |
1.77e-09 |
|
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: 62.00 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 281 EMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQLNTRLCDDEDTLRRHTtvpQVKYVTKTVEVESAQC 360
Cdd:TIGR02168 669 NSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS---ALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 361 KQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDRARLyGLLSKAVGGGNTEVTLRLSKILMYEG 440
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL-KALREALDELRAELTLLNEEAANLRE 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 441 EMERAQGQLEAEMQSLEEeknrvIEEAFIRAESEMKAVHENLAGVRMNLLTLQPALRTLTCDYNCLKRQVqdfpymleKA 520
Cdd:TIGR02168 825 RLESLERRIAATERRLED-----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL--------AL 891
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 688598103 521 IAEAKQEICQVIGEVSSANQELLRKYKREMNLRKKCHNELVRLKGNI 567
Cdd:TIGR02168 892 LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
215-420 |
4.00e-09 |
|
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: 59.78 E-value: 4.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 215 ATDLEKQLEVLESENQRLKQELKTShtqtscsaarcphSQDVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEEL 294
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAAL-------------KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 295 QQQLEEA----AQRRHELQEQLEEASGHRSLNDEQLNTRLCDDEDTLRR----HTTVPQVKYVTKTVEVESAQCKQALME 366
Cdd:COG4942 89 EKEIAELraelEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRlqylKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 688598103 367 AQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDRARLYGLLSKA 420
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEA 222
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
272-573 |
7.43e-09 |
|
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: 60.07 E-value: 7.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 272 ERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEAsghrSLNDEQLNTRLCDDEDTLRRHTTVPQvkyvtk 351
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL----RKELEELSRQISALRKDLARLEAEVE------ 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 352 TVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDRARL------YGLLSKAVGGGN 425
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelraeLTLLNEEAANLR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 426 TEVTLRLSKILMYEGEMERAQGQ----------LEAEMQSLEEEKNRvIEEAFIRAESEMKAVHENLAGVRMNLLTLQPA 495
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQieelsediesLAAEIEELEELIEE-LESELEALLNERASLEEALALLRSELEELSEE 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 496 LRTLTCDYNCLKRQVQDFPYMLEKA---IAEAKQEICQVIGEVSSANQ----ELLRKYKREMNLRKKCHNELVRLKGNIR 568
Cdd:TIGR02168 903 LRELESKRSELRRELEELREKLAQLelrLEGLEVRIDNLQERLSEEYSltleEAEALENKIEDDEEEARRRLKRLENKIK 982
|
....*
gi 688598103 569 VLCRV 573
Cdd:TIGR02168 983 ELGPV 987
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
219-392 |
1.91e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 219 EKQLEVLESENQRLKQELKTSHTQ-TSCSAARCPHSQDVEVLRG--ELCRKDEQWRERERRLAALEMQLQD---RSAVVE 292
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERlEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERldaSSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 293 ELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQLNTRLCDDEDTLRRHTTVPQVKYVTKTVEVEsAQCKQALMEAQARN- 371
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE-ERFAAALGDAVEREl 767
|
170 180
....*....|....*....|..
gi 688598103 372 -TALQEQLSVQRQLLRELEQQL 392
Cdd:COG4913 768 rENLEERIDALRARLNRAEEEL 789
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
185-413 |
2.66e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 185 ITGLRTQVKE--LEEK--------LVDQTQEVERLRSELgaTDLEKQLEVLEsenqrlkqELKTSHTQtsCSAARcphsQ 254
Cdd:COG4913 206 IGDLDDFVREymLEEPdtfeaadaLVEHFDDLERAHEAL--EDAREQIELLE--------PIRELAER--YAAAR----E 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 255 DVEVLrgELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLND----EQLNTRL 330
Cdd:COG4913 270 RLAEL--EYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgdrlEQLEREI 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 331 CDDEDTLRRHTT-VPQVKYVTKTVEVESAQCKQALMEAQARNTALQEQLSvqrQLLRELEQQLHDSQRTSSQLRQQLRTD 409
Cdd:COG4913 348 ERLERELEERERrRARLEALLAALGLPLPASAEEFAALRAEAAALLEALE---EELEALEEALAEAEAALRDLRRELREL 424
|
....
gi 688598103 410 RARL 413
Cdd:COG4913 425 EAEI 428
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
79-332 |
3.20e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.04 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 79 ERVCEFQARLRSEDAAKRLLLQRLQTHDHQLNQdnhqnqeysplYQEPQEQLRLQAGqlnqaasptGVRSSTAltqrpvd 158
Cdd:COG3096 441 DYLAAFRAKEQQATEEVLELEQKLSVADAARRQ-----------FEKAYELVCKIAG---------EVERSQA------- 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 159 FPSALQVSKVHspeRLQKVEGEQLAvitGLRTQVKELeEKLVDQTQEVERLRSELG---------ATDLEKQLEVLESEN 229
Cdd:COG3096 494 WQTARELLRRY---RSQQALAQRLQ---QLRAQLAEL-EQRLRQQQNAERLLEEFCqrigqqldaAEELEELLAELEAQL 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 230 QRLKQELKTshtqtsCSAARCPHSQDVEVLRG---ELCRKDEQWRERERRLAALEMQ----LQDRSAVVEELQQQLE--- 299
Cdd:COG3096 567 EELEEQAAE------AVEQRSELRQQLEQLRArikELAARAPAWLAAQDALERLREQsgeaLADSQEVTAAMQQLLErer 640
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 688598103 300 -------EAAQRRHELQEQLEEASGHRSLNDEQLNtRLCD 332
Cdd:COG3096 641 eatverdELAARKQALESQIERLSQPGGAEDPRLL-ALAE 679
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
190-386 |
3.29e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 190 TQVKELEEKLVDQTQEVERLRSELGA-TDLEKQLEVLESENQRLKQELKtshtqtscsaaRCPHSQDVEVLRGELCRKDE 268
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELE-----------KLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 269 QWRERERRLAALEMQLQDRsavvEELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQLNTRLCDDEDTLRRHTTVPQVKY 348
Cdd:COG4717 140 ELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190
....*....|....*....|....*....|....*...
gi 688598103 349 VTKTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLR 386
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLL 253
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
85-561 |
4.51e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 57.04 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 85 QARLRSEDAakRLLLQRLQTHDHQLNQdnHQNQEYSPLYQEPQEQLRLQAGQLNQAASPtgVRSSTALTQRPVDfpsalq 164
Cdd:pfam05483 201 ELRVQAENA--RLEMHFKLKEDHEKIQ--HLEEEYKKEINDKEKQVSLLLIQITEKENK--MKDLTFLLEESRD------ 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 165 vsKVHSPERLQKVEGEQLavitglrtqvKELEEKLVDQTQEVERL-----RSELGATDLEKQLEVLESENQRLKQELKTS 239
Cdd:pfam05483 269 --KANQLEEKTKLQDENL----------KELIEKKDHLTKELEDIkmslqRSMSTQKALEEDLQIATKTICQLTEEKEAQ 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 240 HTQTScsAARCPHSQDVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEasghr 319
Cdd:pfam05483 337 MEELN--KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEE----- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 320 slndeqLNTRLCDDEDTLRRHTTVPQVKYVTKTVEVESAQCKQAL------MEAQARNTALQEQLSVQRqlLRELEQQLH 393
Cdd:pfam05483 410 ------LKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQARekeihdLEIQLTAIKTSEEHYLKE--VEDLKTELE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 394 DSQRTSSQLrqqlrTDRARLYGLLSKAVGGGNTEVTLRLSK----ILMYEGEMERAQGQL----EAEMQsLEEEKNRVIE 465
Cdd:pfam05483 482 KEKLKNIEL-----TAHCDKLLLENKELTQEASDMTLELKKhqedIINCKKQEERMLKQIenleEKEMN-LRDELESVRE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 466 EaFIRAESEMKA----VHENLAGVRMNLLTLQPALRTLTCDYNCLKRQVQDFPYMLE-----------KAIAEAKQ---- 526
Cdd:pfam05483 556 E-FIQKGDEVKCkldkSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEelhqenkalkkKGSAENKQlnay 634
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 688598103 527 --EICQVIGEVSSANQ---ELLRKYKREMNLRKKCHNELV 561
Cdd:pfam05483 635 eiKVNKLELELASAKQkfeEIIDNYQKEIEDKKISEEKLL 674
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
85-409 |
8.41e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 56.35 E-value: 8.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 85 QARLRSEDAAKRL------LLQRLQTHDHQLNQDNHQNQEYSPLYQEpQEQLRLQAGQLNQ--------AASPTGVRSST 150
Cdd:PRK10246 558 KQLQRDESEAQSLrqeeqaLTQQWQAVCASLNITLQPQDDIQPWLDA-QEEHERQLRLLSQrhelqgqiAAHNQQIIQYQ 636
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 151 A-LTQRPVDFPSALQVSKVHSPErlqkvEGEQLAVITGLRTQVKELEEKlvdQTQEverlrselgaTDLEKQLEVLESEN 229
Cdd:PRK10246 637 QqIEQRQQQLLTALAGYALTLPQ-----EDEEASWLATRQQEAQSWQQR---QNEL----------TALQNRIQQLTPLL 698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 230 QRLKQELKTSHTQTSCSAarcphsqdvevlrgelcrkdEQWRERERRLAALEMQLQdrsavveELQQQLEEAAQRRHELQ 309
Cdd:PRK10246 699 ETLPQSDDLPHSEETVAL--------------------DNWRQVHEQCLSLHSQLQ-------TLQQQDVLEAQRLQKAQ 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 310 EQLEEASGHRSLNDEQLNTRLCDDEDTLRRHTTVPQ-VKYVTKTVEVESAQCKQALMEAQA-RNTALQEQLSVQ--RQLL 385
Cdd:PRK10246 752 AQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQnLENQRQQAQTLVTQTAQALAQHQQhRPDGLDLTVTVEqiQQEL 831
|
330 340
....*....|....*....|....
gi 688598103 386 RELEQQLHDSQRTSSQLRQQLRTD 409
Cdd:PRK10246 832 AQLAQQLRENTTRQGEIRQQLKQD 855
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
172-478 |
8.76e-08 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 8.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 172 ERLQKVEG-EQLAVITGLRTQVKELEEKLVDQTQEVERLRSELgaTDLEKQLE----VLESENQRLKQelKTSHTQTSCS 246
Cdd:TIGR02169 218 KEKREYEGyELLKEKEALERQKEAIERQLASLEEELEKLTEEI--SELEKRLEeieqLLEELNKKIKD--LGEEEQLRVK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 247 AARCPHSQDVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASghrslndeql 326
Cdd:TIGR02169 294 EKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK---------- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 327 ntrlcDDEDTLRRHttvpqvkyvTKTVEVESAQCKQALMEAQARNTALQEQLSvqrqllrELEQQLHDSQRTSSQLRQQL 406
Cdd:TIGR02169 364 -----EELEDLRAE---------LEEVDKEFAETRDELKDYREKLEKLKREIN-------ELKRELDRLQEELQRLSEEL 422
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688598103 407 RTDRARLYGLLSK--AVGGGNTEVTLRLSKIlmyEGEMERAQGQLEAEMQSLE--EEKNRVIEEAFIRAESEMKAV 478
Cdd:TIGR02169 423 ADLNAAIAGIEAKinELEEEKEDKALEIKKQ---EWKLEQLAADLSKYEQELYdlKEEYDRVEKELSKLQRELAEA 495
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
165-570 |
9.05e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 165 VSKVHSPERLQKVEGEQLAVITGLRTQVKELEeKLVDQTQEVERLRSELGA--TDLEKQLEVLESENQRLKQELKTSHTQ 242
Cdd:PRK03918 151 VRQILGLDDYENAYKNLGEVIKEIKRRIERLE-KFIKRTENIEELIKEKEKelEEVLREINEISSELPELREELEKLEKE 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 243 TscsaarcphsQDVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLN 322
Cdd:PRK03918 230 V----------KELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 323 D--EQLNTRLCDDEDTLRRhttvpqvkyvtktVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELE--QQLHDSQRT 398
Cdd:PRK03918 300 EfyEEYLDELREIEKRLSR-------------LEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEelEERHELYEE 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 399 SSQLRQQLRTDRARLYGL-------LSKAVGGGNTEVTLRLSKILMYEGEMERAQGQLEAEMQSLEEEK------NRVIE 465
Cdd:PRK03918 367 AKAKKEELERLKKRLTGLtpeklekELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcGRELT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 466 EAfiRAESEMKAVHENLAGVRMNLLTLQPALRTLtcdyncLKRQVQdfpymLEKAIAEAKQ---------EICQVIGEVS 536
Cdd:PRK03918 447 EE--HRKELLEEYTAELKRIEKELKEIEEKERKL------RKELRE-----LEKVLKKESEliklkelaeQLKELEEKLK 513
|
410 420 430
....*....|....*....|....*....|....
gi 688598103 537 SANQELLRKYKREMNLRKKchnELVRLKGNIRVL 570
Cdd:PRK03918 514 KYNLEELEKKAEEYEKLKE---KLIKLKGEIKSL 544
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
268-574 |
1.51e-07 |
|
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: 55.83 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 268 EQWRERERRLAALEMQLQDRSAVVEELQQQLE------EAAQRRHELQEQLEEASGHRSLND--------EQLNTRLCDD 333
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQLKslerqaEKAERYKELKAELRELELALLVLRleelreelEELQEELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 334 EDTLRRHTT---VPQVKYVTKTVEVESAQCKQAlmEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDR 410
Cdd:TIGR02168 252 EEELEELTAelqELEEKLEELRLEVSELEEEIE--ELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 411 ARLYGLlskavgggNTEVTLRLSKILMYEGEMERAQGQLEAEMQSLEEEKNRV--IEEAFIRAESEMKAVHENLAGVRMN 488
Cdd:TIGR02168 330 SKLDEL--------AEELAELEEKLEELKEELESLEAELEELEAELEELESRLeeLEEQLETLRSKVAQLELQIASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 489 LLTLQPALRTLTCDYNCLKRQVQDFPYMLEKA--------IAEAKQEICQVIGEVSSANQELLRKYKRE---MNLRKKCH 557
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAelkelqaeLEELEEELEELQEELERLEEALEELREELeeaEQALDAAE 481
|
330
....*....|....*..
gi 688598103 558 NELVRLKGNIRVLCRVR 574
Cdd:TIGR02168 482 RELAQLQARLDSLERLQ 498
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
172-570 |
7.16e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 172 ERLQKVEGEQLAVITGLRTQVKELEEKLVDQTQEVERLRSELGATDLEKQLEVLESENQRLKQELKtshtqtscsaarcp 251
Cdd:COG4717 77 EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELA-------------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 252 hsQDVEVLRgELCRKDEQWRERERRLAALEMQLQDRSAVVEEL--------QQQLEEAAQRRHELQEQLEEASGHRSLND 323
Cdd:COG4717 143 --ELPERLE-ELEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 324 ---EQLNTRLCDDEDTLRRHTTVPQVKYVTKTVEVESAQCKQALMEAQARNT---------------ALQEQLSVQRQLL 385
Cdd:COG4717 220 eelEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLiltiagvlflvlgllALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 386 RELEQQLHDSQRTSSQLRQQLRTDRARLYGLLSKAVGGGNTEVTLRLSKILMYEGEMERAQGQLeaEMQSLEEEKNRVIE 465
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 466 EAFIRAESEMKAVHENLAgvrmnlltlqpALRTLTCDYNCLKRQVQDFPYMLEKAIAEAKQEicqvigEVSSANQELLRK 545
Cdd:COG4717 378 EAGVEDEEELRAALEQAE-----------EYQELKEELEELEEQLEELLGELEELLEALDEE------ELEEELEELEEE 440
|
410 420
....*....|....*....|....*
gi 688598103 546 YKREMNLRKKCHNELVRLKGNIRVL 570
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQL 465
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
175-333 |
9.46e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.04 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 175 QKVEGEQLAvitGLRTQVKELEEKLVDQtQEVERLRSELG---------ATDLEKQLEVLESENQRLKQELKTSHTQTSC 245
Cdd:PRK04863 508 QRHLAEQLQ---QLRMRLSELEQRLRQQ-QRAERLLAEFCkrlgknlddEDELEQLQEELEARLESLSESVSEARERRMA 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 246 SAArcpHSQDVEVLRGELCRKDEQWRERERRLAALEMQ----LQDRSAVVEELQQQLE----------EAAQRRHELQEQ 311
Cdd:PRK04863 584 LRQ---QLEQLQARIQRLAARAPAWLAAQDALARLREQsgeeFEDSQDVTEYMQQLLErereltverdELAARKQALDEE 660
|
170 180
....*....|....*....|..
gi 688598103 312 LEEASGHRSLNDEQLNtRLCDD 333
Cdd:PRK04863 661 IERLSQPGGSEDPRLN-ALAER 681
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
184-420 |
1.45e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.65 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 184 VITGLRTQVK---------ELEEKLVDQTQEVERLRSELgaTDLEKQLEVLESENQRLK-------QELKTSHTQTscsa 247
Cdd:COG3096 339 VQTALRQQEKieryqedleELTERLEEQEEVVEEAAEQL--AEAEARLEAAEEEVDSLKsqladyqQALDVQQTRA---- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 248 arCPHSQDVEVLRG--ELCRKDE-QWRERERRLAALEMQLQDRSAVVEELQQQL--EEAAQRRHE--------------- 307
Cdd:COG3096 413 --IQYQQAVQALEKarALCGLPDlTPENAEDYLAAFRAKEQQATEEVLELEQKLsvADAARRQFEkayelvckiagever 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 308 ------LQEQLEEASGHRSLND--EQLNTRLCDDEDTLRRHttvpqvkyvtKTVEVESAQCKQALMEAQARNTALQEQLS 379
Cdd:COG3096 491 sqawqtARELLRRYRSQQALAQrlQQLRAQLAELEQRLRQQ----------QNAERLLEEFCQRIGQQLDAAEELEELLA 560
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 688598103 380 VQRQLLRELEQQLHDSQRTSSQLRQQLRTDRARLYGLLSKA 420
Cdd:COG3096 561 ELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARA 601
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
180-499 |
1.65e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 180 EQLAVITGLRTQVKELEEKLVDQTQEVERLRSELgaTDLEKQLEVLesenqrlkqelktshtQTSCSAARcphsQDVEVL 259
Cdd:PRK04863 366 EQNEVVEEADEQQEENEARAEAAEEEVDELKSQL--ADYQQALDVQ----------------QTRAIQYQ----QAVQAL 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 260 RgelcrKDEQWrererrLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLNDE--QLNTRLCDDedtl 337
Cdd:PRK04863 424 E-----RAKQL------CGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayQLVRKIAGE---- 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 338 rrhttvpqvkyvtktVEVESAQCKQALMEAQARN-TALQEQLSVQRQLLRELEQQLHdSQRTSSQLRQQLRTdrarlygl 416
Cdd:PRK04863 489 ---------------VSRSEAWDVARELLRRLREqRHLAEQLQQLRMRLSELEQRLR-QQQRAERLLAEFCK-------- 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 417 lskavgggntevtlRLSKILMYEGEMERAQGQLEAEMQSLEEEKNRVIEEAF-IRAESE-MKAVHENLAGVRMNLLTLQP 494
Cdd:PRK04863 545 --------------RLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMaLRQQLEqLQARIQRLAARAPAWLAAQD 610
|
....*
gi 688598103 495 ALRTL 499
Cdd:PRK04863 611 ALARL 615
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
114-549 |
2.64e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.51 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 114 HQNQEYSPLYQEPQEQLRLQAGQLNQAASPTGVRSSTALTQRpvdfpsalQVSKVHSPERLQKVEGEQLAVITGLRTQVK 193
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRR--------LLQTLHSQEIHIRDAHEVATSIREISCQQH 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 194 ELEEKLVDQTQEVERLRSELGA--------TDLEKQLEVLESENQRLKQELKTSHTQTSCSAARCPHSQDV--EVLRGEL 263
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLTQKLQSlckeldilQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAitCTAQCEK 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 264 CRKDEQwRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQ---LEEASGH------RSLNDEQLNTRLCDDE 334
Cdd:TIGR00618 456 LEKIHL-QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcpLCGSCIHpnparqDIDNPGPLTRRMQRGE 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 335 DTLRRHTTVPQVKYVTKTVEVESAQCKQALME---------AQARNtALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQ 405
Cdd:TIGR00618 535 QTYAQLETSEEDVYHQLTSERKQRASLKEQMQeiqqsfsilTQCDN-RSKEDIPNLQNITVRLQDLTEKLSEAEDMLACE 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 406 LRTDRARL---YGLLSKAVGGGNTEVTLRLSKILMYEGEMERAQGQLEAEMQSLEEEKNRVIEEAfIRAESEMKAVHENL 482
Cdd:TIGR00618 614 QHALLRKLqpeQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR-QLALQKMQSEKEQL 692
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688598103 483 AGVRMNLLTLQPALRTLTCDYNCLKRQVQDFPYMLEKAIAEAKQEicqvigevSSANQELLRKYKRE 549
Cdd:TIGR00618 693 TYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR--------EDALNQSLKELMHQ 751
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
172-400 |
2.82e-06 |
|
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: 50.53 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 172 ERLQKVEGEQLAVITGLRTQVKELEEKLVDQTQEVERLRSELGAtdLEKQLEVLESENQRLKQELKTSHTQTSCSAARCP 251
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA--LEAELAELEKEIAELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 252 HSQDVEVLRGELcrKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEAsghRSLNDEQLNTRLC 331
Cdd:COG4942 115 RLGRQPPLALLL--SPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL---EALLAELEEERAA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688598103 332 DDEDTLRRHTTVPQVKyvtktvevesaqckQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSS 400
Cdd:COG4942 190 LEALKAERQKLLARLE--------------KELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
172-413 |
7.79e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.02 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 172 ERLQKVEGEQLAVITGLRTQVKELEEKLVDQTQEVERLRSELGATDLEKQLEVLESENQRLKQELKTSHTQTSCSAARcp 251
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEAR-- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 252 hsqdVEVLRGELCRK----------------DEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAaqrRHELQEQLEEA 315
Cdd:COG3206 242 ----LAALRAQLGSGpdalpellqspviqqlRAQLAELEAELAELSARYTPNHPDVIALRAQIAAL---RAQLQQEAQRI 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 316 SGHRSLNDEQLNTRlcddEDTLRRhttvpqvkyvtktvEVESAQCK-QALMEAQARNTALQEQLSVQRQLLRELEQQLhd 394
Cdd:COG3206 315 LASLEAELEALQAR----EASLQA--------------QLAQLEARlAELPELEAELRRLEREVEVARELYESLLQRL-- 374
|
250
....*....|....*....
gi 688598103 395 sqrTSSQLRQQLRTDRARL 413
Cdd:COG3206 375 ---EEARLAEALTVGNVRV 390
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
180-326 |
8.11e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 180 EQLAVitgLRTQVKELEEKLVDQTQEVERLRSELGAtdLEKQLEVL----------------ESENQRLKQELKtshtqt 243
Cdd:COG4913 610 AKLAA---LEAELAELEEELAEAEERLEALEAELDA--LQERREALqrlaeyswdeidvasaEREIAELEAELE------ 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 244 SCSAArcphSQDVEVLRgelcrkdEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLND 323
Cdd:COG4913 679 RLDAS----SDDLAALE-------EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLEL 747
|
...
gi 688598103 324 EQL 326
Cdd:COG4913 748 RAL 750
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
172-465 |
8.84e-06 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 172 ERLQKVEGEQLAVITGLRTQVKELEEKLVDQTQEVERLRSELGATD-----LEKQLEVLES--------ENQRLKQELKT 238
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEedlhkLEEALNDLEArlshsripEIQAELSKLEE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 239 SHTQTSCSAARCPH-----SQDVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLE 313
Cdd:TIGR02169 806 EVSRIEARLREIEQklnrlTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLG 885
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 314 EASGHRslndeqlntrlcddeDTLRRHTTVPQVKYVTKTVEVESAQCKQALMEAQArnTALQEQLSvqrQLLRELEQQLH 393
Cdd:TIGR02169 886 DLKKER---------------DELEAQLRELERKIEELEAQIEKKRKRLSELKAKL--EALEEELS---EIEDPKGEDEE 945
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688598103 394 DSQRTSS--QLRQQLRTDRARLYGLlskavgggnTEVTLRlsKILMYEgEMERAQGQLEAEMQSLEEEKNRVIE 465
Cdd:TIGR02169 946 IPEEELSleDVQAELQRVEEEIRAL---------EPVNML--AIQEYE-EVLKRLDELKEKRAKLEEERKAILE 1007
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
190-466 |
9.82e-06 |
|
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: 49.79 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 190 TQVKELEEKlvdQTQEVERLRSEL-----GATDLEKQLEVLESENQRLKQELKTSHTQTScsaarcphsqdvevlrgelc 264
Cdd:pfam01576 345 AQLQEMRQK---HTQALEELTEQLeqakrNKANLEKAKQALESENAELQAELRTLQQAKQ-------------------- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 265 rkdeqwrERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGhrSLND-EQLNTRLCDDEDTLRRHTTV 343
Cdd:pfam01576 402 -------DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSS--LLNEaEGKNIKLSKDVSSLESQLQD 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 344 PQVKYVTKTVEVESAQCKQALMEAQArnTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDRARLYGLlskavgg 423
Cdd:pfam01576 473 TQELLQEETRQKLNLSTRLRQLEDER--NSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEAL------- 543
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 688598103 424 gnTEVTLRLSKilmyegEMERAQGQLE---AEMQSLEEEKNRVIEE 466
Cdd:pfam01576 544 --EEGKKRLQR------ELEALTQQLEekaAAYDKLEKTKNRLQQE 581
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
98-477 |
1.13e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 98 LLQRLQTHDHQLNQDNHQNQEYSPLYQEPQEQLRLQAGQLNQ-AASPTGVRSSTALTQRPVDFPSALQVSKV---HSPER 173
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRsKEDIPNLQNITVRLQDLTEKLSEAEDMLAceqHALLR 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 174 LQKVEGEQLAVITGLRTQVKELEEKLVDQTQEVERL---RSELGATDLEKQLEVLESENQRLKQELKTSHTQTSCSAARC 250
Cdd:TIGR00618 620 KLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqeRVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 251 PHSQdvEVLRGELCRKDEQWRERERrlaalemQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQLNTRL 330
Cdd:TIGR00618 700 AQCQ--TLLRELETHIEEYDREFNE-------IENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV 770
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 331 CDDEDTLrrhttvpqvkyvtktvevesAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDR 410
Cdd:TIGR00618 771 TAALQTG--------------------AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEE 830
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688598103 411 ARLYGLLSKavgggNTEVTLRLSKILMYEGEMERAQGQL---EAEMQSLEEE-------KNRVIEEAFIRAESEMKA 477
Cdd:TIGR00618 831 EQFLSRLEE-----KSATLGEITHQLLKYEECSKQLAQLtqeQAKIIQLSDKlnginqiKIQFDGDALIKFLHEITL 902
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
171-314 |
1.58e-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: 47.23 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 171 PERLQKVEGEQLAV----------ITGLRTQVKELEEKLVDQTQEVERLRSELGA-------TDLEKQLEVLESENQRLK 233
Cdd:COG1579 30 PAELAELEDELAALearleaakteLEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyEALQKEIESLKRRISDLE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 234 QELKTSHTQtscsaarcphsqdVEVLRGELCRKDEQWRERERRLAALEMQLQDRsavVEELQQQLEEAAQRRHELQEQLE 313
Cdd:COG1579 110 DEILELMER-------------IEELEEELAELEAELAELEAELEEKKAELDEE---LAELEAELEELEAEREELAAKIP 173
|
.
gi 688598103 314 E 314
Cdd:COG1579 174 P 174
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
175-477 |
1.84e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 175 QKVEGEQLAVITGLRTQVKELEEKLVDQTQEVERLRSELGATD--LEKQLEVLEsENQRLKQEL-KTSHTQTSCSAARCP 251
Cdd:PRK02224 198 EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADevLEEHEERRE-ELETLEAEIeDLRETIAETEREREE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 252 HSQDVEVLRGELCRKDEqwrERERRLAALEMQlqdrSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQLnTRLC 331
Cdd:PRK02224 277 LAEEVRDLRERLEELEE---ERDDLLAEAGLD----DADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEA-ESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 332 DDEDTLRRHTTVPQVKyvTKTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQrtssQLRQQLRTDRA 411
Cdd:PRK02224 349 EDADDLEERAEELREE--AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAE----DFLEELREERD 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 412 RLYGLLskavggGNTEVTLRLSKILMYEGEMERAQGQ--------------------------LEAEMQSLEEEKNRViE 465
Cdd:PRK02224 423 ELRERE------AELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvetieedrerveeLEAELEDLEEEVEEV-E 495
|
330
....*....|..
gi 688598103 466 EAFIRAESEMKA 477
Cdd:PRK02224 496 ERLERAEDLVEA 507
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
205-392 |
2.10e-05 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 46.43 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 205 EVERLRSELgaTDLEKQLEVLESENQRLKQEL--------KTSHTQTSCSAARCPHSQDVEVLRGELCRKDEQWRERERR 276
Cdd:pfam15619 12 KIKELQNEL--AELQSKLEELRKENRLLKRLQkrqekalgKYEGTESELPQLIARHNEEVRVLRERLRRLQEKERDLERK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 277 LAALEMQLQDRSAVVEELQQQLEEA-AQRRHELQEQLEEASGHRSLNDEQLNTrlcddedtLRRhttvpQVKYVTKTVEV 355
Cdd:pfam15619 90 LKEKEAELLRLRDQLKRLEKLSEDKnLAEREELQKKLEQLEAKLEDKDEKIQD--------LER-----KLELENKSFRR 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 688598103 356 ESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQL 392
Cdd:pfam15619 157 QLAAEKKKHKEAQEEVKILQEEIERLQQKLKEKEREL 193
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
172-316 |
2.44e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 172 ERLQKVEGEQLAVITGLRTQVKELEEKLVDQTQEVERLRSELGATDLEkQLEVLESENQRLKQELKTshtqtsCSAARCP 251
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD-RLEQLEREIERLERELEE------RERRRAR 363
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688598103 252 HSQDVEVLRGELCRKDEQWRERERRLAALemqLQDRSAVVEELQQQLEEAAQRRHELQEQLEEAS 316
Cdd:COG4913 364 LEALLAALGLPLPASAEEFAALRAEAAAL---LEALEEELEALEEALAEAEAALRDLRRELRELE 425
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
271-544 |
3.55e-05 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 271 RERERRLAAlemQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQLNtRLCDDEDTLRRHTTvpQVKYVT 350
Cdd:TIGR02169 673 PAELQRLRE---RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE-QLEQEEEKLKERLE--ELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 351 KTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQ-RTSSQLRQQLRTDRARLYGLLSkavgggntEVT 429
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRiPEIQAELSKLEEEVSRIEARLR--------EIE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 430 LRLSKILMYEGEMERAQGQLEAEMQSLEEEKNRV---IEEAFIRAEsEMKAVHENlagvrmnlltLQPALRTLTCDYNCL 506
Cdd:TIGR02169 819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIekeIENLNGKKE-ELEEELEE----------LEAALRDLESRLGDL 887
|
250 260 270
....*....|....*....|....*....|....*...
gi 688598103 507 KRQVQDfpymLEKAIAEAKQEICQVIGEVSSANQELLR 544
Cdd:TIGR02169 888 KKERDE----LEAQLRELERKIEELEAQIEKKRKRLSE 921
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
86-411 |
3.72e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 47.37 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 86 ARLRSEDAAKRLLLQRLQThdhQLNQDNHQNQEYsplyQEPQEQLRLQAgqlnQAASPTGVRSSTALTQRPVDFPSALQV 165
Cdd:pfam19220 107 EELRIELRDKTAQAEALER---QLAAETEQNRAL----EEENKALREEA----QAAEKALQRAEGELATARERLALLEQE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 166 SKvhspeRLQKVEGEQLAVITGLRTQVKELEEKLVDQTQEVERLRSELGA--TDLEKQLEVLESENQRLKQELKTSHTQT 243
Cdd:pfam19220 176 NR-----RLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAeqAERERAEAQLEEAVEAHRAERASLRMKL 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 244 SCSAARCPHS-QDVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASgHRSln 322
Cdd:pfam19220 251 EALTARAAATeQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELE-ERA-- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 323 dEQLNTRLCDDEDTLRRHTTvpqvkyvtktvevesaqckqalmeaqaRNTALQEQLSvqrQLLRELEQQLHDSQRTSSQL 402
Cdd:pfam19220 328 -EMLTKALAAKDAALERAEE---------------------------RIASLSDRIA---ELTKRFEVERAALEQANRRL 376
|
....*....
gi 688598103 403 RQQLRTDRA 411
Cdd:pfam19220 377 KEELQRERA 385
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
169-321 |
3.79e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 169 HSPERLQKVEGEQLAVITGLRTQVKELEEKLVDQTQEVERLRSElgATDLEKQLEVLESENQRLKQELKTshtqtscsaA 248
Cdd:COG2433 385 LIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAE--VEELEAELEEKDERIERLERELSE---------A 453
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688598103 249 RcphsqdvEVLRGELcRKDEQWRERERRlaalemqlqdrsavVEELQQQLEEAAQRRHELQEQLEEASGHRSL 321
Cdd:COG2433 454 R-------SEERREI-RKDREISRLDRE--------------IERLERELEEERERIEELKRKLERLKELWKL 504
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
191-567 |
4.73e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 191 QVKELEEKLVDQTQEVERLRSELgaTDLEKQLEVLESENQRLKQELKTSHTQtscsaarcphsqdVEVLRGELCRKDEQW 270
Cdd:TIGR04523 322 KLEEIQNQISQNNKIISQLNEQI--SQLKKELTNSESENSEKQRELEEKQNE-------------IEKLKKENQSYKQEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 271 RERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQLntrlcddedtlrrhttvpqvkyvt 350
Cdd:TIGR04523 387 KNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEI------------------------ 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 351 KTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQrtssqlrQQLRTDRARLYGLLSKavgggNTEVTL 430
Cdd:TIGR04523 443 KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ-------KELKSKEKELKKLNEE-----KKELEE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 431 RLSkilmyegEMERAQGQLEAEMQSLEEEKNRvIEEAFIRAESEMKAVHENL--AGVRMNLLTLQPALRTLTCDYNCLKR 508
Cdd:TIGR04523 511 KVK-------DLTKKISSLKEKIEKLESEKKE-KESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKK 582
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 509 -QVQdfpymLEKAIAEAKQEICQVIGEVSSaNQELLRKYKREMNLRKKCHNELVRLKGNI 567
Cdd:TIGR04523 583 kQEE-----KQELIDQKEKEKKDLIKEIEE-KEKKISSLEKELEKAKKENEKLSSIIKNI 636
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
196-317 |
5.33e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 196 EEKLVDQTQEVERLRSELgatdlEKQLEVLESENQRLKQELKtshtqtscsaarcphsQDVEVLRgelcRKDEQWRERER 275
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEF-----EKELRERRNELQKLEKRLL----------------QKEENLD----RKLELLEKREE 110
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 688598103 276 RLAALEMQLQDRSAVVEELQQQLEEAaqrRHELQEQLEEASG 317
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEEL---IEEQLQELERISG 149
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
83-459 |
8.16e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 8.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 83 EFQARLRSEDAAKRLLLQRLQTHDHQLNQDNHQNQEYSPLyQEPQEQLRLQAGQLNQAASptgvrssTALTQRPVDFPSA 162
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL-EEELEELEAELAELQEELE-------ELLEQLSLATEEE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 163 LQvskvHSPERLQKVEGEQLAvitgLRTQVKELEEKLVDQTQEVERLRSELGATDLEKQLE-------------VLESEN 229
Cdd:COG4717 194 LQ----DLAEELEELQQRLAE----LEEELEEAQEELEELEEELEQLENELEAAALEERLKearlllliaaallALLGLG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 230 QRLKQELKTSHTQTSCSAA------------RCPHSQDVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQ 297
Cdd:COG4717 266 GSLLSLILTIAGVLFLVLGllallflllareKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 298 LEEAAQRRHELQEQLEEA--SGHRSLNDEQLNTRLCDDEDTLRRHttvpqvkyVTKTVEVESAQCKQALMEAQARNTALQ 375
Cdd:COG4717 346 IEELQELLREAEELEEELqlEELEQEIAALLAEAGVEDEEELRAA--------LEQAEEYQELKEELEELEEQLEELLGE 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 376 EQLSVQRQLLRELEQQLHDSQRTSSQLRQQ---LRTDRARLYGLLSKAVGGGNTEvtlrlskilmyegEMERAQGQLEAE 452
Cdd:COG4717 418 LEELLEALDEEELEEELEELEEELEELEEEleeLREELAELEAELEQLEEDGELA-------------ELLQELEELKAE 484
|
....*..
gi 688598103 453 MQSLEEE 459
Cdd:COG4717 485 LRELAEE 491
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
196-465 |
9.43e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 196 EEKLVDQTQEVERLRSELGATDLEKQLEVLESENQRLKQELKTS--------HTQTSCSAARCPHSQDVEVLRGELCRKD 267
Cdd:pfam07888 49 AQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSrekheeleEKYKELSASSEELSEEKDALLAQRAAHE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 268 EQWRERERRLAALEMQLQDRSAVVEELQQQLEEA-AQRRHELQEQleEASGHRSLNDEQLNTRLCDDEDTLRRHttVPQV 346
Cdd:pfam07888 129 ARIRELEEDIKTLTQRVLERETELERMKERAKKAgAQRKEEEAER--KQLQAKLQQTEEELRSLSKEFQELRNS--LAQR 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 347 KYVTKTVEVESAQCKQALMEAQaRNTALQEQLsvqRQLLRELEQQLHDSQRTSSQLRQQLR---TDRARLYGLLSKAVGG 423
Cdd:pfam07888 205 DTQVLQLQDTITTLTQKLTTAH-RKEAENEAL---LEELRSLQERLNASERKVEGLGEELSsmaAQRDRTQAELHQARLQ 280
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 688598103 424 GnTEVTLRLSK--ILMYEGEMERAQgQLEAEMQSLEEEKNRVIE 465
Cdd:pfam07888 281 A-AQLTLQLADasLALREGRARWAQ-ERETLQQSAEADKDRIEK 322
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
188-467 |
9.58e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.57 E-value: 9.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 188 LRTQVKELEEKLVDQTQEVErlrselgATDLEKQLEVLESENQRLKQELKTSHTQTSCSAARcphsqdvevlRGELCRKD 267
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEEKE-------EKDLHERLNGLESELAELDEEIERYEEQREQARET----------RDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 268 EQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEE----------ASGHRSLNDEQLNTR---LCDDE 334
Cdd:PRK02224 244 EEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEleeerddllaEAGLDDADAEAVEARreeLEDRD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 335 DTLRRHTTVPQVKYVTKTVEVESAqcKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDRARLy 414
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEEAESL--REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF- 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 415 gllskavggGNTEVTL-----RLSKILMYEGEMERAQGQLEAEMQSLEE--EKNRVIEEA 467
Cdd:PRK02224 401 ---------GDAPVDLgnaedFLEELREERDELREREAELEATLRTARErvEEAEALLEA 451
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
85-544 |
1.07e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 85 QARLRSEDAAKRLLLQRLQTHDHQLNQD-NHQNQEYSPLYQEPQEQLRLQAGQLNQAASptgvrSSTALTQRPVDFPSAL 163
Cdd:pfam15921 305 QEQARNQNSMYMRQLSDLESTVSQLRSElREAKRMYEDKIEELEKQLVLANSELTEART-----ERDQFSQESGNLDDQL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 164 Q--VSKVHSPERLQKVEGEQLAVI----TGLRTQVKELEEKLVDQTQEVERLRSELGAT------DLEKQLEVLESENQR 231
Cdd:pfam15921 380 QklLADLHKREKELSLEKEQNKRLwdrdTGNSITIDHLRRELDDRNMEVQRLEALLKAMksecqgQMERQMAAIQGKNES 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 232 L---------------------------KQELKTSH-TQTSCSAARCPHSQDVEVLRGELCR-----------------K 266
Cdd:pfam15921 460 LekvssltaqlestkemlrkvveeltakKMTLESSErTVSDLTASLQEKERAIEATNAEITKlrsrvdlklqelqhlknE 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 267 DEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQR-----RHELQEQLEEASGHRSLNDEQLNTR----LCDDEDTL 337
Cdd:pfam15921 540 GDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLvgqhgRTAGAMQVEKAQLEKEINDRRLELQefkiLKDKKDAK 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 338 RRH-------TTVPQVKYV---------TKTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLhdsQRTSSQ 401
Cdd:pfam15921 620 IRElearvsdLELEKVKLVnagserlraVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEM---ETTTNK 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 402 LRQQLRTDRARLY-------------GLLSKAVGGGNTEVTLRLSKILMYEGE---MERAQGQLEAEMQSLEEEKNRVIE 465
Cdd:pfam15921 697 LKMQLKSAQSELEqtrntlksmegsdGHAMKVAMGMQKQITAKRGQIDALQSKiqfLEEAMTNANKEKHFLKEEKNKLSQ 776
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688598103 466 EAFIRAESEMKAVHEnlagvrmnlltlqpaLRTLTCDYNCLKRQVQDFPYMLEKAIAEAKQeiCQVIgeVSSANQELLR 544
Cdd:pfam15921 777 ELSTVATEKNKMAGE---------------LEVLRSQERRLKEKVANMEVALDKASLQFAE--CQDI--IQRQEQESVR 836
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
201-407 |
1.09e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 46.48 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 201 DQTQEVERLRSELgaTDLEKQLEVLESENQRLKQELKTSHTQTSCSAARCP---------HSQDVEVLRGEL--CRKDEQ 269
Cdd:COG3096 833 DPEAELAALRQRR--SELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPqanlladetLADRLEELREELdaAQEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 270 W-RERERRLAALEMQ---LQDRSAVVEELQQQLEEAAQRRHELQEQL---------------EEASG----HRSLNdEQL 326
Cdd:COG3096 911 FiQQHGKALAQLEPLvavLQSDPEQFEQLQADYLQAKEQQRRLKQQIfalsevvqrrphfsyEDAVGllgeNSDLN-EKL 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 327 NTRLCDDEDTLR-----------RHTTVPQV------KYVTKTVEV-ESAQCKQAL-------MEAQARN--TALQEQLS 379
Cdd:COG3096 990 RARLEQAEEARReareqlrqaqaQYSQYNQVlaslksSRDAKQQTLqELEQELEELgvqadaeAEERARIrrDELHEELS 1069
|
250 260
....*....|....*....|....*...
gi 688598103 380 VQRQLLRELEQQLHDSQRTSSQLRQQLR 407
Cdd:COG3096 1070 QNRSRRSQLEKQLTRCEAEMDSLQKRLR 1097
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
173-416 |
1.15e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.83 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 173 RLQKVEGEQLAvitgLRTQVKELEEKLVDQTQEVERLRSELGAT-----DLEKQLEVLESENQRLKQELKTSHTQTSCSA 247
Cdd:pfam19220 77 RLSAAEGELEE----LVARLAKLEAALREAEAAKEELRIELRDKtaqaeALERQLAAETEQNRALEEENKALREEAQAAE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 248 ARCPHS-QDVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQL 326
Cdd:pfam19220 153 KALQRAeGELATARERLALLEQENRRLQALSEEQAAELAELTRRLAELETQLDATRARLRALEGQLAAEQAERERAEAQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 327 ntrlcddEDTLRRHTTvpqvkyvtktvevESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQL 406
Cdd:pfam19220 233 -------EEAVEAHRA-------------ERASLRMKLEALTARAAATEQLLAEARNQLRDRDEAIRAAERRLKEASIER 292
|
250
....*....|
gi 688598103 407 RTDRARLYGL 416
Cdd:pfam19220 293 DTLERRLAGL 302
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
183-496 |
1.27e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 183 AVITGLRTQVKELEEKLVDQTQEVERLRSELgaTDLEKQLEVLESENQRLKQELKTShtqtscsaarcphSQDVEVLRGE 262
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREEL--EQAREELEQLEEELEQARSELEQL-------------EEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 263 LCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQLNtRLCDDEDTLRRHTT 342
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK-ELEEQLESLQEELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 343 VPQVKYVTKTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDRARLYGLLSKAVG 422
Cdd:COG4372 168 ALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688598103 423 GGNTEVTLRLSKILMYEGEMERAQGQLEAEMQSLEEEKNRVIEEAFIRAESEMKAVHENLAGVRMNLLTLQPAL 496
Cdd:COG4372 248 KEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAAL 321
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
268-527 |
1.33e-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: 45.53 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 268 EQWRERERRLAALEMQLQdrsavveELQQQLEEAAQRRHELQEQLeeasghrslndEQLNTRLCDDEDTLRrhttvpqvk 347
Cdd:COG4942 20 DAAAEAEAELEQLQQEIA-------ELEKELAALKKEEKALLKQL-----------AALERRIAALARRIR--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 348 yvtkTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRT--------SSQLRQQLRtdRARLYGLLSK 419
Cdd:COG4942 73 ----ALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllsPEDFLDAVR--RLQYLKYLAP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 420 AVGGGNTEVTLRLSKILMYEGEMERAQGQLEAEMQSLEEEKNRVieeafiraESEMKAVHENLAGVRMNLLTLQPALRTL 499
Cdd:COG4942 147 ARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL--------EALKAERQKLLARLEKELAELAAELAEL 218
|
250 260
....*....|....*....|....*...
gi 688598103 500 TCDYNCLKRQVQDfpymLEKAIAEAKQE 527
Cdd:COG4942 219 QQEAEELEALIAR----LEAEAAAAAER 242
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
281-465 |
1.48e-04 |
|
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: 45.88 E-value: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 281 EMQLQDRSAVVEE--LQQQLEEAAqRRHELQEQLEEASGHRSLNDEQLNTRLCDDED-TLRRHTTVPQVKYVTKTVEVES 357
Cdd:pfam17380 286 ERQQQEKFEKMEQerLRQEKEEKA-REVERRRKLEEAEKARQAEMDRQAAIYAEQERmAMERERELERIRQEERKRELER 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 358 AQckqalmeaqarntalQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLrtDRARLYGLLSKAvgggntevtlRLSKILM 437
Cdd:pfam17380 365 IR---------------QEEIAMEISRMRELERLQMERQQKNERVRQEL--EAARKVKILEEE----------RQRKIQQ 417
|
170 180 190
....*....|....*....|....*....|..
gi 688598103 438 YEGEMERAQGQLEA----EMQSLEEEKNRVIE 465
Cdd:pfam17380 418 QKVEMEQIRAEQEEarqrEVRRLEEERAREME 449
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
172-565 |
1.54e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 172 ERLQKVEGEQLAVITgLRTQVKELEEKLVDQTQEVERLRSELGAtdLEKQLEVLESENQRLKqELKTSHTQTScsaarcp 251
Cdd:PRK03918 283 KELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEING--IEERIKELEEKEERLE-ELKKKLKELE------- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 252 hsQDVEVLRGELcRKDEQWRERERRLAALEMQLQDRSavVEELQQQLEEAAQRRHELQEQLEEASGHRSlndeQLNTRLC 331
Cdd:PRK03918 352 --KRLEELEERH-ELYEEAKAKKEELERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIG----ELKKEIK 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 332 DDEDTLRRhttvpqvkyvTKTVEVESAQCKQALMEAQARNtalqeqlsvqrqLLRELEQQLHDSQRTSSQLRQQLRTDRA 411
Cdd:PRK03918 423 ELKKAIEE----------LKKAKGKCPVCGRELTEEHRKE------------LLEEYTAELKRIEKELKEIEEKERKLRK 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 412 RLygllskavgggntevtLRLSKILMYEGEMeRAQGQLEAEMQSLEEEKNRVIEEAFIRAESEMKAVHENLAGVRMNLLT 491
Cdd:PRK03918 481 EL----------------RELEKVLKKESEL-IKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKS 543
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 688598103 492 LQPALRTLtcdyNCLKRQVQdfpyMLEKAIAEAKQEICQVIGEVSSANQELLRKYKREMNLRKKCHNELVRLKG 565
Cdd:PRK03918 544 LKKELEKL----EELKKKLA----ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKD 609
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
209-407 |
2.01e-04 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 44.67 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 209 LRSELGA-TDLEKQLEVLESENQRLKQELK------TSHTQTSCS-AARCPHSQ------DVEVLRGELCRKDEQWRERE 274
Cdd:pfam15742 36 LRYERGKnLDLKQHNSLLQEENIKIKAELKqaqqklLDSTKMCSSlTAEWKHCQqkirelELEVLKQAQSIKSQNSLQEK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 275 rrLAALEMQLQDRSAVVEELQQQLEEA---------AQRRHELQEQLEEASGHRS-----LNDEQLNTRLCD-DEDTLRR 339
Cdd:pfam15742 116 --LAQEKSRVADAEEKILELQQKLEHAhkvcltdtcILEKKQLEERIKEASENEAklkqqYQEEQQKRKLLDqNVNELQQ 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688598103 340 HTTVPQVKyvTKTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLR---ELEQQLHDSQRTSSQLRQQLR 407
Cdd:pfam15742 194 QVRSLQDK--EAQLEMTNSQQQLRIQQQEAQLKQLENEKRKSDEHLKsnqELSEKLSSLQQEKEALQEELQ 262
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
200-510 |
2.04e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 200 VDQTQEVERLRSELGatDLEKQLEVLESENQRLKQELKTSHTQTSCSAARCPHSQ--DVEVLRGELCRKDEQWRERE--- 274
Cdd:PRK04863 833 ADPEAELRQLNRRRV--ELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNllADETLADRVEEIREQLDEAEeak 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 275 -------RRLAALEMQ---LQDRSAVVEELQQQLEEAAQRRHELQEQLeeasghrslndeqlntRLCDDEDTLRRHttvp 344
Cdd:PRK04863 911 rfvqqhgNALAQLEPIvsvLQSDPEQFEQLKQDYQQAQQTQRDAKQQA----------------FALTEVVQRRAH---- 970
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 345 qVKYvtktvevESAQckqalmEAQARNTALQEQLsvqRQLLRELEQQLhdsqrtsSQLRQQLRTDRARLygllskavggg 424
Cdd:PRK04863 971 -FSY-------EDAA------EMLAKNSDLNEKL---RQRLEQAEQER-------TRAREQLRQAQAQL----------- 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 425 nTEVTLRLSKIlmyEGEMERAQGQLEAEMQSLEEEKNRVIEEAFIRAESEMKAVHENLAGVRM--------------NLL 490
Cdd:PRK04863 1016 -AQYNQVLASL---KSSYDAKRQMLQELKQELQDLGVPADSGAEERARARRDELHARLSANRSrrnqlekqltfceaEMD 1091
|
330 340
....*....|....*....|
gi 688598103 491 TLQPALRTLTCDYNCLKRQV 510
Cdd:PRK04863 1092 NLTKKLRKLERDYHEMREQV 1111
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
251-413 |
2.08e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 251 PHSQDVEVLRG---ELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSlndeqln 327
Cdd:PRK04863 510 HLAEQLQQLRMrlsELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRM------- 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 328 trlcddedTLRRhttvpQVKYVTKTVEvESAQCKQALMEAQARNTALQEQLSVQ---RQLLRELEQQLHDSQRTSSQLRQ 404
Cdd:PRK04863 583 --------ALRQ-----QLEQLQARIQ-RLAARAPAWLAAQDALARLREQSGEEfedSQDVTEYMQQLLERERELTVERD 648
|
....*....
gi 688598103 405 QLRTDRARL 413
Cdd:PRK04863 649 ELAARKQAL 657
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
174-447 |
2.10e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.49 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 174 LQKVEGEQLAVITGLRTQVKELEEKLVDQTQEVERLrsELGATDLEKQLEVLESENQRLKQELKTSHTQTSCSAArcphs 253
Cdd:pfam15921 718 MEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFL--EEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAG----- 790
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 254 qDVEVLRgelcrkdEQWRERERRLAALEMQLQDRSAVVEELQQ--QLEEAAQRRHELQEQLE--EASGHRSLNDEQLNTR 329
Cdd:pfam15921 791 -ELEVLR-------SQERRLKEKVANMEVALDKASLQFAECQDiiQRQEQESVRLKLQHTLDvkELQGPGYTSNSSMKPR 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 330 LCDDEDTLRRHTTVPQVK--------YVTKTV---EVESAQCKQALMEAQAR-NTALQEQLSVQRQLLRELEQQLHDSQR 397
Cdd:pfam15921 863 LLQPASFTRTHSNVPSSQstasflshHSRKTNalkEDPTRDLKQLLQELRSViNEEPTVQLSKAEDKGRAPSLGALDDRV 942
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 688598103 398 TSSQLRQQLRTDRARLYGLLSKAVGGGNTEVTLRlSKILMYEGEMERAQG 447
Cdd:pfam15921 943 RDCIIESSLRSDICHSSSNSLQTEGSKSSETCSR-EPVLLHAGELEDPSS 991
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
191-404 |
2.12e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.33 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 191 QVKELEEKLVDqtqEVERLRSELGATDLEKQLEVLESENQRLKQeLKTSHTQTSCSAARcphSQDVEVLRGELCRKDEQW 270
Cdd:COG3096 476 KAYELVCKIAG---EVERSQAWQTARELLRRYRSQQALAQRLQQ-LRAQLAELEQRLRQ---QQNAERLLEEFCQRIGQQ 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 271 RERErrlAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRslndEQLNTRlcddedtlrrhttVPQVKYVT 350
Cdd:COG3096 549 LDAA---EELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARI----KELAAR-------------APAWLAAQ 608
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 688598103 351 KTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQ 404
Cdd:COG3096 609 DALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIER 662
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
191-407 |
2.16e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.07 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 191 QVKELEEKLVDQTQEVERLRSELgaTDLEKQLEVLESENQRL----------KQELKTSHTQ----TSCSAARCPHSQDV 256
Cdd:pfam05622 191 QVQELHGKLSEESKKADKLEFEY--KKLEEKLEALQKEKERLiierdtlretNEELRCAQLQqaelSQADALLSPSSDPG 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 257 EVLRGEL--------------------CRKDEQWRERerrLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEAS 316
Cdd:pfam05622 269 DNLAAEImpaeireklirlqhenkmlrLGQEGSYRER---LTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 317 GHRSLNDEQlntrlCDDEDTLRRHTTVPQVKyvtktvevesaqckqaLMEAqarntalQEQLSVQRQLLRELEQ-QLHDS 395
Cdd:pfam05622 346 KALQEQGSK-----AEDSSLLKQKLEEHLEK----------------LHEA-------QSELQKKKEQIEELEPkQDSNL 397
|
250
....*....|..
gi 688598103 396 QRTSSQLRQQLR 407
Cdd:pfam05622 398 AQKIDELQEALR 409
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
268-474 |
2.37e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 268 EQWRERERRLAALEMQLQDrsavVEELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQLNTRlcddedtlrrhttvpqvk 347
Cdd:COG4717 71 KELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEKLLQLL------------------ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 348 yvtkTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDRARLYGLLSKAVgggnte 427
Cdd:COG4717 129 ----PLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLA------ 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 688598103 428 vtLRLSKILMYEGEMERAQGQLEAEMQSLEEEKNRVIEEAFIRAESE 474
Cdd:COG4717 199 --EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
76-493 |
2.74e-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: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 76 TLQERVCEFQARLRSEDAAKRLLLQRLQTHDHQLNQDNHQNQEYsplyqepQEQLRLQAGQLNQAASptgvRSSTALTQR 155
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL-------EEELEELEEELEELEE----ELEEAEEEL 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 156 pvdfpSALQVSKVHSPERLQKVEGEQLAVITGLRTQVKELEEKLVDQTQEVERLRSELGA-TDLEKQLEVLESENQRLKQ 234
Cdd:COG1196 354 -----EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAeEALLERLERLEEELEELEE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 235 ELKTShtqtscSAARCPHSQDVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEE 314
Cdd:COG1196 429 ALAEL------EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 315 ASG----HRSLNDEQLNTRLCDDEDTLRRHTTVPQ-----------VKYVTKTVEVESAQCKQALMEAQARNTALQEQLS 379
Cdd:COG1196 503 YEGflegVKAALLLAGLRGLAGAVAVLIGVEAAYEaaleaalaaalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKI 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 380 VQRQLLRELEQQLHDSQR---TSSQLRQQLRTDRARLYGLLSKAVGGGNTEVTLRLSKILMYEGEMERAQGQLEAEMQSL 456
Cdd:COG1196 583 RARAALAAALARGAIGAAvdlVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSL 662
|
410 420 430
....*....|....*....|....*....|....*..
gi 688598103 457 EEEKNRVIEEAFIRAESEMKAVHENLAGVRMNLLTLQ 493
Cdd:COG1196 663 TGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
267-469 |
3.00e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 267 DEQWRERERRLAALEMQLQ---------DRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRslndEQLNTRLCDDEDTL 337
Cdd:COG3206 181 EEQLPELRKELEEAEAALEefrqknglvDLSEEAKLLLQQLSELESQLAEARAELAEAEARL----AALRAQLGSGPDAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 338 RRHTTVPQVKyvtkTVEVESAQCKQALMEAQARNT-------ALQEQL-SVQRQLLRELEQQLHDSQRTSSQLRQQLRTD 409
Cdd:COG3206 257 PELLQSPVIQ----QLRAQLAELEAELAELSARYTpnhpdviALRAQIaALRAQLQQEAQRILASLEAELEALQAREASL 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 688598103 410 RARLYGLLSKAVGGGNTEVTLRlskilMYEGEMERAQGQLEAEMQSLEE---EKN------RVIEEAFI 469
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELR-----RLEREVEVARELYESLLQRLEEarlAEAltvgnvRVIDPAVV 396
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
196-570 |
3.46e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 196 EEKLVDQTQEVERLRSELGATD--LEKQLEVLESENQRL---KQELKTSHTQTSCSAARCPHSQDVEV-----------L 259
Cdd:pfam12128 477 REEQEAANAEVERLQSELRQARkrRDQASEALRQASRRLeerQSALDELELQLFPQAGTLLHFLRKEApdweqsigkviS 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 260 RGELCRKD---EQWRER-----------------------------ERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHE 307
Cdd:pfam12128 557 PELLHRTDldpEVWDGSvggelnlygvkldlkridvpewaaseeelRERLDKAEEALQSAREKQAAAEEQLVQANGELEK 636
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 308 LQEQLEEASghrslndeqlnTRLCDDEDTLRRHTTVPQvkyvtktveVESAQCKQALMEAQAR-NTALQEQLSVQRQLLR 386
Cdd:pfam12128 637 ASREETFAR-----------TALKNARLDLRRLFDEKQ---------SEKDKKNKALAERKDSaNERLNSLEAQLKQLDK 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 387 ELEQQLHDSQRTSSQLRQQLRTDRARLYGLLSKAVGggntevtlRLSKilmyegEMERAQGQLEAEMQSLEEEKNR---- 462
Cdd:pfam12128 697 KHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLA--------LLKA------AIAARRSGAKAELKALETWYKRdlas 762
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 463 --VIEEAFIRAESEMKAVH---ENLAGVRMNLLTLQPALR-TLTCDYNCLKRQVQDfpymLEKAIAEAKQEICQVIGEVS 536
Cdd:pfam12128 763 lgVDPDVIAKLKREIRTLErkiERIAVRRQEVLRYFDWYQeTWLQRRPRLATQLSN----IERAISELQQQLARLIADTK 838
|
410 420 430
....*....|....*....|....*....|....
gi 688598103 537 SANQELLRKykremnlRKKCHNELVRLKGNIRVL 570
Cdd:pfam12128 839 LRRAKLEME-------RKASEKQQVRLSENLRGL 865
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
252-457 |
3.99e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 252 HSQDVEVLRGELCRKDEQWRERERRL--------------AALEMQLQDRS--------------------AVVEELQQQ 297
Cdd:PRK04863 284 HLEEALELRRELYTSRRQLAAEQYRLvemarelaelneaeSDLEQDYQAASdhlnlvqtalrqqekieryqADLEELEER 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 298 LEEAAQRRHELQEQLEEASGHRSLNDE---QLNTRLCDdedtlrrhttVPQVKYVTKTVEVESAQCKQALMEAQ------ 368
Cdd:PRK04863 364 LEEQNEVVEEADEQQEENEARAEAAEEevdELKSQLAD----------YQQALDVQQTRAIQYQQAVQALERAKqlcglp 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 369 --------ARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLrqqlrtdrARLYGLLSKAVGGGNTEVTLRLSKILMYEG 440
Cdd:PRK04863 434 dltadnaeDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQF--------EQAYQLVRKIAGEVSRSEAWDVARELLRRL 505
|
250 260
....*....|....*....|.
gi 688598103 441 EMERAQ----GQLEAEMQSLE 457
Cdd:PRK04863 506 REQRHLaeqlQQLRMRLSELE 526
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
254-563 |
5.81e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 254 QDVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRSLNDEQLNTRLcdd 333
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ--- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 334 edtlrrhTTVPQVKYVTKTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQ--QLHDSQRTSSQLRQQLRTDRA 411
Cdd:COG4372 122 -------KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQelQALSEAEAEQALDELLKEANR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 412 RLYGLLSKAVGGGNTEVTLRLSKILMYEGEMERAQGQLEAEmQSLEEEKNRVIEEAFIRAESEMKAVHENLAGVRMNLLT 491
Cdd:COG4372 195 NAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL-SALLDALELEEDKEELLEEVILKEIEELELAILVEKDT 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688598103 492 LQPALRTLTCDYNCLKRQVQDFPYMLEKAIAEAKQEICQVIGEVSSANQELLRKYKREMNLRKKCHNELVRL 563
Cdd:COG4372 274 EEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
163-512 |
5.86e-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: 44.01 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 163 LQVSKVHSPERLQKVEGEQLAVI---TGLRTQVKELEEKLVDQT----QEVERLRSelgATDLEKQLEVLESENQ-RLKQ 234
Cdd:pfam01576 122 LQLEKVTTEAKIKKLEEDILLLEdqnSKLSKERKLLEERISEFTsnlaEEEEKAKS---LSKLKNKHEAMISDLEeRLKK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 235 ELKTShtqtscsaarcphsQDVEVLR----GELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEE------AAQR 304
Cdd:pfam01576 199 EEKGR--------------QELEKAKrkleGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEetaqknNALK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 305 RH--------ELQEQLEEASGHRSLNDEQ----------LNTRLcddEDTLrrHTTVPQVKYVTKTvEVESAQCKQAL-M 365
Cdd:pfam01576 265 KIreleaqisELQEDLESERAARNKAEKQrrdlgeeleaLKTEL---EDTL--DTTAAQQELRSKR-EQEVTELKKALeE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 366 EAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQL---RQQLRTDRARLYGLLsKAVGGGNTEVtlrlskilmyEGEM 442
Cdd:pfam01576 339 ETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLekaKQALESENAELQAEL-RTLQQAKQDS----------EHKR 407
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 443 ERAQGQLEaEMQSLEEEKNRVIEEAfirAESEMKAVHEnLAGVRMNLLTLQPALRTLTCDYNCLKRQVQD 512
Cdd:pfam01576 408 KKLEGQLQ-ELQARLSESERQRAEL---AEKLSKLQSE-LESVSSLLNEAEGKNIKLSKDVSSLESQLQD 472
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
93-412 |
5.88e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 93 AAKRLLLQRLQTHDHQLNQDNHQNQEYSPLYqepqEQLRLQAGQLNQAASPTGVRSSTALTQRPVDFpsALQVSKVHSPE 172
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQL----EQAKEGLSALNRLLPRLNLLADETLADRVEEI--REQLDEAEEAK 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 173 RLQKVEGEQLAVITGLRTQVKELEEKLVDQTQEVERLRSELgaTDLEKQLEVLESENQRlKQELKTSHTQTSCSAArcph 252
Cdd:PRK04863 911 RFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQ--RDAKQQAFALTEVVQR-RAHFSYEDAAEMLAKN---- 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 253 SQDVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEAsGHRslNDEQLNTRLCD 332
Cdd:PRK04863 984 SDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDL-GVP--ADSGAEERARA 1060
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 333 DEDTLrrhttvpqvkyvtktvevesaqcKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDRAR 412
Cdd:PRK04863 1061 RRDEL-----------------------HARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNAKAG 1117
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
161-480 |
7.61e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.14 E-value: 7.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 161 SALQVSKVHSPERLQKVE-GEQLAVITG-----LRTQVKELEEKL--VDQTQEVERLRSElgatDLEKQLEVLESENQRL 232
Cdd:pfam05622 31 NSLQQENKKLQERLDQLEsGDDSGTPGGkkyllLQKQLEQLQEENfrLETARDDYRIKCE----ELEKEVLELQHRNEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 233 K------QELKTSHT---QTSCSAARCphSQDVEVLR------GELCRKDEQWRERE--------------RRLAALEMQ 283
Cdd:pfam05622 107 TslaeeaQALKDEMDilrESSDKVKKL--EATVETYKkkledlGDLRRQVKLLEERNaeymqrtlqleeelKKANALRGQ 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 284 LQDRSAVVEELQQQLEEAAQRR-------HELQEQLE-----------EASGHRSLNDEQLNTRLCDDEDTLRRHTTVPQ 345
Cdd:pfam05622 185 LETYKRQVQELHGKLSEESKKAdklefeyKKLEEKLEalqkekerliiERDTLRETNEELRCAQLQQAELSQADALLSPS 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 346 VKYVTKTV-EVESAQCKQALMEAQARNTALQE-QLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDRARLYGL------L 417
Cdd:pfam05622 265 SDPGDNLAaEIMPAEIREKLIRLQHENKMLRLgQEGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELqqqveeL 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 688598103 418 SKA---VGGGNTEVTLRLSKILMYEGEMERAQGQLEAEMQSLEEEKNRV----------IEEAFIRAESEMKAVHE 480
Cdd:pfam05622 345 QKAlqeQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQdsnlaqkideLQEALRKKDEDMKAMEE 420
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
172-314 |
9.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 9.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 172 ERLQKVEGEQLAVITGLR----TQVKELEEKLvdqtQEVERLRSE-LGATDLEKQLEVLESENQRLKQELKTSHTQTSCS 246
Cdd:PRK03918 563 KKLDELEEELAELLKELEelgfESVEELEERL----KELEPFYNEyLELKDAEKELEREEKELKKLEEELDKAFEELAET 638
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688598103 247 AARcphsqdVEVLRGELCRK-----DEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEE 314
Cdd:PRK03918 639 EKR------LEELRKELEELekkysEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
171-462 |
1.09e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 171 PERLQKVEGEQLA-VITGLRTQVKELEEKLVDQTQEVERLRSELgatDLEKQLEVLESENQRLKQELKTShtqtscsaar 249
Cdd:PRK02224 455 PECGQPVEGSPHVeTIEEDRERVEELEAELEDLEEEVEEVEERL---ERAEDLVEAEDRIERLEERREDL---------- 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 250 cphSQDVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHR-SLNDeqLNT 328
Cdd:PRK02224 522 ---EELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIeSLER--IRT 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 329 RLCDDEDtlrrhttvpqvkyvtKTVEVESAQCKQAlmEAQARNTALQEQLSVQRQLLRELEQQLHDSQrtssqlRQQLRT 408
Cdd:PRK02224 597 LLAAIAD---------------AEDEIERLREKRE--ALAELNDERRERLAEKRERKRELEAEFDEAR------IEEARE 653
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 688598103 409 DRARLYGLLSKavgggnteVTLRLSKILMYEGEMERAQGQLEAEMQSLEEEKNR 462
Cdd:PRK02224 654 DKERAEEYLEQ--------VEEKLDELREERDDLQAEIGAVENELEELEELRER 699
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
271-477 |
1.11e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.35 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 271 RERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHrslndeqlntrlcDDEDTLRrhttvpqvkyvt 350
Cdd:COG1842 33 RDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEK-------------GREDLAR------------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 351 ktvevESAQcKQALMEAQArnTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDRARLYGL-----LSKAVGGGN 425
Cdd:COG1842 88 -----EALE-RKAELEAQA--EALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAkaqekVNEALSGID 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 688598103 426 T-EVTLRLSkilmyegEMERAQGQLEAEMQSLEE-EKNRVIEEAFIRAESEMKA 477
Cdd:COG1842 160 SdDATSALE-------RMEEKIEEMEARAEAAAElAAGDSLDDELAELEADSEV 206
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
172-410 |
1.45e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 172 ERLQKVEGEQlAVITGLRTQVKELEEKLVDQTQEVERLRSELgaTDLEKQLEVLESEN-------------QRLKQELKT 238
Cdd:TIGR00606 727 EMLGLAPGRQ-SIIDLKEKEIPELRNKLQKVNRDIQRLKNDI--EEQETLLGTIMPEEesakvcltdvtimERFQMELKD 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 239 SHTQTSCSAARCPHS---QDVEVLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQ----------QLEEAAQRR 305
Cdd:TIGR00606 804 VERKIAQQAAKLQGSdldRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSktnelkseklQIGTNLQRR 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 306 HELQEQLEEASGH-RSLNDE--QLNTRLCDDEDTLRRHTTVPQVKYVTKTVEVESAQCKQALMEAQARNT---------- 372
Cdd:TIGR00606 884 QQFEEQLVELSTEvQSLIREikDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymkdienk 963
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 688598103 373 ---ALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDR 410
Cdd:TIGR00606 964 iqdGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMR 1004
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
252-423 |
1.66e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 252 HSQDVEVLRGELCRKDEQWRERERRL--------------AALEMQLQD--------RSAV------------VEELQQQ 297
Cdd:COG3096 283 LSERALELRRELFGARRQLAEEQYRLvemareleelsareSDLEQDYQAasdhlnlvQTALrqqekieryqedLEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 298 LEEAAQRRHELQEQLEEASGHRSLNDEQ---LNTRLCDDEDTLR-RHTTVPQVKYVTKTVEVESAQCKQALME---AQAR 370
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEARLEAAEEEvdsLKSQLADYQQALDvQQTRAIQYQQAVQALEKARALCGLPDLTpenAEDY 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 688598103 371 NTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQlrtdrarlYGLLSKAVGG 423
Cdd:COG3096 443 LAAFRAKEQQATEEVLELEQKLSVADAARRQFEKA--------YELVCKIAGE 487
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
170-419 |
2.00e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.87 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 170 SPERLQKVEGEqlavITGLRTQVKELEEKLVDQTQEVERLRS------ELGATDLEKQLEVL----ESENQRLKQELKts 239
Cdd:COG5185 273 NAESSKRLNEN----ANNLIKQFENTKEKIAEYTKSIDIKKAtesleeQLAAAEAEQELEESkretETGIQNLTAEIE-- 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 240 HTQTSCSAARCPHSQDVEVLRGElcrkdEQWRERERRLAALEMQLqdrSAVVEELQQQLEEAAQRRHELQEQLEEASGHR 319
Cdd:COG5185 347 QGQESLTENLEAIKEEIENIVGE-----VELSKSSEELDSFKDTI---ESTKESLDEIPQNQRGYAQEILATLEDTLKAA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 320 SLNDEQLNTrlcddedtlrrhttvpQVKYVTKTVEVESAQCKQALMEAQARNTALQEQLSVQRQ-----LLRELEQQLHD 394
Cdd:COG5185 419 DRQIEELQR----------------QIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEeaydeINRSVRSKKED 482
|
250 260
....*....|....*....|....*
gi 688598103 395 SQRTSSQLRQQLRTDRARLYGLLSK 419
Cdd:COG5185 483 LNEELTQIESRVSTLKATLEKLRAK 507
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
215-466 |
2.18e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 215 ATDLEKQLEVL------ESENQRLKQELKTSHTQTscsAARCPHSQDVEVLRGELCRKDEQWRERERRLAALEMQLQD-- 286
Cdd:PRK11281 38 EADVQAQLDALnkqkllEAEDKLVQQDLEQTLALL---DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEet 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 287 ----RSAVVEELQQQLEEAAQRRHELQEQLEEAsghrslndeqlNTRLCddedTLRrhtTVPqvkyvtktvevESAQckQ 362
Cdd:PRK11281 115 retlSTLSLRQLESRLAQTLDQLQNAQNDLAEY-----------NSQLV----SLQ---TQP-----------ERAQ--A 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 363 ALMEAQAR----------NTALQEQLSVQRQLLRELEQQLHDSQrtSSQLRQQLRtdrarlygllskavggGNTEVTLRL 432
Cdd:PRK11281 164 ALYANSQRlqqirnllkgGKVGGKALRPSQRVLLQAEQALLNAQ--NDLQRKSLE----------------GNTQLQDLL 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 688598103 433 SKILMYegeMERAQGQLEAEMQSLEE---EKNRVIEE 466
Cdd:PRK11281 226 QKQRDY---LTARIQRLEHQLQLLQEainSKRLTLSE 259
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
172-404 |
2.40e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 172 ERLQKVEGEQLAVITGLRTQVKELEEKLVDQTQE----VERLRSELGATDLEKQLEVLESENQRLKQELKTSHTQTSCSA 247
Cdd:PTZ00121 1584 EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKA 1663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 248 ARCPHSQDVEVLRGELCRKDEqwrERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEasghRSLNDEQLN 327
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAE---EDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE----NKIKAEEAK 1736
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688598103 328 TRlcDDEDTLRRHTTVPQVKYVTKTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLR-ELEQQLHDSQRTSSQLRQ 404
Cdd:PTZ00121 1737 KE--AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRmEVDKKIKDIFDNFANIIE 1812
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
172-470 |
2.82e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 172 ERLQKVEGEQLAVITGLRTQVKELEEKLVDQTQEVERLRS-ELGATDLEKQLEVLESENQRLKQELKTshtqtscsaarc 250
Cdd:COG4372 66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESlQEEAEELQEELEELQKERQDLEQQRKQ------------ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 251 phsqdvevLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLE--EAAQRRHELQEQLEEASghRSLNDEQLNT 328
Cdd:COG4372 134 --------LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalSEAEAEQALDELLKEAN--RNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 329 RLCDDEDTLRRHTTVPQVKYVTKTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRT 408
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688598103 409 DRARLYGLLSKAVGGGNTEVTLRLSKILMYEGEMERAQGQLEAEMQSLEEEKNRVIEEAFIR 470
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQL 345
|
|
| Rootletin |
pfam15035 |
Ciliary rootlet component, centrosome cohesion; |
275-413 |
3.03e-03 |
|
Ciliary rootlet component, centrosome cohesion;
Pssm-ID: 464459 [Multi-domain] Cd Length: 190 Bit Score: 40.02 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 275 RRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEasghrslndeqLNTRLCDDEDTLRRHTTVPQVKYVTKTVE 354
Cdd:pfam15035 2 RKLQAYQEAQQRQAQLVQKLQAKVLQYKKRCSELEQQLLE-----------KTSELEKTELLLRKLTLEPRLQRLEREHS 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 688598103 355 VESAQCKQALMEAQARNTALQEQLSVqrqllreLEQQLHDSQRTSSQLR---QQLRTDRARL 413
Cdd:pfam15035 71 ADLEEALIRLEEERQRSESLSQVNSL-------LREQLEQASRANEALRedlQKLTNDWERA 125
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
325-458 |
3.91e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 40.60 E-value: 3.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 325 QLNTRLCDDedtlrrhttvpQVKYVTKtvEVESAQckQALMEAQARNTALQEQLSV---------QRQLLRELEQQLHDS 395
Cdd:COG3524 169 QLSERARED-----------AVRFAEE--EVERAE--ERLRDAREALLAFRNRNGIldpeataeaLLQLIATLEGQLAEL 233
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688598103 396 QRTSSQLRQQLRTDRARLYGL-------------LSKAVGGGNTEVTL--RLSKILMYEGEMERAQGQLEAEMQSLEE 458
Cdd:COG3524 234 EAELAALRSYLSPNSPQVRQLrrriaalekqiaaERARLTGASGGDSLasLLAEYERLELEREFAEKAYTSALAALEQ 311
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
193-456 |
3.99e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.19 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 193 KELEEKLVDQTQEVERLRSELGATDLEKQL-----EVLESENQrLKQELKTSHtQTSCSAARCPHSQdVEVLRgelcrkd 267
Cdd:PRK10929 82 AELRQQLNNERDEPRSVPPNMSTDALEQEIlqvssQLLEKSRQ-AQQEQDRAR-EISDSLSQLPQQQ-TEARR------- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 268 eQWRERERRL---------------AALEMQLQDRSAVVEELQ-QQLeeAAQRRHELQEQLEEASGHRSlndEQLNTRLC 331
Cdd:PRK10929 152 -QLNEIERRLqtlgtpntplaqaqlTALQAESAALKALVDELElAQL--SANNRQELARLRSELAKKRS---QQLDAYLQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 332 DDEDTLrrhttvpqvkYVTKTVEVESAQCKQALMEAQARN--TALQEQLSVQRQLLRELEQQ------LHDSQRTSS--- 400
Cdd:PRK10929 226 ALRNQL----------NSQRQREAERALESTELLAEQSGDlpKSIVAQFKINRELSQALNQQaqrmdlIASQQRQAAsqt 295
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 401 -QLRQQLRTDRARLYGL-LSKAVGGgntevTLR--LSKIlmyeGEMERAQgQLEAEMQSL 456
Cdd:PRK10929 296 lQVRQALNTLREQSQWLgVSNALGE-----ALRaqVARL----PEMPKPQ-QLDTEMAQL 345
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
180-315 |
4.41e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.50 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 180 EQLAVITGLRTQVKELEEKlvdqtqeverlrselgATDLEKQLEVLESENQRLKQELKtshtqtscsAARcphsQDVEVL 259
Cdd:pfam13851 23 NNLELIKSLKEEIAELKKK----------------EERNEKLMSEIQQENKRLTEPLQ---------KAQ----EEVEEL 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 688598103 260 RGELC--RKD-EQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEA 315
Cdd:pfam13851 74 RKQLEnyEKDkQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAA 132
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
366-537 |
4.57e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 366 EAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDRARLYGllskaVGGGNTEvtlrlskilmyegemera 445
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRG-----NGGDRLE------------------ 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 446 qgQLEAEMQSLEEEKNRViEEAFIRAESEMKAVHENLAGVRMNLLTLQPALRTLTCDYNCLKRQVQDFPYMLEKAIAEAK 525
Cdd:COG4913 342 --QLEREIERLERELEER-ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
170
....*....|..
gi 688598103 526 QEICQVIGEVSS 537
Cdd:COG4913 419 RELRELEAEIAS 430
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
185-406 |
4.95e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 185 ITGLRTQVKELEEKLVDQTQEVERLRSELgaTDLEKQLEVLESE-----NQRLKQELKTSHTQTscsaarcpHSQDVEVL 259
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENEL--NLLEKEKLNIQKNidkikNKLLKLELLLSNLKK--------KIQKNKSL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 260 RGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEasghRSLNDEQLNTRLCDDEDTLrr 339
Cdd:TIGR04523 217 ESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSE----KQKELEQNNKKIKELEKQL-- 290
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 688598103 340 httvpqvkyvtKTVEVESAQCKQAlmEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQL 406
Cdd:TIGR04523 291 -----------NQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQI 344
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
221-413 |
5.29e-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: 39.52 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 221 QLEVLESENQRLKQELKTshtqtscsaarcphsqdvevLRGELCRKDEQWRERERRLAALEMQLQDRSAVVEELQQQLEE 300
Cdd:COG1579 11 DLQELDSELDRLEHRLKE--------------------LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 301 AAQRRHELQEQLEEASGHRSLND-----EQLNTRLCDDEDTLRRhttvpqvkyvtktVEVESAQCKQALMEAQARNTALQ 375
Cdd:COG1579 71 VEARIKKYEEQLGNVRNNKEYEAlqkeiESLKRRISDLEDEILE-------------LMERIEELEEELAELEAELAELE 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 688598103 376 EQLsvqRQLLRELEQQLHDSQRTssqlRQQLRTDRARL 413
Cdd:COG1579 138 AEL---EEKKAELDEELAELEAE----LEELEAEREEL 168
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
271-480 |
5.44e-03 |
|
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: 39.28 E-value: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 271 RERERRLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEAsghRSLNDEQLntrlcddedtlrrhttvpqvkyvt 350
Cdd:pfam04012 32 RDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAA---LTKGNEEL------------------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 351 ktveVESAQCKQALMEAQARntALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDRARLYGL-----LSKAVGGGN 425
Cdd:pfam04012 85 ----AREALAEKKSLEKQAE--ALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKARLKAAkaqeaVQTSLGSLS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 688598103 426 TEVTLRLSKilmyegEMERAQGQLEAEMQSLEEEKNRVIEEAFIRAESEMKAVHE 480
Cdd:pfam04012 159 TSSATDSFE------RIEEKIEEREARADAAAELASAVDLDAKLEQAGIQMEVSE 207
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
190-427 |
5.72e-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: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 190 TQVKELEEKLVDQTQEVERLRSELgaTDLEKQLEVLESENQRLKQELKTshTQTSCSAARcphsQDVEVLRGELCRKDEQ 269
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAEL--DALQAELEELNEEYNELQAELEA--LQAEIDKLQ----AEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 270 WRERER--------------------------RLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEAsghrslnd 323
Cdd:COG3883 88 LGERARalyrsggsvsyldvllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL-------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 324 EQLNTRLcddedtlrrhttvpqvkyvtktvEVESAQCKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLR 403
Cdd:COG3883 160 EALKAEL-----------------------EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
250 260
....*....|....*....|....
gi 688598103 404 QQLRTDRARLYGLLSKAVGGGNTE 427
Cdd:COG3883 217 AAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
196-317 |
6.23e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.10 E-value: 6.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 196 EEKLVDQTQEVERLRSELGATDLEKQLEVLESENQRLKQElktshtqtscsaarcphsqdvEVLRgelcRKDEQWRERER 275
Cdd:pfam12072 52 KEALLEAKEEIHKLRAEAERELKERRNELQRQERRLLQKE---------------------ETLD----RKDESLEKKEE 106
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 688598103 276 RLAALEMQLQDRSAVVEELQQQLEEAAQRRhelQEQLEEASG 317
Cdd:pfam12072 107 SLEKKEKELEAQQQQLEEKEEELEELIEEQ---RQELERISG 145
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
206-323 |
7.02e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.20 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 206 VERLRSELGaTDLEKQLEVLES-ENQRLKQELKTSHTQtscsAARcphsQDVEVLRGELCRKDEQWRERERRL-AALEMQ 283
Cdd:PRK00409 504 IEEAKKLIG-EDKEKLNELIASlEELERELEQKAEEAE----ALL----KEAEKLKEELEEKKEKLQEEEDKLlEEAEKE 574
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 688598103 284 LQDR--------SAVVEELQ--QQLEEAAQRRHELQEQleeasgHRSLND 323
Cdd:PRK00409 575 AQQAikeakkeaDEIIKELRqlQKGGYASVKAHELIEA------RKRLNK 618
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
268-487 |
7.72e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 40.32 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 268 EQWRERERRLAALEMQLQDRSAVVEELQQQL---------------EEAAQRRHELQEQLEEASGHRSLNDEQLNT--RL 330
Cdd:COG3096 843 QRRSELERELAQHRAQEQQLRQQLDQLKEQLqllnkllpqanlladETLADRLEELREELDAAQEAQAFIQQHGKAlaQL 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 331 CDDEDTLRRH-TTVPQVKYVTKTVEVESAQCKQ---ALMEAQARNTAL-----QEQLSVQRQLLRELEQQLHDSQRTSSQ 401
Cdd:COG3096 923 EPLVAVLQSDpEQFEQLQADYLQAKEQQRRLKQqifALSEVVQRRPHFsyedaVGLLGENSDLNEKLRARLEQAEEARRE 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 402 LRQQLRTDRARLygllskavgggnTEVTLRLSKIlmyEGEMERAQGQLEAEMQSLEEEKNRVIEEAFIRAESEMKAVHEN 481
Cdd:COG3096 1003 AREQLRQAQAQY------------SQYNQVLASL---KSSRDAKQQTLQELEQELEELGVQADAEAEERARIRRDELHEE 1067
|
....*.
gi 688598103 482 LAGVRM 487
Cdd:COG3096 1068 LSQNRS 1073
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
269-413 |
7.81e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 39.68 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 269 QWRERERRLAALEMQLQDRSAVVEELQQQleEAAQRRHeLQEQLEEA---SGHRSLndeQLntrLCDDEDTLRRHTTVPQ 345
Cdd:PRK11637 90 KLRETQNTLNQLNKQIDELNASIAKLEQQ--QAAQERL-LAAQLDAAfrqGEHTGL---QL---ILSGEESQRGERILAY 160
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688598103 346 VKYVTKTVEVESAQCKQALMEAQARNTALQEQLSVQRQLLRE-------LEQQLHDSQRTSSQLRQQLRTDRARL 413
Cdd:PRK11637 161 FGYLNQARQETIAELKQTREELAAQKAELEEKQSQQKTLLYEqqaqqqkLEQARNERKKTLTGLESSLQKDQQQL 235
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
260-499 |
8.16e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.02 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 260 RGELCRKDEQWRERER-----RLAALEMQLQDRSAVVEELQQQLEEAAQRRHELQEQLEEASGHRslndEQLNTrLCDDE 334
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEkdlheRLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR----EELET-LEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 335 DTLRRHTTVPQVKYVTKTVEVESAqcKQALMEAQARNTALQEQLSVQRQLLRELEQQLHDSQRTSSQLRQQLRTDRArly 414
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDL--RERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRV--- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 415 gllskAVGGGNTEVTLRLSKILMYEGEMERAQ---GQLEAEMQSLE-------------EEKNRVIEEAFI-------RA 471
Cdd:PRK02224 336 -----AAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAReavedrreeieelEEEIEELRERFGdapvdlgNA 410
|
250 260
....*....|....*....|....*...
gi 688598103 472 ESEMKAVHENLAGVRMNLLTLQPALRTL 499
Cdd:PRK02224 411 EDFLEELREERDELREREAELEATLRTA 438
|
|
| PRK03992 |
PRK03992 |
proteasome-activating nucleotidase; Provisional |
172-234 |
8.40e-03 |
|
proteasome-activating nucleotidase; Provisional
Pssm-ID: 179699 [Multi-domain] Cd Length: 389 Bit Score: 39.82 E-value: 8.40e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688598103 172 ERLQKVEGEqlavITGLRTQVKELEEKLVDQTQEVERLRSELgatdlekqlEVLESENQRLKQ 234
Cdd:PRK03992 1 ERLEALEER----NSELEEQIRQLELKLRDLEAENEKLEREL---------ERLKSELEKLKS 50
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
164-237 |
8.50e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 39.84 E-value: 8.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 164 QVSKVHSPERLQKVEGE--QL-AVITGLRTQVKELEEKLVDQTQEVERLRSELGATDLEKQLEV--------LESENQRL 232
Cdd:COG2433 398 EREKEHEERELTEEEEEirRLeEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIrkdreisrLDREIERL 477
|
....*
gi 688598103 233 KQELK 237
Cdd:COG2433 478 ERELE 482
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
175-314 |
8.69e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 40.19 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688598103 175 QKVEGEQLAVITGLRTQVkelEEKLVDQTQEVERLRSELgatdlEKQLEVLESENQRLKQELKTShTQTSCSAARCPHSQ 254
Cdd:NF041483 505 ERVRTEAIERATTLRRQA---EETLERTRAEAERLRAEA-----EEQAEEVRAAAERAARELREE-TERAIAARQAEAAE 575
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 688598103 255 DVEVLRgelcrkdeqwRERERRLAALEMQLQD--------RSAVVEELQQQLEEAAQRRHELQEQLEE 314
Cdd:NF041483 576 ELTRLH----------TEAEERLTAAEEALADaraeaeriRREAAEETERLRTEAAERIRTLQAQAEQ 633
|
|
| |
