|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
7-338 |
0e+00 |
|
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: 631.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 7 IPVRVALRCRPLVPKENNEGCKMCLTFVPGEQQVIVGTEKSFTYDYVFDPSAEQEEVYNSAVAPLIKGLFKGYNATVLAY 86
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 87 GQTGSGKTYSMGGAYTHNqENEPTVGVIPRTVIALFREIHQRP-EWEFNLKVSYLEIYNEEILDLLYAARDKTNTISIRE 165
Cdd:cd01372 81 GQTGSGKTYTMGTAYTAE-EDEEQVGIIPRAIQHIFKKIEKKKdTFEFQLKVSFLEIYNEEIRDLLDPETDKKPTISIRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 166 DPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQRKEG---------DKNNSFRSKL 236
Cdd:cd01372 160 DSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNgpiapmsadDKNSTFTSKF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 237 HLVDLAGSERQKKTKAEGDRLKEGISINRGLLCLGNVISALGDESKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSP 316
Cdd:cd01372 240 HFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSP 319
|
330 340
....*....|....*....|..
gi 18202613 317 ADSNMEETLNTLRYADRARKIK 338
Cdd:cd01372 320 ADSNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
8-344 |
3.17e-158 |
|
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: 475.52 E-value: 3.17e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 8 PVRVALRCRPLVPKENNEGCKMCLTFVPGEQQVIV-------GTEKSFTYDYVFDPSAEQEEVYNSAVAPLIKGLFKGYN 80
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTvrspknrQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 81 ATVLAYGQTGSGKTYSMGGaythnqeNEPTVGVIPRTVIALFREI-HQRPEWEFNLKVSYLEIYNEEILDLLYAARDKtn 159
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG-------TPDSPGIIPRALKDLFEKIdKREEGWQFSVKVSYLEIYNEKIRDLLNPSSKK-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 160 tISIREDPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQRKEGDKNNSFR-SKLHL 238
Cdd:smart00129 152 -LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKaSKLNL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 239 VDLAGSERQKKTKAEGDRLKEGISINRGLLCLGNVISALGDESKKGgFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPAD 318
Cdd:smart00129 231 VDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSR-HIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSS 309
|
330 340
....*....|....*....|....*.
gi 18202613 319 SNMEETLNTLRYADRARKIKNKPIVN 344
Cdd:smart00129 310 SNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
14-337 |
6.45e-153 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 461.27 E-value: 6.45e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 14 RCRPLVPKENNEGCKMCLTFVPGEQQVI-------VGTEKSFTYDYVFDPSAEQEEVYNSAVAPLIKGLFKGYNATVLAY 86
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVesshltnKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 87 GQTGSGKTYSMGGAYTHnqeneptVGVIPRTVIALFREIHQRPE-WEFNLKVSYLEIYNEEILDLLYAARDKTNTISIRE 165
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQ-------PGIIPRALEDLFDRIQKTKErSEFSVKVSYLEIYNEKIRDLLSPSNKNKRKLRIRE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 166 DPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQ--RKEGDKNNSFRSKLHLVDLAG 243
Cdd:pfam00225 154 DPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQrnRSTGGEESVKTGKLNLVDLAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 244 SERQKKT-KAEGDRLKEGISINRGLLCLGNVISALGDesKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNME 322
Cdd:pfam00225 234 SERASKTgAAGGQRLKEAANINKSLSALGNVISALAD--KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYE 311
|
330
....*....|....*
gi 18202613 323 ETLNTLRYADRARKI 337
Cdd:pfam00225 312 ETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
8-335 |
9.97e-146 |
|
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: 442.46 E-value: 9.97e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 8 PVRVALRCRPLVPKENNeGCKMCLTFVPGEQQVI------VGTEKSFTYDYVFDPSAEQEEVYNSAVAPLIKGLFKGYNA 81
Cdd:cd00106 1 NVRVAVRVRPLNGREAR-SAKSVISVDGGKSVVLdppknrVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 82 TVLAYGQTGSGKTYSMGGAYTHNQeneptvGVIPRTVIALFREIHQRPE--WEFNLKVSYLEIYNEEILDLLyaARDKTN 159
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPDPEQR------GIIPRALEDIFERIDKRKEtkSSFSVSASYLEIYNEKIYDLL--SPVPKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 160 TISIREDPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQR-KEGDKNNSFRSKLHL 238
Cdd:cd00106 152 PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRnREKSGESVTSSKLNL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 239 VDLAGSERQKKTKAEGDRLKEGISINRGLLCLGNVISALGDesKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPAD 318
Cdd:cd00106 232 VDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD--GQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSS 309
|
330
....*....|....*..
gi 18202613 319 SNMEETLNTLRYADRAR 335
Cdd:cd00106 310 ENFEETLSTLRFASRAK 326
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
9-344 |
4.42e-120 |
|
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: 376.31 E-value: 4.42e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 9 VRVALRCRPLVPKENNEGCKmCLTFVPGEQQVIV-------------GTEKSFTYDYVF------DPS-AEQEEVYNSAV 68
Cdd:cd01365 3 VKVAVRVRPFNSREKERNSK-CIVQMSGKETTLKnpkqadknnkatrEVPKSFSFDYSYwshdseDPNyASQEQVYEDLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 69 APLIKGLFKGYNATVLAYGQTGSGKTYSMGGAythnqENEPtvGVIPRTVIALFREIHQRPEWE--FNLKVSYLEIYNEE 146
Cdd:cd01365 82 EELLQHAFEGYNVCLFAYGQTGSGKSYTMMGT-----QEQP--GIIPRLCEDLFSRIADTTNQNmsYSVEVSYMEIYNEK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 147 ILDLLyAARDKTN--TISIREDPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQRK 224
Cdd:cd01365 155 VRDLL-NPKPKKNkgNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 225 ---EGDKNNSFRSKLHLVDLAGSERQKKTKAEGDRLKEGISINRGLLCLGNVISALGDESKKGG-----FVPYRDSKLTR 296
Cdd:cd01365 234 hdaETNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKSkkkssFIPYRDSVLTW 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 18202613 297 LLQDSLGGNSHTLMIACVSPADSNMEETLNTLRYADRARKIKNKPIVN 344
Cdd:cd01365 314 LLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
9-337 |
7.47e-118 |
|
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: 369.10 E-value: 7.47e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 9 VRVALRCRPLVPKENNEGCKMCLTFVPGEQQVIVGT--------EKSFTYDYVFDPSAEQEEVYNSAVAPLIKGLFKGYN 80
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNpkatanepPKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 81 ATVLAYGQTGSGKTYSMGGaythNQENEPTVGVIPRTVIALFREIHQRPEW-EFNLKVSYLEIYNEEILDLLyaARDKTN 159
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEG----KREDPELRGIIPNSFAHIFGHIARSQNNqQFLVRVSYLEIYNEEIRDLL--GKDQTK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 160 TISIREDPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIE--QRKEGDKNNSFRSKLH 237
Cdd:cd01371 157 RLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIEcsEKGEDGENHIRVGKLN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 238 LVDLAGSERQKKTKAEGDRLKEGISINRGLLCLGNVISALGDesKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPA 317
Cdd:cd01371 237 LVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD--GKSTHIPYRDSKLTRLLQDSLGGNSKTVMCANIGPA 314
|
330 340
....*....|....*....|
gi 18202613 318 DSNMEETLNTLRYADRARKI 337
Cdd:cd01371 315 DYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
9-337 |
3.94e-115 |
|
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: 362.43 E-value: 3.94e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 9 VRVALRCRPLVPKENNEGCKMC--------LTFVPGEQQVIV--------------GTEKSFTYDYVFDPSAEQEEVYNS 66
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIvkvmdnhmLVFDPKDEEDGFfhggsnnrdrrkrrNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 67 AVAPLIKGLFKGYNATVLAYGQTGSGKTYSMGGAythnqENEPtvGVIPRTVIALFREI-HQRPEWEFNLKVSYLEIYNE 145
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGT-----PQEP--GLMVLTMKELFKRIeSLKDEKEFEVSMSYLEIYNE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 146 EILDLLyaaRDKTNTISIREDPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQ--R 223
Cdd:cd01370 155 TIRDLL---NPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQqdK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 224 KEGDKNNSFRSKLHLVDLAGSERQKKTKAEGDRLKEGISINRGLLCLGNVISALGDESKKGGFVPYRDSKLTRLLQDSLG 303
Cdd:cd01370 232 TASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLLKDSLG 311
|
330 340 350
....*....|....*....|....*....|....
gi 18202613 304 GNSHTLMIACVSPADSNMEETLNTLRYADRARKI 337
Cdd:cd01370 312 GNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
9-339 |
4.25e-114 |
|
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: 358.83 E-value: 4.25e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 9 VRVALRCRPLVPKENNEGCKmCLTFVPGEQQVIV-----GTEKSFTYDYVFDPSAEQEEVYNSaVAPLIKGLFKGYNATV 83
Cdd:cd01366 4 IRVFCRVRPLLPSEENEDTS-HITFPDEDGQTIEltsigAKQKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 84 LAYGQTGSGKTYSMGGaythnqeNEPTVGVIPRTVIALFREIHQRPE--WEFNLKVSYLEIYNEEILDLLYAARDKTNTI 161
Cdd:cd01366 82 FAYGQTGSGKTYTMEG-------PPESPGIIPRALQELFNTIKELKEkgWSYTIKASMLEIYNETIRDLLAPGNAPQKKL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 162 SIREDPKEG-IKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQRKEGDKNNSfRSKLHLVD 240
Cdd:cd01366 155 EIRHDSEKGdTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEIS-VGKLNLVD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 241 LAGSERQKKTKAEGDRLKEGISINRGLLCLGNVISALgdeSKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSN 320
Cdd:cd01366 234 LAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL---RQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESN 310
|
330
....*....|....*....
gi 18202613 321 MEETLNTLRYADRARKIKN 339
Cdd:cd01366 311 LNETLNSLRFASKVNSCEL 329
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
9-337 |
6.27e-111 |
|
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: 350.09 E-value: 6.27e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 9 VRVALRCRPLVPKENNEGCKmCLTFVPGEQQVIVGTEK-SFTYDYVFDPSAEQEEVYNSAVAPLIKGLFKGYNATVLAYG 87
Cdd:cd01374 2 ITVTVRVRPLNSREIGINEQ-VAWEIDNDTIYLVEPPStSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 88 QTGSGKTYSMGGAythnqENEPtvGVIPRTVIALFREIHQRPEWEFNLKVSYLEIYNEEILDLLyaARDKTNtISIREDP 167
Cdd:cd01374 81 QTSSGKTFTMSGD-----EDEP--GIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLL--SPTSQN-LKIRDDV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 168 KEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQRKEGDKNNS--FRSKLHLVDLAGSE 245
Cdd:cd01374 151 EKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGtvRVSTLNLIDLAGSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 246 RQKKTKAEGDRLKEGISINRGLLCLGNVISALGdESKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNMEETL 325
Cdd:cd01374 231 RAAQTGAAGVRRKEGSHINKSLLTLGTVISKLS-EGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETL 309
|
330
....*....|..
gi 18202613 326 NTLRYADRARKI 337
Cdd:cd01374 310 NTLKFASRAKKI 321
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
9-346 |
1.00e-108 |
|
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: 345.46 E-value: 1.00e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 9 VRVALRCRPLVPKENNEGCKMCLTFVPGEQQVIVGTE--------KSFTYDYVFDPSAEQEEVYNSAVAPLIKGLFKGYN 80
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVRTGgladksstKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 81 ATVLAYGQTGSGKTYSMGGAYT----HNQENEPTVGVIPRTVIALFREIHQRPEwEFNLKVSYLEIYNEEILDLLYAARD 156
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMEGDRSpneeYTWELDPLAGIIPRTLHQLFEKLEDNGT-EYSVKVSYLEIYNEELFDLLSPSSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 157 KTNTISIREDP--KEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQRKEGDKNNSFR- 233
Cdd:cd01364 163 VSERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEELVk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 234 -SKLHLVDLAGSERQKKTKAEGDRLKEGISINRGLLCLGNVISALGDeskKGGFVPYRDSKLTRLLQDSLGGNSHTLMIA 312
Cdd:cd01364 243 iGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLGGRTKTSIIA 319
|
330 340 350
....*....|....*....|....*....|....
gi 18202613 313 CVSPADSNMEETLNTLRYADRARKIKNKPIVNTD 346
Cdd:cd01364 320 TISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
9-337 |
8.60e-108 |
|
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: 342.00 E-value: 8.60e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 9 VRVALRCRPLVPKENNEGCKMCLTFvPGEQQVIVGT---EKSFTYDYVFDPSAEQEEVYNSAVAPLIKGLFKGYNATVLA 85
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKF-DPEDTVVIATsetGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 86 YGQTGSGKTYSMGGAyTHNQENEptvGVIPRTVIALFREIHQRPE-WEFNLKVSYLEIYNEEILDLLYAARDKtntISIR 164
Cdd:cd01369 83 YGQTSSGKTYTMEGK-LGDPESM---GIIPRIVQDIFETIYSMDEnLEFHVKVSYFEIYMEKIRDLLDVSKTN---LSVH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 165 EDPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQRKEGDKnNSFRSKLHLVDLAGS 244
Cdd:cd01369 156 EDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETE-KKKSGKLYLVDLAGS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 245 ERQKKTKAEGDRLKEGISINRGLLCLGNVISALGDesKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNMEET 324
Cdd:cd01369 235 EKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD--GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESET 312
|
330
....*....|...
gi 18202613 325 LNTLRYADRARKI 337
Cdd:cd01369 313 LSTLRFGQRAKTI 325
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
8-346 |
1.41e-102 |
|
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: 328.70 E-value: 1.41e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 8 PVRVALRCRPLVPKENNEGCKMCLTFVPGEQQVIVG-TEKSFTYDYVFDPSAEQEEVYNSAVAPLIKGLFKGYNATVLAY 86
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 87 GQTGSGKTYSMGG------AYTHNQEneptvGVIPRTVIALFREIHQRPE-----WEFNLKVSYLEIYNEEILDLLyaar 155
Cdd:cd01373 82 GQTGSGKTYTMWGpsesdnESPHGLR-----GVIPRIFEYLFSLIQREKEkagegKSFLCKCSFLEIYNEQIYDLL---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 156 DKTNT-ISIREDPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQR-KEGDKNNSFR 233
Cdd:cd01373 153 DPASRnLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWeKKACFVNIRT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 234 SKLHLVDLAGSERQKKTKAEGDRLKEGISINRGLLCLGNVISALGDESK-KGGFVPYRDSKLTRLLQDSLGGNSHTLMIA 312
Cdd:cd01373 233 SRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgKQRHVCYRDSKLTFLLRDSLGGNAKTAIIA 312
|
330 340 350
....*....|....*....|....*....|....
gi 18202613 313 CVSPADSNMEETLNTLRYADRARKIKNKPIVNTD 346
Cdd:cd01373 313 NVHPSSKCFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
42-571 |
4.30e-90 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 302.43 E-value: 4.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 42 VGTEKSFTYDYVFDPSAEQEEVYNSAVAPLIKGLFKGYNATVLAYGQTGSGKTYSMGGaythnQENEPtvGVIPRTVIAL 121
Cdd:COG5059 52 KSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG-----TEEEP--GIIPLSLKEL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 122 FREIHQRPEW-EFNLKVSYLEIYNEEILDLLyaaRDKTNTISIREDPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTV 200
Cdd:COG5059 125 FSKLEDLSMTkDFAVSISYLEIYNEKIYDLL---SPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTT 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 201 ASTAMNSQSSRSHAIFTISIEQRKEgDKNNSFRSKLHLVDLAGSERQKKTKAEGDRLKEGISINRGLLCLGNVISALGDE 280
Cdd:COG5059 202 ASTEINDESSRSHSIFQIELASKNK-VSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDK 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 281 sKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNMEETLNTLRYADRARKIKNKPIVN----TDPQAAELQR-L 355
Cdd:COG5059 281 -KKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNsssdSSREIEEIKFdL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 356 KLQVQELQVLLLQAHGGTLPvLNSMEPSENLQSLMERNKNLEKENG---KLSRELGEAAVQTAQFLEKIIMTEQQNEKLG 432
Cdd:COG5059 360 SEDRSEIEILVFREQSQLSQ-SSLSGIFAYMQSLKKETETLKSRIDlimKSIISGTFERKKLLKEEGWKYKSTLQFLRIE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 433 SKM--EELKQHAACKVNLQRLVETLEdQELKDNVEVIQNLQQVIVQLqdessgiagsieamdEEAASFPVPEEDSGEKRS 510
Cdd:COG5059 439 IDRllLLREEELSKKKTKIHKLNKLR-HDLSSLLSSIPEETSDRVES---------------EKASKLRSSASTKLNLRS 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18202613 511 SDGFTT--NHALRQAQLSKELIELNKALvmkealakkmAQNDRQLEPIQSEYLNNIKHLESEV 571
Cdd:COG5059 503 SRSHSKfrDHLNGSNSSTKELSLNQVDL----------AGSERKVSQSVGELLRETQSLNKSL 555
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
8-335 |
5.65e-85 |
|
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: 279.39 E-value: 5.65e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 8 PVRVALRCRPLVPKENNEGCKMCLTFVPGEQQVIV-----GTEKSFTYDYVFDPSAEQEEVYNSAVAPLIKGLFKGYNAT 82
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELAdprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNAT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 83 VLAYGQTGSGKTYSMggaytHNQENEPtvGVIPRTVIALFReIHQRPEWEFNLKVSYLEIYNEEILDLLyaaRDKTNTIS 162
Cdd:cd01376 81 VFAYGSTGAGKTFTM-----LGSPEQP--GLMPLTVMDLLQ-MTRKEAWALSFTMSYLEIYQEKILDLL---EPASKELV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 163 IREDPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQRKEGDKNNSFRSKLHLVDLA 242
Cdd:cd01376 150 IREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRTGKLNLIDLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 243 GSERQKKTKAEGDRLKEGISINRGLLCLGNVISALGDESKKggfVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNME 322
Cdd:cd01376 230 GSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLPR---IPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQ 306
|
330
....*....|...
gi 18202613 323 ETLNTLRYADRAR 335
Cdd:cd01376 307 DTLSTLNFAARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
8-333 |
2.27e-79 |
|
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: 264.16 E-value: 2.27e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 8 PVRVALRCRPLVPKENNEGcKMCLTFVPGEQQVIVGTEK------------SFTYDYVFDPSAEQEEVYNSAVAPLIKGL 75
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKK-EIDVVSVPSKLTLIVHEPKlkvdltkyienhTFRFDYVFDESSSNETVYRSTVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 76 FKGYNATVLAYGQTGSGKTYSMGGAYTHNQENEPtvgvIPRTVIA-LFREIHQrPEWEFNLKV--SYLEIYNEEILDLLy 152
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKG----IYALAARdVFRLLNK-LPYKDNLGVtvSFFEIYGGKVFDLL- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 153 aarDKTNTISIREDPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQRKEgdknNSF 232
Cdd:cd01367 154 ---NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGT----NKL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 233 RSKLHLVDLAGSERQKKTKAEG-DRLKEGISINRGLLCLGNVISALGDESKKggfVPYRDSKLTRLLQDSL-GGNSHTLM 310
Cdd:cd01367 227 HGKLSFVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQNKAH---IPFRGSKLTQVLKDSFiGENSKTCM 303
|
330 340
....*....|....*....|...
gi 18202613 311 IACVSPADSNMEETLNTLRYADR 333
Cdd:cd01367 304 IATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
44-335 |
1.18e-76 |
|
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: 256.74 E-value: 1.18e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 44 TEKSFTYDYVFDpSAEQEEVYNSAVAPLIKGLFKGYNATVLAYGQTGSGKTYSMGGAythnQENEPTVGVIPRTVIALFR 123
Cdd:cd01375 46 EDWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGG----TENYKHRGIIPRALQQVFR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 124 EIHQRPEWEFNLKVSYLEIYNEEILDLL----YAARDKTnTISIREDPKEGIKICGLTERDVKTALDTLSCLEQGNSSRT 199
Cdd:cd01375 121 MIEERPTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVT-PMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 200 VASTAMNSQSSRSHAIFTISIEQRKEGDKNNSFR-SKLHLVDLAGSERQKKTKAEGDRLKEGISINRGLLCLGNVISALG 278
Cdd:cd01375 200 IASHTMNKNSSRSHCIFTIHLEAHSRTLSSEKYItSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALS 279
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 18202613 279 DesKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNMEETLNTLRYADRAR 335
Cdd:cd01375 280 D--KDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
8-335 |
1.14e-74 |
|
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: 251.54 E-value: 1.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 8 PVRVALRCRPLVPKENNEGCKMCLTFV--------PGEQQVIVGTEKS-------FTYDYVFDPSAEQEEVYNSAVAPLI 72
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVInsttvvlhPPKGSAANKSERNggqketkFSFSKVFGPNTTQKEFFQGTALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 73 KGLFKGYNATVLAYGQTGSGKTYSMGGaythnqeNEPTVGVIPRTVIALFREIHqrpewEFNLKVSYLEIYNEEILDLL- 151
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTMQG-------SPGDGGILPRSLDVIFNSIG-----GYSVFVSYIEIYNEYIYDLLe 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 152 ---YAARDKTNTISIREDPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQ------ 222
Cdd:cd01368 150 pspSSPTKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQapgdsd 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 223 -RKEGDKNNSFRSKLHLVDLAGSERQKKTKAEGDRLKEGISINRGLLCLGNVISALGDESKKG--GFVPYRDSKLTRLLQ 299
Cdd:cd01368 230 gDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGtnKMVPFRDSKLTHLFQ 309
|
330 340 350
....*....|....*....|....*....|....*.
gi 18202613 300 DSLGGNSHTLMIACVSPADSNMEETLNTLRYADRAR 335
Cdd:cd01368 310 NYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
9-344 |
1.09e-66 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 247.16 E-value: 1.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 9 VRVALRCRPLVPKENNEgckMCLTFVPGEQQVIVGteKSFTYDYVFDPSAEQEEVYNSAVAPLIKGLFKGYNATVLAYGQ 88
Cdd:PLN03188 100 VKVIVRMKPLNKGEEGE---MIVQKMSNDSLTING--QTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 89 TGSGKTYSM-GGAYTHNQEN--EPTVGVIPRTVIALFREI------HQRPEWEFNLKVSYLEIYNEEILDLLYAARdktN 159
Cdd:PLN03188 175 TGSGKTYTMwGPANGLLEEHlsGDQQGLTPRVFERLFARIneeqikHADRQLKYQCRCSFLEIYNEQITDLLDPSQ---K 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 160 TISIREDPKEGIKICGLTERDVKTALDTLSCLEQGNSSRTVASTAMNSQSSRSHAIFTISIEQR--KEGDKNNSFR-SKL 236
Cdd:PLN03188 252 NLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRckSVADGLSSFKtSRI 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 237 HLVDLAGSERQKKTKAEGDRLKEGISINRGLLCLGNVISALGDESKKGG--FVPYRDSKLTRLLQDSLGGNSHTLMIACV 314
Cdd:PLN03188 332 NLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKqrHIPYRDSRLTFLLQESLGGNAKLAMVCAI 411
|
330 340 350
....*....|....*....|....*....|
gi 18202613 315 SPADSNMEETLNTLRYADRARKIKNKPIVN 344
Cdd:PLN03188 412 SPSQSCKSETFSTLRFAQRAKAIKNKAVVN 441
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
30-316 |
1.93e-20 |
|
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: 89.71 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 30 CLTFVPGEQQVIVGTEKSFTYDYVFDPSAEQEEVYNSAvAPLIKGLFKGYN-ATVLAYGQTGSGKTYSMggaythnqene 108
Cdd:cd01363 2 LVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGESGAGKTETM----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 109 ptVGVIPRTVIALFreihqrpewefnlkvSYLEIYNEEILDLLYaardktntisiredpkegiKICGLTERDVKTALDTL 188
Cdd:cd01363 70 --KGVIPYLASVAF---------------NGINKGETEGWVYLT-------------------EITVTLEDQILQANPIL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 189 scleqgNSSRTvASTAMNSQSSRSHAIFTIsieqrkegdknnsfrsklhLVDLAGSERqkktkaegdrlkegisINRGLL 268
Cdd:cd01363 114 ------EAFGN-AKTTRNENSSRFGKFIEI-------------------LLDIAGFEI----------------INESLN 151
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 18202613 269 CLGNVISAlgdeskkggfvpyrdskltrllqdslggnSHTLMIACVSP 316
Cdd:cd01363 152 TLMNVLRA-----------------------------TRPHFVRCISP 170
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
9-151 |
7.09e-19 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 84.19 E-value: 7.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 9 VRVALRCRPLVPKEnnegCKMCLTFVPGEQQVIVGTEKSFTYDYVFDPSAEQEEVYN--SAvapLIKGLFKGYNATVLAY 86
Cdd:pfam16796 22 IRVFARVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQeiSQ---LVQSCLDGYNVCIFAY 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18202613 87 GQTGSGKTysmggaythnqeneptVGVIPRTVIALFREIHQ-RPEWEFNLKVSYLEIYNEEILDLL 151
Cdd:pfam16796 95 GQTGSGSN----------------DGMIPRAREQIFRFISSlKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
448-1001 |
8.18e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.64 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 448 LQRLVETLEDQELKDNVEVIQNLQQVIVQLQDESSGIAGSIEAMDEEAASFPVPEEDSGEKRSSDGFTTNHALRQA-QLS 526
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKAdEAK 1308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 527 KELIELNKALVMK----------EALAKKMAQNDRQLEPIQSEYLNNIKHLES---EVGVLQKEKEELILALHSAKKDNN 593
Cdd:PTZ00121 1309 KKAEEAKKADEAKkkaeeakkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAaeeKAEAAEKKKEEAKKKADAAKKKAE 1388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 594 QAKLSERRRKRLQELEGQMTELKKKLGEQSKLLKLRESTEKTvakmnqeiqgMKMQRVQLMRQMKEDAEKFRTWKQQKTK 673
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK----------KKADEAKKKAEEAKKADEAKKKAEEAKK 1458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 674 EVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKEALQRQKEAMEKRKDSQSKGMEGAAsrvKNWLANE 753
Cdd:PTZ00121 1459 AEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK---KAEEAKK 1535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 754 VEVLVSTEEAQR--HLNDLLEDRKilAQDIAQLKQKTDAGERIPTKIRRRTYTVAELENLEEEASVTKQIESLETEMELR 831
Cdd:PTZ00121 1536 ADEAKKAEEKKKadELKKAEELKK--AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 832 SAQIADLQQKLLDAdgEEEMVKRRWETISNIMEAKCALKYLITELVSSKVAGSKLESSVKQNRAHVADLQKNIFEERNQM 911
Cdd:PTZ00121 1614 KAEEAKIKAEELKK--AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA 1691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 912 AEM--ETEHQSQLMQLEQHHQEKILYLlSQLQQKQASVPVTIEELPAEEitEREKQLMERLKFQDEEIEKMKALCEKNQQ 989
Cdd:PTZ00121 1692 EALkkEAEEAKKAEELKKKEAEEKKKA-EELKKAEEENKIKAEEAKKEA--EEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
570
....*....|..
gi 18202613 990 LLQENDMYKQKL 1001
Cdd:PTZ00121 1769 KAEEIRKEKEAV 1780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
436-980 |
8.51e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 8.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 436 EELKQHAACKVNLQRLVETLEDQElkdnvEVIQNLQQVIVQLQDESSGIAGSIEAMDEEAASfpvpEEDSGEKRSSDgft 515
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELE-----AELEELEAELEELEAELAELEAELEELRLELEE----LELELEEAQAE--- 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 516 tnHALRQAQLSKELIELNKALVMKEALAKKMAQNDRQLEPIQSEYLN---NIKHLESEVGVLQKEKEELILALHSAKK-- 590
Cdd:COG1196 290 --EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEleeELEELEEELEEAEEELEEAEAELAEAEEal 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 591 DNNQAKLSERRRKRLQELEGQMTELKKKLGEQSKLLKLR---ESTEKTVAKMNQEIQGMKMQRVQLMRQMKEDAEKFRTw 667
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEeaeEALLERLERLEEELEELEEALAELEEEEEEEEEALEE- 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 668 KQQKTKEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKEAL-QRQKEAMEKRKDSQSKGMEGAASRV 746
Cdd:COG1196 447 AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEaDYEGFLEGVKAALLLAGLRGLAGAV 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 747 KNWLA--NEVEVLVSTEEAQRHLNDLLEDRKILAQDIAQLKQKTD--AGERIPTKIRRRTYTVAELENLEEEASVTKQIE 822
Cdd:COG1196 527 AVLIGveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLVAS 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 823 SLETEMELRSAQIADLQQKLLDADGEEEMVKRRWETISNIMEAKCALKYLITELVSSKVAGSKLESSVKQNRAHVADLQK 902
Cdd:COG1196 607 DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAE 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 903 NIFEERNQMAEMETEHQSQLMQLEQHHQEKILYLLSQLQQKQ---------------------ASVPVTIEELPAEEITE 961
Cdd:COG1196 687 RLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEqleaereelleelleeeelleEEALEELPEPPDLEELE 766
|
570
....*....|....*....
gi 18202613 962 REKQLMERlkfqdeEIEKM 980
Cdd:COG1196 767 RELERLER------EIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
405-978 |
2.96e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 405 RELGEAAVQTAQFLEKIIMTEQQNEKLGSKMEEL-KQHAACKVNLQRLVETLEDQELKDNvEVIQNLQQVIVQLQDESSG 483
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELeAELAELEAELEELRLELEELELELE-EAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 484 IAGSIEAMDEEAASFpvpEEDSGEKRSSDGFTTNHALRQAQLSKELIELNKALvmkEALAKKMAQNDRQLEPIQSEYLNN 563
Cdd:COG1196 304 IARLEERRRELEERL---EELEEELAELEEELEELEEELEELEEELEEAEEEL---EEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 564 IKHLESEVGVLQKEKEELILALHSAKKDNNQAKLSERRRKRLQElegqmtELKKKLGEQSKLLKLRESTEKTVAKMNQEI 643
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE------ELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 644 QgmkmqrvqlmrqmkedaekfrtwkqqktkEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKEAL-Q 722
Cdd:COG1196 452 A-----------------------------ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEaD 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 723 RQKEAMEKRKDSQSKGMEGAASRVKNWLA--NEVEVLVSTEEAQRHLNDLLEDRKILAQDIAQLKQKTD-AGERIPTKIR 799
Cdd:COG1196 503 YEGFLEGVKAALLLAGLRGLAGAVAVLIGveAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgRATFLPLDKI 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 800 RRTYTVAELENLEEEASVTKQIESLETEMELRSAQIADLQQKLLDADGEEEMVKRRWETISNimeakcALKYLITELVSS 879
Cdd:COG1196 583 RARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAG------RLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 880 KVAGSKLESSVKQNRAHVADLQKNIFEERNQMAEMETEHQSQLMQLEQHHQEKILYLLSQLQQKQASVPVTIEELPAEEI 959
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570
....*....|....*....
gi 18202613 960 TEREKQLMERLKFQDEEIE 978
Cdd:COG1196 737 LLEELLEEEELLEEEALEE 755
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
649-1004 |
1.46e-09 |
|
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: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 649 QRVQLMRQmKEDAEKFRtwkqqktkeviQLKEKDRKRQYELLKLE-RDFQKQANVLRRKTEEAASANKRLKEALQRQKEA 727
Cdd:COG1196 201 QLEPLERQ-AEKAERYR-----------ELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 728 MEKRKDSQskgmegaasrvknwlanevevlvstEEAQRHLNDLLEDRKILAQDIAQLKQktdagERIPTKIRRRTYTVAE 807
Cdd:COG1196 269 LEELRLEL-------------------------EELELELEEAQAEEYELLAELARLEQ-----DIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 808 LENLEEEASVTKQIESLETEMELRSAQIADLQQKLLDADGEEEMVKRRWETISNIMEAKcalkylitelvsskvagsklE 887
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA--------------------E 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 888 SSVKQNRAHVADLQKNIFEERNQMAEMETEHQSQLMQLEQHHQEKIlyllsQLQQKQASVpvtieelpAEEITEREKQLM 967
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE-----ELEEALAEL--------EEEEEEEEEALE 445
|
330 340 350
....*....|....*....|....*....|....*..
gi 18202613 968 ERLKFQDEEIEKMKALCEKNQQLLQENDMYKQKLALL 1004
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
550-866 |
1.03e-08 |
|
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: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 550 DRQLEPIQS---------EYLNNIKHLESEVGVLQ-KEKEELILALHSAKKDNNQAKLSERRRkrLQELEGQMTELKKKL 619
Cdd:TIGR02168 199 ERQLKSLERqaekaerykELKAELRELELALLVLRlEELREELEELQEELKEAEEELEELTAE--LQELEEKLEELRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 620 GEQSKLL----KLRESTEKTVAKMNQEIQGMKMQRVQLMRQMKEDAEKFRTWKQQKtkeviqlkekdrkrqyelLKLERD 695
Cdd:TIGR02168 277 SELEEEIeelqKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL------------------DELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 696 FQKQANVLRRKTEEAASANKRLKEAlQRQKEAMEKRKDSQSKGMEGAASRVKNwLANEVEVLVST-EEAQRHLNDLLEDR 774
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEEL-EAELEELESRLEELEEQLETLRSKVAQ-LELQIASLNNEiERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 775 KILAQDIAQLKQKTDAGERIPTKIRrrtytvaELENLEEEASVTKQIESLETEMELRSAQIADLQQKLLDADGEEEMVKR 854
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAE-------LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
330
....*....|..
gi 18202613 855 RWETISNIMEAK 866
Cdd:TIGR02168 490 RLDSLERLQENL 501
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
391-765 |
3.48e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 58.23 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 391 ERNKNLEKENGKLSRELGEAAVQTAQFLEKIIMTEQQNEKLGSKMEELKQHAACKVNLQRLVETLED----QELKDNVEV 466
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkkkaDEAKKKAEE 1442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 467 IQNLQQviVQLQDESSGIAGSIEAMDEEAASFPVPEEDSGEKRSSDGF---------TTNHALRQAQLSKELIELNKALV 537
Cdd:PTZ00121 1443 AKKADE--AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAkkkaeeakkKADEAKKAAEAKKKADEAKKAEE 1520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 538 MKEALAKKMAQNDRQLEPIQSEylNNIKHLESEVGVLQKEKEELILALHSAKKDNNQAKLSERRRKRLQELEGQMTELKK 617
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKA--EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 618 KLGEQSKLLKLRESTEKTVAKMNQEiqgmKMQRVQLMRQMKEDAEKFRTWKQQKTKEVIQLKEKDRKRQYELLKLERDFQ 697
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAE----ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDK 1674
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18202613 698 KQANVLRRKTEEaasankRLKEALQRQKEAMEKRKDSQSKGMEGAASRVKNWLANEVEV-LVSTEEAQR 765
Cdd:PTZ00121 1675 KKAEEAKKAEED------EKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnKIKAEEAKK 1737
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
405-793 |
1.64e-07 |
|
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: 55.84 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 405 RELGEAAVQTAQFLEKIIMTEQQNEKLGSKMEELKQHAACKVNLQRLVETLEDQELKDNVEVIQNLQQVIVQLQDEssgi 484
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE---- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 485 agsieamdeeaasfpvpeedsgekrssdgfttnhalrQAQLSKELIELNKALvmkEALAKKMAQNDRQLEPIQSEYLNNI 564
Cdd:TIGR02169 253 -------------------------------------LEKLTEEISELEKRL---EEIEQLLEELNKKIKDLGEEEQLRV 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 565 KhleSEVGVLQKEKEELILALhsAKKDNNQAKLSERRRK---RLQELEGQMTELKKKLGEQSKLlklrestektVAKMNQ 641
Cdd:TIGR02169 293 K---EKIGELEAEIASLERSI--AEKERELEDAEERLAKleaEIDKLLAEIEELEREIEEERKR----------RDKLTE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 642 EIQGMKMQRVQLMRQMKEDAEKFRTWKQqktkEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKEAL 721
Cdd:TIGR02169 358 EYAELKEELEDLRAELEEVDKEFAETRD----ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18202613 722 QRQKEAMEKRKDSQS--KGMEGAASRVKNWLANEVEVLVSTEEAQRHLNDLLEDrkiLAQDIAQLKQKTDAGER 793
Cdd:TIGR02169 434 AKINELEEEKEDKALeiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSK---LQRELAEAEAQARASEE 504
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
391-915 |
1.86e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 391 ERNKNLEKENGKLSRELGEAAvqtaqflEKIIMTEQQNEKLGSKMEELKQHAACKVNLQRLVETLEdQELKDNVEVIQNL 470
Cdd:PRK03918 193 ELIKEKEKELEEVLREINEIS-------SELPELREELEKLEKEVKELEELKEEIEELEKELESLE-GSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 471 QQVIVQLQDEssgiagsIEAMDEEAASFPVPEEDsgekrssdgfttnhALRQAQLSKELIELNKALvmkEALAKKMAQND 550
Cdd:PRK03918 265 EERIEELKKE-------IEELEEKVKELKELKEK--------------AEEYIKLSEFYEEYLDEL---REIEKRLSRLE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 551 RQLEPIQsEYLNNIKHLESEVGVLQKEKEELilalhsaKKDNNQAKLSERRRKRLQELEGQMTELKKKLGEQS------- 623
Cdd:PRK03918 321 EEINGIE-ERIKELEEKEERLEELKKKLKEL-------EKRLEELEERHELYEEAKAKKEELERLKKRLTGLTpekleke 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 624 --KLLKLRESTEKTVAKMNQEIQGMKMQRVQLMRQM----------------------KEDAEKFRTWKQQKTKEVIQLK 679
Cdd:PRK03918 393 leELEKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrelteehrKELLEEYTAELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 680 EKDRKRQYELLKLERDFQKQANVLRRKT--EEAASANKRLK----EALQRQKEAMEKRKdSQSKGMEGAASRVKNWLANE 753
Cdd:PRK03918 473 EKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKkynlEELEKKAEEYEKLK-EKLIKLKGEIKSLKKELEKL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 754 VEVLVSTEEAQRHLNDLLEDRKILAQDIAQLKQKTDagERIPTKIRR-----RTYtVAELENLEEEASVTKQIESLETEM 828
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKELEELGFESV--EELEERLKElepfyNEY-LELKDAEKELEREEKELKKLEEEL 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 829 ELRSAQIADLQQKLLDADGEEEMVKRRW--ETISNIMEAKCALkylitelvSSKVAGskLESSVKQNRAHVADLQKNIFE 906
Cdd:PRK03918 629 DKAFEELAETEKRLEELRKELEELEKKYseEEYEELREEYLEL--------SRELAG--LRAELEELEKRREEIKKTLEK 698
|
....*....
gi 18202613 907 ERNQMAEME 915
Cdd:PRK03918 699 LKEELEERE 707
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
574-1004 |
4.17e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 574 LQKEKEELILAlhSAKKDNNQAKLSERRRKRLQELEGQMTELKKKLGEQSKLLKLRESTEKTVAKMNQEIQGMKM----- 648
Cdd:COG4717 51 LEKEADELFKP--QGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllqll 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 649 ----QRVQLMRQMKEDAEKFRTWKQQKtKEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEA-ASANKRLKEALQR 723
Cdd:COG4717 129 plyqELEALEAELAELPERLEELEERL-EELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 724 QKEAMEKRKDSQSKGMEgaasrvknwLANEVEVLVSTEEAQrHLNDLLEDRKILAQDIAQLKQKTDAGERIPTKIRRRTY 803
Cdd:COG4717 208 LAELEEELEEAQEELEE---------LEEELEQLENELEAA-ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 804 TVAELENLEEEASVTKQIESLETEMELRSAQIADLQQKLLDADGEEEMVKRRWETISNIMEAKcALKYLITELVSSKVAG 883
Cdd:COG4717 278 VLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELL-ELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 884 SKLESSVKQNRAHvaDLQKNIFEERNqmAEMETEHQSQLMQLEQHHQ--EKILYLLSQLQQKQASVPVTIEELPAEEITE 961
Cdd:COG4717 357 EELEEELQLEELE--QEIAALLAEAG--VEDEEELRAALEQAEEYQElkEELEELEEQLEELLGELEELLEALDEEELEE 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 18202613 962 REKQLMERLKFQDEEIE-----------KMKALCEKN--QQLLQENDMYKQKLALL 1004
Cdd:COG4717 433 ELEELEEELEELEEELEelreelaeleaELEQLEEDGelAELLQELEELKAELREL 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
350-854 |
5.71e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 5.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 350 AELQRLKLQVQELQVLLLQAHGGTLPVLNSMEPSEN-LQSLMERNKNLEKENGKLSRELGEAAVQTAQFLEKIIMTEQQN 428
Cdd:COG1196 267 AELEELRLELEELELELEEAQAEEYELLAELARLEQdIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 429 EKLGSKMEELKQHAAckVNLQRLVEtlEDQELKDNVEVIQNLQQVIVQLQDESSGIAGSIEAMDEEAAsfpvpeedsgek 508
Cdd:COG1196 347 EEAEEELEEAEAELA--EAEEALLE--AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE------------ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 509 rssdgfttNHALRQAQLSKELIELNKALVMKEALAKKMAQNDRQLEPIQSEYLNNIKHLESEVGVLQKEKEELILALHSA 588
Cdd:COG1196 411 --------ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 589 KKDNNQAKLSERRRKRLQ---ELEGQMTELKKKLGEQSKLLK-----------------------LRESTEKTVAKMNQE 642
Cdd:COG1196 483 LEELAEAAARLLLLLEAEadyEGFLEGVKAALLLAGLRGLAGavavligveaayeaaleaalaaaLQNIVVEDDEVAAAA 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 643 IQGMKMQRV-----QLMRQMKEDAEKFRTWKQQKTKEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRL 717
Cdd:COG1196 563 IEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTL 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 718 KEALQRQKEAMEKRKDSQSKGMEGAASRVKNWLANEVEVLVSTEEAQRHLNDLLEDRKILAQDIAQLKQKTDAgeriptk 797
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE------- 715
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 18202613 798 iRRRTYTVAELENLEEEASVTKQIESLETEMELRSAQIADLQQKLLDADGEEEMVKR 854
Cdd:COG1196 716 -RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
348-994 |
7.16e-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: 53.91 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 348 QAAELQRLKLQVQELQVLLLQAHggtlpvlnsmepsenLQSLMERNKNLEKENGKLSRELGEAAVQTAQFLEKIimteQQ 427
Cdd:TIGR02168 211 KAERYKELKAELRELELALLVLR---------------LEELREELEELQEELKEAEEELEELTAELQELEEKL----EE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 428 NEKLGSKMEELKQHAACKV-NLQRLVETLEdQELKDNVEVIQNLQQVIVQLQDESS-GIAGSIEAMDEEAASFPVPEEDS 505
Cdd:TIGR02168 272 LRLEVSELEEEIEELQKELyALANEISRLE-QQKQILRERLANLERQLEELEAQLEeLESKLDELAEELAELEEKLEELK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 506 GEKRS-SDGFTTNHALRQAQLSKeLIELNKALvmkEALAKKMAQNDRQLEPIQSEYLNN---IKHLESEVGVLQKEKEEL 581
Cdd:TIGR02168 351 EELESlEAELEELEAELEELESR-LEELEEQL---ETLRSKVAQLELQIASLNNEIERLearLERLEDRRERLQQEIEEL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 582 ILALHSAKKDNNQAKLSERRRKrLQELEGQMTELKKKLGEQSKLLklRESTEKTVAKMNQEIQgmKMQRVQLMRQMKEDA 661
Cdd:TIGR02168 427 LKKLEEAELKELQAELEELEEE-LEELQEELERLEEALEELREEL--EEAEQALDAAERELAQ--LQARLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 662 EKF----RTWKQQKTK---------EVIQLKEKDRK---------RQY------ELLKLERDFQKQANVLRRKTEEAASA 713
Cdd:TIGR02168 502 EGFsegvKALLKNQSGlsgilgvlsELISVDEGYEAaieaalggrLQAvvvenlNAAKKAIAFLKQNELGRVTFLPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 714 NKRLKEALQRQkeamekrkdsQSKGMEGAASrvknWLANEVEvlvSTEEAQRHLNDLLeDRKILAQDIAQ---LKQKTDA 790
Cdd:TIGR02168 582 KGTEIQGNDRE----------ILKNIEGFLG----VAKDLVK---FDPKLRKALSYLL-GGVLVVDDLDNaleLAKKLRP 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 791 GERIPTK----IRRR-TYTVAELENLEEEASVTKQIESLEtemelrsAQIADLQQKLLDADGEEEMVKRRWETI-SNIME 864
Cdd:TIGR02168 644 GYRIVTLdgdlVRPGgVITGGSAKTNSSILERRREIEELE-------EKIEELEEKIAELEKALAELRKELEELeEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 865 AKCALKYLITELVSSKVAGSKLESSVKQNRAHVADLQKNIFEERNQMAEMETEHQsQLMQLEQHHQEKILYLLSQLQQKQ 944
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIEQLK 795
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 18202613 945 ASVPVTIEELPA-EEITEREKQLMERLKFQDEEIEKMKALCEKNQQLLQEN 994
Cdd:TIGR02168 796 EELKALREALDElRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
521-995 |
8.40e-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: 53.52 E-value: 8.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 521 RQAQLSKELIELNKALVMKEALAKKMAQNDRQLEPIQSEYLNNIKHLESEVGVLQKEKEELILALHSAKKD-NNQAKLSE 599
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEElESLEAELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 600 RRRKRLQELEGQMTELKKKLGEQSKLLKLRESTEKTVAKmnqeiqgmkmqRVQLMRQMKEDAEKFRT-WKQQKTKEVIQL 678
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN-----------EIERLEARLERLEDRRErLQQEIEELLKKL 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 679 KEKDRKR-QYELLKLERDFQKQANVLRRKTEEAASANKRLKEALQRQKEAMEK------RKDSQSKGM---EGAASRVKN 748
Cdd:TIGR02168 431 EEAELKElQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaqlqaRLDSLERLQenlEGFSEGVKA 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 749 WLANEVEV---------LVSTEE---------AQRHLNDLL-EDRKILAQDIAQLKQKtDAGER---IPTKIRRRTYTVA 806
Cdd:TIGR02168 511 LLKNQSGLsgilgvlseLISVDEgyeaaieaaLGGRLQAVVvENLNAAKKAIAFLKQN-ELGRVtflPLDSIKGTEIQGN 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 807 ELENLEEEASVTKQIESLET-EMELRSA--------------QIADLQQKLLDADG-----EEEMVKRRW-------ETI 859
Cdd:TIGR02168 590 DREILKNIEGFLGVAKDLVKfDPKLRKAlsyllggvlvvddlDNALELAKKLRPGYrivtlDGDLVRPGGvitggsaKTN 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 860 SNIMEAKCALKYLITELVSSKVAGSKLESSVKQNRAHVADLQKNIFEERNQMAEMETEHQSQLMQLEQHHQEkilylLSQ 939
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE-----VEQ 744
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 18202613 940 LQQKQASVPVTIEELPAE--EITEREKQLMERLKFQDEEIEKMKALCEKNQQLLQEND 995
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEieELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
353-993 |
1.10e-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: 53.26 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 353 QRLKLQVQELQVLLLQAHGGTLPVLNSMEPSEN-LQSLMERNKNLEKENGKLSRELGEAAVQTAQFLEKIIMTEQQNEKL 431
Cdd:pfam01576 408 KKLEGQLQELQARLSESERQRAELAEKLSKLQSeLESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNL 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 432 GSKMEELKQHAAckvNLQRLVEtlEDQELKDNVEV-IQNLQQVIVQLQDESSGIAGSIEAMDEeaasfpvpeedsGEKRs 510
Cdd:pfam01576 488 STRLRQLEDERN---SLQEQLE--EEEEAKRNVERqLSTLQAQLSDMKKKLEEDAGTLEALEE------------GKKR- 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 511 sdgfttnhalrqaqLSKELIELNKALVMKEALAKKMAQNDRQLEPIQSEYLNNIKHLESEVGVLQKEK---------EEL 581
Cdd:pfam01576 550 --------------LQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQkkfdqmlaeEKA 615
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 582 ILALHSAKKDNNQAKLSERRRKRL---QELEgQMTELKKKLGEQSKLLKLR---------------ESTEKTVAKMNQEI 643
Cdd:pfam01576 616 ISARYAEERDRAEAEAREKETRALslaRALE-EALEAKEELERTNKQLRAEmedlvsskddvgknvHELERSKRALEQQV 694
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 644 QGMKMQRVQLMR--QMKEDAE-----KFRTWKQQKTKEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKR 716
Cdd:pfam01576 695 EEMKTQLEELEDelQATEDAKlrlevNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKK 774
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 717 LK---EALQRQKEAMEKRKDSQSKGMEGAASRVKNWLANEVEVLVSTEEAQRHLNDLLEDRKILAQDIAQLKQKTDAGER 793
Cdd:pfam01576 775 LEldlKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASER 854
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 794 IptkirRRTYTVAELENLEEEASVTKQIESLETEMELRSAQIADLQQKLLDADGEEEMVKRRWETISNIMEAkcalkyLI 873
Cdd:pfam01576 855 A-----RRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQ------LT 923
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 874 TELVSSKVAGSKLESSVKQNRAHVADLQKNIFEE--------RNQMAEMETEHQSQLMQLEQHHQEKILY--LLSQLQQK 943
Cdd:pfam01576 924 TELAAERSTSQKSESARQQLERQNKELKAKLQEMegtvkskfKSSIAALEAKIAQLEEQLEQESRERQAAnkLVRRTEKK 1003
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*....
gi 18202613 944 QASVPVTIEEL---------PAEEITEREKQLMERLKFQDEEIEKMKALCEKNQQLLQE 993
Cdd:pfam01576 1004 LKEVLLQVEDErrhadqykdQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDD 1062
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
519-743 |
1.25e-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: 52.07 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 519 ALRQAQLSKELIELNKALvmkEALAKKMAQNDRQLEPIQSEylnnIKHLESEVGVLQKEKEELILALhsAKKDNNQAKLS 598
Cdd:COG4942 19 ADAAAEAEAELEQLQQEI---AELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQEL--AALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 599 ERRRKRLQELEGQMTELKK------KLGEQSKL-LKLRESTEKTVAKMNQEIQGMKMQRVQLMRQMKEDAEKFRTWKQQK 671
Cdd:COG4942 90 KEIAELRAELEAQKEELAEllralyRLGRQPPLaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18202613 672 TKEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKE------ALQRQKEAMEKRKDSQSKGMEGAA 743
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqeaeELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
525-804 |
1.66e-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: 52.76 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 525 LSKELIELNKALvmkEALAKKMAQNDRQLEPIQSEYLNN---IKHLESEVGVLQKEKEELILALHSAKKDNNQAKLSERR 601
Cdd:TIGR02169 721 IEKEIEQLEQEE---EKLKERLEELEEDLSSLEQEIENVkseLKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQ 797
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 602 ------RKRLQELEGQMTELKKKLgeqSKLLKLRESTEKTVAKMNQEIQGMKMQRVQLmRQMKEDAEKFRTWKQQKTKEv 675
Cdd:TIGR02169 798 aelsklEEEVSRIEARLREIEQKL---NRLTLEKEYLEKEIQELQEQRIDLKEQIKSI-EKEIENLNGKKEELEEELEE- 872
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 676 IQLKEKDRKRQYELLKLERD-FQKQANVLRRKTEEAASANKRLKEALQRQKEAME------------KRKDSQSKGMEGA 742
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDeLEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleeelseiedpKGEDEEIPEEELS 952
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18202613 743 ASRVKNWLaNEVEVLVST------------EEAQRHLNDLLEDRKILAQDIAQLKQKTDAGERIPTKIRRRTYT 804
Cdd:TIGR02169 953 LEDVQAEL-QRVEEEIRAlepvnmlaiqeyEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFE 1025
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
552-912 |
2.20e-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: 52.38 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 552 QLEPIQSEYLNNIKHLEsevgvLQKEKEELILALHSAKKDNNQAKLSE------RRRKRLQELEGQMTELKKKLGEQSKL 625
Cdd:TIGR02169 199 QLERLRREREKAERYQA-----LLKEKREYEGYELLKEKEALERQKEAierqlaSLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 626 L-----KLRESTEKTVAKMNQEIQGMKMQRVQLMRQMKEDAEKFrtwkQQKTKEVIQLKEKDRKRQYELLKLERDFQKQA 700
Cdd:TIGR02169 274 LeelnkKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKEREL----EDAEERLAKLEAEIDKLLAEIEELEREIEEER 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 701 NVLRRKTEEAASankrlkealqRQKEAMEKRKDSQSKGMEGAASRVKnwLANEVEVLVST----EEAQRHLNDLLEDRKI 776
Cdd:TIGR02169 350 KRRDKLTEEYAE----------LKEELEDLRAELEEVDKEFAETRDE--LKDYREKLEKLkreiNELKRELDRLQEELQR 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 777 LAQDIAQLKQK-TDAGERIPTKIRRRTytvaelenleeeaSVTKQIESLETEMELRSAQIADLQQKLLDADGEEEMV-KR 854
Cdd:TIGR02169 418 LSEELADLNAAiAGIEAKINELEEEKE-------------DKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVeKE 484
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 18202613 855 RWETISNIMEAKCALKYLITELVSSKVAGSKLESSVKQNRAHVADLQKniFEERNQMA 912
Cdd:TIGR02169 485 LSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGS--VGERYATA 540
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
383-787 |
4.33e-06 |
|
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: 51.20 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 383 SENLQSLMERNKNLEKENGKLSRELGEAAVQTAQFLEKIIMTEQQNEKLGSKMEELKQHAACKVNLQRLVETLED--QEL 460
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKssKQR 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 461 KDNVEVIQNLQQVIVQLQDESSG--------------IAGSIEAMDEEAASFPVPEED-----SGEKRSSDGFTTNHALR 521
Cdd:TIGR00606 656 AMLAGATAVYSQFITQLTDENQSccpvcqrvfqteaeLQEFISDLQSKLRLAPDKLKSteselKKKEKRRDEMLGLAPGR 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 522 QAQLSKELIELNKALVMKEALAKKMA-------QNDRQLEPIQSEyLNNIKHLESEVGVLQKEKEEL-----ILALHSAK 589
Cdd:TIGR00606 736 QSIIDLKEKEIPELRNKLQKVNRDIQrlkndieEQETLLGTIMPE-EESAKVCLTDVTIMERFQMELkdverKIAQQAAK 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 590 KDNNQAKLSERRRKrlQELEGQMTELKKKLGEQSKLLKLRESTEKTVAKMNQEIQGMKMQRVQL------MRQMKEDAEK 663
Cdd:TIGR00606 815 LQGSDLDRTVQQVN--QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIgtnlqrRQQFEEQLVE 892
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 664 FRTWKQQKTKEVIQLKEKDRKRQYellKLERDFQKQANVLRRKTEEAASANKRLKEALQRQKEAMEKRKDSQSKGMEGAA 743
Cdd:TIGR00606 893 LSTEVQSLIREIKDAKEQDSPLET---FLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKD 969
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 18202613 744 SRVKNWLANEVEVLVSTEEAQRHLNDLLEDRKILAQDIAQLKQK 787
Cdd:TIGR00606 970 DYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQ 1013
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
429-790 |
5.01e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 429 EKLGSKMEELKQHAAckvNLQRLVETLEDQelkdnvevIQNLQQVIVQLQDESSGIAGSIEAMDEEAASFPVPEEdsgek 508
Cdd:TIGR02168 680 EELEEKIEELEEKIA---ELEKALAELRKE--------LEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 509 rssdgfttNHALRQAQLSKELIELNkalVMKEALAKKMAQNDRQLEpiqsEYLNNIKHLESEVGVLQKEKEELILALHSA 588
Cdd:TIGR02168 744 --------QLEERIAQLSKELTELE---AEIEELEERLEEAEEELA----EAEAEIEELEAQIEQLKEELKALREALDEL 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 589 KKDNNQAKLSERR-RKRLQELEGQMTELKKKLGEqskLLKLRESTEKTVAKMNQEIQGMKMQRVQLMRQMKEdaekfrtw 667
Cdd:TIGR02168 809 RAELTLLNEEAANlRERLESLERRIAATERRLED---LEEQIEELSEDIESLAAEIEELEELIEELESELEA-------- 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 668 KQQKTKEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKEALQrqkeamekrkdsqskGMEGAASRVK 747
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLE---------------GLEVRIDNLQ 942
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 18202613 748 NWLANEVEVLVstEEAQRHLNDLLEDRKILAQDIAQLKQKTDA 790
Cdd:TIGR02168 943 ERLSEEYSLTL--EEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
581-801 |
6.58e-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: 49.76 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 581 LILALHSAKKDNNQAKLSERRRKRLQELEGQMTELKKKL----GEQSKLLKLRESTEKTVAKMNQEIQGMKMQRVQLMRQ 656
Cdd:COG4942 5 LLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELaalkKEEKALLKQLAALERRIAALARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 657 MKEDAEKFRTWKQQKTKEVIQLKEKDRKRQ------YELLKLERDFQKQANVLRRKTEEAASANKRLKEALQRQKEAMEK 730
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYrlgrqpPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18202613 731 RKDSQSKGMEGAASRVKNWLANEVEVLVSTEEAQRHLNDLLEDRKILAQDIAQLKQKTDAGERIPTKIRRR 801
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
564-787 |
8.47e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 564 IKHLESEVGVLQK--EKEELILALHSAKKDNNQAKLSERR--RKRLQELEGQMTELKKKLGEQSKLLKLRESTEKTVAKM 639
Cdd:PRK03918 171 IKEIKRRIERLEKfiKRTENIEELIKEKEKELEEVLREINeiSSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 640 NQEIQGMKMQRVQLMRQMKEDAEKFRT------------WKQQKTKEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKT 707
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEEleekvkelkelkEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 708 EEAASANKRLKEALQRQKEAMEK--------RKDSQSKGMEGAASRVKNWLANEV--EVLVSTEEAQRHLNDLLEDRKIL 777
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRleeleerhELYEEAKAKKEELERLKKRLTGLTpeKLEKELEELEKAKEEIEEEISKI 410
|
250
....*....|
gi 18202613 778 AQDIAQLKQK 787
Cdd:PRK03918 411 TARIGELKKE 420
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
541-783 |
9.26e-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: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 541 ALAKKMAQN--DRQLEPIQSEYLNNIKHLESEVGVLQKEKEELILALHSAKKDNNQAKLSERRR---KRLQELEGQMTEL 615
Cdd:COG3206 152 AVANALAEAylEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKlllQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 616 KKKLGE-QSKLLKLRESTEKTVAKM-----NQEIQGMKMQRVQLMRQMKEDAEKFrtwkQQKTKEVIQLKEkdrkrqyEL 689
Cdd:COG3206 232 RAELAEaEARLAALRAQLGSGPDALpellqSPVIQQLRAQLAELEAELAELSARY----TPNHPDVIALRA-------QI 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 690 LKLERDFQKQANVLRRKTEEAASANKRLKEALQRQKEAMEKRkdsqSKGMEGAASRVKNwLANEVEVlvsteeAQRHLND 769
Cdd:COG3206 301 AALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR----LAELPELEAELRR-LEREVEV------ARELYES 369
|
250
....*....|....
gi 18202613 770 LLEDRKILAQDIAQ 783
Cdd:COG3206 370 LLQRLEEARLAEAL 383
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
351-1000 |
1.20e-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: 49.97 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 351 ELQRLKLQVQELQVLLlQAHGGTLPVLNSMEPSENLQSLMERNKNLEKENGKLSRELGEAAVQTAQFLEKIIMTEQQNEK 430
Cdd:TIGR00618 261 LLKQLRARIEELRAQE-AVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSS 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 431 LGSKMEELKQ-HAACKVNLQRLVETLEDQELKDN----VEVIQNLQQVIVQLQDESSGIAGSIEAMDEEAASfpVPEEDS 505
Cdd:TIGR00618 340 IEEQRRLLQTlHSQEIHIRDAHEVATSIREISCQqhtlTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAT--IDTRTS 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 506 geKRSSDGFTTNHALRQAQLSKELIELnkalvmKEALAKKMAQNDRQLEPIQSEYLNNIKHLESEVGVLQK--EKEELIL 583
Cdd:TIGR00618 418 --AFRDLQGQLAHAKKQQELQQRYAEL------CAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihLQETRKK 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 584 ALHSAKKdNNQAKLSERRRKRLQELEGQMTELKKKLGEQSKLLKLrestEKTVAKMNQEIQGMKMQRVQLMRQMKEDAEK 663
Cdd:TIGR00618 490 AVVLARL-LELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRG----EQTYAQLETSEEDVYHQLTSERKQRASLKEQ 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 664 FrTWKQQKTKEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKEALQRQKEAMEKRKDSQSKGMEgaa 743
Cdd:TIGR00618 565 M-QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQE--- 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 744 srvknwlanevEVLVSTEEAQRHLNDLLEDRKILAQDIAQLKQKTDAgeriptkirrrtytvaelenleeeasvtkQIES 823
Cdd:TIGR00618 641 -----------LALKLTALHALQLTLTQERVREHALSIRVLPKELLA-----------------------------SRQL 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 824 LETEMELRSAQIA----DLQQKLLDADGEEEMVKRRWETISNIMEAKCALKyliTELVSSKVAGSKLESSVKQNRAHVAD 899
Cdd:TIGR00618 681 ALQKMQSEKEQLTywkeMLAQCQTLLRELETHIEEYDREFNEIENASSSLG---SDLAAREDALNQSLKELMHQARTVLK 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 900 LQKNIFEERNQMAEMETEHQSQLMQLEQHHQEKILYL---LSQLQQKQASVPVTIEELPAEEITEREKQLMERLKFQDEE 976
Cdd:TIGR00618 758 ARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLReedTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRL 837
|
650 660
....*....|....*....|....
gi 18202613 977 IEKMKALCEKNQQLLQENDMYKQK 1000
Cdd:TIGR00618 838 EEKSATLGEITHQLLKYEECSKQL 861
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
383-742 |
1.22e-05 |
|
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: 49.73 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 383 SENLQSLMERNKnLEKENGKLSRELGEAAVQTAQFLEKIIMTEQQNEKLGSKmeelkqHAACKVNLQRLVETLEDQelkd 462
Cdd:pfam15921 356 SELTEARTERDQ-FSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDR------DTGNSITIDHLRRELDDR---- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 463 NVEViQNLQQVIVQLQDESSGiagsieAMDEEAASFPVPEEdSGEKRSS---DGFTTNHALRQA--QLSKELIELNKALV 537
Cdd:pfam15921 425 NMEV-QRLEALLKAMKSECQG------QMERQMAAIQGKNE-SLEKVSSltaQLESTKEMLRKVveELTAKKMTLESSER 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 538 MKEALAKKMAQNDRQLEPIQSEY----------LNNIKHLESEVGVLQKEKEEL-ILALHSAKKDN----------NQAK 596
Cdd:pfam15921 497 TVSDLTASLQEKERAIEATNAEItklrsrvdlkLQELQHLKNEGDHLRNVQTECeALKLQMAEKDKvieilrqqieNMTQ 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 597 LSERRRKRLQELEGQMTELKKKLGEQSKLLK----LRESTEKTVAKMNQEIQGMKMQRVQLMRQMKEDAEKFRTWKQQKT 672
Cdd:pfam15921 577 LVGQHGRTAGAMQVEKAQLEKEINDRRLELQefkiLKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERD 656
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 673 keviQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKEALQRQKEAMEKRKDSQsKGMEGA 742
Cdd:pfam15921 657 ----QLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL-KSMEGS 721
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
388-1004 |
2.58e-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: 48.91 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 388 SLMERNKNLEKENGKLSRELGEAAVQTAQFLEKIIMTEQQNEKLGSKMEELKQhaackvNLQRLVETLE--DQELKDNVE 465
Cdd:TIGR02169 354 KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKR------ELDRLQEELQrlSEELADLNA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 466 VIQNLQQVIVQLQDESSGIAGSIEAMDEEAASFP---VPEEDSGEKRSSDgfttnhalrQAQLSKELIELNKALVMKEAL 542
Cdd:TIGR02169 428 AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadlSKYEQELYDLKEE---------YDRVEKELSKLQRELAEAEAQ 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 543 AKKMAQNDRQLEPIQSEYLNNIKHLESEVGVLQKEKEELILALHSAK---------KDNNQAK-----LSERRRKRLQEL 608
Cdd:TIGR02169 499 ARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAgnrlnnvvvEDDAVAKeaielLKRRKAGRATFL 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 609 EgqMTELKKKLGEQSKLLK---------LRESTEK-----------TVAKMNQEIQGMKMQRVQLMRQMKEDAEK----- 663
Cdd:TIGR02169 579 P--LNKMRDERRDLSILSEdgvigfavdLVEFDPKyepafkyvfgdTLVVEDIEAARRLMGKYRMVTLEGELFEKsgamt 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 664 --FRTwkqQKTKEVIQLKEKDrkrqyELLKLERDFQKQANVLRRKTEEAASANKRLKEALQRQKEAMEKRKDSQSKG--M 739
Cdd:TIGR02169 657 ggSRA---PRGGILFSRSEPA-----ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIeqL 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 740 EGAASRVKNWLANEVEVLVSTEEAQRHLNDLLEDrkiLAQDIAQLKQKTDAGERIPTKIRRRtytvaelENLEEEASVTK 819
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKE---LEARIEELEEDLHKLEEALNDLEAR-------LSHSRIPEIQA 798
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 820 QIESLETEMELRSAQIADLQQKLLDADGEEE--------MVKRRWETISNIMEAKCALKYLITELVSSKVAGSKLESSVK 891
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekeiqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 892 QNRAHVADLQKNIFEERNQMAEMETEHQSQLMQLEQ--HHQEKILYLLSQLQQKQAS--------VPVTIEELPAEEITE 961
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKkrKRLSELKAKLEALEEELSEiedpkgedEEIPEEELSLEDVQA 958
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 18202613 962 REKQLMERLkfQDEEIEKMKALCEKNQQLLQENDmYKQKLALL 1004
Cdd:TIGR02169 959 ELQRVEEEI--RALEPVNMLAIQEYEEVLKRLDE-LKEKRAKL 998
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
517-755 |
2.59e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 517 NHALRQAQLSKELIELNKALVMK--EALAKKMAQNDRQLEP--IQSEYLNNIKHLESEVGVLQKEKEELILALHSAKKDN 592
Cdd:PTZ00121 1577 NMALRKAEEAKKAEEARIEEVMKlyEEEKKMKAEEAKKAEEakIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 593 NQAKLSERRRKRLQELEGQMTELKKKLGEQSKLLKLRESTEKTVAKMNQEIQGMKMQRVQLMRQMKEdAEKFRTWKQQKT 672
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK-AEEENKIKAEEA 1735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 673 KEviqlKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKEALqrQKEAMEKRKDSQSKGMEGAASRVKNWLAN 752
Cdd:PTZ00121 1736 KK----EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV--IEEELDEEDEKRRMEVDKKIKDIFDNFAN 1809
|
...
gi 18202613 753 EVE 755
Cdd:PTZ00121 1810 IIE 1812
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
448-876 |
2.71e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 448 LQRLVETLEDQ--ELKDNVEVIQNLQQVIVQLQDESSGIAGSIEAMDEEAASFPVPEEDSGEKRSSDGFTT--NHALRQA 523
Cdd:COG4717 76 LEEELKEAEEKeeEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPErlEELEERL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 524 QLSKELIELNKALvmKEALAKKMAQNDRQLEPIQSEYLNNIKHLESEVGVLQKEKEELILALHSAKKDNnqaklsERRRK 603
Cdd:COG4717 156 EELRELEEELEEL--EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL------EELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 604 RLQELEGQMT--ELKKKLGEQSKLLKLR------ESTEKTVAKMNQEIQGMKMQRVQLMRQMKEDAEKFRTWKQQKTKEV 675
Cdd:COG4717 228 ELEQLENELEaaALEERLKEARLLLLIAaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 676 IQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKEALQRQKEAMEKRKdsqskgMEGAASRVKNWLAnevE 755
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ------LEELEQEIAALLA---E 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 756 VLVSTEEAQRHLNDLLEDRKILAQDIAQLKQKtdageriptkIRRRTYTVAELENLEEEASVTKQIESLETEMELRSAQI 835
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQ----------LEELLGELEELLEALDEEELEEELEELEEELEELEEEL 448
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 18202613 836 ADLQQKLLDADGEeemvKRRWETISNIMEAKCALKYLITEL 876
Cdd:COG4717 449 EELREELAELEAE----LEQLEEDGELAELLQELEELKAEL 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
623-1004 |
2.79e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 2.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 623 SKLLKLRESTEKTVAKMNQEiqgmkMQRVQ-LMRQMKEDAEKFRTwKQQKTKEVIQLKEKDRKRQYELLKLERDFQKQAn 701
Cdd:TIGR02168 168 SKYKERRKETERKLERTREN-----LDRLEdILNELERQLKSLER-QAEKAERYKELKAELRELELALLVLRLEELREE- 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 702 vlRRKTEEAASANKRLKEALQRQKEAmekrKDSQSKGMEGAASRVKNwlanevevlvSTEEAQRHLNDLLEDRKILAQDI 781
Cdd:TIGR02168 241 --LEELQEELKEAEEELEELTAELQE----LEEKLEELRLEVSELEE----------EIEELQKELYALANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 782 AQLKQKtdageriptkirrrtytvaelenleeeasvtkqIESLETEMELRSAQIADLQQKLLDADGEEEMVKRRWETISN 861
Cdd:TIGR02168 305 QILRER---------------------------------LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 862 IMEA-KCALKYLITELVSSKVAGSKLESSVKQNRAHVADLQKNIFEERNQMAEMETEHQSQLMQLEQHHQEKILYLLSQL 940
Cdd:TIGR02168 352 ELESlEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18202613 941 QQKQASVPVTIEELPAE--EITEREKQLMERLKFQDEEIEKMKalcEKNQQLLQENDMYKQKLALL 1004
Cdd:TIGR02168 432 EAELKELQAELEELEEEleELQEELERLEEALEELREELEEAE---QALDAAERELAQLQARLDSL 494
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
507-741 |
3.03e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 507 EKRSSDGFTTNHALRQAQLSKELIELNKALVMKEALAKKMAQNDRQLEPIQSEYLNNIKHLESEvGVLQKEKEELILALH 586
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIE-EVMKLYEEEKKMKAE 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 587 SAKKDNNQAKLSERRRKRLQELEGQMTELKKKLGEQSKLLKLRESTEKTVAKMNQEI--------QGMKMQRVQLMRQMK 658
Cdd:PTZ00121 1611 EAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAkkaeedkkKAEEAKKAEEDEKKA 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 659 EDAEKFRTWKQQKTKEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEE-----------AASANKRLKEALQRQKEA 727
Cdd:PTZ00121 1691 AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEdkkkaeeakkdEEEKKKIAHLKKEEEKKA 1770
|
250
....*....|....
gi 18202613 728 MEKRKDSQSKGMEG 741
Cdd:PTZ00121 1771 EEIRKEKEAVIEEE 1784
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
389-994 |
4.17e-05 |
|
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: 48.12 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 389 LMERNKNLEKENGKLSRELGEAAVQTAQFLEKIIMTEQQN-----EKLGSKMEELKQHAACKVNLQRLVetledqelKDN 463
Cdd:TIGR00606 473 ILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADldrklRKLDQEMEQLNHHTTTRTQMEMLT--------KDK 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 464 VEVIQNLQQVIVQLQDESSGIAGSieamdeeaasFPVPE--EDSGEKRSSDGFTTNHALRQAQLskeliELNKALVMKEA 541
Cdd:TIGR00606 545 MDKDEQIRKIKSRHSDELTSLLGY----------FPNKKqlEDWLHSKSKEINQTRDRLAKLNK-----ELASLEQNKNH 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 542 LAKKMAQNDRQLEPIQSEYLN--NIKHLESEVGVLQKE-----KEELILALHSAKKDNNQAKLSERRR------KRLQEL 608
Cdd:TIGR00606 610 INNELESKEEQLSSYEDKLFDvcGSQDEESDLERLKEEiekssKQRAMLAGATAVYSQFITQLTDENQsccpvcQRVFQT 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 609 EGQMTELKKKLgeQSKLLKL---RESTEKTVAKMNQEIQGMKMQrvqlmrqmkedAEKFRTWKQQKTKEVIQLKEKDRKR 685
Cdd:TIGR00606 690 EAELQEFISDL--QSKLRLApdkLKSTESELKKKEKRRDEMLGL-----------APGRQSIIDLKEKEIPELRNKLQKV 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 686 QYELLKLERDFQKQANVLRRKTEEAASANKRLK-----EALQRQKEAMEKRKDSQSKGMEGA-ASRVKNWLANEVEvlvS 759
Cdd:TIGR00606 757 NRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTdvtimERFQMELKDVERKIAQQAAKLQGSdLDRTVQQVNQEKQ---E 833
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 760 TEEAQRHLNDLLEDRKILAQD----IAQLKQKTDagERIPTKIRRRTYTVAELENLEEEASVTKQIESLETEMELRSAQI 835
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKLIQDqqeqIQHLKSKTN--ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQD 911
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 836 ADLQQKLLDADGEEEMVKRRWETISNIMEAKCalkylitelvsskvagSKLESSVKQNRAHVADLQKNIFEERN-QMAEM 914
Cdd:TIGR00606 912 SPLETFLEKDQQEKEELISSKETSNKKAQDKV----------------NDIKEKVKNIHGYMKDIENKIQDGKDdYLKQK 975
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 915 ETEHQSQLMQLE--QHHQEKILYLLSQLQQ----KQASVPVTIEELPAEEITEREKQLMERLKFQDEEIEKMKALCEKNQ 988
Cdd:TIGR00606 976 ETELNTVNAQLEecEKHQEKINEDMRLMRQdidtQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQE 1055
|
....*..
gi 18202613 989 -QLLQEN 994
Cdd:TIGR00606 1056 hQKLEEN 1062
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
525-866 |
4.86e-05 |
|
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: 47.91 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 525 LSKELIELNKALVMKEALAKKMAQNDRQLEPIQSEylnnIKHLESEVGVLQKEKEELILALHSAKKDNNQAklserrRKR 604
Cdd:pfam12128 585 LDLKRIDVPEWAASEEELRERLDKAEEALQSAREK----QAAAEEQLVQANGELEKASREETFARTALKNA------RLD 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 605 LQELEGQMTELKKKLGEQSKLLKlrESTEKTVAKMNQEIQGMKMQRVQLMRQMKEDAEKFRTWKQQKTKEVI-------- 676
Cdd:pfam12128 655 LRRLFDEKQSEKDKKNKALAERK--DSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEgaldaqla 732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 677 ---------------QLKEKDRKRQYELLKLERDFQkqaNVLRRKTeEAASANKRLKEALQRQKEAMEKRKDSQSKgmeg 741
Cdd:pfam12128 733 llkaaiaarrsgakaELKALETWYKRDLASLGVDPD---VIAKLKR-EIRTLERKIERIAVRRQEVLRYFDWYQET---- 804
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 742 AASRVKNWLANEVEVLVSTEEAQRHLNDLLEDRKIlaqDIAQLKQKTDAGERIPTKIRRRTYTVAELENLEEEASVTKQI 821
Cdd:pfam12128 805 WLQRRPRLATQLSNIERAISELQQQLARLIADTKL---RRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKEDANS 881
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 18202613 822 ESLETEMELRSAQIADLQQKLldaDGEEEMVKRRWETISNIMEAK 866
Cdd:pfam12128 882 EQAQGSIGERLAQLEDLKLKR---DYLSESVKKYVEHFKNVIADH 923
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
381-644 |
5.44e-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: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 381 EPSENLQSLMERNKNLEKENGKLSRELGEAAVQTAQFLEKIIMTEQQNEKLGSKMEELKqhaACKVNLQRLVETLEDqel 460
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE---EDLHKLEEALNDLEA--- 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 461 KDNVEVIQNLQQVIVQLQDESSGIAGSIEAMDEEAASFPVPEEDSGEKRssdgfttNHALRQAQLSKELIELNKALVmkE 540
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI-------QELQEQRIDLKEQIKSIEKEI--E 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 541 ALAKKMAQNDRQLEPIQSEylnnIKHLESEVGVLQKEKEELILALHSAKKDNNQAKLS-ERRRKRLQELEGQMTELKKKL 619
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAA----LRDLESRLGDLKKERDELEAQLRELERKIEELEAQiEKKRKRLSELKAKLEALEEEL 933
|
250 260 270
....*....|....*....|....*....|.
gi 18202613 620 GEQSKLLKLRES------TEKTVAKMNQEIQ 644
Cdd:TIGR02169 934 SEIEDPKGEDEEipeeelSLEDVQAELQRVE 964
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
458-701 |
1.15e-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: 45.91 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 458 QELKDNVEVIQNLQQVIVQLQDESSGIAGSIEAMDEEAAsfpvpeedsgekrssdgfttnhalrqaQLSKELIELNKALv 537
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA---------------------------ALARRIRALEQEL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 538 mkEALAKKMAQNDRQLEPIQSEYLNNIKHLESEVGVLQKEKEELILALHSAKKDNNQA--------KLSERRRKRLQELE 609
Cdd:COG4942 79 --AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAvrrlqylkYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 610 GQMTELKKKLGEQSKLLKLRESTEKTVAKMNQEIQGMKMQRVQLMRQMKEDaekfrtwKQQKTKEVIQLKEKDRKRQYEL 689
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKE-------LAELAAELAELQQEAEELEALI 229
|
250
....*....|..
gi 18202613 690 LKLERDFQKQAN 701
Cdd:COG4942 230 ARLEAEAAAAAE 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
674-1001 |
1.53e-04 |
|
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: 46.21 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 674 EVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEE-AASANKRLKEALQRQKEAMEKRKDSQSKGMEGAASRVKNWLAN 752
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREKAERYQALLKEKREyEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 753 EVEVLVSTEEAQRHLNDLLEDRKIlaqdiaqlkqktdageRIPTKIRrrtytvaelenleeeaSVTKQIESLEtemelrs 832
Cdd:TIGR02169 267 LEEIEQLLEELNKKIKDLGEEEQL----------------RVKEKIG----------------ELEAEIASLE------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 833 AQIADLQQKLLDADgeeemvKRRWETISNIMEAKCALKYLITELVSSKVAGSKLESSVKQNRAHVADLQKNIFEERNQMA 912
Cdd:TIGR02169 308 RSIAEKERELEDAE------ERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFA 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 913 EMETEHQSQLMQLEQ--HHQEKILYLLSQLQQKQASVPVTIEELPAE--EITEREKQLMERLKFQDEEIEKMKalcEKNQ 988
Cdd:TIGR02169 382 ETRDELKDYREKLEKlkREINELKRELDRLQEELQRLSEELADLNAAiaGIEAKINELEEEKEDKALEIKKQE---WKLE 458
|
330
....*....|...
gi 18202613 989 QLLQENDMYKQKL 1001
Cdd:TIGR02169 459 QLAADLSKYEQEL 471
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
429-1005 |
1.63e-04 |
|
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: 46.12 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 429 EKLGSKMEELKQHAACKVN-LQRLVETLEDqELKDNVEVIQNLQQVivqlqdessgiagsieamdeeaasfpvpeedsge 507
Cdd:TIGR00618 197 ELLTLRSQLLTLCTPCMPDtYHERKQVLEK-ELKHLREALQQTQQS---------------------------------- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 508 krssdgfttnhalrQAQLSKELIELNKALVMKEALAKKMAQndrqlepiqseylnnIKHLESEVGVLQKEKEELILALHS 587
Cdd:TIGR00618 242 --------------HAYLTQKREAQEEQLKKQQLLKQLRAR---------------IEELRAQEAVLEETQERINRARKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 588 AKKDNNQAKLSERRRKR---LQELEGQMTELKKKLGEQSKLLKLRESTEKTVAKMNQEIQGMKMQRVQlmrqmkedAEKF 664
Cdd:TIGR00618 293 APLAAHIKAVTQIEQQAqriHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA--------HEVA 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 665 RTWKQQKTKEvIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKE--ALQRQKEAMEKRKDSQSKGMEGA 742
Cdd:TIGR00618 365 TSIREISCQQ-HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAfrDLQGQLAHAKKQQELQQRYAELC 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 743 ASRVKNwlaneveVLVSTEEAQRHLNDLLEDRKILAQDIAQLKQKTDAGERIPTKIRRRtytvaELENLEEEASVTKQIE 822
Cdd:TIGR00618 444 AAAITC-------TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLAR-----LLELQEEPCPLCGSCI 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 823 SLETEMEL---------RSAQIAD----LQQKLLDADGE-EEMVKRRWETISNIMEAKCALKYLITELVSSKVAGSKLES 888
Cdd:TIGR00618 512 HPNPARQDidnpgpltrRMQRGEQtyaqLETSEEDVYHQlTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 889 SVKQnrahVADLQKNIFEERNQMAEMETEHQSQLmQLEQHHQEKILYL---LSQLQQKQASVPVTIEELPAEEITE---R 962
Cdd:TIGR00618 592 ITVR----LQDLTEKLSEAEDMLACEQHALLRKL-QPEQDLQDVRLHLqqcSQELALKLTALHALQLTLTQERVREhalS 666
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 18202613 963 EKQLMERLKFQDEeiEKMKALCEKNQQLLQENDMYKQKLALLH 1005
Cdd:TIGR00618 667 IRVLPKELLASRQ--LALQKMQSEKEQLTYWKEMLAQCQTLLR 707
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
387-618 |
1.75e-04 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 45.02 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 387 QSLMERNKNLEKENGKLSRELGEAAVQTAQFLEKIIMTEQQNEKLGSKMEELKQHAACKVNLQRlvetLEDQELKDNVEV 466
Cdd:pfam04849 90 QSLLKQNSVLTERNEALEEQLGSAREEILQLRHELSKKDDLLQIYSNDAEESETESSCSTPLRR----NESFSSLHGCVQ 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 467 IQNLQQVIVQLQDESsgiagsiEAMDEEAASFPVPEEDSGEKrssdgfttnhalrQAQL----SKELIELNKALV-MKEA 541
Cdd:pfam04849 166 LDALQEKLRGLEEEN-------LKLRSEASHLKTETDTYEEK-------------EQQLmsdcVEQLSEANQQMAeLSEE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 542 LAKKMAQNDRQLEPIqSEYLNNIKHLESEVGVLQKEKEELILALHSAKKDNNQ--AKLSERRRK------RLQELEGQMT 613
Cdd:pfam04849 226 LARKMEENLRQQEEI-TSLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQltSELQELQDRyaeclgMLHEAQEELK 304
|
....*
gi 18202613 614 ELKKK 618
Cdd:pfam04849 305 ELRKK 309
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
669-865 |
2.23e-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: 45.14 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 669 QQKTKEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKEaLQRQKEAMEKRKDSQSKGM-EGAASRVK 747
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-LEKEIAELRAELEAQKEELaELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 748 NWLANEVEVLVSTEEAQRHLNDLLEDRKILAQDIAQLKQKTDAGERIPTKirRRTYTVAELENLEEEASVTKQIESLETE 827
Cdd:COG4942 116 LGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL--RAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190
....*....|....*....|....*....|....*...
gi 18202613 828 MELRSAQIADLQQKLLDADGEEEMVKRRWETISNIMEA 865
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
521-793 |
7.37e-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: 43.96 E-value: 7.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 521 RQAQLSKELIELNKALVMKEALAKKMaQNDRQLEPIQSEYLNNIK-----HLESEVGVLQKEKEELILALHSAKKDNNQA 595
Cdd:pfam17380 287 RQQQEKFEKMEQERLRQEKEEKAREV-ERRRKLEEAEKARQAEMDrqaaiYAEQERMAMERERELERIRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 596 KLSE--------RRRKRLQELEGQMTEL---------KKKLGEQSKLLKLRESTEKT--VAKMNQEIQGMKMQRVQLMRQ 656
Cdd:pfam17380 366 RQEEiameisrmRELERLQMERQQKNERvrqeleaarKVKILEEERQRKIQQQKVEMeqIRAEQEEARQREVRRLEEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 657 MKEDAEKFRTWKQQKTKEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKT-EEAASANKRLKEALQRQKEAMEKRKDSQ 735
Cdd:pfam17380 446 REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEER 525
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 736 SKGMEGAASRVKnwlanevevlvsTEEAQRHLNDLLEDRKILAQ--DIAQLKQKTDAGER 793
Cdd:pfam17380 526 QKAIYEEERRRE------------AEEERRKQQEMEERRRIQEQmrKATEERSRLEAMER 573
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
383-866 |
7.77e-04 |
|
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: 43.94 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 383 SENLQSLMERNKNLEKENGKLSRELgEAAVQTAQFLEKIIMTE-----QQNEKLGSKMEELKQ----HAACKVNLQRLVE 453
Cdd:pfam05483 281 DENLKELIEKKDHLTKELEDIKMSL-QRSMSTQKALEEDLQIAtkticQLTEEKEAQMEELNKakaaHSFVVTEFEATTC 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 454 TLEdqelkdnvEVIQNLQQVIVQLQDESSGIAGSIEamdeeaasfpvpeEDSGEKRSSDGFTTNHALRQAQLSKELIELN 533
Cdd:pfam05483 360 SLE--------ELLRTEQQRLEKNEDQLKIITMELQ-------------KKSSELEEMTKFKNNKEVELEELKKILAEDE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 534 KALVMK---EALAKKMAQNDRQLEPIQSEYLNNIKHLESEVGVLQ-------KEKEELILALHSAKKDN-----NQAKLS 598
Cdd:pfam05483 419 KLLDEKkqfEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKtseehylKEVEDLKTELEKEKLKNieltaHCDKLL 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 599 ERRRKRLQELEGQMTELKKklgEQSKLLKLRESTEKtvakMNQEIQGMKMQRVQLMRQMKEDAEKFRTWKQQKTKEVIQL 678
Cdd:pfam05483 499 LENKELTQEASDMTLELKK---HQEDIINCKKQEER----MLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKS 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 679 KEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKEaLQRQKEAMEKRKDSQSKGMEGAASRVKNWLANEVEVLV 758
Cdd:pfam05483 572 EENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE-LHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 759 STEEAQRHLNDLLEDRKI----LAQDIAQLKQKTDAGERIPTKIRRR---TYTVAELENLEEEASVTKQIE--------- 822
Cdd:pfam05483 651 KFEEIIDNYQKEIEDKKIseekLLEEVEKAKAIADEAVKLQKEIDKRcqhKIAEMVALMEKHKHQYDKIIEerdselgly 730
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 18202613 823 ------------SLETEMELRSAQIADLQQKLLDADGEEEMVKRRWETISNIMEAK 866
Cdd:pfam05483 731 knkeqeqssakaALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
554-765 |
1.33e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 554 EPIQSEYLNNIKHLESEVGVLQKEKEELILALHSAKKDNNQAKlserrrKRLQELEGQMTELKKKLGE-QSKLLKLREST 632
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ------AELEALQAEIDKLQAEIAEaEAEIEERREEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 633 EKTVAKMNQEIQGMKM--------------QRVQLMRQMKE-DAEKFRTWKQQKtKEVIQLKEKDRKRQYELLKLERDFQ 697
Cdd:COG3883 89 GERARALYRSGGSVSYldvllgsesfsdflDRLSALSKIADaDADLLEELKADK-AELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18202613 698 KQANVLRRKTEEAASANKRLKE---ALQRQKEAMEKRKDSQSKGMEGAASRVKNWLANEVEVLVSTEEAQR 765
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAeeaAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
375-634 |
1.49e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.14 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 375 PVLNSMEPSENLQSLMERNKNLEKE--NGKLSRELGEaaVQTAQFLEKIIMTEQQNEKLGSKMEELKQHAACKVNLQRLV 452
Cdd:COG5022 801 PLLSLLGSRKEYRSYLACIIKLQKTikREKKLRETEE--VEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVE 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 453 ETL-EDQELKDNVEVIQNLQQVIVQLQDESSGIAGSIEAmDEEAASFPVPEEDSGEKRSSDGF-TTNHALRQAQLSKELI 530
Cdd:COG5022 879 LAErQLQELKIDVKSISSLKLVNLELESEIIELKKSLSS-DLIENLEFKTELIARLKKLLNNIdLEEGPSIEYVKLPELN 957
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 531 ELN-------KALVMKEALAKKMAQNDRQLEPIQSEYLN---NIKHLESEVGVLQKEKEEL------ILALHSAKKDNNQ 594
Cdd:COG5022 958 KLHevesklkETSEEYEDLLKKSTILVREGNKANSELKNfkkELAELSKQYGALQESTKQLkelpveVAELQSASKIISS 1037
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 18202613 595 AKLSERRRKRLQELEGQMTELKKKLGEQSKLLKLRESTEK 634
Cdd:COG5022 1038 ESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSL 1077
|
|
| HemX |
COG2959 |
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis ... |
666-786 |
1.68e-03 |
|
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis HemX, COG0755, no evidence of involvement in heme biosynthesis) [General function prediction only];
Pssm-ID: 442199 [Multi-domain] Cd Length: 361 Bit Score: 42.26 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 666 TWKQQKtkeviQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKEALQRQKEAMEKRKDSQSKGMEGAASR 745
Cdd:COG2959 51 GWQQLQ-----QQQAELAQLAQQLAALQQQAQELRALAQQLQELLQQLAARLAQLEQRLAELQQQLAALQQLLQSLSGSS 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18202613 746 VKNWLANEVEVLVST------------------EEAQ---RHLND--LLEDRKILAQDIAQLKQ 786
Cdd:COG2959 126 RDDWLLAEAEYLLRLagqqlqlegdvktalaalQSADarlARLNDpsLLPVRRAIARDIARLRA 189
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
341-725 |
1.80e-03 |
|
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: 42.36 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 341 PIVNTdpqAAELQRLKLQVQELQVLLLQAhggtlpvlnsmepSENLQSLMERNKNLEKENGKLSRELGEAAVQTAQFLEK 420
Cdd:pfam19220 35 PIEAI---LRELPQAKSRLLELEALLAQE-------------RAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 421 IIMTEQQNEKLGSkmeELKQHAAckvnlqrLVETLEDQeLKDNVEVIQNLQQVIVQLQDESSGIAGSIEAMDEEAASFpv 500
Cdd:pfam19220 99 LREAEAAKEELRI---ELRDKTA-------QAEALERQ-LAAETEQNRALEEENKALREEAQAAEKALQRAEGELATA-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 501 pEEDSG----EKRSSDGFTTNHALRQAQLSKELIELNKALvmkEALAKKMAQNDRQLEPIQSEYLNNIKHLESEVGVLQK 576
Cdd:pfam19220 166 -RERLAlleqENRRLQALSEEQAAELAELTRRLAELETQL---DATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 577 EKEELILALHSAKKDNNQA-KLSERRRKRLQELEGQMTELKKKLGEQSKLLKLREST----EKTVAKMNQEIQGMKMQRV 651
Cdd:pfam19220 242 ERASLRMKLEALTARAAATeQLLAEARNQLRDRDEAIRAAERRLKEASIERDTLERRlaglEADLERRTQQFQEMQRARA 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18202613 652 QLMrqmkEDAEKFRTWKQQKTKEVIQLKEKDRKRQYELLKLERDFQKQanvlrRKTEEAAsaNKRLKEALQRQK 725
Cdd:pfam19220 322 ELE----ERAEMLTKALAAKDAALERAEERIASLSDRIAELTKRFEVE-----RAALEQA--NRRLKEELQRER 384
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
328-1009 |
2.23e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 328 LRYADRARKIKNKpIVNTDPQA----AELQRLKLQ----VQELQVLLLQAHGGTLPVLNSMEPS------ENLQSLMERN 393
Cdd:TIGR01612 1107 IKYADEINKIKDD-IKNLDQKIdhhiKALEEIKKKsenyIDEIKAQINDLEDVADKAISNDDPEeiekkiENIVTKIDKK 1185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 394 KNLEKENGKLSRELGEAavqtaqflekiimteqqnEKLGSKMEELKQ-HAACKVNLQRLVETLEDQELKDNVEVIQNLQQ 472
Cdd:TIGR01612 1186 KNIYDEIKKLLNEIAEI------------------EKDKTSLEEVKGiNLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEA 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 473 VIVQLQDESSGiagSIEAMDEEAASFPVPEEDSGEKRSSDGFTTNHALRQAQlSKELIEL-NKALVMKEALAKKMAQNDR 551
Cdd:TIGR01612 1248 YIEDLDEIKEK---SPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKH-DENISDIrEKSLKIIEDFSEESDINDI 1323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 552 QLEpIQSEYLNNIKHlESEVGVLQKEKEEL--ILALHSAKKDNNQAKLS----ERRRKRLQELEGQMTELKKKLGEQSKL 625
Cdd:TIGR01612 1324 KKE-LQKNLLDAQKH-NSDINLYLNEIANIynILKLNKIKKIIDEVKEYtkeiEENNKNIKDELDKSEKLIKKIKDDINL 1401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 626 LKLRESTEKTV--AKMNQEIQGMKMQRVQLMRQMKEDAEKFRTWKQQKTKEVIQLKE---KDRKRQYeLLKLER-----D 695
Cdd:TIGR01612 1402 EECKSKIESTLddKDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNiemADNKSQH-ILKIKKdnatnD 1480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 696 FQKQANVLRrkteEAASANKRLKEALQRQKEAMEKRKD--SQSKgmegaasrvknwlaNEVEVLV---STEEAQRHLNDL 770
Cdd:TIGR01612 1481 HDFNINELK----EHIDKSKGCKDEADKNAKAIEKNKElfEQYK--------------KDVTELLnkySALAIKNKFAKT 1542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 771 LEDRKILAQDIAQLKQK----TDAGERIPTKIRRRTYTVAELENLEEEAS-----VTKQIESLETEMelrsAQIADLQQK 841
Cdd:TIGR01612 1543 KKDSEIIIKEIKDAHKKfileAEKSEQKIKEIKKEKFRIEDDAAKNDKSNkaaidIQLSLENFENKF----LKISDIKKK 1618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 842 LLDADGEEEMVKRRWETIS-NIMEakcalkyliTELVSSKVAGSKLESSVKQnrahVADLQKNIFEERNQMAEMETEHQS 920
Cdd:TIGR01612 1619 INDCLKETESIEKKISSFSiDSQD---------TELKENGDNLNSLQEFLES----LKDQKKNIEDKKKELDELDSEIEK 1685
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 921 QLMQLEQHHQEKILYLLSQLQQKQASVPVTIEELpAEEITEREKQLMERLKFQD-EEIEKMKALCEKNQQLlqeNDMYKQ 999
Cdd:TIGR01612 1686 IEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESI-KELIEPTIENLISSFNTNDlEGIDPNEKLEEYNTEI---GDIYEE 1761
|
730
....*....|
gi 18202613 1000 KLALLHVASG 1009
Cdd:TIGR01612 1762 FIELYNIIAG 1771
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
436-931 |
2.52e-03 |
|
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: 42.41 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 436 EELKQHAACKVNLQRLVETLEDQELKDNVEVIQNLQQVIVqlqdessgiagSIEAMDEEAASFPVP-EEDSGEK-RSSDG 513
Cdd:pfam15921 141 EDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMML-----------SHEGVLQEIRSILVDfEEASGKKiYEHDS 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 514 FTTNHaLRQ--AQLSKELIELNKALvmkEALAKKMAQNDRQLEPIQSEYLNNIKHL----ESEVGVLQKEKEELILAL-- 585
Cdd:pfam15921 210 MSTMH-FRSlgSAISKILRELDTEI---SYLKGRIFPVEDQLEALKSESQNKIELLlqqhQDRIEQLISEHEVEITGLte 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 586 --HSAKKDNNQAK-----LSERRR-------KRLQELEGQMTELKKKLGEQSKLLKLR-ESTEKTVAKMNQEIQGMKMQR 650
Cdd:pfam15921 286 kaSSARSQANSIQsqleiIQEQARnqnsmymRQLSDLESTVSQLRSELREAKRMYEDKiEELEKQLVLANSELTEARTER 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 651 VQLMRQ---MKEDAEKFRTWKQQKTKEvIQLKEKDRKRQYEllkleRDFQKQANV--LRRKTEEAASANKRLKEALQRQK 725
Cdd:pfam15921 366 DQFSQEsgnLDDQLQKLLADLHKREKE-LSLEKEQNKRLWD-----RDTGNSITIdhLRRELDDRNMEVQRLEALLKAMK 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 726 EAMEKRKDSQSKGMEGAASRVKNwLANEVEVLVSTEEAQRHLNDLLEDRKILAQD--------IAQLKQKTDAGERIP-- 795
Cdd:pfam15921 440 SECQGQMERQMAAIQGKNESLEK-VSSLTAQLESTKEMLRKVVEELTAKKMTLESsertvsdlTASLQEKERAIEATNae 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 796 -TKIRRRT-----YTVAELENLEEEASVTKQIESLETEMELRSAQIADLQQKLldaDGEEEMVKRRWETISNIMEAKCAL 869
Cdd:pfam15921 519 iTKLRSRVdlklqELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQI---ENMTQLVGQHGRTAGAMQVEKAQL 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 870 KYLIT----ELVSSKVAGSKLESSVKQNRAHVADLQ-----------------KNIFEERNQM----------------- 911
Cdd:pfam15921 596 EKEINdrrlELQEFKILKDKKDAKIRELEARVSDLElekvklvnagserlravKDIKQERDQLlnevktsrnelnslsed 675
|
570 580 590
....*....|....*....|....*....|..
gi 18202613 912 ------------AEMETEHQSQLMQLEQHHQE 931
Cdd:pfam15921 676 yevlkrnfrnksEEMETTTNKLKMQLKSAQSE 707
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
380-1001 |
2.78e-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: 41.96 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 380 MEPSENLQSLMERNKNLEKENGKLSRELGEAAVQTaqflekiimTEQQNEKLGSKMEELKQHAACKVNLQRLVETL--ED 457
Cdd:TIGR00606 265 MKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGT---------DEQLNDLYHNHQRTVREKERELVDCQRELEKLnkER 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 458 QEL---KDNVEVIQNLQQVIVQLQDESSGIAGSIEAMDEEAASFPVPEEDSGEKRSSDGFTTNHALRQAQLSKELIELNK 534
Cdd:TIGR00606 336 RLLnqeKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 535 ALVMKEALAKkmaqndRQLEPIQSEYLNNIKHLESEVGVLQKEKEELILALHSAKK----DNNQAKLSERRRKRLQEL-- 608
Cdd:TIGR00606 416 DLQSKERLKQ------EQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegsSDRILELDQELRKAERELsk 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 609 --EGQMTELKKK-----LGEQSKLLKLRESTEKTVAKMNQEIQGMKmQRVQLMRQMKEDAEKFRTWKQQKTKEVI-QLKE 680
Cdd:TIGR00606 490 aeKNSLTETLKKevkslQNEKADLDRKLRKLDQEMEQLNHHTTTRT-QMEMLTKDKMDKDEQIRKIKSRHSDELTsLLGY 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 681 KDRKRQyellkLERDFQKQANVLRRKTEEAASANKRLK--EALQRQKEAMEKRKDSQSKGMEgaasrvknwlaNEVEVLV 758
Cdd:TIGR00606 569 FPNKKQ-----LEDWLHSKSKEINQTRDRLAKLNKELAslEQNKNHINNELESKEEQLSSYE-----------DKLFDVC 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 759 STEEAQRHLNDLLEDRKILAQDIAQLKQKTDAGERIPTKIRRRTYTVAELENLEeeasvtkqiesLETEMELRSAqIADL 838
Cdd:TIGR00606 633 GSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRV-----------FQTEAELQEF-ISDL 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 839 QQKLLDADGEEEMVK---RRWETISNIMEAKCALKYLITELVsskvagsklESSVKQNRAHVADLQKNIFEERNQMAEME 915
Cdd:TIGR00606 701 QSKLRLAPDKLKSTEselKKKEKRRDEMLGLAPGRQSIIDLK---------EKEIPELRNKLQKVNRDIQRLKNDIEEQE 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 916 TEHQSQLMQLEQHHQ-EKILYLLSQLQQKQASVPVTIEELPAE----EITEREKQLMERLKFQDEEIEKMKALCEKNQQL 990
Cdd:TIGR00606 772 TLLGTIMPEEESAKVcLTDVTIMERFQMELKDVERKIAQQAAKlqgsDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKL 851
|
650
....*....|.
gi 18202613 991 LQENDMYKQKL 1001
Cdd:TIGR00606 852 IQDQQEQIQHL 862
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
633-1002 |
3.74e-03 |
|
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: 41.65 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 633 EKTVAKMNQEIQGMKMQRVQLmRQMKEdaEKFRTWKQQKtkeviQLKEKDRKRQYELlklerdfQKQANVLRRKTEEAAS 712
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERL-RQEKE--EKAREVERRR-----KLEEAEKARQAEM-------DRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 713 ANKRLKEALQRQKEAMEKRKDSQSKGMEGAASRVKNWLANEV----EVLVSTEEAQRHLNDLLEDRKilaQDIAQLKQKT 788
Cdd:pfam17380 346 RERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERqqknERVRQELEAARKVKILEEERQ---RKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 789 DAGERIPTKIRRRTYTVAELENLEEEASVTKQIESLETEMELRSAQIADLQQKLLDADGEEEMVKRRWETISNIMEakca 868
Cdd:pfam17380 423 EQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE---- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 869 lkyliTELVSSKVAGSKLESSVKQNRAHVADLQKNIFEERNQMAEMETEHQSQLMQLEQHHQEKILyllsqlqqkqasvp 948
Cdd:pfam17380 499 -----KELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMR-------------- 559
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 18202613 949 VTIEELPAEEITEREKQLMERLKfqdeEIEKMKALCEKNQQLLQENDMYKQKLA 1002
Cdd:pfam17380 560 KATEERSRLEAMEREREMMRQIV----ESEKARAEYEATTPITTIKPIYRPRIS 609
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
348-495 |
3.83e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 348 QAAELQRLKLQVQELQVLLLQAHGgtlpVLNSMEPSENLqslmernknLEKENGKLSRELGEAAVQTAQFLEKIIMTEQQ 427
Cdd:PRK04863 521 RLSELEQRLRQQQRAERLLAEFCK----RLGKNLDDEDE---------LEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18202613 428 NEKLGSKMEELKQHAACKVNLQRLVETLEDQ---ELKDNVEVIQNLQQVIVQ---LQDESSGIAGSIEAMDEEA 495
Cdd:PRK04863 588 LEQLQARIQRLAARAPAWLAAQDALARLREQsgeEFEDSQDVTEYMQQLLERereLTVERDELAARKQALDEEI 661
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
691-993 |
4.99e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.18 E-value: 4.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 691 KLERDFQKQANVLRRKTEEAASANKRLKEalqrQKEAMEKRKDsqskgmegaasrvknwlaNEVEVLVSTEEAQRHLNDL 770
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEE----QREQARETRD------------------EADEVLEEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 771 LEDRKILAQDIAQ-LKQKTDAGERIPTKIRRRtytvaelenleeeASVTKQIESLETEMELRSAQIADLQQKLLDADGEE 849
Cdd:PRK02224 257 EAEIEDLRETIAEtEREREELAEEVRDLRERL-------------EELEEERDDLLAEAGLDDADAEAVEARREELEDRD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 850 EMVKRRwetisnimeakcalkyliteLVSSKVAGSKLESSVKQNRAHVADLQKNIFEERNQMAEMETEHQSQLMQLEQhH 929
Cdd:PRK02224 324 EELRDR--------------------LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED-R 382
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18202613 930 QEKILYLLSQLQQKQASV---PVTIEELPA--EEITEREKQLMERLKFQDEEIEKMKALCEKNQQLLQE 993
Cdd:PRK02224 383 REEIEELEEEIEELRERFgdaPVDLGNAEDflEELREERDELREREAELEATLRTARERVEEAEALLEA 451
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
523-849 |
5.84e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.66 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 523 AQLSKELIELNKALVMKEALAKKMAQNDRQLEPIQSEYLNNIKHLESEVGVLQKEKEELILALHSAKKDNNQAklserrR 602
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQL------E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 603 KRLQELEGQMTELKKKLGEQSKLLKLRESTEKTVAKMNQEIQGMKMQRVQLMRQMKEDAEKFRTWKQQKTKEVIQLKEKD 682
Cdd:COG4372 80 EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 683 RKRQYELLKLERDFQKQAN-VLRRKTEEAASANKRLKEALQRQKEAMEKRKDSQSKGMEGAASRVKNWLANEVEVLVSTE 761
Cdd:COG4372 160 ESLQEELAALEQELQALSEaEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 762 EAQRHLNDLLEDRKILAQDIAQLKQKTDAGERIPTKIRRRTYTVAELENLEEEASVTKQIESLETEMELRSAQIADLQQK 841
Cdd:COG4372 240 DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLA 319
|
....*...
gi 18202613 842 LLDADGEE 849
Cdd:COG4372 320 ALLELAKK 327
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
387-730 |
6.27e-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: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 387 QSLMERNKNLEKENGKLSRELGEAAVQTAQFLEKIIMTEQQNEKLGSKMEELKQHAAckvnlqRLVETLEDQELKDNVE- 465
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII------KNNSEIKDLTNQDSVKe 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 466 -VIQNLQQVIVQLQDESSGIAGSIEAMDEEaasfpvpeedsgekrssdgfttnhalrQAQLSKELIELNKALVMKEALAK 544
Cdd:TIGR04523 454 lIIKNLDNTRESLETQLKVLSRSINKIKQN---------------------------LEQKQKELKSKEKELKKLNEEKK 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 545 KMAQNDRQLEPIQSEYLNNIKHLESEVgvlqKEKEELILALHSAKKDNNQAKLSERRRKRLQELEGQMTELKKklgEQSK 624
Cdd:TIGR04523 507 ELEEKVKDLTKKISSLKEKIEKLESEK----KEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQ---TQKS 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 625 LLKLRESTEKTVAKMNQEIQGMKMQRVQLMRQMKEDAEKFRTWKQQKTKEVIQLKEKDRKRQYeLLKLERDFQKQANVLR 704
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNK-LKQEVKQIKETIKEIR 658
|
330 340
....*....|....*....|....*.
gi 18202613 705 RKTEEAASANKRLKEALQRQKEAMEK 730
Cdd:TIGR04523 659 NKWPEIIKKIKESKTKIDDIIELMKD 684
|
|
| PLN02678 |
PLN02678 |
seryl-tRNA synthetase |
648-763 |
6.36e-03 |
|
seryl-tRNA synthetase
Pssm-ID: 215364 [Multi-domain] Cd Length: 448 Bit Score: 40.46 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 648 MQRVQLMRQMK-EDAEKFRTWKQQKTK------EVIQLKEKDRKRQYELLKLERDF---QKQANVLRRKTEEAASANKRl 717
Cdd:PLN02678 1 MLDINLFREEKgGDPELIRESQRRRFAsvelvdEVIALDKEWRQRQFELDSLRKEFnklNKEVAKLKIAKEDATELIAE- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 18202613 718 KEALQRQKEAMEKRKDSQSKGMEGAASRVKNWLANEVEvlVSTEEA 763
Cdd:PLN02678 80 TKELKKEITEKEAEVQEAKAALDAKLKTIGNLVHDSVP--VSNDEA 123
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
589-730 |
8.23e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18202613 589 KKDNNQAKLSERRRKR-LQELEGQMTELKKK--LGEQSKLLKLRESTEKTVAKMNQEIQgmkmqrvqlmrqmkedaekfr 665
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRiLEEAKKEAEAIKKEalLEAKEEIHKLRNEFEKELRERRNELQ--------------------- 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18202613 666 twkqQKTKEVIQLKEKDRKRQYELLKLERDFQKQANVLRRKTEEAASANKRLKEALQRQKEAMEK 730
Cdd:PRK12704 86 ----KLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
|
|
| |
