|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
8-337 |
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: 626.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 8 IPVRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVVGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAY 87
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 88 GQTGSGKTYSMGGAYTAEqENEPTVGVIPRVIQLLFKEID-KKSDFEFTLKVSYLEIYNEEILDLLCPSR-EKAQINIRE 165
Cdd:cd01372 81 GQTGSGKTYTMGTAYTAE-EDEEQVGIIPRAIQHIFKKIEkKKDTFEFQLKVSFLEIYNEEIRDLLDPETdKKPTISIRE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 166 DPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKK---------SDKNSSFRSKL 236
Cdd:cd01372 160 DSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKngpiapmsaDDKNSTFTSKF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 237 HLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGD-DKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSP 315
Cdd:cd01372 240 HFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDeSKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSP 319
|
330 340
....*....|....*....|..
gi 116686122 316 ADSNLEETLNTLRYADRARKIK 337
Cdd:cd01372 320 ADSNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
9-343 |
1.18e-163 |
|
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: 489.78 E-value: 1.18e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 9 PVRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVV-------GTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYN 81
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTvrspknrQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 82 ATVLAYGQTGSGKTYSMGGayTAEQEneptvGVIPRVIQLLFKEIDK-KSDFEFTLKVSYLEIYNEEILDLLCPSREKaq 160
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG--TPDSP-----GIIPRALKDLFEKIDKrEEGWQFSVKVSYLEIYNEKIRDLLNPSSKK-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 161 INIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSFR-SKLHLV 239
Cdd:smart00129 152 LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKaSKLNLV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 240 DLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSN 319
Cdd:smart00129 232 DLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSSN 311
|
330 340
....*....|....*....|....
gi 116686122 320 LEETLNTLRYADRARKIKNKPIVN 343
Cdd:smart00129 312 LEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
15-336 |
5.39e-155 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 467.05 E-value: 5.39e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 15 RCRPLVPKEISEGCQMCLSFVPGEPQVV-------VGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAY 87
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVesshltnKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 88 GQTGSGKTYSMGGaytaeqeNEPTVGVIPRVIQLLFKEIDK-KSDFEFTLKVSYLEIYNEEILDLLCPSREKAQ-INIRE 165
Cdd:pfam00225 81 GQTGSGKTYTMEG-------SDEQPGIIPRALEDLFDRIQKtKERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRkLRIRE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 166 DPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSD--KNSSFRSKLHLVDLAG 243
Cdd:pfam00225 154 DPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTggEESVKTGKLNLVDLAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 244 SERQKKT-KAEGDRLKEGININRGLLCLGNVISALGDDKKGgFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEE 322
Cdd:pfam00225 234 SERASKTgAAGGQRLKEAANINKSLSALGNVISALADKKSK-HIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSSNYEE 312
|
330
....*....|....
gi 116686122 323 TLNTLRYADRARKI 336
Cdd:pfam00225 313 TLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
9-334 |
6.08e-150 |
|
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: 453.64 E-value: 6.08e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 9 PVRVALRCRPLVPKEiSEGCQMCLSFVPG------EPQVVVGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNA 82
Cdd:cd00106 1 NVRVAVRVRPLNGRE-ARSAKSVISVDGGksvvldPPKNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 83 TVLAYGQTGSGKTYSMGGAYTAEQeneptvGVIPRVIQLLFKEIDK--KSDFEFTLKVSYLEIYNEEILDLLCPSrEKAQ 160
Cdd:cd00106 80 TIFAYGQTGSGKTYTMLGPDPEQR------GIIPRALEDIFERIDKrkETKSSFSVSASYLEIYNEKIYDLLSPV-PKKP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 161 INIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKS-DKNSSFRSKLHLV 239
Cdd:cd00106 153 LSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREkSGESVTSSKLNLV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 240 DLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDdKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSN 319
Cdd:cd00106 233 DLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD-GQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSEN 311
|
330
....*....|....*
gi 116686122 320 LEETLNTLRYADRAR 334
Cdd:cd00106 312 FEETLSTLRFASRAK 326
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
10-343 |
4.81e-118 |
|
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: 370.91 E-value: 4.81e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 10 VRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVV------------GTDKSFTYDFVF------DPS-TEQEEVFNTAVA 70
Cdd:cd01365 3 VKVAVRVRPFNSREKERNSKCIVQMSGKETTLKNpkqadknnkatrEVPKSFSFDYSYwshdseDPNyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 71 PLIKGVFKGYNATVLAYGQTGSGKTYSMGGAytaeqENEPtvGVIPRVIQLLFKEIDKKSDFE--FTLKVSYLEIYNEEI 148
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMGT-----QEQP--GIIPRLCEDLFSRIADTTNQNmsYSVEVSYMEIYNEKV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 149 LDLLCPSREKAQIN--IREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRK-- 224
Cdd:cd01365 156 RDLLNPKPKKNKGNlkVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRhd 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 225 -KSDKNSSFRSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGG------FVPYRDSKLTRLL 297
Cdd:cd01365 236 aETNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSGKskkkssFIPYRDSVLTWLL 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 116686122 298 QDSLGGNSHTLMIACVSPADSNLEETLNTLRYADRARKIKNKPIVN 343
Cdd:cd01365 316 KENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
10-338 |
7.51e-116 |
|
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: 363.84 E-value: 7.51e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 10 VRVALRCRPLVPKEISEGcQMCLSFVPGEPQVVVGTD-----KSFTYDFVFDPSTEQEEVFNTaVAPLIKGVFKGYNATV 84
Cdd:cd01366 4 IRVFCRVRPLLPSEENED-TSHITFPDEDGQTIELTSigakqKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 85 LAYGQTGSGKTYSMGGaytaeqeNEPTVGVIPRVIQLLFKEI--DKKSDFEFTLKVSYLEIYNEEILDLLCPSREKAQ-I 161
Cdd:cd01366 82 FAYGQTGSGKTYTMEG-------PPESPGIIPRALQELFNTIkeLKEKGWSYTIKASMLEIYNETIRDLLAPGNAPQKkL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 162 NIREDPKEG-IKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSfRSKLHLVD 240
Cdd:cd01366 155 EIRHDSEKGdTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEIS-VGKLNLVD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 241 LAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGddKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNL 320
Cdd:cd01366 234 LAGSERLNKSGATGDRLKETQAINKSLSALGDVISALR--QKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAESNL 311
|
330
....*....|....*...
gi 116686122 321 EETLNTLRYADRARKIKN 338
Cdd:cd01366 312 NETLNSLRFASKVNSCEL 329
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
10-336 |
3.97e-115 |
|
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: 362.16 E-value: 3.97e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 10 VRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVVGTD--------KSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYN 81
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVRNPkataneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 82 ATVLAYGQTGSGKTYSMGGayTAEQENEPtvGVIPRVIQLLFKEIDKKSDF-EFTLKVSYLEIYNEEILDLLCPSREKaQ 160
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEG--KREDPELR--GIIPNSFAHIFGHIARSQNNqQFLVRVSYLEIYNEEIRDLLGKDQTK-R 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 161 INIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKK-SDKNSSFR-SKLHL 238
Cdd:cd01371 158 LELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKgEDGENHIRvGKLNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 239 VDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGgFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADS 318
Cdd:cd01371 238 VDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDGKST-HIPYRDSKLTRLLQDSLGGNSKTVMCANIGPADY 316
|
330
....*....|....*...
gi 116686122 319 NLEETLNTLRYADRARKI 336
Cdd:cd01371 317 NYDETLSTLRYANRAKNI 334
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
10-336 |
7.22e-115 |
|
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: 360.88 E-value: 7.22e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 10 VRVALRCRPLVPKEISEGCQmCLSFVPGEPQVVVGTDK-SFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAYG 88
Cdd:cd01374 2 ITVTVRVRPLNSREIGINEQ-VAWEIDNDTIYLVEPPStSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 89 QTGSGKTYSMGGAytaeqENEPtvGVIPRVIQLLFKEIDKKSDFEFTLKVSYLEIYNEEILDLLCPsrEKAQINIREDPK 168
Cdd:cd01374 81 QTSSGKTFTMSGD-----EDEP--GIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSP--TSQNLKIRDDVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 169 EGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDK--NSSFRSKLHLVDLAGSER 246
Cdd:cd01374 152 KGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELeeGTVRVSTLNLIDLAGSER 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 247 QKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLNT 326
Cdd:cd01374 232 AAQTGAAGVRRKEGSHINKSLLTLGTVISKLSEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAESHVEETLNT 311
|
330
....*....|
gi 116686122 327 LRYADRARKI 336
Cdd:cd01374 312 LKFASRAKKI 321
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
10-336 |
1.76e-114 |
|
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: 360.89 E-value: 1.76e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 10 VRVALRCRPLVPKEISEGC--------QMCLSFVPGEPQVVV--------------GTDKSFTYDFVFDPSTEQEEVFNT 67
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFrrivkvmdNHMLVFDPKDEEDGFfhggsnnrdrrkrrNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 68 AVAPLIKGVFKGYNATVLAYGQTGSGKTYSMGGAytaeqENEPtvGVIPRVIQLLFKEIDK-KSDFEFTLKVSYLEIYNE 146
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGT-----PQEP--GLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 147 EILDLLCPSreKAQINIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQ--RK 224
Cdd:cd01370 155 TIRDLLNPS--SGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQqdKT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 225 KSDKNSSFRSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGD-DKKGGFVPYRDSKLTRLLQDSLGG 303
Cdd:cd01370 233 ASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADpGKKNKHIPYRDSKLTRLLKDSLGG 312
|
330 340 350
....*....|....*....|....*....|...
gi 116686122 304 NSHTLMIACVSPADSNLEETLNTLRYADRARKI 336
Cdd:cd01370 313 NCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
10-343 |
2.95e-110 |
|
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: 349.70 E-value: 2.95e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 10 VRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVV--------GTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYN 81
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 82 ATVLAYGQTGSGKTYSMGGAYTAEQ----ENEPTVGVIPRVIQLLFKEIDKkSDFEFTLKVSYLEIYNEEILDLLCPSRE 157
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMEGDRSPNEeytwELDPLAGIIPRTLHQLFEKLED-NGTEYSVKVSYLEIYNEELFDLLSPSSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 158 KA-QINIREDP--KEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSFR- 233
Cdd:cd01364 163 VSeRLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEELVk 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 234 -SKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDdkKGGFVPYRDSKLTRLLQDSLGGNSHTLMIAC 312
Cdd:cd01364 243 iGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE--RAPHVPYRESKLTRLLQDSLGGRTKTSIIAT 320
|
330 340 350
....*....|....*....|....*....|.
gi 116686122 313 VSPADSNLEETLNTLRYADRARKIKNKPIVN 343
Cdd:cd01364 321 ISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
10-336 |
5.89e-109 |
|
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: 345.08 E-value: 5.89e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 10 VRVALRCRPLVPKEISEGCQMCLSFvPGEPQVVVGTD---KSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLA 86
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKF-DPEDTVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 87 YGQTGSGKTYSMGGAytaeQENEPTVGVIPRVIQLLFKEIDK-KSDFEFTLKVSYLEIYNEEILDLLCPSreKAQINIRE 165
Cdd:cd01369 83 YGQTSSGKTYTMEGK----LGDPESMGIIPRIVQDIFETIYSmDENLEFHVKVSYFEIYMEKIRDLLDVS--KTNLSVHE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 166 DPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSfRSKLHLVDLAGSE 245
Cdd:cd01369 157 DKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQENVETEKKK-SGKLYLVDLAGSE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 246 RQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKgGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLN 325
Cdd:cd01369 236 KVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKK-THIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESETLS 314
|
330
....*....|.
gi 116686122 326 TLRYADRARKI 336
Cdd:cd01369 315 TLRFGQRAKTI 325
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
9-345 |
8.04e-106 |
|
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: 337.56 E-value: 8.04e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 9 PVRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVVG-TDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAY 87
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 88 GQTGSGKTYSM-GGAYTAEQENEPTVGVIPRVIQLLFKEIDKKSD-----FEFTLKVSYLEIYNEEILDLLCPSreKAQI 161
Cdd:cd01373 82 GQTGSGKTYTMwGPSESDNESPHGLRGVIPRIFEYLFSLIQREKEkagegKSFLCKCSFLEIYNEQIYDLLDPA--SRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 162 NIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQR-KKSDKNSSFRSKLHLVD 240
Cdd:cd01373 160 KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWeKKACFVNIRTSRLNLVD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 241 LAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGGF--VPYRDSKLTRLLQDSLGGNSHTLMIACVSPADS 318
Cdd:cd01373 240 LAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQrhVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSK 319
|
330 340
....*....|....*....|....*..
gi 116686122 319 NLEETLNTLRYADRARKIKNKPIVNID 345
Cdd:cd01373 320 CFGETLSTLRFAQRAKLIKNKAVVNED 346
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
43-352 |
9.64e-90 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 301.66 E-value: 9.64e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 43 VGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAYGQTGSGKTYSMGGaytaeQENEPtvGVIPRVIQLL 122
Cdd:COG5059 52 KSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG-----TEEEP--GIIPLSLKEL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 123 FKEIDKKSDF-EFTLKVSYLEIYNEEILDLLCPSREKaqINIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVA 201
Cdd:COG5059 125 FSKLEDLSMTkDFAVSISYLEIYNEKIYDLLSPNEES--LNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 202 STAMNSQSSRSHAIFTISLEQRKKsDKNSSFRSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDK 281
Cdd:COG5059 203 STEINDESSRSHSIFQIELASKNK-VSGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKK 281
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 116686122 282 KGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLNTLRYADRARKIKNKPIVN----IDPQTAELN 352
Cdd:COG5059 282 KSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNsssdSSREIEEIK 356
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
9-334 |
2.19e-82 |
|
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: 272.45 E-value: 2.19e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 9 PVRVALRCRPLVPKEISEGCQMCLSFVpGEPQVVV------GTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNA 82
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELadprnhGETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 83 TVLAYGQTGSGKTYSMGGaytaeQENEPtvGVIPRVIQLLFkEIDKKSDFEFTLKVSYLEIYNEEILDLLCPSreKAQIN 162
Cdd:cd01376 80 TVFAYGSTGAGKTFTMLG-----SPEQP--GLMPLTVMDLL-QMTRKEAWALSFTMSYLEIYQEKILDLLEPA--SKELV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 163 IREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSFRSKLHLVDLA 242
Cdd:cd01376 150 IREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRTGKLNLIDLA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 243 GSERQKKTKAEGDRLKEGININRGLLCLGNVISALgdDKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEE 322
Cdd:cd01376 230 GSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL--NKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERTFYQD 307
|
330
....*....|..
gi 116686122 323 TLNTLRYADRAR 334
Cdd:cd01376 308 TLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
45-334 |
3.30e-78 |
|
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: 261.36 E-value: 3.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 45 TDKSFTYDFVFDpSTEQEEVFNTAVAPLIKGVFKGYNATVLAYGQTGSGKTYSMGGAytaeQENEPTVGVIPRVIQLLFK 124
Cdd:cd01375 46 EDWSFKFDGVLH-NASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGG----TENYKHRGIIPRALQQVFR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 125 EIDKKSDFEFTLKVSYLEIYNEEILDLLCPSREKAQ----INIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTV 200
Cdd:cd01375 121 MIEERPTKAYTVHVSYLEIYNEQLYDLLSTLPYVGPsvtpMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRII 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 201 ASTAMNSQSSRSHAIFTISLEQRKKSDKNSSFR-SKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGD 279
Cdd:cd01375 201 ASHTMNKNSSRSHCIFTIHLEAHSRTLSSEKYItSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSD 280
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 116686122 280 dKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLNTLRYADRAR 334
Cdd:cd01375 281 -KDRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
9-332 |
9.04e-77 |
|
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: 256.84 E-value: 9.04e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 9 PVRVALRCRPLVPKEISEGCQMCLSfVPGEPQVVV------------GTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGV 76
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIDVVS-VPSKLTLIVhepklkvdltkyIENHTFRFDYVFDESSSNETVYRSTVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 77 FKGYNATVLAYGQTGSGKTYSMGGAYTAEQENEPTVGVIPRVIQLLFKEIDKKSDFEFTlkVSYLEIYNEEILDLLcpsR 156
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTMGGDFSGQEESKGIYALAARDVFRLLNKLPYKDNLGVT--VSFFEIYGGKVFDLL---N 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 157 EKAQINIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKksdKNSSFrSKL 236
Cdd:cd01367 155 RKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRG---TNKLH-GKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 237 HLVDLAGSERQKKTKAEG-DRLKEGININRGLLCLGNVISALGDDKKggFVPYRDSKLTRLLQDSL-GGNSHTLMIACVS 314
Cdd:cd01367 231 SFVDLAGSERGADTSSADrQTRMEGAEINKSLLALKECIRALGQNKA--HIPFRGSKLTQVLKDSFiGENSKTCMIATIS 308
|
330
....*....|....*...
gi 116686122 315 PADSNLEETLNTLRYADR 332
Cdd:cd01367 309 PGASSCEHTLNTLRYADR 326
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
9-334 |
3.09e-75 |
|
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: 253.09 E-value: 3.09e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 9 PVRVALRCRPLVPKEISEGCQMCL------SFVPGEPQVVVGTDKS---------FTYDFVFDPSTEQEEVFNTAVAPLI 73
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIevinstTVVLHPPKGSAANKSErnggqketkFSFSKVFGPNTTQKEFFQGTALPLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 74 KGVFKGYNATVLAYGQTGSGKTYSMGGaytaeqeNEPTVGVIPRVIQLLFKEIDKKSDFeftlkVSYLEIYNEEILDLLC 153
Cdd:cd01368 82 QDLLHGKNGLLFTYGVTNSGKTYTMQG-------SPGDGGILPRSLDVIFNSIGGYSVF-----VSYIEIYNEYIYDLLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 154 PS-----REKAQINIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQ------ 222
Cdd:cd01368 150 PSpssptKKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQapgdsd 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 223 -RKKSDKNSSFRSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGGF---VPYRDSKLTRLLQ 298
Cdd:cd01368 230 gDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTnkmVPFRDSKLTHLFQ 309
|
330 340 350
....*....|....*....|....*....|....*.
gi 116686122 299 DSLGGNSHTLMIACVSPADSNLEETLNTLRYADRAR 334
Cdd:cd01368 310 NYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
10-355 |
1.61e-70 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 259.48 E-value: 1.61e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 10 VRVALRCRPLVPKEISEgcqMCLSFVPGEPQVVVGtdKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAYGQ 89
Cdd:PLN03188 100 VKVIVRMKPLNKGEEGE---MIVQKMSNDSLTING--QTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 90 TGSGKTYSM-GGAYTAEQEN--EPTVGVIPRVIQLLFKEIDKKS------DFEFTLKVSYLEIYNEEILDLLCPSREKAQ 160
Cdd:PLN03188 175 TGSGKTYTMwGPANGLLEEHlsGDQQGLTPRVFERLFARINEEQikhadrQLKYQCRCSFLEIYNEQITDLLDPSQKNLQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 161 IniREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKS--DKNSSFR-SKLH 237
Cdd:PLN03188 255 I--REDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSvaDGLSSFKtSRIN 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 238 LVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGG---FVPYRDSKLTRLLQDSLGGNSHTLMIACVS 314
Cdd:PLN03188 333 LVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGkqrHIPYRDSRLTFLLQESLGGNAKLAMVCAIS 412
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 116686122 315 PADSNLEETLNTLRYADRARKIKNKPIVNIDPQTaELNHLK 355
Cdd:PLN03188 413 PSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQD-DVNFLR 452
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
46-315 |
1.80e-22 |
|
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: 95.49 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 46 DKSFTYDFVFDPSTEQEEVFNTAvAPLIKGVFKGYN-ATVLAYGQTGSGKTYSMggaytaeqeneptVGVIPRVIQLLFK 124
Cdd:cd01363 17 SKIIVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGESGAGKTETM-------------KGVIPYLASVAFN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 125 EIDKKS-DFEFTLKVSYLEIYNeEILDLLcPSREKAqiniredpkegikivgltektvlvaldtvscleqGNnsrtvAST 203
Cdd:cd01363 83 GINKGEtEGWVYLTEITVTLED-QILQAN-PILEAF----------------------------------GN-----AKT 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 204 AMNSQSSRSHAIFTIsleqrkksdknssfrsklhLVDLAGSERqkktkaegdrlkeginINRGLLCLGNVISAlgddkkg 283
Cdd:cd01363 122 TRNENSSRFGKFIEI-------------------LLDIAGFEI----------------INESLNTLMNVLRA------- 159
|
250 260 270
....*....|....*....|....*....|..
gi 116686122 284 gfvpyrdskltrllqdslggnSHTLMIACVSP 315
Cdd:cd01363 160 ---------------------TRPHFVRCISP 170
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
3-152 |
4.39e-17 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 79.19 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 3 EEVKGiPVRVALRCRPLVPKEisegCQMCLSFVPGEPQVVVGTDKSFTYDFVFDPSTEQEEVFNTaVAPLIKGVFKGYNA 82
Cdd:pfam16796 16 QELKG-NIRVFARVRPELLSE----AQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQE-ISQLVQSCLDGYNV 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116686122 83 TVLAYGQTGSGKtysmggaytaeqenepTVGVIPRVIQLLFKEI-DKKSDFEFTLKVSYLEIYNEEILDLL 152
Cdd:pfam16796 90 CIFAYGQTGSGS----------------NDGMIPRAREQIFRFIsSLKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
517-1033 |
5.42e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.82 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 517 LRQAQMSKELVELNKALALKEALARKMTQNDSQLQpiqyQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAklsE 596
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELELEEAQAEEYELLAELARLEQDIARL---E 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 597 RRRK----RLQELEGQIADLKKKLNEQSKLLklkESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEV 672
Cdd:COG1196 309 ERRReleeRLEELEEELAELEEELEELEEEL---EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 673 IQLKERDRKRQyELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEIE 752
Cdd:COG1196 386 EELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 753 VMVSTEEAKRHLNDLLEDRKILAQDVAQLK-----EKKESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEM 827
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLllleaEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 828 EFRSAQ------------IADLQQKLL------------DAESEDRPKQRWENIATILEAKCALKYLigELVSSKIQVSK 883
Cdd:COG1196 545 AAALQNivveddevaaaaIEYLKAAKAgratflpldkirARAALAAALARGAIGAAVDLVASDLREA--DARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 884 LESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQHQEKvlyLLSQLQQSQMAEKQLEESVSEKEQQLLSTL 963
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE---LLAALLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 964 KCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQvASRQKHLPKDTLLSPDSSFEYVPPKPKPSRVKEK 1033
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAER-EELLEELLEEEELLEEEALEELPEPPDLEELERE 768
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
385-971 |
3.31e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 385 LQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQhaacklDLQKLVETLEDQELKENVE 464
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA------EEYELLAELARLEQDIARL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 465 iicnlQQLITQLSDEtvacmaaaIDTAVEQEAQVETspetsrssdafttQHALRQAQMSKELVELNKALALKEALARKMT 544
Cdd:COG1196 308 -----EERRRELEER--------LEELEEELAELEE-------------ELEELEEELEELEEELEEAEEELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 545 QNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLK 624
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 625 LKESTErtvsklnqeirmmknqrvqlmrqmkedaekfRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKT 704
Cdd:COG1196 442 EALEEA-------------------------------AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 705 EEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVkNWLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEK 784
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL-IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 785 KESGEN--PPPKLRRRTFSLTEVRGQVSESEdsitkqIESLETEMEFRSAQIADLQQKLLDAESEDRPKQRWENIATILE 862
Cdd:COG1196 570 KAGRATflPLDKIRARAALAAALARGAIGAA------VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 863 AKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQHQEKVLYLLSQLQQSQ 942
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
570 580
....*....|....*....|....*....
gi 116686122 943 MAEKQLEESVSEKEQQLLSTLKCQDEELE 971
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEEEA 752
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
491-1004 |
1.17e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 491 AVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELevin 570
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEA---- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 571 lQKEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQEIRMMKNQRVQL 650
Cdd:PTZ00121 1321 -KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKK 1399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 651 MRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEA--------AAANKRLKDALQKQR 722
Cdd:PTZ00121 1400 AEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAkkaeeakkKAEEAKKADEAKKKA 1479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 723 EVADKRKETQSRGMEGTA----ARVKNWLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRR 798
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKkadeAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKK 1559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 799 TFSLTEVRGQVSESED--------SITKQIESLETEmEFRSAQIADLQQKLLDAESEDRPKQRWENIATILEAKCALKYL 870
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDknmalrkaEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQL 1638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 871 IGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQ-QHQEKVLYLLSQLQQSQMAEKQLE 949
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlKKEAEEAKKAEELKKKEAEEKKKA 1718
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 116686122 950 ESVSEKEQQllstLKCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQVASRQK 1004
Cdd:PTZ00121 1719 EELKKAEEE----NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKK 1769
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
385-734 |
1.44e-09 |
|
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: 62.78 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 385 LQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQhaacklDLQKLVETLED--QELKEN 462
Cdd:TIGR02169 690 LSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE------DLSSLEQEIENvkSELKEL 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 463 VEIICNLQQLITQLSDETvacmaaaidTAVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKaLALKEALARK 542
Cdd:TIGR02169 764 EARIEELEEDLHKLEEAL---------NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 543 MTQNdsqLQPIQYQYQDNIKELELEVINLQKEKEELVLELqtakkdanqaklsERRRKRLQELEGQIADLKKKLNE-QSK 621
Cdd:TIGR02169 834 EIQE---LQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL-------------EELEAALRDLESRLGDLKKERDElEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 622 LLKLKESTERTVSKLNQEIRMMKNQRVQLmrQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLR 701
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKL--EALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNM 975
|
330 340 350
....*....|....*....|....*....|...
gi 116686122 702 RKTEEAAAANKRLKDALQKQREVADKRKETQSR 734
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEKRAKLEEERKAILER 1008
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
558-847 |
4.27e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 558 QDNIKELE--LEVINLQKEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSK 635
Cdd:COG1196 192 EDILGELErqLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 636 LNQEIRMMK---NQRVQLMRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANK 712
Cdd:COG1196 272 LRLELEELElelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 713 RLKDALQKQREVADKRKETQSRGMEGTAARVKNW------LGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKE 786
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAeelleaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116686122 787 SGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLLDAESE 847
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR 492
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
493-992 |
5.38e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 493 EQEAQVEtspETSRSSDAFTTQHALRQAQMSKELVELNKalaLKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQ 572
Cdd:PTZ00121 1221 EDAKKAE---AVKKAEEAKKDAEEAKKAEEERNNEEIRK---FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADE 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 573 KEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQEIRMMKNQRVQLMR 652
Cdd:PTZ00121 1295 AKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 653 QMKEDAEKFRQWKQKKDK--EVIQLKERDRKRQYELLKLERNfQKQSNVLRRKTEEAAAAN--------KRLKDALQKQR 722
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAA-KKKADEAKKKAEEKKKADeakkkaeeAKKADEAKKKA 1453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 723 EVADKRKETQSRGMEGTAARVKNWLGNEI----EVMVSTEEAKRHLNDL--LEDRKILAQDVAQLKEKKESGENPPPKLR 796
Cdd:PTZ00121 1454 EEAKKAEEAKKKAEEAKKADEAKKKAEEAkkadEAKKKAEEAKKKADEAkkAAEAKKKADEAKKAEEAKKADEAKKAEEA 1533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 797 RRTFSLTEVRgQVSESEDsiTKQIESLETEMEFRSAqiadlQQKLLDAESEDRPKQRWENIATILEAKC-ALKYLIGELV 875
Cdd:PTZ00121 1534 KKADEAKKAE-EKKKADE--LKKAEELKKAEEKKKA-----EEAKKAEEDKNMALRKAEEAKKAEEARIeEVMKLYEEEK 1605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 876 SSKIQVSKLESSLKQSktscADMQKMLFEERNHFAEIETELQAELVRMEQQHQEKVLYLLSQLQQSQMAE---KQLEES- 951
Cdd:PTZ00121 1606 KMKAEEAKKAEEAKIK----AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEedkKKAEEAk 1681
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 116686122 952 -VSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRENEIIKQ 992
Cdd:PTZ00121 1682 kAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
598-994 |
1.26e-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: 59.69 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 598 RRKRLQELEGQIADLKKKLNEQSKLLKlkestertvsKLNQEIRMMKNQRVQLMRQMKEDAEKFRQwkQKKDKEVIQLKE 677
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALA----------ELRKELEELEEELEQLRKELEELSRQISA--LRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 678 RDRKRQYELLKLER-NFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETqsrgmegtaarvknwlgneievMVS 756
Cdd:TIGR02168 743 EQLEERIAQLSKELtELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE----------------------LKA 800
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 757 TEEAKRHLNDLLEDrkiLAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSAQIAD 836
Cdd:TIGR02168 801 LREALDELRAELTL---LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEA 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 837 LQqklldaesedrpKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETEL 916
Cdd:TIGR02168 878 LL------------NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 917 QAELVRMEQQHQEKVLYLLSQLQQSQMAEKQLEESVS-------------EKEQQLLSTLKCQDEELEKMRevcEQNQQL 983
Cdd:TIGR02168 946 SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKelgpvnlaaieeyEELKERYDFLTAQKEDLTEAK---ETLEEA 1022
|
410
....*....|..
gi 116686122 984 LRE-NEIIKQKL 994
Cdd:TIGR02168 1023 IEEiDREARERF 1034
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
518-839 |
1.56e-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: 59.30 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 518 RQAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELvlelqTAKKDANQAKLSER 597
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL-----EERLEEAEEELAEA 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 598 RRKRlQELEGQIADLKKKLNEQSKLLKlkeSTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDK---EVIQ 674
Cdd:TIGR02168 781 EAEI-EELEAQIEQLKEELKALREALD---ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEElseDIES 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 675 LKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRgmegtaarvknwlgneievm 754
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRE-------------------- 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 755 vsTEEAKRHLNDLLEDRKILAQDVAQLKEK-----KESGENPPPKLRRRTFSLTEVRGQVSESEDSITK----------Q 819
Cdd:TIGR02168 917 --LEELREKLAQLELRLEGLEVRIDNLQERlseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaaieE 994
|
330 340
....*....|....*....|
gi 116686122 820 IESLETEMEFRSAQIADLQQ 839
Cdd:TIGR02168 995 YEELKERYDFLTAQKEDLTE 1014
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
377-993 |
2.17e-08 |
|
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: 58.90 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 377 ITVEPSENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMlERIILTEQANEKMNAKLEELRQHAACKLdLQKLVETLED 456
Cdd:TIGR00606 431 IRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSS-DRILELDQELRKAERELSKAEKNSLTET-LKKEVKSLQN 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 457 QELkENVEIICNLQQLITQLSDETVACMAAAIDTAVEQEAQVETSPETSRSSDAFTTQ--------------HALRQ--A 520
Cdd:TIGR00606 509 EKA-DLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnkkqledwlHSKSKeiN 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 521 QMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNI------KELELEVINLQKE-----KEELVLELQTAKKDA 589
Cdd:TIGR00606 588 QTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEiekssKQRAMLAGATAVYSQ 667
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 590 NQAKLSERRR------KRLQELEGQIADLKKKLNEQSKLLKLK-ESTERTVSKLNQEIRMMKNQrvqlmrqmkedAEKFR 662
Cdd:TIGR00606 668 FITQLTDENQsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKlKSTESELKKKEKRRDEMLGL-----------APGRQ 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 663 QWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDA-----LQKQREVADKRKETQSRGME 737
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVtimerFQMELKDVERKIAQQAAKLQ 816
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 738 GtaarvknwlgneIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRGQVSESedsiT 817
Cdd:TIGR00606 817 G------------SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTN----L 880
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 818 KQIESLETEMEFRSAQIADLQQKLLDAESEDRPkqrwenIATILEAKCALKyliGELVSSKiqvsklESSLKQSKTSCAD 897
Cdd:TIGR00606 881 QRRQQFEEQLVELSTEVQSLIREIKDAKEQDSP------LETFLEKDQQEK---EELISSK------ETSNKKAQDKVND 945
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 898 MQKMLFEERNHFAEIETELQAELVRMEQQHQEKVLYLLSQLQQSQMAEKQLEESVSEKEQQLLS------------TLKC 965
Cdd:TIGR00606 946 IKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTqkiqerwlqdnlTLRK 1025
|
650 660
....*....|....*....|....*...
gi 116686122 966 QDEELEKMREVCEQNQQLLRENEIIKQK 993
Cdd:TIGR00606 1026 RENELKEVEEELKQHLKEMGQMQVLQMK 1053
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
527-853 |
2.41e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 527 VELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELE--LEVINLQKEKEELVLELQTAKKDANQAKLsERRRKRLQE 604
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkaERYQALLKEKREYEGYELLKEKEALERQK-EAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 605 LEGQIADLKKKLNEQSKLLklkESTERTVSKLNQEIR-MMKNQRVQLMRQMKE---------DAEKFRQWKQKK-DKEVI 673
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRL---EEIEQLLEELNKKIKdLGEEEQLRVKEKIGEleaeiasleRSIAEKERELEDaEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 674 QLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEgtaarvknwlgneieV 753
Cdd:TIGR02169 326 KLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------------Y 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 754 MVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSAQ 833
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQE 470
|
330 340
....*....|....*....|
gi 116686122 834 IADLQQKLLDAESEDRPKQR 853
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKLQR 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
657-996 |
5.16e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.77 E-value: 5.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 657 DAEKFRQWKQKKDK-EVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDaLQKQREVADKRKETQSRG 735
Cdd:TIGR02169 660 RAPRGGILFSRSEPaELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGE-IEKEIEQLEQEEEKLKER 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 736 MEGTAARVKnwlgneiEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKES-----GENPPPKLRRRTFSLTEVRGQVS 810
Cdd:TIGR02169 739 LEELEEDLS-------SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 811 ESEDSITKQIESLETEMEFRSAQIADLQQKLLDAESedrpkQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQ 890
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE-----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 891 SKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQhQEKVLYLLSQLQQSQMAEKQLEESVSEK--EQQLLSTLKCQDE 968
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL-KAKLEALEEELSEIEDPKGEDEEIPEEElsLEDVQAELQRVEE 965
|
330 340 350
....*....|....*....|....*....|...
gi 116686122 969 ELEKMREVC-----EQNQQLLRENEIIKQKLTL 996
Cdd:TIGR02169 966 EIRALEPVNmlaiqEYEEVLKRLDELKEKRAKL 998
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
383-844 |
7.51e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.87 E-value: 7.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 383 ENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQHAACKLDLQKLVETLEDQELKEN 462
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 463 VEIIcNLQQLITQLSDETVACMAAAIDTAVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKALALKEALARK 542
Cdd:COG1196 421 EELE-ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 543 MTQNDSQLQPIQYQYQ-DNIKELELEVINLQKEKEELVLELQTAKkdanQAKLSERRRKRLQELEGQIADLKKKLNEQSK 621
Cdd:COG1196 500 EADYEGFLEGVKAALLlAGLRGLAGAVAVLIGVEAAYEAALEAAL----AAALQNIVVEDDEVAAAAIEYLKAAKAGRAT 575
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 622 LLKLKESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFR----------QWKQKKDKEVIQLKERDRKRQYELLKLER 691
Cdd:COG1196 576 FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYvlgdtllgrtLVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 692 NFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEIEVMVSTEEAKRHLNDLLEDR 771
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 772 KILAQDVAQLKEKKESGENPPPKLrrrtFSLTEVRGQVseseDSITKQIESL--------------ETEMEFRSAQIADL 837
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEP----PDLEELEREL----ERLEREIEALgpvnllaieeyeelEERYDFLSEQREDL 807
|
490
....*....|
gi 116686122 838 QQ---KLLDA 844
Cdd:COG1196 808 EEareTLEEA 817
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
516-810 |
7.58e-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: 56.99 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 516 ALRQAQMS---KELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQT-----AKK 587
Cdd:TIGR02168 221 ELRELELAllvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaneiSRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 588 DANQAKLSERRR---KRLQELEGQIADLKKKLNEQSKLLKlkestertvsKLNQEIRMMKNQRVQLMRQMKEDAEKFRQW 664
Cdd:TIGR02168 301 EQQKQILRERLAnleRQLEELEAQLEELESKLDELAEELA----------ELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 665 KQKKDKeviQLKERDRKRQyELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVK 744
Cdd:TIGR02168 371 ESRLEE---LEEQLETLRS-KVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELE 446
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116686122 745 NWLgneievmvstEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRGQVS 810
Cdd:TIGR02168 447 EEL----------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
460-988 |
9.59e-08 |
|
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: 56.52 E-value: 9.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 460 KENVEIICNLQQL--ITQLSDETVACMAAAIDTAVEQEAQVETspETSRSSDAFTTQHALRQAQmSKELVELNKALALKE 537
Cdd:TIGR00618 163 KEKKELLMNLFPLdqYTQLALMEFAKKKSLHGKAELLTLRSQL--LTLCTPCMPDTYHERKQVL-EKELKHLREALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 538 ALARKMTQND------SQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRKR---LQELEGQ 608
Cdd:TIGR00618 240 QSHAYLTQKReaqeeqLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAqriHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 609 IADLKKKLNEQSKLLKLKESTERTVSKLN----QEIRMMKNQRVQLMR-----QMKEDAEKFRQWKQKK--DKEVIQL-- 675
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIEEQRRLLQtlhsQEIHIRDAHEVATSIreiscQQHTLTQHIHTLQQQKttLTQKLQSlc 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 676 ----KERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDA-------LQKQREVADKRKETQSRGMEGTAARVK 744
Cdd:TIGR00618 400 keldILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAaitctaqCEKLEKIHLQESAQSLKEREQQLQTKE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 745 NWLGNEIEVmvSTEEAKRhLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRR------RTFSLTEVRGQVSESEDSITK 818
Cdd:TIGR00618 480 QIHLQETRK--KAVVLAR-LLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRmqrgeqTYAQLETSEEDVYHQLTSERK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 819 QIESLETEMEfrsaQIADLQQKLldAESEDRPKQRWENIATILEAkcaLKYLIGELVSSKIQVSKLESSLKQSKTSCADM 898
Cdd:TIGR00618 557 QRASLKEQMQ----EIQQSFSIL--TQCDNRSKEDIPNLQNITVR---LQDLTEKLSEAEDMLACEQHALLRKLQPEQDL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 899 QKMLFEERNhfaeIETELQAELVRMEQqhqekvlYLLSQLQQSQ----MAEKQLEESVSEKEQQLLSTLKCQDEELEKMR 974
Cdd:TIGR00618 628 QDVRLHLQQ----CSQELALKLTALHA-------LQLTLTQERVrehaLSIRVLPKELLASRQLALQKMQSEKEQLTYWK 696
|
570
....*....|....
gi 116686122 975 EVCEQNQQLLRENE 988
Cdd:TIGR00618 697 EMLAQCQTLLRELE 710
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
413-1004 |
1.29e-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: 56.22 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 413 TAQMLERI--ILTEqanekMNAKLEELRQHAACKLDLQKLVETLEDQELkenveiicnlqQLITQLSDETVACMAAAIDT 490
Cdd:TIGR02168 184 TRENLDRLedILNE-----LERQLKSLERQAEKAERYKELKAELRELEL-----------ALLVLRLEELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 491 AVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVIN 570
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 571 LQKEKEELVLELQTAKKDANQAK-LSERRRKRLQELEGQIADLKKKLNEQSKLLklkESTERTVSKLNQEIRMMKNQRVQ 649
Cdd:TIGR02168 328 LESKLDELAEELAELEEKLEELKeELESLEAELEELEAELEELESRLEELEEQL---ETLRSKVAQLELQIASLNNEIER 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 650 LMRQMKEDAEKFRQWKQKKDKEVIQLKERDRKR-QYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKR 728
Cdd:TIGR02168 405 LEARLERLEDRRERLQQEIEELLKKLEEAELKElQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 729 KETQSRG---------MEGTAARVKNWLGNE-------------IEVMVSTEEAKR-----HLNDLL-EDRKILAQDVAQ 780
Cdd:TIGR02168 485 AQLQARLdslerlqenLEGFSEGVKALLKNQsglsgilgvlselISVDEGYEAAIEaalggRLQAVVvENLNAAKKAIAF 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 781 LKEKKESGENPPPKLRRRTFSLTEVRGQVSESED---------------------------------------------- 814
Cdd:TIGR02168 565 LKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgflgvakdlvkfdpklrkalsyllggvlvvddldnalelakklrpg 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 815 ---------------SITKQIESLETEMEFRSAQIADLQQKLLDAESEdrpkqrweniatILEAKCALKYLigelvssKI 879
Cdd:TIGR02168 645 yrivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEK------------IAELEKALAEL-------RK 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 880 QVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQHQEkvlylLSQLQQSQMAEKQLEESVSEKEQQL 959
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE-----LTELEAEIEELEERLEEAEEELAEA 780
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 116686122 960 LSTLKCQDEELEKMREVCEQNQQLLREneiIKQKLTLLQVASRQK 1004
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDE---LRAELTLLNEEAANL 822
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
383-1012 |
2.50e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.36 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 383 ENLQSLMEKNQSLVEENEKLsrglseaagqtaqmlERIILTEQANEKMNAKLEELRQHAAcKLDLQKLVETLEDQeLKEN 462
Cdd:pfam02463 173 EALKKLIEETENLAELIIDL---------------EELKLQELKLKEQAKKALEYYQLKE-KLELEEEYLLYLDY-LKLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 463 VEIICNLQQLITQLSDETvACMAAAIDTAVEQEAQVETSPETSRSSDAFTTqhaLRQAQMSKELVELNKALALKEALARK 542
Cdd:pfam02463 236 EERIDLLQELLRDEQEEI-ESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE---EELKLLAKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 543 MTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELV-----LELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLN 617
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEikreaEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 618 EQSKLLKLKESTERTVSKLN---QEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEV----IQLKERDRKRQYELLKLE 690
Cdd:pfam02463 392 LKEEELELKSEEEKEAQLLLelaRQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEkeelEKQELKLLKDELELKKSE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 691 RNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVAD--KRKETQSRGMEGTAARVKNWLGNEIEVMVSTEEAKRHLNDLL 768
Cdd:pfam02463 472 DLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSglKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIV 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 769 EDRKILAQDVAQLKEKKESGENPPPKLRRRTFS----LTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLLDA 844
Cdd:pfam02463 552 EVSATADEVEERQKLVRALTELPLGARKLRLLIpklkLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKD 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 845 ESEDRPKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCAD--MQKMLFEERNHFAEIETELQAELVR 922
Cdd:pfam02463 632 TELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKaeSELAKEEILRRQLEIKKKEQREKEE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 923 MEQQHQEKVLYLLS--QLQQSQMAEKQLEESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQVA 1000
Cdd:pfam02463 712 LKKLKLEAEELLADrvQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
650
....*....|..
gi 116686122 1001 SRQKHLPKDTLL 1012
Cdd:pfam02463 792 KEEKLKAQEEEL 803
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
636-1025 |
3.94e-07 |
|
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: 54.36 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 636 LNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEViQLKERDRKRQYELLKLERN--FQKQSNVLRRKTEEAAAANKR 713
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEE-KAREVERRRKLEEAEKARQaeMDRQAAIYAEQERMAMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 714 LKDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEI----EVMVSTEEAKRHLNDLLED--RKILAQDVAQLKEKKES 787
Cdd:pfam17380 350 LERIRQEERKRELERIRQEEIAMEISRMRELERLQMERqqknERVRQELEAARKVKILEEErqRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 788 GENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETemefrsaQIADLQQKLLDAESEDRPKQRWENIATileakcal 867
Cdd:pfam17380 430 EEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQ-------QEEERKRKKLELEKEKRDRKRAEEQRR-------- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 868 KYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEErnhfaeiETELQAELVRMEQQHQEKVLYLLSQLQQSQMAEKQ 947
Cdd:pfam17380 495 KILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-------ERRREAEEERRKQQEMEERRRIQEQMRKATEERSR 567
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116686122 948 LEesVSEKEQQLLSTLKcqdeELEKMREVCEQNQQLLRENEIIKQKLTLLQVASRQKHLPKDTLLSPdssfEYVPPKP 1025
Cdd:pfam17380 568 LE--AMEREREMMRQIV----ESEKARAEYEATTPITTIKPIYRPRISEYQPPDVESHMIRFTTQSP----EWATPSP 635
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
382-745 |
4.80e-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: 54.29 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 382 SENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQM---LERIILTEQANEKMNAKLEELRQHAACKLDLQKLVETLEDQE 458
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALrkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 459 LKENVEIICNLQQLITQLSDEtvacMAAAIDTAVEQEAQVetspetSRSSDAFTTQhALRQAQMSKELVELNKALALKEA 538
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEE----LKALREALDELRAEL------TLLNEEAANL-RERLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 539 LARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAklserrRKRLQELEGQIADLKKKLNE 618
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL------SEELRELESKRSELRRELEE 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 619 QSKLLklkESTERTVSKLNQEIRmmkNQRVQLMRQMKEDAEKFRQWKQKKDKEVIQLKERdrkrqyeLLKLERNFQKQSN 698
Cdd:TIGR02168 920 LREKL---AQLELRLEGLEVRID---NLQERLSEEYSLTLEEAEALENKIEDDEEEARRR-------LKRLENKIKELGP 986
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 116686122 699 VLRRKTEEAAAANKRlKDALQKQREVADKRKETQSRGMEGTAARVKN 745
Cdd:TIGR02168 987 VNLAAIEEYEELKER-YDFLTAQKEDLTEAKETLEEAIEEIDREARE 1032
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
538-726 |
8.36e-07 |
|
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: 52.84 E-value: 8.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 538 ALARKMTQNDSQLQPIQYQyqdnIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERR--------RKRLQELEGQI 609
Cdd:COG4942 17 AQADAAAEAEAELEQLQQE----IAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqelaalEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 610 ADLKKKLNEQSKLLK-------LKESTERTVSKLNQE-----IRMMK------NQRVQLMRQMKEDAEKFRQWKQKKDKE 671
Cdd:COG4942 93 AELRAELEAQKEELAellralyRLGRQPPLALLLSPEdfldaVRRLQylkylaPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 116686122 672 VIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVAD 726
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
650-997 |
8.82e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 650 LMRQMKEDAEK-FRQWKQKKDKEVIQLKERDRKRQyELLKLERNFQKQSNVLRRKTEEAAAANKRLKDAlqkQREVADKR 728
Cdd:COG4717 47 LLERLEKEADElFKPQGRKPELNLKELKELEEELK-EAEEKEEEYAELQEELEELEEELEELEAELEEL---REELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 729 KETQSRGMEGTAARVKNWLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEK-KESGENPPPKLRRRTFSLTEVRG 807
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 808 QVSESEDSITKQIESLETEMEFRSAQIADLQQKLLDAESEDRPKQrWENIATILEAKCALKYLIGELVSSKIQVSKL--- 884
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKE-ARLLLLIAAALLALLGLGGSLLSLILTIAGVlfl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 885 ---------ESSLKQSKTSCADMQKMLF---------EERNHFAE---IETELQAELVRMEQQHQEKVLYLLSQLQQsqm 943
Cdd:COG4717 282 vlgllallfLLLAREKASLGKEAEELQAlpaleeleeEELEELLAalgLPPDLSPEELLELLDRIEELQELLREAEE--- 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 116686122 944 AEKQLEESVSEKE-QQLLSTLKCQDEE-LEKMREVCEQNQQLLRENEIIKQKLTLL 997
Cdd:COG4717 359 LEEELQLEELEQEiAALLAEAGVEDEEeLRAALEQAEEYQELKEELEELEEQLEEL 414
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
802-1004 |
9.49e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 9.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 802 LTEVRGQVSESEDSITK-----QIESLETEMEFRSAQIADLQQKLLDAESEdrpkqrweniatILEAKCALKYLIGELVS 876
Cdd:COG3206 184 LPELRKELEEAEAALEEfrqknGLVDLSEEAKLLLQQLSELESQLAEARAE------------LAEAEARLAALRAQLGS 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 877 SKIQVSKLESS--LKQSKTSCADMQKMLFEERNHFAE-------IETELQAELVRMEQQHQEKVLYLLSQLQQSQMAEKQ 947
Cdd:COG3206 252 GPDALPELLQSpvIQQLRAQLAELEAELAELSARYTPnhpdviaLRAQIAALRAQLQQEAQRILASLEAELEALQAREAS 331
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 116686122 948 LEESVSEKEQQLLSTLKCQDEELEKMREVcEQNQQLLREneiIKQKLTLLQVASRQK 1004
Cdd:COG3206 332 LQAQLAQLEARLAELPELEAELRRLEREV-EVARELYES---LLQRLEEARLAEALT 384
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
380-1005 |
1.19e-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: 53.13 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 380 EPSENLQSLMEKNQSLV------EENEKLSRGLSEAAGQTAQMLEriiltEQANEKMNAKLEELRQHAACKLDLQKLVET 453
Cdd:TIGR00606 256 EIEHNLSKIMKLDNEIKalksrkKQMEKDNSELELKMEKVFQGTD-----EQLNDLYHNHQRTVREKERELVDCQRELEK 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 454 L--EDQELKENVEIICNlQQLITQLSDETVACMAAAIDTAVEQEA------QVETSPETSRSSDAFTTQHALRQAQMSKE 525
Cdd:TIGR00606 331 LnkERRLLNQEKTELLV-EQGRLQLQADRHQEHIRARDSLIQSLAtrleldGFERGPFSERQIKNFHTLVIERQEDEAKT 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 526 LVELNKALALKEALARKmtqndsQLQPIQYQYQDNIKELELEVINLQKEKEEL---VLELQTA--------KKD------ 588
Cdd:TIGR00606 410 AAQLCADLQSKERLKQE------QADEIRDEKKGLGRTIELKKEILEKKQEELkfvIKELQQLegssdrilELDqelrka 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 589 ------ANQAKLSERRRKRLQELEGQIADLKKKL----------NEQSKLLKLKESTERTVSKLNQEIRMMKNQRVQLMR 652
Cdd:TIGR00606 484 erelskAEKNSLTETLKKEVKSLQNEKADLDRKLrkldqemeqlNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELT 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 653 QMKED---AEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVAD--- 726
Cdd:TIGR00606 564 SLLGYfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDler 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 727 -KRKETQSRGMEGTAARVKNWLGNEIEVMVSTEEA-----------KRHLNDLLEDrkiLAQDVAQLKEKKESGENPPPK 794
Cdd:TIGR00606 644 lKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqtEAELQEFISD---LQSKLRLAPDKLKSTESELKK 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 795 L-RRRTFSLTEVRGQVSESeDSITKQIESLETEMEFRSAQIADLQQKLLDAESEDRPKQRWENIATILEAKCALK---YL 870
Cdd:TIGR00606 721 KeKRRDEMLGLAPGRQSII-DLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMerfQM 799
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 871 IGELVSSKI--QVSKLESSLKQSKTSCADMQKmlfEERNHFAEIETELQAELVRMEQQHQEKVLYLLSQLQQSQMAEKQL 948
Cdd:TIGR00606 800 ELKDVERKIaqQAAKLQGSDLDRTVQQVNQEK---QEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI 876
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 116686122 949 EESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQVASRQKH 1005
Cdd:TIGR00606 877 GTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKE 933
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
503-800 |
1.23e-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: 53.15 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 503 ETSRSSDAFTTQHALRQAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKEL---ELEVINLQKEKEELV 579
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIeelEEDLHKLEEALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 580 LELQTAKKDANQAKLSERRrKRLQELEGQIADLKKKLNeqsKLLKLKESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAE 659
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLE-EEVSRIEARLREIEQKLN---RLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 660 KFRQWKQKKDKevIQLKERDRKRQYELLKLER-NFQKQSNVLRRKTEEAAA----ANKRLKDALQKQREVADKRKETQSR 734
Cdd:TIGR02169 862 KKEELEEELEE--LEAALRDLESRLGDLKKERdELEAQLRELERKIEELEAqiekKRKRLSELKAKLEALEEELSEIEDP 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 735 GME-----------GTAARVKNWLGNEIEVMVST--------EEAKRHLNDLLEDRKILAQDVAQLKEKKESGEnpppKL 795
Cdd:TIGR02169 940 KGEdeeipeeelslEDVQAELQRVEEEIRALEPVnmlaiqeyEEVLKRLDELKEKRAKLEEERKAILERIEEYE----KK 1015
|
....*
gi 116686122 796 RRRTF 800
Cdd:TIGR02169 1016 KREVF 1020
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
561-838 |
1.43e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 561 IKELELEVINLQK--EKEELVLELQTAKKDANQAKLSERR--RKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKL 636
Cdd:PRK03918 171 IKEIKRRIERLEKfiKRTENIEELIKEKEKELEEVLREINeiSSELPELREELEKLEKEVKELEELKEEIEELEKELESL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 637 NQEIRMMKNQRVQLMRQMKEDAEKFR------------QWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKT 704
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEeleekvkelkelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 705 EEAAAANKRLKdalqkqrEVADKRKETQSRGMEgtaarvknwlgneievmvsteeakrhlndlLEDRKILAQDVAQLKE- 783
Cdd:PRK03918 331 KELEEKEERLE-------ELKKKLKELEKRLEE------------------------------LEERHELYEEAKAKKEe 373
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 116686122 784 ----KKESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQ 838
Cdd:PRK03918 374 lerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
591-835 |
1.47e-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: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 591 QAKLSERRRKRLQELEGQIADLKKKLN----EQSKLLKLKESTERTVSKLNQEIRMMKNQRVQLMRQMKEdaekfrqwkq 666
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAalkkEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 667 kKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKEtQSRGMEGTAARVKnw 746
Cdd:COG4942 88 -LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARRE-QAEELRADLAELA-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 747 lgneiEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENpppKLRRRTFSLTEVRGQVSESEDSITKQIESLETE 826
Cdd:COG4942 164 -----ALRAELEAERAELEALLAELEEERAALEALKAERQKLLA---RLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*....
gi 116686122 827 MEFRSAQIA 835
Cdd:COG4942 236 AAAAAERTP 244
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
518-994 |
4.56e-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: 51.33 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 518 RQAQMSKELVELNKALAlkeALARKMTQNDSQLQPIQYQYQDNiKELELEVINLQKEKEELVLELQT---AKKDANQAKL 594
Cdd:pfam01576 20 RQQKAESELKELEKKHQ---QLCEEKNALQEQLQAETELCAEA-EEMRARLAARKQELEEILHELESrleEEEERSQQLQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 595 SERrrKRLQElegQIADLKKKLNEQ----SKLLKLKESTERTVSKLNQEIRMMKNQRVQLMRQMK--------------- 655
Cdd:pfam01576 96 NEK--KKMQQ---HIQDLEEQLDEEeaarQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKlleeriseftsnlae 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 656 --EDAEKFRQWKQKKDKEVIQLKERDRK----RQyELLKLERNFQKQSNVLR------------------RKTEEAAAAN 711
Cdd:pfam01576 171 eeEKAKSLSKLKNKHEAMISDLEERLKKeekgRQ-ELEKAKRKLEGESTDLQeqiaelqaqiaelraqlaKKEEELQAAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 712 KRLKD-------ALQKQREVADKRKETQS-----RGMEGTAARVKNWLGNEIEVMvsteeaKRHLNDLL-------EDRK 772
Cdd:pfam01576 250 ARLEEetaqknnALKKIRELEAQISELQEdleseRAARNKAEKQRRDLGEELEAL------KTELEDTLdttaaqqELRS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 773 ILAQDVAQLK----EKKESGENPPPKLRRRTFS----LTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLLDA 844
Cdd:pfam01576 324 KREQEVTELKkaleEETRSHEAQLQEMRQKHTQaleeLTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 845 ESEDR--PKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAEL-- 920
Cdd:pfam01576 404 EHKRKklEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETrq 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116686122 921 -----VRMEQQHQEKVlYLLSQLQQSQMAEKQLEESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRENEIIKQKL 994
Cdd:pfam01576 484 klnlsTRLRQLEDERN-SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQL 561
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
384-913 |
4.74e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 384 NLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQHaacKLDLQKLVETLE-------- 455
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKE---VKELEELKEEIEelekeles 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 456 -DQELKENVEIICNLQQLITQLSDETvacmaaaidtaVEQEAQVETSPETSRSSDAFTTqhalrqaqMSKELVELNKALA 534
Cdd:PRK03918 250 lEGSKRKLEEKIRELEERIEELKKEI-----------EELEEKVKELKELKEKAEEYIK--------LSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 535 LKEALARKMTQndsQLQPIQYQYQDnIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADL-K 613
Cdd:PRK03918 311 EIEKRLSRLEE---EINGIEERIKE-LEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLtP 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 614 KKLNEQSKLL-KLKESTERTVSKLNQEIRMMKNQRVQLMRQM----------------------KEDAEKFRQWKQKKDK 670
Cdd:PRK03918 387 EKLEKELEELeKAKEEIEEEISKITARIGELKKEIKELKKAIeelkkakgkcpvcgrelteehrKELLEEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 671 EVIQLKERDRKRQYELLKLERNFQKQSNVLRRKT--EEAAAANKRLK----DALQKQREVADKRKEtQSRGMEGTAARVK 744
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKkynlEELEKKAEEYEKLKE-KLIKLKGEIKSLK 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 745 NWLGNEIEVMVSTEEAKRHLNDLLEDRKILaqdvaqLKEKKESGENPPPKLRRRTFSL-------TEVRGQVSESEDsIT 817
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAEL------LKELEELGFESVEELEERLKELepfyneyLELKDAEKELER-EE 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 818 KQIESLETEMEFRSAQIADLQQKLLDAESEDRPKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCAD 897
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
570
....*....|....*.
gi 116686122 898 MQKMLFEERNHFAEIE 913
Cdd:PRK03918 699 LKEELEEREKAKKELE 714
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
558-876 |
9.00e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 558 QDNIKELELevinLQKEKEELVLELQTAKKDANQAK-----LSERRR------------KRLQELEGQIADLKKKLNE-- 618
Cdd:COG4913 606 FDNRAKLAA----LEAELAELEEELAEAEERLEALEaeldaLQERREalqrlaeyswdeIDVASAEREIAELEAELERld 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 619 --QSKLLKLkestERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEVIQLKER-DRKRQYELLKLERnfqk 695
Cdd:COG4913 682 asSDDLAAL----EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAeDLARLELRALLEE---- 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 696 qsnvlRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKN-WLGNEIEVMVSTEEA---KRHLNDLLEDR 771
Cdd:COG4913 754 -----RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNReWPAETADLDADLESLpeyLALLDRLEEDG 828
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 772 kiLAQDVAQLKE--KKESGENpppklrrrtfsLTEVRGQVSESEDSITKQIE----SLEtEMEF-------------RSA 832
Cdd:COG4913 829 --LPEYEERFKEllNENSIEF-----------VADLLSKLRRAIREIKERIDplndSLK-RIPFgpgrylrlearprPDP 894
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 116686122 833 QIADLQQKLLDAESedrpkQRWENIATILEAKC-ALKYLIGELVS 876
Cdd:COG4913 895 EVREFRQELRAVTS-----GASLFDEELSEARFaALKRLIERLRS 934
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
385-988 |
1.13e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 385 LQSLMEKNQSLVEENEKLSRGLSEAAGQtaqmleriiLTEQANEkMNAKLEELRQHAACKLD-LQKLVETLEDQELKENv 463
Cdd:pfam01576 192 LEERLKKEEKGRQELEKAKRKLEGESTD---------LQEQIAE-LQAQIAELRAQLAKKEEeLQAALARLEEETAQKN- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 464 EIICNLQQLITQLSD--ETVACMAAAIDTAVEQEAQVETSPETSRSS-----DAFTTQHALRqAQMSKELVELnkalalK 536
Cdd:pfam01576 261 NALKKIRELEAQISElqEDLESERAARNKAEKQRRDLGEELEALKTEledtlDTTAAQQELR-SKREQEVTEL------K 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 537 EALARKMTQNDSQLQPIQYQYQDNIKEL--ELEV-----INLQKEKEEL---VLELQTAKKDANQAKL-SERRRKRLqel 605
Cdd:pfam01576 334 KALEEETRSHEAQLQEMRQKHTQALEELteQLEQakrnkANLEKAKQALeseNAELQAELRTLQQAKQdSEHKRKKL--- 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 606 EGQIADLKKKLNEqskllklkesTERTVSKLNQEIRMMKNQrVQLMRQMKEDAEKfrqWKQKKDKEVIQLKERDRKRQYE 685
Cdd:pfam01576 411 EGQLQELQARLSE----------SERQRAELAEKLSKLQSE-LESVSSLLNEAEG---KNIKLSKDVSSLESQLQDTQEL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 686 LLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEgtaarVKNWLGNEIEVMVSTEEAKRHLN 765
Cdd:pfam01576 477 LQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSD-----MKKKLEEDAGTLEALEEGKKRLQ 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 766 DLLEDRKILAQDVAQLKEKKESGENP-PPKLRRRTFSLTEVRGQVSESEDSiTKQIESLETEMEFRSAQIADLQQKlldA 844
Cdd:pfam01576 552 RELEALTQQLEEKAAAYDKLEKTKNRlQQELDDLLVDLDHQRQLVSNLEKK-QKKFDQMLAEEKAISARYAEERDR---A 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 845 ESEDRPKQ-RWENIATILE-----------AKCALKYLIGELVSSKIQVSKLESSLKQSKTScadMQKMLFEERNHFAEI 912
Cdd:pfam01576 628 EAEAREKEtRALSLARALEealeakeelerTNKQLRAEMEDLVSSKDDVGKNVHELERSKRA---LEQQVEEMKTQLEEL 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 913 ETELQA---------------------ELVRMEQQHQEKVLYLLSQLQQSQM--------------AEKQLEESVSEKEQ 957
Cdd:pfam01576 705 EDELQAtedaklrlevnmqalkaqferDLQARDEQGEEKRRQLVKQVRELEAelederkqraqavaAKKKLELDLKELEA 784
|
650 660 670
....*....|....*....|....*....|.
gi 116686122 958 QLLSTLKCQDEELEKMREVCEQNQQLLRENE 988
Cdd:pfam01576 785 QIDAANKGREEAVKQLKKLQAQMKDLQRELE 815
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
693-1003 |
1.61e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 693 FQKQSNVLRRKTEEAAAANKRLKDA----------LQKQREVADKRKETQSRGmegtaarvknwlgNEIEVMVSTeeakR 762
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRLEDIlnelerqlksLERQAEKAERYKELKAEL-------------RELELALLV----L 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 763 HLNDLLEDRKILAQDVAQLKEKKESGENpppKLRRRTFSLTEVRGQVSESEDSI----------TKQIESLETEMEFRSA 832
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTA---ELQELEEKLEELRLEVSELEEEIeelqkelyalANEISRLEQQKQILRE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 833 QIADLQQKLLDAESE-DRPKQRWENIATILEA-KCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFA 910
Cdd:TIGR02168 310 RLANLERQLEELEAQlEELESKLDELAEELAElEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 911 EIETElqaelvrmEQQHQEKVLYLLSQLQQSQMAEKQLEESVSEKEQQL----LSTLKCQDEELEKMRE-VCEQNQQLLR 985
Cdd:TIGR02168 390 QLELQ--------IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeeaeLKELQAELEELEEELEeLQEELERLEE 461
|
330
....*....|....*...
gi 116686122 986 ENEIIKQKLTLLQVASRQ 1003
Cdd:TIGR02168 462 ALEELREELEEAEQALDA 479
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
386-1004 |
2.01e-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: 49.20 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 386 QSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLErIILTEQANEKMNAKLEELRQHAacklDLQKLVETLEDQElKENVEI 465
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSS-IEEQRRLLQTLHSQEIHIRDAH----EVATSIREISCQQ-HTLTQH 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 466 ICNLQQLITQLSDETvacMAAAIDTAVEQEAQVETSPETSRssdafttQHALRQ--AQMSKELVELNKALALKEALARKM 543
Cdd:TIGR00618 381 IHTLQQQKTTLTQKL---QSLCKELDILQREQATIDTRTSA-------FRDLQGqlAHAKKQQELQQRYAELCAAAITCT 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 544 TQNDSQLQPIQYQYQDNIKELElevinlQKEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKL---NEQS 620
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKERE------QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdiDNPG 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 621 KLLKLKESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEVIQ---LKERDRKRQYELLKLERNFQKQS 697
Cdd:TIGR00618 525 PLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCdnrSKEDIPNLQNITVRLQDLTEKLS 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 698 NVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAArvknwlgneievmvsteeAKRHLNDLLEDRKILAQD 777
Cdd:TIGR00618 605 EAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL------------------HALQLTLTQERVREHALS 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 778 VAQLKEKK-ESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFR-------SAQIADLQQKLLDAESEDR 849
Cdd:TIGR00618 667 IRVLPKELlASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFneienasSSLGSDLAAREDALNQSLK 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 850 PKQRweniatilEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKM--LFEERNH-FAEIETELQAEL------ 920
Cdd:TIGR00618 747 ELMH--------QARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFnrLREEDTHlLKTLEAEIGQEIpsdedi 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 921 ----VRMEQQHQEKVLYLLSQLQQSQMAEKQLEESVSEKEQQLLSTLKCQDE--ELEKMREVCEQNQQLLRENEIIK--Q 992
Cdd:TIGR00618 819 lnlqCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKiiQLSDKLNGINQIKIQFDGDALIKflH 898
|
650
....*....|..
gi 116686122 993 KLTLLQVASRQK 1004
Cdd:TIGR00618 899 EITLYANVRLAN 910
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
393-985 |
3.43e-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: 48.30 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 393 QSLVEENEKLSRGLSEAAGQTAQMLERIILteQANEKMNAKLEEL------------RQHAACKLDLQKLVETLEDQELK 460
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYNRRRS--KIKEQNNRDIAGIkdklakireardRQLAVAEDDLQALESELREQLEA 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 461 ENVEIICNLQQLITQLSDETVacmaaaidtaveQEAQVETSPETsrssdafTTQHALRQAQMSKELVELNKALALKEALA 540
Cdd:pfam12128 431 GKLEFNEEEYRLKSRLGELKL------------RLNQATATPEL-------LLQLENFDERIERAREEQEAANAEVERLQ 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 541 RKMTQNDSQLQpiqyQYQDNIKELELEVINLQKEKEELVLELqtakkDANQAKLSERRRKRLQELEGQIA---------- 610
Cdd:pfam12128 492 SELRQARKRRD----QASEALRQASRRLEERQSALDELELQL-----FPQAGTLLHFLRKEAPDWEQSIGkvispellhr 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 611 -DLKKKLNEQSKllklkeSTERTVSKLNQEI-RMMKNQRVQLMRQMKEDAEKF-------RQWKQKKDKEVIQLKERDRK 681
Cdd:pfam12128 563 tDLDPEVWDGSV------GGELNLYGVKLDLkRIDVPEWAASEEELRERLDKAeealqsaREKQAAAEEQLVQANGELEK 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 682 RQYELLKLERNFQKQSNVLRRKTEEaaaaNKRLKDALQKQREVADKRKETQSRGMEGTaarvKNWLGNEIEVMVST--EE 759
Cdd:pfam12128 637 ASREETFARTALKNARLDLRRLFDE----KQSEKDKKNKALAERKDSANERLNSLEAQ----LKQLDKKHQAWLEEqkEQ 708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 760 AKRHLNDLLEDRKILAQD----VAQLKEKKESGENpppKLRRRTFSLTEVRGQVSESEDSITKQIESLETEmefrsaqIA 835
Cdd:pfam12128 709 KREARTEKQAYWQVVEGAldaqLALLKAAIAARRS---GAKAELKALETWYKRDLASLGVDPDVIAKLKRE-------IR 778
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 836 DLQQKLLDAEsEDRPK----QRWENiATILEAKCALkyligelvssKIQVSKLESSLKQSKtscADMQKMLFEERNHFAE 911
Cdd:pfam12128 779 TLERKIERIA-VRRQEvlryFDWYQ-ETWLQRRPRL----------ATQLSNIERAISELQ---QQLARLIADTKLRRAK 843
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 116686122 912 IETELQAElvrMEQQHQEKVLYLLSQLQQSQMAEKQLEESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLR 985
Cdd:pfam12128 844 LEMERKAS---EKQQVRLSENLRGLRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
521-994 |
3.86e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 521 QMSKELVELNKALALKEALARKMTQNDSQLQPIQyqyqDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRK 600
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLE----GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 601 RLQELEGQIADLKKKLNEQSKLL----KLKESTERTVSKL---NQEIRMMKNQRVQLMRQ---MKEDAEKFRQWKQKKDK 670
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLsrleEEINGIEERIKELeekEERLEELKKKLKELEKRleeLEERHELYEEAKAKKEE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 671 --------------EVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQK----QREVADKRKEtq 732
Cdd:PRK03918 374 lerlkkrltgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcGRELTEEHRK-- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 733 sRGMEGTAARVKNWLGNEIEVMVSTEEAKRHL----NDLLEDRKILAQ-----------------DVAQLKEKKESGEnp 791
Cdd:PRK03918 452 -ELLEEYTAELKRIEKELKEIEEKERKLRKELreleKVLKKESELIKLkelaeqlkeleeklkkyNLEELEKKAEEYE-- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 792 ppKLRRRtfsLTEVRGQVSESEDSItKQIESLETEMEFRSAQIADLQQKLLDAESEDRP---KQRWENIATILEAKCALK 868
Cdd:PRK03918 529 --KLKEK---LIKLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKELEElgfESVEELEERLKELEPFYN 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 869 YLIgELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRM-EQQHQEKVLYLLSQLQQSQMAEKQ 947
Cdd:PRK03918 603 EYL-ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYsEEEYEELREEYLELSRELAGLRAE 681
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 116686122 948 LEESVSEKEQ--QLLSTLKCQDEELEKMREVCEQNQQLLRENEIIKQKL 994
Cdd:PRK03918 682 LEELEKRREEikKTLEKLKEELEEREKAKKELEKLEKALERVEELREKV 730
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
649-853 |
4.23e-05 |
|
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: 47.45 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 649 QLMRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKR 728
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 729 KETQSRGMEGTAARVKNWLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGEnpppKLRRRTFSLTEVRGQ 808
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 116686122 809 VSESEDSITKQIESLETEMEFRSAQIADLQQKLLDAESEDRPKQR 853
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
537-672 |
4.32e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 47.77 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 537 EALARKMTQNDSQLQPIqyqyqdniKELELEVINLQKEKEELVLELQTAKKDanqaklserrrkRLQELEGQIADLKKKL 616
Cdd:COG0542 397 EAAARVRMEIDSKPEEL--------DELERRLEQLEIEKEALKKEQDEASFE------------RLAELRDELAELEEEL 456
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 617 NEqsklLKLKESTERT----VSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEV 672
Cdd:COG0542 457 EA----LKARWEAEKElieeIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEV 512
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
383-699 |
4.35e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 47.64 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 383 ENLQSLMEKNQSLVEENEKLSrglSEAAGQTAQMLERIiltEQANEKMNAKLEELRQHAACKLDLQKLV-ETLEDQELKE 461
Cdd:COG5185 246 EDLAQTSDKLEKLVEQNTDLR---LEKLGENAESSKRL---NENANNLIKQFENTKEKIAEYTKSIDIKkATESLEEQLA 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 462 NVEIICNLQQLITQlSDETVACMAAAIDTAVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNkalALKEALAR 541
Cdd:COG5185 320 AAEAEQELEESKRE-TETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIE---STKESLDE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 542 KMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLS-ERRRKRLQELEGQIADLKKKLNEQS 620
Cdd:COG5185 396 IPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElNKVMREADEESQSRLEEAYDEINRS 475
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116686122 621 KLLKLKEStERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRqwkQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNV 699
Cdd:COG5185 476 VRSKKEDL-NEELTQIESRVSTLKATLEKLRAKLERQLEGVR---SKLDQVAESLKDFMRARGYAHILALENLIPASEL 550
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
484-718 |
4.42e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 484 MAAAIDTAVEQ-------EAQVETspetsrssdafttqhALRQAQMSKELVELNKALalkEALARKMTQNDSQLQPIQ-Y 555
Cdd:COG4913 223 TFEAADALVEHfddleraHEALED---------------AREQIELLEPIRELAERY---AAARERLAELEYLRAALRlW 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 556 QYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAK-----LSERRR----KRLQELEGQIADLKKKLNEQS-KLLKL 625
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALReeldeLEAQIRgnggDRLEQLEREIERLERELEERErRRARL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 626 KESTERTVSKLNQEIRMMKNQRVQLmRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKlERNF--QKQSNVlrrk 703
Cdd:COG4913 365 EALLAALGLPLPASAEEFAALRAEA-AALLEALEEELEALEEALAEAEAALRDLRRELRELEA-EIASleRRKSNI---- 438
|
250
....*....|....*
gi 116686122 704 TEEAAAANKRLKDAL 718
Cdd:COG4913 439 PARLLALRDALAEAL 453
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
509-995 |
4.65e-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: 48.04 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 509 DAFTTQHALRQAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKD 588
Cdd:TIGR00618 155 AQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 589 ANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQEIrmmkNQRVQLMRqMKEDAEKFRQWKQKK 668
Cdd:TIGR00618 235 LQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERI----NRARKAAP-LAAHIKAVTQIEQQA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 669 DKEVIQLKERDRKRQYELLKLErnfqkqsnvlrrkteeaaaankrlkDALQKQREVADKRKETQSrgmegtaarvknWLG 748
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRA-------------------------AHVKQQSSIEEQRRLLQT------------LHS 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 749 NEIEVMVSTEEAKRHLnDLLEDRKILAQDVAQLKEKKESGEnpppklrrrtfsltevrgQVSESEDSITKQIESLETEME 828
Cdd:TIGR00618 353 QEIHIRDAHEVATSIR-EISCQQHTLTQHIHTLQQQKTTLT------------------QKLQSLCKELDILQREQATID 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 829 FRSAQIADLQQKLLDAESEDRPKQRWENI--ATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCaDMQKMLFEER 906
Cdd:TIGR00618 414 TRTSAFRDLQGQLAHAKKQQELQQRYAELcaAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIH-LQETRKKAVV 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 907 NHFAEIETELQAELVRMEQQ-HQEKVLYLLSQLQQSQMaeKQLEESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLR 985
Cdd:TIGR00618 493 LARLLELQEEPCPLCGSCIHpNPARQDIDNPGPLTRRM--QRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ 570
|
490
....*....|
gi 116686122 986 ENEIIKQKLT 995
Cdd:TIGR00618 571 SFSILTQCDN 580
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
382-986 |
5.39e-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: 47.81 E-value: 5.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 382 SENLQSLMEKNQSLVE-ENEKLSRGLSEAAGQTAQMLERIiltEQANEKMNAKLEELRQHAACKLDLQKLVETLEDQELK 460
Cdd:pfam15921 294 ANSIQSQLEIIQEQARnQNSMYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQ 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 461 ENVEIICNLQQLITQLSdetvacmaaaidtavEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKALALKEALA 540
Cdd:pfam15921 371 ESGNLDDQLQKLLADLH---------------KREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALL 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 541 RKMT-----QNDSQLQPIQYQyQDNIKELELEVINLQKEKEEL--VLELQTAKKdanqaklserrrKRLQELEGQIADLK 613
Cdd:pfam15921 436 KAMKsecqgQMERQMAAIQGK-NESLEKVSSLTAQLESTKEMLrkVVEELTAKK------------MTLESSERTVSDLT 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 614 KKLNEQSKLLklkESTERTVSKLNQEIRMmknqRVQLMRQMKEDAEKFRQWKQKKDKEVIQLKERDRkrQYELLKlernf 693
Cdd:pfam15921 503 ASLQEKERAI---EATNAEITKLRSRVDL----KLQELQHLKNEGDHLRNVQTECEALKLQMAEKDK--VIEILR----- 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 694 QKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGM--EGTAARVKnwlgnEIEVMVSTEEakrhlndlLEDR 771
Cdd:pfam15921 569 QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIlkDKKDAKIR-----ELEARVSDLE--------LEKV 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 772 KILAQDVAQLKEKKESGEnpppklrRRTFSLTEVRGQVSESeDSITKQIESLETEMEFRSAQIADLQQKLldaesedrpk 851
Cdd:pfam15921 636 KLVNAGSERLRAVKDIKQ-------ERDQLLNEVKTSRNEL-NSLSEDYEVLKRNFRNKSEEMETTTNKL---------- 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 852 qrweniatileaKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQaelvrmeqqhqekv 931
Cdd:pfam15921 698 ------------KMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQ-------------- 751
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 116686122 932 lyLLSQLQQSQMAEKQLEESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRE 986
Cdd:pfam15921 752 --FLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
548-728 |
5.66e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 548 SQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQ-----AKLSERRRKRLQELEGQIADLKKKLNEQSKL 622
Cdd:COG3883 26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKlqaeiAEAEAEIEERREELGERARALYRSGGSVSYL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 623 LKLKEST--ERTVSKLNQEIRMMKNQRvQLMRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVL 700
Cdd:COG3883 106 DVLLGSEsfSDFLDRLSALSKIADADA-DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
|
170 180
....*....|....*....|....*...
gi 116686122 701 RRKTEEAAAANKRlKDALQKQREVADKR 728
Cdd:COG3883 185 AQLSAEEAAAEAQ-LAELEAELAAAEAA 211
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
537-940 |
5.87e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 5.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 537 EALARKMTQNDSQLQPIQyQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRK---RLQELEGQIADLK 613
Cdd:COG4717 74 KELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEAleaELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 614 KKLNEQSKLLKLKESTERTVSKLNQEIRMMKNQR----VQLMRQMKEDAEKFRQWKQKKDKEVIQLKER--DRKRQYELL 687
Cdd:COG4717 153 ERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQRLAELEEELEEAQEEleELEEELEQL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 688 KLERNFQKQSNVLRRKTEEAAAANKRLkDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEIEVMVSTEEAKRhLNDL 767
Cdd:COG4717 233 ENELEAAALEERLKEARLLLLIAAALL-ALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE-LQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 768 LEDRKILAQDVAQLKEKKESGENPPPKLRRRTFS-LTEVRGQVSESEDSITK-QIESLETEME--FRSAQ---IADLQQK 840
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDrIEELQELLREAEELEEElQLEELEQEIAalLAEAGvedEEELRAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 841 LLDAESEDRPKQRWENIATILEAKcALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERnhfAEIETELQA-- 918
Cdd:COG4717 391 LEQAEEYQELKEELEELEEQLEEL-LGELEELLEALDEEELEEELEELEEELEELEEELEELREEL---AELEAELEQle 466
|
410 420
....*....|....*....|....*
gi 116686122 919 ---ELVRMEQQHQEkvlyLLSQLQQ 940
Cdd:COG4717 467 edgELAELLQELEE----LKAELRE 487
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
383-646 |
9.87e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 9.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 383 ENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERII-LTEQANEKMNAKLE--ELRQhaackLDlQKLVETLED-QE 458
Cdd:PRK11281 66 EQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEaLKDDNDEETRETLStlSLRQ-----LE-SRLAQTLDQlQN 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 459 LKENVEIICNlqQLITQlsdETVACMA-AAIDTAVEQEAQVetspeTSRSSDAFTTQHALRQAQMSKELVELnKALALKE 537
Cdd:PRK11281 140 AQNDLAEYNS--QLVSL---QTQPERAqAALYANSQRLQQI-----RNLLKGGKVGGKALRPSQRVLLQAEQ-ALLNAQN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 538 ALARKMTQNDSQLQPI---QYQY-QDNIKELELEVINLQKEKEELVLEL--QTAKKDANQAKLSERRRKRL--QELegqi 609
Cdd:PRK11281 209 DLQRKSLEGNTQLQDLlqkQRDYlTARIQRLEHQLQLLQEAINSKRLTLseKTVQEAQSQDEAARIQANPLvaQEL---- 284
|
250 260 270
....*....|....*....|....*....|....*..
gi 116686122 610 aDLKKKLNEqskllKLKESTERTVSKLNQEIRmMKNQ 646
Cdd:PRK11281 285 -EINLQLSQ-----RLLKATEKLNTLTQQNLR-VKNW 314
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
514-793 |
1.03e-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: 46.66 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 514 QHALRQAQMSKeLVELNKALALKEAlaRKMTQNDSQLQPIQYQYQDNI---KELELEVINLQKEK--------EELVLEL 582
Cdd:pfam17380 298 QERLRQEKEEK-AREVERRRKLEEA--EKARQAEMDRQAAIYAEQERMameRERELERIRQEERKrelerirqEEIAMEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 583 QTAKKDANQAKLSERRRKRL-QELEgqiADLKKKLNEQSKLLKLKEStERTVSKLNQEIRMMKNQRVQLMRQMKE-DAEK 660
Cdd:pfam17380 375 SRMRELERLQMERQQKNERVrQELE---AARKVKILEEERQRKIQQQ-KVEMEQIRAEQEEARQREVRRLEEERArEMER 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 661 FRQWKQKKDKEVIQLK--ERDRKRQYELLKLERNFQKQSNVLRRKT-EEAAAANKRLKDALQKQREVADKRKETQSRGM- 736
Cdd:pfam17380 451 VRLEEQERQQQVERLRqqEEERKRKKLELEKEKRDRKRAEEQRRKIlEKELEERKQAMIEEERKRKLLEKEMEERQKAIy 530
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116686122 737 ---EGTAARVKNWLGNEIE--------VMVSTEEAKRhLNDLLEDRKILAQDVAQLKEKKESGENPPP 793
Cdd:pfam17380 531 eeeRRREAEEERRKQQEMEerrriqeqMRKATEERSR-LEAMEREREMMRQIVESEKARAEYEATTPI 597
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
447-847 |
1.25e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 447 LQKLVETLEDQELKENVEIICNLQQLITQLSDETVACMAAAIDTAVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKEL 526
Cdd:COG4717 39 LLAFIRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 527 VELNKALALKEALARkMTQNDSQLQPIQYQYqDNIKELELEVINLQKEKEELVLELQTAKKDANQAK--LSERRRKRLQE 604
Cdd:COG4717 119 EKLEKLLQLLPLYQE-LEALEAELAELPERL-EELEERLEELRELEEELEELEAELAELQEELEELLeqLSLATEEELQD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 605 LEGQIADLKKKLNEQSKLLklkESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEK------------------------ 660
Cdd:COG4717 197 LAEELEELQQRLAELEEEL---EEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallglggsllslil 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 661 -------------------FRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQ 721
Cdd:COG4717 274 tiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 722 REVADKRKETQsrgMEGTAARVKNWLGneiEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEkkesgenpppklRRRTFS 801
Cdd:COG4717 354 REAEELEEELQ---LEELEQEIAALLA---EAGVEDEEELRAALEQAEEYQELKEELEELEE------------QLEELL 415
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 116686122 802 LTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLLDAESE 847
Cdd:COG4717 416 GELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAE 461
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
379-789 |
1.28e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 379 VEPSENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQHAACKLDLQKLVETLED-- 456
Cdd:PRK03918 282 VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEErh 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 457 QELKENVEIICNLQQLITQLSDETVACMAAAIDTAVEQEAQVETSPETSRSsdafttqhalRQAQMSKELVELNKAL-AL 535
Cdd:PRK03918 362 ELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITA----------RIGELKKEIKELKKAIeEL 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 536 KEA------LARKMTQNDSqlQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKdanqAKLSERRRKRLQELEGQI 609
Cdd:PRK03918 432 KKAkgkcpvCGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEK----VLKKESELIKLKELAEQL 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 610 ADLKKKLNEQSkLLKLKESTERtVSKLNQEIRMMKNQrvqlMRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKL 689
Cdd:PRK03918 506 KELEEKLKKYN-LEELEKKAEE-YEKLKEKLIKLKGE----IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 690 ERNFQKQSNVLRRKTEEAAAANKR---LKDALQKQREVADKRKETQSR---------GMEGTAARVKNWLgNEIEVMVST 757
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEyleLKDAEKELEREEKELKKLEEEldkafeelaETEKRLEELRKEL-EELEKKYSE 658
|
410 420 430
....*....|....*....|....*....|..
gi 116686122 758 EEAKRHLNDLLEDRKILAQDVAQLKEKKESGE 789
Cdd:PRK03918 659 EEYEELREEYLELSRELAGLRAELEELEKRRE 690
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
535-743 |
1.36e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 535 LKEALARKMTQNDSQLQPIQYQ---YQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERR---RKRLQELEGQ 608
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQlpeLRKELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLaeaRAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 609 IADLKKKLNEQSKLLKlKESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEVIQLKERDRK----RQY 684
Cdd:COG3206 242 LAALRAQLGSGPDALP-ELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRilasLEA 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 685 ELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVA----------DKRKETQ-SRGMEGTAARV 743
Cdd:COG3206 321 ELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEvarelyesllQRLEEARlAEALTVGNVRV 390
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
86-280 |
1.47e-04 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 45.89 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 86 AYGQTGSGKTYSMggaytAEQENEPTVGVIPRVIQLLFKEIDKKSDFEFTLKvsYLEIYNEEILDLLCPSREKAQINIRE 165
Cdd:COG5059 387 AYMQSLKKETETL-----KSRIDLIMKSIISGTFERKKLLKEEGWKYKSTLQ--FLRIEIDRLLLLREEELSKKKTKIHK 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 166 DPKEGIKIVGLTEKTVLVALDTVSCLEQGNNsRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSfrskLHLVDLAGSE 245
Cdd:COG5059 460 LNKLRHDLSSLLSSIPEETSDRVESEKASKL-RSSASTKLNLRSSRSHSKFRDHLNGSNSSTKELS----LNQVDLAGSE 534
|
170 180 190
....*....|....*....|....*....|....*
gi 116686122 246 RqKKTKAEGDRLKEGININRGLLCLGNVISALGDD 280
Cdd:COG5059 535 R-KVSQSVGELLRETQSLNKSLSSLGDVIHALGSK 568
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
522-997 |
1.70e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.88 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 522 MSKELVELNKALA--------LKEALARKMTQNDSQLQPIQYQYQDNIKEL----ELEVINLQKEKeelvlelQTAKKDA 589
Cdd:pfam15921 222 ISKILRELDTEISylkgrifpVEDQLEALKSESQNKIELLLQQHQDRIEQLisehEVEITGLTEKA-------SSARSQA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 590 NQAK-----LSERRR-------KRLQELEGQIADLKKKLNEQSKLLKLK-ESTERTVSKLNQEIRMMKNQRvqlmrqmke 656
Cdd:pfam15921 295 NSIQsqleiIQEQARnqnsmymRQLSDLESTVSQLRSELREAKRMYEDKiEELEKQLVLANSELTEARTER--------- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 657 daEKFRQWKQKKDKEVIQLKERDRKRQYELlklerNFQKQSNvlrRKTEEAAAANKRLKDALQkqREVADKRKETQSrgM 736
Cdd:pfam15921 366 --DQFSQESGNLDDQLQKLLADLHKREKEL-----SLEKEQN---KRLWDRDTGNSITIDHLR--RELDDRNMEVQR--L 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 737 EGTAARVKNWLGNEIEVMVSTEEAKrhlNDLLEDRKILAqdvAQLKEKKEsgenpppKLRRRTFSLTEVRGQVSESEDSI 816
Cdd:pfam15921 432 EALLKAMKSECQGQMERQMAAIQGK---NESLEKVSSLT---AQLESTKE-------MLRKVVEELTAKKMTLESSERTV 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 817 TKQIESL---ETEMEFRSAQIADLQQKLldaeseDRPKQRWENIATILEAkcaLKYLIGELVSSKIQVSKLESSLKQSKT 893
Cdd:pfam15921 499 SDLTASLqekERAIEATNAEITKLRSRV------DLKLQELQHLKNEGDH---LRNVQTECEALKLQMAEKDKVIEILRQ 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 894 SCADMQKMLfeerNHFAEIETELQAELVRMEQQHQEKVLYL--LSQLQQSQMAE-KQLEESVSEKEQQLLSTLKCQDEEL 970
Cdd:pfam15921 570 QIENMTQLV----GQHGRTAGAMQVEKAQLEKEINDRRLELqeFKILKDKKDAKiRELEARVSDLELEKVKLVNAGSERL 645
|
490 500
....*....|....*....|....*..
gi 116686122 971 EKMREVCEQNQQLLRENEIIKQKLTLL 997
Cdd:pfam15921 646 RAVKDIKQERDQLLNEVKTSRNELNSL 672
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
537-975 |
1.89e-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: 45.87 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 537 EALARKMTQNDSQLQPIQYQYQDNIKELELE---VINLQKEKEELVLELQTAKKDaNQAKLSERRRKR-----LQELEGQ 608
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQrkaIQELQFENEKVSLKLEEEIQE-NKDLIKENNATRhlcnlLKETCAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 609 IADLKKKLNEQskllklKESTERTVSKLNQEIRMM-----------KNQRVQLMRQMKEDAEKFRQWKQKKDKEViqlke 677
Cdd:pfam05483 167 SAEKTKKYEYE------REETRQVYMDLNNNIEKMilafeelrvqaENARLEMHFKLKEDHEKIQHLEEEYKKEI----- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 678 rdrkrqyellkleRNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKET---QSRGMEGTAARvKNWLGNEIE-V 753
Cdd:pfam05483 236 -------------NDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKtklQDENLKELIEK-KDHLTKELEdI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 754 MVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLR-RRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSA 832
Cdd:pfam05483 302 KMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKaAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 833 QIADLQQKLLDAESEDRPKQ----RWENIATILEAKCALKY------------------LIGELVSSKIQVSKLESSLKQ 890
Cdd:pfam05483 382 ITMELQKKSSELEEMTKFKNnkevELEELKKILAEDEKLLDekkqfekiaeelkgkeqeLIFLLQAREKEIHDLEIQLTA 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 891 SKTS-------CADMQKMLFEERNHFAEIETE---LQAELVRMEQQHQEKVLYLLSQLQQSQMAEKQLE------ESVSE 954
Cdd:pfam05483 462 IKTSeehylkeVEDLKTELEKEKLKNIELTAHcdkLLLENKELTQEASDMTLELKKHQEDIINCKKQEErmlkqiENLEE 541
|
490 500
....*....|....*....|.
gi 116686122 955 KEQQLLSTLKCQDEELEKMRE 975
Cdd:pfam05483 542 KEMNLRDELESVREEFIQKGD 562
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
518-861 |
2.12e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 45.73 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 518 RQAQMSKELVELNKALALKEALARKMTQNDSQLQpIQYQYQDNIKELELEV-------INLQKEKEELVLELQTAKKDAN 590
Cdd:pfam02463 154 RRLEIEEEAAGSRLKRKKKEALKKLIEETENLAE-LIIDLEELKLQELKLKeqakkalEYYQLKEKLELEEEYLLYLDYL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 591 QaklseRRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLN----QEIRMMKNQRVQLMRQMKEDAEKFRQWKQ 666
Cdd:pfam02463 233 K-----LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENkeeeKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 667 KKDKEVIQLKERDRKRQYELLKLER------NFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRG--MEG 738
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKekeeieELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLEseRLS 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 739 TAARVKNWLGNEIEVMVST-----EEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRGQVSESE 813
Cdd:pfam02463 388 SAAKLKEEELELKSEEEKEaqlllELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 116686122 814 DSITKQIESLETEMEFRSAQIADLQQKLLDAESEDRPKQRWENIATIL 861
Cdd:pfam02463 468 KKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLAL 515
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
503-828 |
2.80e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.52 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 503 ETSRSSDAFTTQHALRQAQMSKELVELNKA-----LALKEA-LARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKE 576
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAeedknMALRKAeEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 577 ELVLELQTAKKDANQAKL--------SERRRKRLQELEGQIADLKKKLNEQSKL---LKLKESTERTVSKLNQEIRMMKN 645
Cdd:PTZ00121 1623 EELKKAEEEKKKVEQLKKkeaeekkkAEELKKAEEENKIKAAEEAKKAEEDKKKaeeAKKAEEDEKKAAEALKKEAEEAK 1702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 646 QRVQLMRQMKEDAEKFRQWKQKKDKEVIQL-----KERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQK 720
Cdd:PTZ00121 1703 KAEELKKKEAEEKKKAEELKKAEEENKIKAeeakkEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIE 1782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 721 qrEVADKRKETQSRGMEGTAARVKNWLGNEIEvmvSTEEAKRHLNDlleDRKILAQDVAQLKEKKESGENPPPKLRRRTF 800
Cdd:PTZ00121 1783 --EELDEEDEKRRMEVDKKIKDIFDNFANIIE---GGKEGNLVIND---SKEMEDSAIKEVADSKNMQLEEADAFEKHKF 1854
|
330 340
....*....|....*....|....*...
gi 116686122 801 SLTEVRGQVSESEDSITKQIESLETEME 828
Cdd:PTZ00121 1855 NKNNENGEDGNKEADFNKEKDLKEDDEE 1882
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
521-976 |
3.51e-04 |
|
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: 45.01 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 521 QMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERR-R 599
Cdd:TIGR04523 100 KLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLlE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 600 KRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQEIRMMKNQRVQLMRQmkedaekfrqwKQKKDKEVIQLKERD 679
Cdd:TIGR04523 180 KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDN-----------IEKKQQEINEKTTEI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 680 RKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEIEVMVSTEe 759
Cdd:TIGR04523 249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQ- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 760 akrhlNDLLEDRKI---LAQDVAQLKEKKESGENPPPKLRRRtfsLTEVRGQV----------SESEDSITKQIESLETE 826
Cdd:TIGR04523 328 -----NQISQNNKIisqLNEQISQLKKELTNSESENSEKQRE---LEEKQNEIeklkkenqsyKQEIKNLESQINDLESK 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 827 MEFRSAQIADLQQKLLDAESEDRPK-QRWENI-ATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFE 904
Cdd:TIGR04523 400 IQNQEKLNQQKDEQIKKLQQEKELLeKEIERLkETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 116686122 905 ERNHFAEIETELQA------ELVRMEQQHQEKVLYLLSQLQQSQMAEKQLEESVSEKEQQlLSTLKcqdEELEKMREV 976
Cdd:TIGR04523 480 IKQNLEQKQKELKSkekelkKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK-ISDLE---DELNKDDFE 553
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
524-720 |
3.81e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.13 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 524 KELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEeLVLELQTAKKDANQAKLSERRRKRLQ 603
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKE-LVEKIKELEKELEKAKKALEKNEKLK 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 604 ELEGQIADLKKKLNEQSKllKLKESTERtVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKD---KEVIQLKERDR 680
Cdd:COG1340 164 ELRAELKELRKEAEEIHK--KIKELAEE-AQELHEEMIELYKEADELRKEADELHKEIVEAQEKADelhEEIIELQKELR 240
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 116686122 681 KRQYELLKLernfqKQSNVLRRKTEEAAAANKRLKDALQK 720
Cdd:COG1340 241 ELRKELKKL-----RKKQRALKREKEKEELEEKAEEIFEK 275
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
758-975 |
4.05e-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: 44.37 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 758 EEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLT----EVRGQVSESEDSI---TKQIESLETEMEFR 830
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALArrirALEQELAALEAELaelEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 831 SAQIADLQQKLLDAESEDRPKQ--RWENIATILEAKCALKYLIGELvsskiqvSKLESSLKQSKTSCADMQKMLFEERNH 908
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALllSPEDFLDAVRRLQYLKYLAPAR-------REQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116686122 909 FAEIETELQAELVRMEQQHQEKVLyLLSQLQQSQMAEKQLEESVSEKEQQLLSTLKCQDEELEKMRE 975
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQK-LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
775-986 |
4.49e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 775 AQDVAQLKEKKEsgenpppKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLldAESEDRPKQRW 854
Cdd:COG4942 19 ADAAAEAEAELE-------QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL--AALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 855 ENIATILEAKCALKYLIGELVSSkIQVSKLESSLKQ--SKTSCADMQKML------FEERNHFAEIETELQAELVRMEQQ 926
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRA-LYRLGRQPPLALllSPEDFLDAVRRLqylkylAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 927 HQEKVLYLLSQLQQSQMAEKQLEESVSEKeQQLLSTLKCQDEELEKMREVCEQNQQLLRE 986
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAER-QKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
561-986 |
6.67e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 561 IKELELEVINLQKEKEELVlelqtAKKDANQAKLS--ERRRKRLQELEGQIADLKKKlneqskllklKESTERTVSKLNQ 638
Cdd:PRK02224 215 LAELDEEIERYEEQREQAR-----ETRDEADEVLEehEERREELETLEAEIEDLRET----------IAETEREREELAE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 639 EIRMMKNQRVQLMRQMK-------------EDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTE 705
Cdd:PRK02224 280 EVRDLRERLEELEEERDdllaeaglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 706 EAAAANKRLKDALQKQREVADKRKETQS---RGMEGTAARVKNwlgneieVMVSTEEAKRHLNDLLEDRKILAQDVAQLK 782
Cdd:PRK02224 360 ELREEAAELESELEEAREAVEDRREEIEeleEEIEELRERFGD-------APVDLGNAEDFLEELREERDELREREAELE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 783 EKKESGENPPPKLRRrtfsLTEVR-----GQ-VSESEDSIT-----KQIESLETEMEFRSAQIADLQQKLLDAESedrpk 851
Cdd:PRK02224 433 ATLRTARERVEEAEA----LLEAGkcpecGQpVEGSPHVETieedrERVEELEAELEDLEEEVEEVEERLERAED----- 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 852 qrweniatileakcaLKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQHQ--E 929
Cdd:PRK02224 504 ---------------LVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEeaE 568
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 116686122 930 KVLYLLSQLQQSQMAEKQLEESVsEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRE 986
Cdd:PRK02224 569 EAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELNDE 624
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
345-841 |
1.03e-03 |
|
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: 43.42 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 345 DPQTAELNHLKQQvqqlqvlllqahggtlpgsitvepSENLQSLMEKNQSLVEENEKLSRglsEAAGQTAQMLERIILTE 424
Cdd:TIGR00618 372 CQQHTLTQHIHTL------------------------QQQKTTLTQKLQSLCKELDILQR---EQATIDTRTSAFRDLQG 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 425 Q-----ANEKMNAK-LEELRQHAACKLDLQKLVETLED---QELKENVEIICNLQQlITQLSDETVACMAAAIDTAVEQE 495
Cdd:TIGR00618 425 QlahakKQQELQQRyAELCAAAITCTAQCEKLEKIHLQesaQSLKEREQQLQTKEQ-IHLQETRKKAVVLARLLELQEEP 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 496 AQVETS---------------PETSRSSDAFTTQHALRQA--QMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQ 558
Cdd:TIGR00618 504 CPLCGScihpnparqdidnpgPLTRRMQRGEQTYAQLETSeeDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 559 DNIKELELEVINLQKEKEELvLELQTAKKDANQAKLSERRRKrlQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQ 638
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLTEKL-SEAEDMLACEQHALLRKLQPE--QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERV 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 639 EIRMMKNQRVQLM----RQMKEDAEKFRQWKQKKDKEVI-QLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAA----A 709
Cdd:TIGR00618 661 REHALSIRVLPKEllasRQLALQKMQSEKEQLTYWKEMLaQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAaredA 740
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 710 ANKRLKDALQKQREVADKRKETQSRGMEgtAARVKNWLGNEIEVMVSTEEAKRHLndLLEDRKILAQDVAQLKEKKESG- 788
Cdd:TIGR00618 741 LNQSLKELMHQARTVLKARTEAHFNNNE--EVTAALQTGAELSHLAAEIQFFNRL--REEDTHLLKTLEAEIGQEIPSDe 816
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 116686122 789 --------------ENPPPKLRRRTFSLTEVRGQVSESEDSiTKQIESLETEmefrSAQIADLQQKL 841
Cdd:TIGR00618 817 dilnlqcetlvqeeEQFLSRLEEKSATLGEITHQLLKYEEC-SKQLAQLTQE----QAKIIQLSDKL 878
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
386-621 |
1.37e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 42.32 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 386 QSLMEKNQSLVEENEKLSRGLSEAAGQTAQM-----------------LERIILTEQANEKMNAKLEELRQHAACKLD-L 447
Cdd:pfam04849 90 QSLLKQNSVLTERNEALEEQLGSAREEILQLrhelskkddllqiysndAEESETESSCSTPLRRNESFSSLHGCVQLDaL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 448 QKLVETLEDQELKenveiicnLQQLITQLSDETvacmaaaiDTAVEQEAQVetspetsrssdafttqhalrQAQMSKELV 527
Cdd:pfam04849 170 QEKLRGLEEENLK--------LRSEASHLKTET--------DTYEEKEQQL--------------------MSDCVEQLS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 528 ELNKALA-LKEALARKMTQNDSQLQPIQyQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQ--AKLSErRRKRLQE 604
Cdd:pfam04849 214 EANQQMAeLSEELARKMEENLRQQEEIT-SLLAQIVDLQHKCKELGIENEELQQHLQASKEAQRQltSELQE-LQDRYAE 291
|
250
....*....|....*..
gi 116686122 605 LEGQIADLKKKLNEQSK 621
Cdd:pfam04849 292 CLGMLHEAQEELKELRK 308
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
508-641 |
2.17e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 508 SDAFTTqhALR-----------QAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKE 576
Cdd:PRK00409 488 SNAFEI--AKRlglpeniieeaKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEED 565
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 116686122 577 ELVLEL-QTAKKDANQAKL-SERRRKRLQEL---------EGQIADLKKKLNEQSKLL---KLKESTERTVSKLNQEIR 641
Cdd:PRK00409 566 KLLEEAeKEAQQAIKEAKKeADEIIKELRQLqkggyasvkAHELIEARKRLNKANEKKekkKKKQKEKQEELKVGDEVK 644
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
433-983 |
2.42e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.33 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 433 KLEELRQHAACKLDlqKLVETLEDQElkENVEIICNLQQLITQLSDETVACM---AAAIDTAVEQEAQVETSPETSRS-- 507
Cdd:PRK02224 224 RYEEQREQARETRD--EADEVLEEHE--ERREELETLEAEIEDLRETIAETErerEELAEEVRDLRERLEELEEERDDll 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 508 -----SDAFTTQHALRQAQMSKELVELNKALAlKEALARKMTQNDSQlqpiqyQYQDNIKELELEVINLQKEKEELVLEL 582
Cdd:PRK02224 300 aeaglDDADAEAVEARREELEDRDEELRDRLE-ECRVAAQAHNEEAE------SLREDADDLEERAEELREEAAELESEL 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 583 QTAKKDAnqaklsERRRKRLQELEGQIADLKKKLNeqskllklkestertvsklnqeirmmkNQRVQLmrqmkEDAEKFR 662
Cdd:PRK02224 373 EEAREAV------EDRREEIEELEEEIEELRERFG---------------------------DAPVDL-----GNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 663 QwkqkkdkevIQLKERDRKRQyELLKLERNFQKQSNVLrRKTEEAAAANK-----------RLKDALQKQREvadkRKET 731
Cdd:PRK02224 415 E---------ELREERDELRE-REAELEATLRTARERV-EEAEALLEAGKcpecgqpvegsPHVETIEEDRE----RVEE 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 732 QSRGMEGTAARVKNwLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTfslTEVRGQVSE 811
Cdd:PRK02224 480 LEAELEDLEEEVEE-VEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERA---AELEAEAEE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 812 SEDSITKQIESLETEMEfrsaQIADLQQKLldAESEDRpKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQS 891
Cdd:PRK02224 556 KREAAAEAEEEAEEARE----EVAELNSKL--AELKER-IESLERIRTLLAAIADAEDEIERLREKREALAELNDERRER 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 892 ktscadmqkmLFEERNHFAEIETELQAElvRMEQQHQEKvlyllsqlQQSQMAEKQLEESVSEKEQQ---LLSTLKCQDE 968
Cdd:PRK02224 629 ----------LAEKRERKRELEAEFDEA--RIEEAREDK--------ERAEEYLEQVEEKLDELREErddLQAEIGAVEN 688
|
570
....*....|....*
gi 116686122 969 ELEKMREVCEQNQQL 983
Cdd:PRK02224 689 ELEELEELRERREAL 703
|
|
| MUTSd |
smart00533 |
DNA-binding domain of DNA mismatch repair MUTS family; |
524-702 |
2.63e-03 |
|
DNA-binding domain of DNA mismatch repair MUTS family;
Pssm-ID: 214710 [Multi-domain] Cd Length: 308 Bit Score: 41.52 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 524 KELVELNKALALKEALARKMTQNDSQLQ-PIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRKrL 602
Cdd:smart00533 79 RDLLRLYDSLEGLKEIRQLLESLDGPLLgLLLKVILEPLLELLELLLELLNDDDPLEVNDGGLIKDGFDPELDELREK-L 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 603 QELEGQIADLKKKLNEQSKLLKLKestERTVSKLNQEIRMMKNQRVQL-----MRQMKEDAEKFRQWK-QKKDKEVIQLK 676
Cdd:smart00533 158 EELEEELEELLKKEREELGIDSLK---LGYNKVHGYYIEVTKSEAKKVpkdfiRRSSLKNTERFTTPElKELENELLEAK 234
|
170 180
....*....|....*....|....*..
gi 116686122 677 ERDRKRQYELLK-LERNFQKQSNVLRR 702
Cdd:smart00533 235 EEIERLEKEILReLLEKVLEYLEELRA 261
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
424-635 |
2.77e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 424 EQANEKMNAKLEELRQHAACKLDLQKLVETLEDQeLKENVEIICNLQQLITQLSDEtvacmaaaIDTAVEQEAQVETSPE 503
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERR-IAALARRIRALEQELAALEAE--------LAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 504 TSRSSDAFTTQHALRQAQMSKELVELN--------KALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEK 575
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLALLLSpedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALL 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116686122 576 EELVLELQTAKKD-ANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSK 635
Cdd:COG4942 181 AELEEERAALEALkAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
666-841 |
2.89e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 666 QKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKN 745
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 746 WLGNEIEvmvSTEEAKRHLND----LLEDRKILAQDVAQLKEKkesgenpppklrrrtfsLTEVRGQVSESEDSITKQIE 821
Cdd:COG1579 93 ALQKEIE---SLKRRISDLEDeileLMERIEELEEELAELEAE-----------------LAELEAELEEKKAELDEELA 152
|
170 180
....*....|....*....|
gi 116686122 822 SLETEMEFRSAQIADLQQKL 841
Cdd:COG1579 153 ELEAELEELEAEREELAAKI 172
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
368-581 |
4.94e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.43 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 368 AHGGTLPGSITVEPSENLQSLMEKNQSLVEENEKLSRGLSEaagqTAQMLERIILTEQANEKMNAKLEELR-QHAACKLD 446
Cdd:PLN02939 211 LIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIE----VAETEERVFKLEKERSLLDASLRELEsKFIVAQED 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 447 LQKLVeTLEDQELKENVEiicNLQQLITQLSDEtVACMAAAIDTAVEQEAQVETSPETsrssdafttqhaLRQAQMSK-- 524
Cdd:PLN02939 287 VSKLS-PLQYDCWWEKVE---NLQDLLDRATNQ-VEKAALVLDQNQDLRDKVDKLEAS------------LKEANVSKfs 349
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 525 -ELVEL--NKALALKEALARKMTQNDSQLQpiqyQYQDNIKELELEVINLQKEKEELVLE 581
Cdd:PLN02939 350 sYKVELlqQKLKLLEERLQASDHEIHSYIQ----LYQESIKEFQDTLSKLKEESKKRSLE 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
577-824 |
5.23e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 577 ELVLELQTAKKDANQAKlseRRRKRLQELEGQIADLKKKLNeqsKLLKLKESTERTVSklnQEIRMMKNQRVQLMRQMKE 656
Cdd:COG4913 215 EYMLEEPDTFEAADALV---EHFDDLERAHEALEDAREQIE---LLEPIRELAERYAA---ARERLAELEYLRAALRLWF 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 657 DAEKFRQWKQkkdkEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRgm 736
Cdd:COG4913 286 AQRRLELLEA----ELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERER-- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 737 egTAARVKNWLgNEIEVMVSTEEAkrhlnDLLEDRKILAQDVAQLKEKKESGENpppKLRRRTFSLTEVRGQvsesEDSI 816
Cdd:COG4913 360 --RRARLEALL-AALGLPLPASAE-----EFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRE----LREL 424
|
....*...
gi 116686122 817 TKQIESLE 824
Cdd:COG4913 425 EAEIASLE 432
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
384-617 |
6.36e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 6.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 384 NLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERI-ILTEQanekmnakLEELRqhaacKLDLQKLvetlEDQELKE- 461
Cdd:COG0497 152 GLEELLEEYREAYRAWRALKKELEELRADEAERARELdLLRFQ--------LEELE-----AAALQPG----EEEELEEe 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 462 -----NVE-IICNLQQLITQLSDETVACM------------AAAIDTAVE------QEAQVETSpETSRSsdaftTQHAL 517
Cdd:COG0497 215 rrrlsNAEkLREALQEALEALSGGEGGALdllgqalralerLAEYDPSLAelaerlESALIELE-EAASE-----LRRYL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 518 RQAQMS-KELVELNKALALKEALARKmtqndsqlqpiqyqYQDNIKEL---------ELEVI-NLQKEKEELVLELQTAK 586
Cdd:COG0497 289 DSLEFDpERLEEVEERLALLRRLARK--------------YGVTVEELlayaeelraELAELeNSDERLEELEAELAEAE 354
|
250 260 270
....*....|....*....|....*....|...
gi 116686122 587 KDANQA--KLSERRRKRLQELEGQIADLKKKLN 617
Cdd:COG0497 355 AELLEAaeKLSAARKKAAKKLEKAVTAELADLG 387
|
|
| PRK00566 |
PRK00566 |
DNA-directed RNA polymerase subunit beta'; Provisional |
536-606 |
8.56e-03 |
|
DNA-directed RNA polymerase subunit beta'; Provisional
Pssm-ID: 234794 [Multi-domain] Cd Length: 1156 Bit Score: 40.44 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 536 KEALARKMTQNDSQLQPIQYQYQDN---------IKELeLEVINLQKEKEELVLELQTAKKDANQAKLSerrrKRLQELE 606
Cdd:PRK00566 141 DTPLEKKQLLTEEEYREALEEYGDEfvakmgaeaIKEL-LKNIDLEAEAEELREELKETGSEQKRKKAL----KRLKVVE 215
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
561-682 |
8.90e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 561 IKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRR--KRLQ----ELEGQIADLKK---KLNEQSKLLKLKESTE- 630
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEqvERLEaeveELEAELEEKDErieRLERELSEARSEERREi 461
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 116686122 631 ---RTVSKLNQEIRMMKNQRvqlmRQMKEDAEKFRQwKQKKDKEVIQLKERDRKR 682
Cdd:COG2433 462 rkdREISRLDREIERLEREL----EEERERIEELKR-KLERLKELWKLEHSGELV 511
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
649-992 |
8.94e-03 |
|
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: 40.48 E-value: 8.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 649 QLMRQMKEDAEKFRQWKQKKDKEVIQlKERDRKRQYELLKLERN----FQKQSNVLRRKTEEAAAANKRLKDALQKQREV 724
Cdd:pfam05483 78 RLYSKLYKEAEKIKKWKVSIEAELKQ-KENKLQENRKIIEAQRKaiqeLQFENEKVSLKLEEEIQENKDLIKENNATRHL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 725 ADKRKETQSRGMEGTAarvknwlgneiEVMVSTEEAKRHLNDLLEDrkiLAQDVAQLKEKKESGENPPPKLRrrtFSLTE 804
Cdd:pfam05483 157 CNLLKETCARSAEKTK-----------KYEYEREETRQVYMDLNNN---IEKMILAFEELRVQAENARLEMH---FKLKE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 805 VRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLLD-----AESEDRPKQ-------RWENIATILEAKcalKYLIG 872
Cdd:pfam05483 220 DHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDltfllEESRDKANQleektklQDENLKELIEKK---DHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 873 ELVSSKIQVSKLESSLKQ--------SKTSC--ADMQKMLFEERNH----FAEIETELQA------ELVRMEQQHQEKvl 932
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKAleedlqiaTKTICqlTEEKEAQMEELNKakaaHSFVVTEFEAttcsleELLRTEQQRLEK-- 374
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 116686122 933 yllsQLQQSQMAEKQLEESVSEKEQqlLSTLKCQDE-ELEKMREVCEQNQQLLRENEIIKQ 992
Cdd:pfam05483 375 ----NEDQLKIITMELQKKSSELEE--MTKFKNNKEvELEELKKILAEDEKLLDEKKQFEK 429
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
598-894 |
9.10e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 598 RRKRLQELEGQIADLKKKLNEQSKL------------LKLKESTERTVSKLNQeIRMMKNQRVQLMRQMK-EDAEKFRQW 664
Cdd:COG5022 808 SRKEYRSYLACIIKLQKTIKREKKLreteevefslkaEVLIQKFGRSLKAKKR-FSLLKKETIYLQSAQRvELAERQLQE 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 665 KQKKDKEVIQLKERDRKRQYELLKLERNFQkqsNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEG---TAA 741
Cdd:COG5022 887 LKIDVKSISSLKLVNLELESEIIELKKSLS---SDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNklhEVE 963
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 742 RVKNWLGNEIEVMV-STEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRG--QVSESEDSITK 818
Cdd:COG5022 964 SKLKETSEEYEDLLkKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSasKIISSESTELS 1043
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 116686122 819 QIESLETEMEFRSAQIADLQQKLLDAESedrPKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTS 894
Cdd:COG5022 1044 ILKPLQKLKGLLLLENNQLQARYKALKL---RRENSLLDDKQLYQLESTENLLKTINVKDLEVTNRNLVKPANVLQ 1116
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
385-724 |
9.63e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.06 E-value: 9.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 385 LQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQHAACKLDLQKLVETLEDQ--ELKEN 462
Cdd:pfam05622 23 VSLLQEEKNSLQQENKKLQERLDQLESGDDSGTPGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEvlELQHR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 463 VEIICNLQQLITQLSDETVACMAAAiDTAVEQEAQVETSPE----------TSRSSDAFTTQHALRQAQMSKELVELNKA 532
Cdd:pfam05622 103 NEELTSLAEEAQALKDEMDILRESS-DKVKKLEATVETYKKkledlgdlrrQVKLLEERNAEYMQRTLQLEEELKKANAL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 533 LALKEALARKMTQNDSQLQPIQYQY---QDNIKELELEVINLQKEKEELVLELQTAKK--------DANQAKLS------ 595
Cdd:pfam05622 182 RGQLETYKRQVQELHGKLSEESKKAdklEFEYKKLEEKLEALQKEKERLIIERDTLREtneelrcaQLQQAELSqadall 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 596 -----------------ERRRK--RLQeLEGQIADLKKKLNEQSKLLKLK---ESTERTVSKLNQEIRMmKNQRVQLMRQ 653
Cdd:pfam05622 262 spssdpgdnlaaeimpaEIREKliRLQ-HENKMLRLGQEGSYRERLTELQqllEDANRRKNELETQNRL-ANQRILELQQ 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 116686122 654 MKEDAEKFRQW-----------KQKKDKEVIQLKERDRKRQYELLKLERNFQKQSN-----------VLRRKTEEAAAAN 711
Cdd:pfam05622 340 QVEELQKALQEqgskaedssllKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSnlaqkidelqeALRKKDEDMKAME 419
|
410
....*....|...
gi 116686122 712 KRLKDALQKQREV 724
Cdd:pfam05622 420 ERYKKYVEKAKSV 432
|
|
| |
