|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
25-373 |
0e+00 |
|
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: 625.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 25 DAIKVFVRIRPPAERSGsaDGEQNLCLSVLSSTSLRLHSNPePKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGT 104
Cdd:cd01373 1 DAVKVFVRIRPPAEREG--DGEYGQCLKKLSSDTLVLHSKP-PKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 105 IFAYGQTGSGKTFTMMGPSESDN-FSHNLRGVIPRSFEYLFSLIDREKEKAGAGKSFLCKCSFIEIYNEQIYDLLDSASA 183
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDNeSPHGLRGVIPRIFEYLFSLIQREKEKAGEGKSFLCKCSFLEIYNEQIYDLLDPASR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 184 GLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVNIRTSLLNL 263
Cdd:cd01373 158 NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFVNIRTSRLNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 264 VDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDVGNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPG 343
Cdd:cd01373 238 VDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPS 317
|
330 340 350
....*....|....*....|....*....|
gi 74752937 344 SRCFGETLSTLNFAQRAKLIKNKAVVNEDT 373
Cdd:cd01373 318 SKCFGETLSTLRFAQRAKLIKNKAVVNEDT 347
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
26-361 |
6.10e-154 |
|
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: 467.50 E-value: 6.10e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 26 AIKVFVRIRPPAERSGSadgEQNLCLSVLSSTSLRLHSN----PEPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGY 101
Cdd:cd00106 1 NVRVAVRVRPLNGREAR---SAKSVISVDGGKSVVLDPPknrvAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 102 NGTIFAYGQTGSGKTFTMMGPSESDnfshnlRGVIPRSFEYLFSLIDREKEKagaGKSFLCKCSFIEIYNEQIYDLLDSA 181
Cdd:cd00106 78 NGTIFAYGQTGSGKTYTMLGPDPEQ------RGIIPRALEDIFERIDKRKET---KSSFSVSASYLEIYNEKIYDLLSPV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 182 -SAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVNIRTSL 260
Cdd:cd00106 149 pKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVTSSK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 261 LNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgnGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANV 340
Cdd:cd00106 229 LNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD---GQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACI 305
|
330 340
....*....|....*....|.
gi 74752937 341 HPGSRCFGETLSTLNFAQRAK 361
Cdd:cd00106 306 SPSSENFEETLSTLRFASRAK 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
26-370 |
1.41e-151 |
|
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: 461.66 E-value: 1.41e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 26 AIKVFVRIRPPAERSGSADGEQNLCLSVLSSTSLRLHSNPEP---KTFTFDHVADVDTTQESVFATVAKSIVESCMSGYN 102
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKNRqgeKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 103 GTIFAYGQTGSGKTFTMMGPSESdnfshnlRGVIPRSFEYLFSLIDREKEkagaGKSFLCKCSFIEIYNEQIYDLLDSAS 182
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIGTPDS-------PGIIPRALKDLFEKIDKREE----GWQFSVKVSYLEIYNEKIRDLLNPSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 183 AGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVNIRTSLLN 262
Cdd:smart00129 150 KKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 263 LVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHP 342
Cdd:smart00129 230 LVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQ--HSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSP 307
|
330 340
....*....|....*....|....*...
gi 74752937 343 GSRCFGETLSTLNFAQRAKLIKNKAVVN 370
Cdd:smart00129 308 SSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
32-363 |
1.46e-143 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 440.09 E-value: 1.46e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 32 RIRPPAERSGSADGEQNL-CLSVLSSTSLRLHSNP--EPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGTIFAY 108
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVsVESVDSETVESSHLTNknRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 109 GQTGSGKTFTMMGPSESdnfshnlRGVIPRSFEYLFSLIDREKEKagagKSFLCKCSFIEIYNEQIYDLLDSASA---GL 185
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQ-------PGIIPRALEDLFDRIQKTKER----SEFSVKVSYLEIYNEKIRDLLSPSNKnkrKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 186 YLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEI-VNIRTSLLNLV 264
Cdd:pfam00225 150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGeESVKTGKLNLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 265 DLAGSERQKDTH-AEGMRLKEAGNINRSLSCLGQVITALVDvgnGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPG 343
Cdd:pfam00225 230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD---KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPS 306
|
330 340
....*....|....*....|
gi 74752937 344 SRCFGETLSTLNFAQRAKLI 363
Cdd:pfam00225 307 SSNYEETLSTLRFASRAKNI 326
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
25-363 |
2.61e-111 |
|
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: 354.07 E-value: 2.61e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 25 DAIKVFVRIRPPAERSGSADGEQNLCLSVLSST-SLRlhsNPE------PKTFTFDHVADVDTTQESVFATVAKSIVESC 97
Cdd:cd01371 1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQvSVR---NPKatanepPKTFTFDAVFDPNSKQLDVYDETARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 98 MSGYNGTIFAYGQTGSGKTFTMMGPSESDnfshNLRGVIPRSFEYLFSLIDREKEKagagKSFLCKCSFIEIYNEQIYDL 177
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDP----ELRGIIPNSFAHIFGHIARSQNN----QQFLVRVSYLEIYNEEIRDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 178 L-DSASAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVN- 255
Cdd:cd01371 150 LgKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 256 IRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgnGKQRHVCYRDSKLTFLLRDSLGGNAKTA 335
Cdd:cd01371 230 IRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD---GKSTHIPYRDSKLTRLLQDSLGGNSKTV 306
|
330 340
....*....|....*....|....*...
gi 74752937 336 IIANVHPGSRCFGETLSTLNFAQRAKLI 363
Cdd:cd01371 307 MCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
26-363 |
1.76e-110 |
|
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: 351.25 E-value: 1.76e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 26 AIKVFVRIRPPAERSGSADGEqnlCLSVLSSTSLrLHSNPEPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGTI 105
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQ---VAWEIDNDTI-YLVEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 106 FAYGQTGSGKTFTMMGPSESDnfshnlrGVIPRSFEYLFSLIDREKEKAgagksFLCKCSFIEIYNEQIYDLLDSASAGL 185
Cdd:cd01374 77 FAYGQTSSGKTFTMSGDEDEP-------GIIPLAIRDIFSKIQDTPDRE-----FLLRVSYLEIYNEKINDLLSPTSQNL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 186 YLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVN-IRTSLLNLV 264
Cdd:cd01374 145 KIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGtVRVSTLNLI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 265 DLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALvdvGNGK-QRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPG 343
Cdd:cd01374 225 DLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKL---SEGKvGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPA 301
|
330 340
....*....|....*....|
gi 74752937 344 SRCFGETLSTLNFAQRAKLI 363
Cdd:cd01374 302 ESHVEETLNTLKFASRAKKI 321
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
27-365 |
4.74e-107 |
|
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: 342.27 E-value: 4.74e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 27 IKVFVRIRPPaerSGSADGEQNLCLSVLSSTSLRLH---SNPEPKTFTFDHVADVDTTQESVFATVaKSIVESCMSGYNG 103
Cdd:cd01366 4 IRVFCRVRPL---LPSEENEDTSHITFPDEDGQTIEltsIGAKQKEFSFDKVFDPEASQEDVFEEV-SPLVQSALDGYNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 104 TIFAYGQTGSGKTFTMMGPSESDnfshnlrGVIPRSFEYLFSLIdreKEKAGAGKSFLCKCSFIEIYNEQIYDLLDSASA 183
Cdd:cd01366 80 CIFAYGQTGSGKTYTMEGPPESP-------GIIPRALQELFNTI---KELKEKGWSYTIKASMLEIYNETIRDLLAPGNA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 184 G---LYLR-EHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEivNIRTS 259
Cdd:cd01366 150 PqkkLEIRhDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTG--EISVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 260 LLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALvdvgNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIAN 339
Cdd:cd01366 228 KLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL----RQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVN 303
|
330 340
....*....|....*....|....*.
gi 74752937 340 VHPGSRCFGETLSTLNFAQRAKLIKN 365
Cdd:cd01366 304 ISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
26-364 |
1.05e-103 |
|
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: 333.53 E-value: 1.05e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 26 AIKVFVRIRP--PAERSgsaDGEQNlCLSVLSST-SLRLHSNpepKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYN 102
Cdd:cd01372 2 SVRVAVRVRPllPKEII---EGCRI-CVSFVPGEpQVTVGTD---KSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 103 GTIFAYGQTGSGKTFTMMGPSESDNFSHNLrGVIPRSFEYLFSLIDREKEkagaGKSFLCKCSFIEIYNEQIYDLLDSAS 182
Cdd:cd01372 75 ATVLAYGQTGSGKTYTMGTAYTAEEDEEQV-GIIPRAIQHIFKKIEKKKD----TFEFQLKVSFLEIYNEEIRDLLDPET 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 183 ---AGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVNIR-- 257
Cdd:cd01372 150 dkkPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSad 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 258 ------TSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvGNGKQRHVCYRDSKLTFLLRDSLGGN 331
Cdd:cd01372 230 dknstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGD-ESKKGAHVPYRDSKLTRLLQDSLGGN 308
|
330 340 350
....*....|....*....|....*....|...
gi 74752937 332 AKTAIIANVHPGSRCFGETLSTLNFAQRAKLIK 364
Cdd:cd01372 309 SHTLMIACVSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
25-363 |
3.85e-102 |
|
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: 328.52 E-value: 3.85e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 25 DAIKVFVRIRPPAERSGSADGEqnLCLSVLSSTSLRLHSNPEPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGT 104
Cdd:cd01369 2 CNIKVVCRFRPLNELEVLQGSK--SIVKFDPEDTVVIATSETGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 105 IFAYGQTGSGKTFTMMGPSESDnfshNLRGVIPRSFEYLFSLIdrekEKAGAGKSFLCKCSFIEIYNEQIYDLLDSASAG 184
Cdd:cd01369 80 IFAYGQTSSGKTYTMEGKLGDP----ESMGIIPRIVQDIFETI----YSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 185 LYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIEsmEKSNEIVNIRTSLLNLV 264
Cdd:cd01369 152 LSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVK--QENVETEKKKSGKLYLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 265 DLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgnGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPGS 344
Cdd:cd01369 230 DLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD---GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSS 306
|
330
....*....|....*....
gi 74752937 345 RCFGETLSTLNFAQRAKLI 363
Cdd:cd01369 307 YNESETLSTLRFGQRAKTI 325
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
25-370 |
3.53e-98 |
|
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: 318.91 E-value: 3.53e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 25 DAIKVFVRIRPPAERSGSADG-------EQNLCLSVLSSTSLRLHSNPE-PKTFTFDHVAD-VDT------TQESVFATV 89
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSkcivqmsGKETTLKNPKQADKNNKATREvPKSFSFDYSYWsHDSedpnyaSQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 90 AKSIVESCMSGYNGTIFAYGQTGSGKTFTMMGPSESdnfshnlRGVIPRSFEYLFSLIDREKEKAgagKSFLCKCSFIEI 169
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQ-------PGIIPRLCEDLFSRIADTTNQN---MSYSVEVSYMEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 170 YNEQIYDLLDS----ASAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITI- 244
Cdd:cd01365 151 YNEKVRDLLNPkpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLt 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 245 -ESMEKSNEIVNIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDVGN----GKQRHVCYRDSK 319
Cdd:cd01365 231 qKRHDAETNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskKKSSFIPYRDSV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 74752937 320 LTFLLRDSLGGNAKTAIIANVHPGSRCFGETLSTLNFAQRAKLIKNKAVVN 370
Cdd:cd01365 311 LTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
27-400 |
1.88e-97 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 342.30 E-value: 1.88e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 27 IKVFVRIRPPaersgSADGEQNLCLSVLSSTSLRLHSnpepKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGTIF 106
Cdd:PLN03188 100 VKVIVRMKPL-----NKGEEGEMIVQKMSNDSLTING----QTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVF 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 107 AYGQTGSGKTFTMMGPSE---SDNFSHNLRGVIPRSFEYLFSLIDREKEK-AGAGKSFLCKCSFIEIYNEQIYDLLDSAS 182
Cdd:PLN03188 171 AYGQTGSGKTYTMWGPANgllEEHLSGDQQGLTPRVFERLFARINEEQIKhADRQLKYQCRCSFLEIYNEQITDLLDPSQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 183 AGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKS--NEIVNIRTSL 260
Cdd:PLN03188 251 KNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSvaDGLSSFKTSR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 261 LNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDVGN-GKQRHVCYRDSKLTFLLRDSLGGNAKTAIIAN 339
Cdd:PLN03188 331 INLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCA 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74752937 340 VHPGSRCFGETLSTLNFAQRAKLIKNKAVVNEDTQGNVSQLQAEVKRLKEQLAEL-ASGQTP 400
Cdd:PLN03188 411 ISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDDVNFLREVIRQLRDELQRVkANGNNP 472
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
27-372 |
9.13e-94 |
|
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: 306.56 E-value: 9.13e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 27 IKVFVRIRP--PAERSGSADGEQNL---CLSVLSSTSLRLHSNPEpKTFTFDHVADVDTTQESVFATVAKSIVESCMSGY 101
Cdd:cd01364 4 IQVVVRCRPfnLRERKASSHSVVEVdpvRKEVSVRTGGLADKSST-KTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 102 NGTIFAYGQTGSGKTFTMMGpSESDNFSHNLR-----GVIPRSFEYLFSLIDREkekagaGKSFLCKCSFIEIYNEQIYD 176
Cdd:cd01364 83 NCTIFAYGQTGTGKTYTMEG-DRSPNEEYTWEldplaGIIPRTLHQLFEKLEDN------GTEYSVKVSYLEIYNEELFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 177 LLDSAS-----AGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSN 251
Cdd:cd01364 156 LLSPSSdvserLRMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 252 EIVN-IRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgngKQRHVCYRDSKLTFLLRDSLGG 330
Cdd:cd01364 236 DGEElVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE----RAPHVPYRESKLTRLLQDSLGG 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 74752937 331 NAKTAIIANVHPGSRCFGETLSTLNFAQRAKLIKNKAVVNED 372
Cdd:cd01364 312 RTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
27-363 |
1.60e-91 |
|
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: 300.03 E-value: 1.60e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 27 IKVFVRIRPPAERSGSA------------------DGEQNLCLSVLSSTSLRLHSNPEPKTFTFDHVADVDTTQESVFAT 88
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEgfrrivkvmdnhmlvfdpKDEEDGFFHGGSNNRDRRKRRNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 89 VAKSIVESCMSGYNGTIFAYGQTGSGKTFTMMGPSESDnfshnlrGVIPRSFEYLFSLIDREKEKagagKSFLCKCSFIE 168
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP-------GLMVLTMKELFKRIESLKDE----KEFEVSMSYLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 169 IYNEQIYDLLDSASAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESME 248
Cdd:cd01370 151 IYNETIRDLLNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 249 KSNEIV-NIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvGNGKQRHVCYRDSKLTFLLRDS 327
Cdd:cd01370 231 KTASINqQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD-PGKKNKHIPYRDSKLTRLLKDS 309
|
330 340 350
....*....|....*....|....*....|....*.
gi 74752937 328 LGGNAKTAIIANVHPGSRCFGETLSTLNFAQRAKLI 363
Cdd:cd01370 310 LGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
26-361 |
3.22e-84 |
|
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: 279.08 E-value: 3.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 26 AIKVFVRIRPPAERSGS--ADGEQNLCLSVLSSTSLR---LHSNPEPKTFTFDHVADvDTTQESVFATVAKSIVESCMSG 100
Cdd:cd01375 1 KVQAFVRVRPTDDFAHEmiKYGEDGKSISIHLKKDLRrgvVNNQQEDWSFKFDGVLH-NASQELVYETVAKDVVSSALAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 101 YNGTIFAYGQTGSGKTFTMMGPSEsdNFSHnlRGVIPRSFEYLFSLIDREKEKAgagksFLCKCSFIEIYNEQIYDLLDS 180
Cdd:cd01375 80 YNGTIFAYGQTGAGKTFTMTGGTE--NYKH--RGIIPRALQQVFRMIEERPTKA-----YTVHVSYLEIYNEQLYDLLST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 181 ------ASAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIV 254
Cdd:cd01375 151 lpyvgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLSSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 255 NIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALvdvGNGKQRHVCYRDSKLTFLLRDSLGGNAKT 334
Cdd:cd01375 231 KYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIAL---SDKDRTHVPFRQSKLTHVLRDSLGGNCNT 307
|
330 340
....*....|....*....|....*..
gi 74752937 335 AIIANVHPGSRCFGETLSTLNFAQRAK 361
Cdd:cd01375 308 VMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
25-361 |
2.44e-79 |
|
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: 265.41 E-value: 2.44e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 25 DAIKVFVRIRPPAERSGSADGEqnLCLSVLSSTSLRLHS------NPEPKT-------FTFDHVADVDTTQESVFATVAK 91
Cdd:cd01368 1 DPVKVYLRVRPLSKDELESEDE--GCIEVINSTTVVLHPpkgsaaNKSERNggqketkFSFSKVFGPNTTQKEFFQGTAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 92 SIVESCMSGYNGTIFAYGQTGSGKTFTMMGPSESdnfshnlRGVIPRSFEYLFSLIdrekekagagKSFLCKCSFIEIYN 171
Cdd:cd01368 79 PLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGD-------GGILPRSLDVIFNSI----------GGYSVFVSYIEIYN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 172 EQIYDLLDSAS-------AGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITI 244
Cdd:cd01368 142 EYIYDLLEPSPssptkkrQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 245 ------ESMEKSNEIVNIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITAL-VDVGNGKQRHVCYRD 317
Cdd:cd01368 222 vqapgdSDGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLrENQLQGTNKMVPFRD 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 74752937 318 SKLTFLLRDSLGGNAKTAIIANVHPGSRCFGETLSTLNFAQRAK 361
Cdd:cd01368 302 SKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
27-361 |
1.05e-75 |
|
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: 254.35 E-value: 1.05e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 27 IKVFVRIRPPAERSGSADGEQnlCLSVLSSTSLRLhSNP----EPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYN 102
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPS--CVSGIDSCSVEL-ADPrnhgETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 103 GTIFAYGQTGSGKTFTMMGpsesdnfSHNLRGVIPRSFEYLFSLIDREKEKAGAgksflcKCSFIEIYNEQIYDLLDSAS 182
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLG-------SPEQPGLMPLTVMDLLQMTRKEAWALSF------TMSYLEIYQEKILDLLEPAS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 183 AGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEkSNEIVNIRTSLLN 262
Cdd:cd01376 146 KELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRE-RLAPFRQRTGKLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 263 LVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALvdvgNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHP 342
Cdd:cd01376 225 LIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL----NKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAP 300
|
330
....*....|....*....
gi 74752937 343 GSRCFGETLSTLNFAQRAK 361
Cdd:cd01376 301 ERTFYQDTLSTLNFAARSR 319
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
27-504 |
2.72e-73 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 255.82 E-value: 2.72e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 27 IKVFVRIRPpaersgsadGEQNLCLSVLSSTSLRLHSNPEPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGTIF 106
Cdd:COG5059 24 IKSTIRIIP---------GELGERLINTSKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 107 AYGQTGSGKTFTMMGpsesdnfSHNLRGVIPRSFEYLFSLIDREKekagAGKSFLCKCSFIEIYNEQIYDLLDSASAGLY 186
Cdd:COG5059 95 AYGQTGSGKTYTMSG-------TEEEPGIIPLSLKELFSKLEDLS----MTKDFAVSISYLEIYNEKIYDLLSPNEESLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 187 LREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIvnIRTSLLNLVDL 266
Cdd:COG5059 164 IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGT--SETSKLSLVDL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 267 AGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPGSRC 346
Cdd:COG5059 242 AGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGD--KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 347 FGETLSTLNFAQRAKLIKNKAVVNedtqgNVSQLQAEVKRLKEQLAELASGQTPPESFLTRDKKKTNYMEYFQEAMLFFK 426
Cdd:COG5059 320 FEETINTLKFASRAKSIKNKIQVN-----SSSDSSREIEEIKFDLSEDRSEIEILVFREQSQLSQSSLSGIFAYMQSLKK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 427 KSEQEKKS--LIEKVTQL---EDLTLKKEKFiQSNKMIVKFREDQIIRLEKLHKESRggFLPEEQDRLLSELRNEIQTLR 501
Cdd:COG5059 395 ETETLKSRidLIMKSIISgtfERKKLLKEEG-WKYKSTLQFLRIEIDRLLLLREEEL--SKKKTKIHKLNKLRHDLSSLL 471
|
...
gi 74752937 502 EQI 504
Cdd:COG5059 472 SSI 474
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
27-361 |
2.04e-65 |
|
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a protein expressed in neurons, which has been associated with axonal transport and neuron development; alternative splice forms have been implicated in lysosomal translocation. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found in the middle (M-type) of the protein chain. M-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second (KIF2 may be slower). To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276818 [Multi-domain] Cd Length: 328 Bit Score: 224.87 E-value: 2.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 27 IKVFVRIRP---PAERSGSAD---GEQNLCLSVLS-STSLRLHSNPEPKTFTFDHVADVDTTQESVFATVAKSIVESCMS 99
Cdd:cd01367 2 IKVCVRKRPlnkKEVAKKEIDvvsVPSKLTLIVHEpKLKVDLTKYIENHTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 100 GYNGTIFAYGQTGSGKTFTMMGpseSDNFSHNLRGVIPRSFEYLFSLIDREKEKAGAGKSflckCSFIEIYNEQIYDLLd 179
Cdd:cd01367 82 GGKATCFAYGQTGSGKTYTMGG---DFSGQEESKGIYALAARDVFRLLNKLPYKDNLGVT----VSFFEIYGGKVFDLL- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 180 SASAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKsneivNIRTS 259
Cdd:cd01367 154 NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGT-----NKLHG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 260 LLNLVDLAGSERQKDT-HAEGMRLKEAGNINRSLSCLGQVITALVDvgngKQRHVCYRDSKLTFLLRDSL-GGNAKTAII 337
Cdd:cd01367 229 KLSFVDLAGSERGADTsSADRQTRMEGAEINKSLLALKECIRALGQ----NKAHIPFRGSKLTQVLKDSFiGENSKTCMI 304
|
330 340
....*....|....*....|....
gi 74752937 338 ANVHPGSRCFGETLSTLNFAQRAK 361
Cdd:cd01367 305 ATISPGASSCEHTLNTLRYADRVK 328
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
29-301 |
3.23e-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: 95.10 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 29 VFVRIRPPaersgsadgeqnlclsvlsstsLRLHSNPEPKTFTFDHVADVDTTQESVFATVAKsIVESCMSGYNG-TIFA 107
Cdd:cd01363 1 VLVRVNPF----------------------KELPIYRDSKIIVFYRGFRRSESQPHVFAIADP-AYQSMLDGYNNqSIFA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 108 YGQTGSGKTFTMMgpsesdnfshnlrGVIPRSFEYLFSLIDREKEKAGAGKSFLCKCSfieiyNEQIYDLLDSasaglyl 187
Cdd:cd01363 58 YGESGAGKTETMK-------------GVIPYLASVAFNGINKGETEGWVYLTEITVTL-----EDQILQANPI------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 188 rehikkgvfvvgaveqvvtsaAEAYqvlsggwrnrRVASTSMNRESSRSHAVFTItiesmeksneivnirtsllnLVDLA 267
Cdd:cd01363 113 ---------------------LEAF----------GNAKTTRNENSSRFGKFIEI--------------------LLDIA 141
|
250 260 270
....*....|....*....|....*....|....
gi 74752937 268 GSERqkdthaegmrlkeagnINRSLSCLGQVITA 301
Cdd:cd01363 142 GFEI----------------INESLNTLMNVLRA 159
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
27-178 |
2.19e-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: 80.34 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 27 IKVFVRIRPPAERsgsadgeqNLCLSVLSSTSLRLHSNPEPKTFTFDHVADVDTTQESVFATVaKSIVESCMSGYNGTIF 106
Cdd:pfam16796 22 IRVFARVRPELLS--------EAQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIF 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74752937 107 AYGQTGSGKTftmmgpsesdnfshnlRGVIPRSFEYLFSLIdrekEKAGAGKSFLCKCSFIEIYNEQIYDLL 178
Cdd:pfam16796 93 AYGQTGSGSN----------------DGMIPRAREQIFRFI----SSLKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
579-1339 |
1.23e-16 |
|
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: 85.88 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 579 ANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENL---LEATKACKRQEVSQLNKihaet 655
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisrLEQQKQILRERLANLER----- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 656 lkiittptkayqlhsrpvpklSPEMGSFGSLYTQNSSILDNDILNEpvppemneqafeaISEELRTVQEQMSALQAKLDE 735
Cdd:TIGR02168 317 ---------------------QLEELEAQLEELESKLDELAEELAE-------------LEEKLEELKEELESLEAELEE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 736 EEHKNLKLQQHVDKLEHHSTQmqelFSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELS 815
Cdd:TIGR02168 363 LEAELEELESRLEELEEQLET----LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKEL 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 816 SVKLEYSsfktnqEKEFNKLSERHMHVQLQLDNLRLENEKLLESkacLQDSYDNLQEImKFEIDQLSRNLQNFKKENETL 895
Cdd:TIGR02168 439 QAELEEL------EEELEELQEELERLEEALEELREELEEAEQA---LDAAERELAQL-QARLDSLERLQENLEGFSEGV 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 896 KSDLNN----------LMELLEAEKERNNKLSLQFEEDKEN----SSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEE 961
Cdd:TIGR02168 509 KALLKNqsglsgilgvLSELISVDEGYEAAIEAALGGRLQAvvveNLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQG 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 962 SLLATEK-------VISSLEKSRDSDKKVVADLMNQIqelrtSVCektETIDTLKQELKDINCKYNSALVDREesrvLIK 1034
Cdd:TIGR02168 589 NDREILKniegflgVAKDLVKFDPKLRKALSYLLGGV-----LVV---DDLDNALELAKKLRPGYRIVTLDGD----LVR 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1035 KQEVdILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEV 1114
Cdd:TIGR02168 657 PGGV-ITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1115 EQKKNEynfkMRQLEHVMDSAAEDpqspktpphfQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRM 1194
Cdd:TIGR02168 736 ARLEAE----VEQLEERIAQLSKE----------LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1195 KEQLREME----NLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQqlknEQEESIKERLAKSKIVEEMLKMKADL 1270
Cdd:TIGR02168 802 REALDELRaeltLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS----EDIESLAAEIEELEELIEELESELEA 877
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74752937 1271 EEVQSALYNKEMECLR--MTDEVERTQTLESKAfQEKEQLRSKLEEMYEERERTSQEMEMLRKQV-ECLAEE 1339
Cdd:TIGR02168 878 LLNERASLEEALALLRseLEELSEELRELESKR-SELRRELEELREKLAQLELRLEGLEVRIDNLqERLSEE 948
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
582-1320 |
3.32e-13 |
|
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: 74.77 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 582 EKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQ-----------KANLNLENL----------LEATKAC 640
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQmerdamadirrRESQSQEDLrnqlqntvheLEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 641 KRQ-------EVSQLNKI---HAETLKIITTPTKAYQLHSrpvPKLSPEMGSFGSLYTQNSSILDNDILNEPvppemnEQ 710
Cdd:pfam15921 161 KEDmledsntQIEQLRKMmlsHEGVLQEIRSILVDFEEAS---GKKIYEHDSMSTMHFRSLGSAISKILREL------DT 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 711 AFEAISEELRTVQEQMSALQAklDEEEHKNLKLQQHVDKLEH-------HSTQMQELFSSERidwtKQQEELLSQLNVLE 783
Cdd:pfam15921 232 EISYLKGRIFPVEDQLEALKS--ESQNKIELLLQQHQDRIEQlisehevEITGLTEKASSAR----SQANSIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 784 KQlqeTQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEfnklserhmhvqlqldnLRLENEKLLESKAcl 863
Cdd:pfam15921 306 EQ---ARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQ-----------------LVLANSELTEART-- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 864 qdsydnlqeimkfEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKL------------SLQFEEDKENSSKEI 931
Cdd:pfam15921 364 -------------ERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidHLRRELDDRNMEVQR 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 932 LK-VLEAVRQEKQketAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSvcEKTETIDTLKQ 1010
Cdd:pfam15921 431 LEaLLKAMKSECQ---GQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS--ERTVSDLTASL 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1011 ELKDINCKYNSALVDREESRVLIKKQEVDILDLK-----------ETLRLRIlsedIERDMLCEDLAHATEQLNMLTEAS 1079
Cdd:pfam15921 506 QEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhlrnvqtecEALKLQM----AEKDKVIEILRQQIENMTQLVGQH 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1080 KKHSGLLQSAQEELT------------------KKEALIQELQHKLNQKKEEveqKKNEYNFKMRQLEHVMDSAAEDPQS 1141
Cdd:pfam15921 582 GRTAGAMQVEKAQLEkeindrrlelqefkilkdKKDAKIRELEARVSDLELE---KVKLVNAGSERLRAVKDIKQERDQL 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1142 PKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREME-------NLRLESQQLIEK 1214
Cdd:pfam15921 659 LNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdghamKVAMGMQKQITA 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1215 NwllQGQLDDIKRQ---KENSDQNHPDNQQLKNEQEESIKERLA-----KSKIVEEMLKMKADLEEVQSALYNKEMECLR 1286
Cdd:pfam15921 739 K---RGQIDALQSKiqfLEEAMTNANKEKHFLKEEKNKLSQELStvateKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
810 820 830
....*....|....*....|....*....|....
gi 74752937 1287 MTDEVERTQTLESKafQEKEQLRSKLEEMYEERE 1320
Cdd:pfam15921 816 ASLQFAECQDIIQR--QEQESVRLKLQHTLDVKE 847
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
773-1329 |
1.87e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 773 EELLSQLNVLEKQlQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQ-EKEFNKLSERHMHVQLQLDNLRL 851
Cdd:COG1196 196 GELERQLEPLERQ-AEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEElEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 852 ENEKL-LESKACLQDSYDNLQEIMKFE--IDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQfEEDKENSS 928
Cdd:COG1196 275 ELEELeLELEEAQAEEYELLAELARLEqdIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE-LEEAEEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 929 KEILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTL 1008
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1009 KQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLRILSEDIERdmlcEDLAHATEQLNMLTEASKKHSGLLQS 1088
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL----EELAEAAARLLLLLEAEADYEGFLEG 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1089 AQEELTKK-----------------------EALIQELQHKLNQKKEEVEQKKNEY---NFKMRQLEHVMDSAAEDPQSP 1142
Cdd:COG1196 510 VKAALLLAglrglagavavligveaayeaalEAALAAALQNIVVEDDEVAAAAIEYlkaAKAGRATFLPLDKIRARAALA 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1143 KTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDRE-------VKNAEILRMKEQLREMENLRLESQQLIEKN 1215
Cdd:COG1196 590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLeaalrraVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1216 wLLQGQLDDIKRQKENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQ 1295
Cdd:COG1196 670 -LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580 590
....*....|....*....|....*....|....
gi 74752937 1296 TLESKAFQEKEQLRSKLEemyEERERTSQEMEML 1329
Cdd:COG1196 749 EEEALEELPEPPDLEELE---RELERLEREIEAL 779
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1044-1334 |
2.69e-11 |
|
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: 68.54 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1044 KETLRLRILSEDIERdmLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNF 1123
Cdd:TIGR02168 222 LRELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1124 KMRQLEHVMDSAAEDPQSPKtpphfqtHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMEN 1203
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLE-------ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1204 LRLESQQLIEKnwlLQGQLDDIKRQkENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEME 1283
Cdd:TIGR02168 373 RLEELEEQLET---LRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 74752937 1284 CLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEERERTSQEMEMLRKQVE 1334
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
773-1376 |
4.11e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 773 EELLSQLNVLEKQLQETQtKNDFLKSEVHDLRV-----VLHSADKELSSVKLEYSSfktnQEKEFNKLSERHMHVQLQLD 847
Cdd:TIGR02168 196 NELERQLKSLERQAEKAE-RYKELKAELRELELallvlRLEELREELEELQEELKE----AEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 848 NLRLENEKLLESKACLQDSYDNLQEimkfEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLslqfeEDKENS 927
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALAN----EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-----AEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 928 SKEILKVLEAVRQEKQKETAKCEqqmAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDT 1007
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELE---AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1008 LKQELKDINCKYNSALVDREESRVLIKKQEVDILD--------LKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEAS 1079
Cdd:TIGR02168 419 LQQEIEELLKKLEEAELKELQAELEELEEELEELQeelerleeALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1080 KKHSGLLQSAQEELTKKE-------------------------ALIQELQH----KLNQKKEEVE-QKKNEYNFKMRQLE 1129
Cdd:TIGR02168 499 ENLEGFSEGVKALLKNQSglsgilgvlselisvdegyeaaieaALGGRLQAvvveNLNAAKKAIAfLKQNELGRVTFLPL 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1130 HVM---DSAAEDPQSPKTPPHFQThLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNA------------EILR- 1193
Cdd:TIGR02168 579 DSIkgtEIQGNDREILKNIEGFLG-VAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrpgyrivtldgDLVRp 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1194 --------------MKEQLREMENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQQLKNEQEESI---KERLAK 1256
Cdd:TIGR02168 658 ggvitggsaktnssILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDLAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1257 SKIVEEMLKMKADLEEVQSALYNKEMECLRmtDEVERTQTLESKAFQEKEQLRSKLEEMYEERERTSQEMEMLRKQVECL 1336
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELE--ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 74752937 1337 AEENGKLVGHQNLHQKiqYVVRLKKENVRLAEETEKLRAE 1376
Cdd:TIGR02168 816 NEEAANLRERLESLER--RIAATERRLEDLEEQIEELSED 853
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
696-1376 |
4.78e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 696 NDILNEpvppemneqafeaISEELRTVQEQMS-ALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSseridwtkQQEE 774
Cdd:TIGR02168 192 EDILNE-------------LERQLKSLERQAEkAERYKELKAELRELELALLVLRLEELREELEELQE--------ELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 775 LLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSsfKTNQEKEFNKLSERHMHVQLQLDNLRLEN- 853
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIS--RLEQQKQILRERLANLERQLEELEAQLEEl 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 854 -EKLLESKACLQDSYDNLQEIMKfEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQfEEDKENSSKEIL 932
Cdd:TIGR02168 329 eSKLDELAEELAELEEKLEELKE-ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ-IASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 933 KVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEkvISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQEL 1012
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1013 KDINCKYNSALVDREESR-----------------------------------------------VLIK-----KQEVDI 1040
Cdd:TIGR02168 485 AQLQARLDSLERLQENLEgfsegvkallknqsglsgilgvlselisvdegyeaaieaalggrlqaVVVEnlnaaKKAIAF 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1041 LDLKETLRLRILSEDIERD------------------------------------------MLCEDLAHATEQLNMLTE- 1077
Cdd:TIGR02168 565 LKQNELGRVTFLPLDSIKGteiqgndreilkniegflgvakdlvkfdpklrkalsyllggvLVVDDLDNALELAKKLRPg 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1078 --------------------ASKKHSGLLQSAQE--ELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSA 1135
Cdd:TIGR02168 645 yrivtldgdlvrpggvitggSAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1136 AEDpqspktpphfQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEKn 1215
Cdd:TIGR02168 725 SRQ----------ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ- 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1216 wlLQGQLDDIKRQKENSdqnhpdNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQ 1295
Cdd:TIGR02168 794 --LKEELKALREALDEL------RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1296 TLESKAFQEKEQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGKLV-GHQNLHQKI-QYVVRLKKENVRLAEETEKL 1373
Cdd:TIGR02168 866 ELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRrELEELREKLaQLELRLEGLEVRIDNLQERL 945
|
...
gi 74752937 1374 RAE 1376
Cdd:TIGR02168 946 SEE 948
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1034-1334 |
3.26e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 61.29 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1034 KKQEVDILDLKETLRLRILSEDIERDMlcedlahatEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEE 1113
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREV---------ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1114 VEQKKNEynfKMRQLEHVMDSaaedpQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLN-----------E 1182
Cdd:pfam17380 357 ERKRELE---RIRQEEIAMEI-----SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQqqkvemeqiraE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1183 DREVKNAEILRMKEQ-LREMENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQQLKNEQEESIKERLA--KSKI 1259
Cdd:pfam17380 429 QEEARQREVRRLEEErAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerKQAM 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1260 VEEMLKMK---ADLEEVQSALYNKEMEclRMTDEVERTQTLESKAFQEKEQL------RSKLEEMYEERERTSQEMEMLR 1330
Cdd:pfam17380 509 IEEERKRKlleKEMEERQKAIYEEERR--REAEEERRKQQEMEERRRIQEQMrkateeRSRLEAMEREREMMRQIVESEK 586
|
....
gi 74752937 1331 KQVE 1334
Cdd:pfam17380 587 ARAE 590
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
554-1313 |
1.61e-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: 59.60 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 554 ISGMEKSDKNQQGFSPKAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENL 633
Cdd:TIGR00618 169 LMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 634 LEATKACKRQEvsqlnkihaETLKIITTPTKAYQLHSRPVPKLSPEmgsfgslytqnssiLDNDILNEPVPPEMN--EQA 711
Cdd:TIGR00618 249 REAQEEQLKKQ---------QLLKQLRARIEELRAQEAVLEETQER--------------INRARKAAPLAAHIKavTQI 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 712 FEAISEELRTVQEQMsalqAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSErIDWTKQQEELLSQLNVLEKQLQETQt 791
Cdd:TIGR00618 306 EQQAQRIHTELQSKM----RSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQE-IHIRDAHEVATSIREISCQQHTLTQ- 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 792 kndflksEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERHMhVQLQLDNLRLENEKLLESKACLQDSYDNLQ 871
Cdd:TIGR00618 380 -------HIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD-LQGQLAHAKKQQELQQRYAELCAAAITCTA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 872 EIMKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQ-EKQKETAKCE 950
Cdd:TIGR00618 452 QCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIdNPGPLTRRMQ 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 951 QQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESR 1030
Cdd:TIGR00618 532 RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1031 VLIKKQEVDILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEE-LTKKEALIQELQHKLNQ 1109
Cdd:TIGR00618 612 CEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKElLASRQLALQKMQSEKEQ 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1110 ---KKEEVEQKkneyNFKMR-QLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRA-SKTSLEHLVtklnEDR 1184
Cdd:TIGR00618 692 ltyWKEMLAQC----QTLLReLETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHqARTVLKART----EAH 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1185 EVKNAEILRMKEQLREMENLRLESQQLIEKNWLLQGQLDDIKRQKEnsdQNHPDNQQLKNEQEESIKERLA--------K 1256
Cdd:TIGR00618 764 FNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIG---QEIPSDEDILNLQCETLVQEEEqflsrleeK 840
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 74752937 1257 SKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLE 1313
Cdd:TIGR00618 841 SATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFL 897
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
706-1378 |
2.58e-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: 58.83 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 706 EMNEQAFEAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQEL-FSSERIDWTKQQEELLSQLNVLEK 784
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLeETQERINRARKAAPLAAHIKAVTQ 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 785 QLQETQTKNDFLKSEVHDLRVVLHSADKELSsvkleyssfktnQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQ 864
Cdd:TIGR00618 305 IEQQAQRIHTELQSKMRSRAKLLMKRAAHVK------------QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISC 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 865 DSYDNLQEIMKFE--IDQLSRNLQNFKKENETLKSDLNNLMELLEAEK-ERNNKLSLQFEEDKENSSKEILKVLEAVRQE 941
Cdd:TIGR00618 373 QQHTLTQHIHTLQqqKTTLTQKLQSLCKELDILQREQATIDTRTSAFRdLQGQLAHAKKQQELQQRYAELCAAAITCTAQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 942 KQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRdsdKKVVADLMNQIQELRTSVCEKTEtidtlkqelkdincKYNS 1021
Cdd:TIGR00618 453 CEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRK---KAVVLARLLELQEEPCPLCGSCI--------------HPNP 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1022 ALVDREESRVLIKKQEvDILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQ 1101
Cdd:TIGR00618 516 ARQDIDNPGPLTRRMQ-RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1102 ELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDS---AAEDPQSPKTPPHFQTHLAKLLET---QEQEIEDGRASKTSLEH 1175
Cdd:TIGR00618 595 RLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLqdvRLHLQQCSQELALKLTALHALQLTltqERVREHALSIRVLPKEL 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1176 LVTKLNEDREVKN--AEILRMKEQLREMENLRLESQQLIEKNWLLQGQLDDIKR-QKENSDQNHPDNQQLKNEQEESIKE 1252
Cdd:TIGR00618 675 LASRQLALQKMQSekEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSsLGSDLAAREDALNQSLKELMHQART 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1253 RLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESKafQEKEQLRSKLEEMYEERERTSQEMEMLRKQ 1332
Cdd:TIGR00618 755 VLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLK--TLEAEIGQEIPSDEDILNLQCETLVQEEEQ 832
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 74752937 1333 VECLAEENGKLVgHQNLHQKIQYVVRLK------KENVRLAEETEKLRAENV 1378
Cdd:TIGR00618 833 FLSRLEEKSATL-GEITHQLLKYEECSKqlaqltQEQAKIIQLSDKLNGINQ 883
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
882-1387 |
2.72e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 882 SRNLQNFKKENETLKSD-LNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLE 960
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADeAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 961 ESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRtsvceKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEvdi 1040
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-----KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE--- 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1041 ldlkETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKhsgllqsaQEELTKKEALIQELQHKlnQKKEEVEQKKNE 1120
Cdd:PTZ00121 1429 ----EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK--------AEEAKKADEAKKKAEEA--KKADEAKKKAEE 1494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1121 YNFKMRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDR---EVKNAEILRMKEQ 1197
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKkaeEKKKAEEAKKAEE 1574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1198 LREMENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQ------QLKNEQEESIKERLAKSKIVEEMLKMKADLE 1271
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1272 EVQSALYNKEMECLRMTDEVERTQTLESKAFQEK---EQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGKLVGHQN 1348
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKkaaEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
490 500 510
....*....|....*....|....*....|....*....
gi 74752937 1349 LHQKIQYVVRlKKENVRLAEETEKLRAENVFLKEKKRSE 1387
Cdd:PTZ00121 1735 AKKEAEEDKK-KAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
709-1235 |
2.87e-08 |
|
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: 58.49 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 709 EQAFEAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERiDWTKQQEELLSQLNVLEKQLQE 788
Cdd:TIGR04523 151 EKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK-KKIQKNKSLESQISELKKQNNQ 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 789 TQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKT---NQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKAclQD 865
Cdd:TIGR04523 230 LKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKqlsEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--QD 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 866 SYDNLQEIMKFEIDQLsRNLQNFKKENETLKSDLNNLMELLEAEKE----RNNKLSLQFEE--------DKENSSK--EI 931
Cdd:TIGR04523 308 WNKELKSELKNQEKKL-EEIQNQISQNNKIISQLNEQISQLKKELTnsesENSEKQRELEEkqneieklKKENQSYkqEI 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 932 LKV---LEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTL 1008
Cdd:TIGR04523 387 KNLesqINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1009 KQELKDINCKYNSALVDREESRVLIKKQEVDILDLKEtlrlrilsediERDMLCEDLAHATEQLNMLTEASKKHSGLLQS 1088
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNE-----------EKKELEEKVKDLTKKISSLKEKIEKLESEKKE 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1089 AQEELTKKEALIQELqhKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDpqspktpphfQTHLAKLLETQEQEIEDGRA 1168
Cdd:TIGR04523 536 KESKISDLEDELNKD--DFELKKENLEKEIDEKNKEIEELKQTQKSLKKK----------QEEKQELIDQKEKEKKDLIK 603
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74752937 1169 SKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEknwLLQGQLDDIKRQKENSDQN 1235
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK---QIKETIKEIRNKWPEIIKK 667
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
711-1114 |
3.59e-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: 58.16 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 711 AFEAISEELRTVQEQMSALQAKLDEEEHKNLK--LQQHVDKLEHHSTQMqelfSSERIDWTKQQEELLSQLNVLEKQLQE 788
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELssLQSELRRIENRLDEL----SQELSDASRKIGEIEKEIEQLEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 789 tqtkndfLKSEVHDLRVVLHSADKELssvkleyssfkTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLESkaclqDSYD 868
Cdd:TIGR02169 735 -------LKERLEELEEDLSSLEQEI-----------ENVKSELKELEARIEELEEDLHKLEEALNDLEAR-----LSHS 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 869 NLQEIMKfEIDQLSRNLQNFKKENETLKSDLNNLMELLE-AEKERNNKLSLQfeEDKENSSKEILKVLEAVRQEKQKETA 947
Cdd:TIGR02169 792 RIPEIQA-ELSKLEEEVSRIEARLREIEQKLNRLTLEKEyLEKEIQELQEQR--IDLKEQIKSIEKEIENLNGKKEELEE 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 948 KCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINckynsALVDRE 1027
Cdd:TIGR02169 869 ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-----DPKGED 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1028 ESrvlIKKQEVDILDLKETLrlrilsEDIERDMlcedlaHATEQLNMLT----EASKKHSGLLQSAQEELTKKEALIQEL 1103
Cdd:TIGR02169 944 EE---IPEEELSLEDVQAEL------QRVEEEI------RALEPVNMLAiqeyEEVLKRLDELKEKRAKLEEERKAILER 1008
|
410
....*....|.
gi 74752937 1104 QHKLNQKKEEV 1114
Cdd:TIGR02169 1009 IEEYEKKKREV 1019
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
708-1272 |
4.64e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.77 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 708 NEQAFEAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSeridwTKQQEELLSQlnvLEKQLQ 787
Cdd:PRK03918 198 KEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS-----KRKLEEKIRE---LEERIE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 788 ETQTKNDFLKSEVHDLRVVLHSADK--ELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQLDNLrleneklleskaclqd 865
Cdd:PRK03918 270 ELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL---------------- 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 866 sydnlqEIMKFEIDQLSRNLQNFKKENETLKSDLnNLMELLEAEKERNNKLSlqfEEDKENSSKEILKVLEAVRQEKQKE 945
Cdd:PRK03918 334 ------EEKEERLEELKKKLKELEKRLEELEERH-ELYEEAKAKKEELERLK---KRLTGLTPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 946 TAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQiqelrtsvcEKTETIDTLKQELKDINCKYNSALVD 1025
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE---------HRKELLEEYTAELKRIEKELKEIEEK 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1026 REESRVLIKKQEVDILDLKETLRLRILSEDIE------RDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEAL 1099
Cdd:PRK03918 475 ERKLRKELRELEKVLKKESELIKLKELAEQLKeleeklKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEEL 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1100 IQELQhKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQSPKTPPHFQTHLAKlleTQEQEIEDGRASKTSLEHLVTK 1179
Cdd:PRK03918 555 KKKLA-ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELK---DAEKELEREEKELKKLEEELDK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1180 LNEDREVKNAEILRMKEQLREM------ENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQQLKNEQEesikER 1253
Cdd:PRK03918 631 AFEELAETEKRLEELRKELEELekkyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE----ER 706
|
570
....*....|....*....
gi 74752937 1254 LAKSKIVEEMLKMKADLEE 1272
Cdd:PRK03918 707 EKAKKELEKLEKALERVEE 725
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
919-1274 |
5.92e-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: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 919 QFEEDKENSSKEilkvLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVA----DLMNQIQEL 994
Cdd:TIGR02169 167 EFDRKKEKALEE----LEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLkekeALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 995 RTSVCEKTETIDTLKQELKDINCKYNSALVDREE-SRVLIKKQEVDILDLKEtlRLRILSEDIERdmlCED-LAHATEQL 1072
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKE--KIGELEAEIAS---LERsIAEKEREL 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1073 NMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQSPKTpphfqthL 1152
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD-------Y 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1153 AKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEKnwlLQGQLDDIKRQKENS 1232
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK---QEWKLEQLAADLSKY 467
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 74752937 1233 DQNHpdnQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQ 1274
Cdd:TIGR02169 468 EQEL---YDLKEEYDRVEKELSKLQRELAEAEAQARASEERV 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
709-1228 |
6.45e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 6.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 709 EQAFEAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERidwtKQQEELLSQLNVLEKQLQE 788
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL----AELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 789 TQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKefnKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYD 868
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE---AEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 869 NLQEIMKFE--IDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKV--LEAVRQEKQK 944
Cdd:COG1196 391 ALRAAAELAaqLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEeaLLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 945 ETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQE----------LKD 1014
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEaaleaalaaaLQN 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1015 INCKYNSALVDREESRVLIKKQEVDILDLKETLRLRILSEDIERDMLCEDLA------------------------HATE 1070
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDlvasdlreadaryyvlgdtllgrtLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1071 QLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEynfkMRQLEHVMDSAAEDpqspktpphfQT 1150
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE----LEELAERLAEEELE----------LE 696
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74752937 1151 HLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEKNW-LLQGQLDDIKRQ 1228
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLeELERELERLERE 775
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
714-1329 |
7.50e-08 |
|
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: 57.11 E-value: 7.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 714 AISEELRTVQEQMSALQAKLDEEEHKNlklqqhvdklehHSTQMQELfsseRIDWTKQQEELLSQLNVLEKQLQETQTKN 793
Cdd:pfam01576 316 AAQQELRSKREQEVTELKKALEEETRS------------HEAQLQEM----RQKHTQALEELTEQLEQAKRNKANLEKAK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 794 DFLKSEVHDLRVVLhsadKELSSVKLEYSSFKTNQEKEFNKLSERHMhvqlqlDNLRLENEkLLESKACLQDSYDNLQEI 873
Cdd:pfam01576 380 QALESENAELQAEL----RTLQQAKQDSEHKRKKLEGQLQELQARLS------ESERQRAE-LAEKLSKLQSELESVSSL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 874 MkfeiDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFE--EDKENSSKEILKVLEAVRQEKQKETAKCEQ 951
Cdd:pfam01576 449 L----NEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRqlEDERNSLQEQLEEEEEAKRNVERQLSTLQA 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 952 QMAKVQKLEESLLATekvISSLEKSRDSDKKVVADLMNQIQElRTSVCEKTE-TIDTLKQELKDInckynsaLVDREESR 1030
Cdd:pfam01576 525 QLSDMKKKLEEDAGT---LEALEEGKKRLQRELEALTQQLEE-KAAAYDKLEkTKNRLQQELDDL-------LVDLDHQR 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1031 VLI----KKQ---------EVDILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKE 1097
Cdd:pfam01576 594 QLVsnleKKQkkfdqmlaeEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1098 ALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMdSAAEDP--------QSPKTpphfqTHLAKLLETQEQEIEDGRAS 1169
Cdd:pfam01576 674 DDVGKNVHELERSKRALEQQVEEMKTQLEELEDEL-QATEDAklrlevnmQALKA-----QFERDLQARDEQGEEKRRQL 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1170 KTSLEHLVTKLNEDREVKnAEILRMKEQLrEMENLRLESQ---------QLIEKNWLLQGQLDDIKRQKEnsdqnhpDNQ 1240
Cdd:pfam01576 748 VKQVRELEAELEDERKQR-AQAVAAKKKL-ELDLKELEAQidaankgreEAVKQLKKLQAQMKDLQRELE-------EAR 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1241 QLKNEQEESIKERLAKSKIVE-EMLKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEER 1319
Cdd:pfam01576 819 ASRDEILAQSKESEKKLKNLEaELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEEL 898
|
650
....*....|
gi 74752937 1320 ERTSQEMEML 1329
Cdd:pfam01576 899 EEEQSNTELL 908
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
724-1332 |
8.99e-08 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 56.75 E-value: 8.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 724 EQMSALQAKLDEEEHKNLKLQQHVDKLEhhsTQMQELFSSERIDWTKQQEELlsqlnvleKQLQETQTKNDFLKSEVHDL 803
Cdd:pfam10174 226 AKTKALQTVIEMKDTKISSLERNIRDLE---DEVQMLKTNGLLHTEDREEEI--------KQMEVYKSHSKFMKNKIDQL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 804 rvvlhsaDKELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQLDNLRLENEKllesKACLQDSYDNLQ---EIMKFEIDQ 880
Cdd:pfam10174 295 -------KQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQR----AAILQTEVDALRlrlEEKESFLNK 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 881 LSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAkVQKLE 960
Cdd:pfam10174 364 KTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTA-LTTLE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 961 ESLLATEKVISSLEKSRDSDKKvvadlmnqiqelrtsvcEKTETIDTLKQELKDINCKYNSALVDREEsrvlikkQEVDI 1040
Cdd:pfam10174 443 EALSEKERIIERLKEQREREDR-----------------ERLEELESLKKENKDLKEKVSALQPELTE-------KESSL 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1041 LDLKEtlrlrilsedierdmlcedlaHATeqlNMLTEASKKHSGLLQSAQEELTKKEALIQ-ELQHKLNQKKEEVEQKKN 1119
Cdd:pfam10174 499 IDLKE---------------------HAS---SLASSGLKKDSKLKSLEIAVEQKKEECSKlENQLKKAHNAEEAVRTNP 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1120 EYNFKMRQLEHVMDSAAEDpqSPKTpphfQTHLAKLLET-QEQEIEdgrasktslehlvtKLNEDREVKNAEIL---RMK 1195
Cdd:pfam10174 555 EINDRIRLLEQEVARYKEE--SGKA----QAEVERLLGIlREVENE--------------KNDKDKKIAELESLtlrQMK 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1196 EQLREMENLRLESQQLIEKNwllQGQLDDIKRQKENSDQNHpdnqqlKNEQEESIKERLAKSKivEEMLKMKADLEEVQS 1275
Cdd:pfam10174 615 EQNKKVANIKHGQQEMKKKG---AQLLEEARRREDNLADNS------QQLQLEELMGALEKTR--QELDATKARLSSTQQ 683
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74752937 1276 ALYNKE--MECLRMTDEVERTQTLESK------AFQEKEQLRSKLEEMYEERERTSQEMEMLRKQ 1332
Cdd:pfam10174 684 SLAEKDghLTNLRAERRKQLEEILEMKqeallaAISEKDANIALLELSSSKKKKTQEEVMALKRE 748
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
828-1327 |
9.58e-08 |
|
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: 56.72 E-value: 9.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 828 QEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEIMKfEIDQLSRNLQNFKKENETLksdLNNLMELLE 907
Cdd:pfam01576 10 KEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCA-EAEEMRARLAARKQELEEI---LHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 908 AEKERNNKLSLQFEEDKENSS--KEILKVLEAVRQEKQKETAKCEqqmAKVQKLEESLLATEKVISSLEKSRDSDKKVVA 985
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQdlEEQLDEEEAARQKLQLEKVTTE---AKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 986 DLMNQIQELRtsvcEKTETIDTLKQelkdincKYNSALVDREESRvliKKQEVDILDLkETLRLRILSEDIE-RDMLCED 1064
Cdd:pfam01576 163 EFTSNLAEEE----EKAKSLSKLKN-------KHEAMISDLEERL---KKEEKGRQEL-EKAKRKLEGESTDlQEQIAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1065 LAHATEQLNMLTEASKKHSGLLQSAQEELTKKEAL---IQELQHKLNQKKEEVEQKKNEYNFKMRQ-------------- 1127
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLEEETAQKNNAlkkIRELEAQISELQEDLESERAARNKAEKQrrdlgeelealkte 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1128 LEHVMDSAAEDPQSPKTPPHFQTHLAKLLEtqeqeiEDGRASKTSLEHLvtklnedREVKNAEILRMKEQL----REMEN 1203
Cdd:pfam01576 308 LEDTLDTTAAQQELRSKREQEVTELKKALE------EETRSHEAQLQEM-------RQKHTQALEELTEQLeqakRNKAN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1204 LRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPD-NQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEM 1282
Cdd:pfam01576 375 LEKAKQALESENAELQAELRTLQQAKQDSEHKRKKlEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEG 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 74752937 1283 ECLRMTDEV-------ERTQTLESKAFQEKEQLRSKLEEMYEERERTSQEME 1327
Cdd:pfam01576 455 KNIKLSKDVsslesqlQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLE 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
713-1340 |
1.98e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.84 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 713 EAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHH---STQMQE----LFSSERIDWTKQQEELLSQLNVLEKQ 785
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYqalLKEKREyegyELLKEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 786 LQETQTKNDFLKSEVHDLRVVLHSADKELS---------------SVKLEYSSFKTNQ---EKEFNKLSERHMHVQLQLD 847
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELNKKIKdlgeeeqlrvkekigELEAEIASLERSIaekERELEDAEERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 848 NLRLENEKLLES-------KACLQDSYDNLQEIMKF------EIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNN 914
Cdd:TIGR02169 333 KLLAEIEELEREieeerkrRDKLTEEYAELKEELEDlraeleEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 915 KLSLQFEEDKENSSKEI------LKVLEAVRQEKQKETAKCEQQM----AKVQKLEESLLATEKVISSLEKSRDSDKKVV 984
Cdd:TIGR02169 413 EELQRLSEELADLNAAIagieakINELEEEKEDKALEIKKQEWKLeqlaADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 985 ADLMNQIQELRTSVCEKTETIDTLKQ----------ELKDINCKYNSAL------------------------------- 1023
Cdd:TIGR02169 493 AEAEAQARASEERVRGGRAVEEVLKAsiqgvhgtvaQLGSVGERYATAIevaagnrlnnvvveddavakeaiellkrrka 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1024 ------------VDREESRVLIKKQEVDI-LDLKE-----------TLRLRILSEDIE--RDMLCE-------------- 1063
Cdd:TIGR02169 573 gratflplnkmrDERRDLSILSEDGVIGFaVDLVEfdpkyepafkyVFGDTLVVEDIEaaRRLMGKyrmvtlegelfeks 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1064 ---------------DLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQL 1128
Cdd:TIGR02169 653 gamtggsraprggilFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEE 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1129 EHVMDSAAEdpqspktpphfqthLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLRE--MENLRL 1206
Cdd:TIGR02169 733 EKLKERLEE--------------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsrIPEIQA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1207 ESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQQLKNEQEESIKE-RLAKSKIVEEMLKMKADLEEVQSALYNKEMECL 1285
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDlKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 74752937 1286 RMTDEVERTQTLESKAFQEKEQLRSKLEEMYEERERTSQEMEMLRKQVECLAEEN 1340
Cdd:TIGR02169 879 DLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
863-1374 |
2.31e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 863 LQDSYDNLQEIMKfEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLS---LQFEEDKENSSKEiLKVLEAVR 939
Cdd:PRK03918 160 YENAYKNLGEVIK-EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISselPELREELEKLEKE-VKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 940 Q---EKQKETAKCEQQMAKvqkLEESLLATEKVISSLEKSRDSDKKVVADLmNQIQELRTSVCEKTETIDTLKQELKDIN 1016
Cdd:PRK03918 238 EeieELEKELESLEGSKRK---LEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1017 CKYNSALVDREESRVLIKKQEVDILDLKETLR-----LRILSEDIERDMLCEDLAHATEQLNML-TEASKKHSGLLQSAQ 1090
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKklkelEKRLEELEERHELYEEAKAKKEELERLkKRLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1091 EELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEhvmdsAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASK 1170
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK-----KAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1171 TSLEHLVTKL-NEDREVKNA-----EILRMKEQLREMENLRLESQQL----IEKNW----LLQGQLDDIKRQKENSDQNH 1236
Cdd:PRK03918 469 KEIEEKERKLrKELRELEKVlkkesELIKLKELAEQLKELEEKLKKYnleeLEKKAeeyeKLKEKLIKLKGEIKSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1237 PDNQQLKNEQEE------SIKERLAK--SKIVEEMLKMKADLEEVQSAL---YNKEMECLRMTDEVERTQtleskafQEK 1305
Cdd:PRK03918 549 EKLEELKKKLAElekkldELEEELAEllKELEELGFESVEELEERLKELepfYNEYLELKDAEKELEREE-------KEL 621
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74752937 1306 EQLRSKLEEMYEERERTSQEMEMLRKQVeclaEENGKLVGHQNLHQKIQYVVRLKKENVRLAEETEKLR 1374
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKEL----EELEKKYSEEEYEELREEYLELSRELAGLRAELEELE 686
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
952-1185 |
2.77e-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: 54.38 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 952 QMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRV 1031
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1032 LIKKQEvdiLDLKETLRLRILSEDIERDML------CEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQH 1105
Cdd:COG4942 98 ELEAQK---EELAELLRALYRLGRQPPLALllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1106 KLNQKKEEVEQKKNEYNFKMRQLEHVMDSaaedpqspktpphfqthLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDRE 1185
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLAR-----------------LEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1044-1258 |
5.35e-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: 53.61 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1044 KETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNF 1123
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1124 KMRQLEHVMDSAAED----PQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLR 1199
Cdd:COG4942 109 LLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 74752937 1200 EMENLRLESQQLIEKnwlLQGQLDDIKRQKENSDQNHPDNQQLKNEQEESIKERLAKSK 1258
Cdd:COG4942 189 ALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1086-1387 |
6.63e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1086 LQSAQEELTKKEALIQELQHKLNQKKEEVEQ--KKNEYNFKMRQLEHVMDSAAEDpqspktpphfqtHLAKLLETQEQEI 1163
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERQAEKaeRYRELKEELKELEAELLLLKLR------------ELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1164 EDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREM-ENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQQL 1242
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1243 KNE----QEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEE 1318
Cdd:COG1196 329 EEEleelEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74752937 1319 RERTSQEMEMLRKQVECLAEENGKLVghQNLHQKIQYVVRLKKENVRLAEETEKLRAENVFLKEKKRSE 1387
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELE--EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
423-1321 |
7.89e-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: 53.82 E-value: 7.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 423 LFFKKSEQEKKSLIEKVTQLEDLTLKKEKFIQSNKMIVKfREDQIIRLEKLHKESRGGFLPEEQDRLLSELRNEIQTLRE 502
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKE-QAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 503 QIEhhprvAKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQ-----QGFSPKAQKEPCL 577
Cdd:pfam02463 245 LLR-----DEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSEllkleRRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 578 FANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKACKRQEVSQLNKIHAETLK 657
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 658 IittptkayqlhSRPVPKLSPEMGSFGSLYTQNSSILDNDILNEPVPPEMNEQAFEAISEELRTVQEQMSALQAKLDEEE 737
Cdd:pfam02463 400 K-----------SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELK 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 738 HKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQE--ELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELS 815
Cdd:pfam02463 469 KSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKarSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTA 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 816 SVKLEYSSFKTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEIMKFEIDQLSRNLQNFKKENEtL 895
Cdd:pfam02463 549 VIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVE-G 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 896 KSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEK 975
Cdd:pfam02463 628 ILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQR 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 976 SRDSDKKVVADLMNQIQELRTSVCEK-TETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLRIlsE 1054
Cdd:pfam02463 708 EKEELKKLKLEAEELLADRVQEAQDKiNEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE--K 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1055 DIERDMLCEDLAHATEQLNMLTEAsKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMrqlehvmds 1134
Cdd:pfam02463 786 LKVEEEKEEKLKAQEEELRALEEE-LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEE--------- 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1135 aaedpqspktpphfqthlaKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEiLRMKEQLREMENLRLESQQLIEK 1214
Cdd:pfam02463 856 -------------------LERLEEEITKEELLQELLLKEEELEEQKLKDELESKE-EKEKEEKKELEEESQKLNLLEEK 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1215 NwllqgQLDDIKRQKENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERT 1294
Cdd:pfam02463 916 E-----NEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERY 990
|
890 900
....*....|....*....|....*..
gi 74752937 1295 QTLESKaFQEKEQLRSKLEEMYEERER 1321
Cdd:pfam02463 991 NKDELE-KERLEEEKKKLIRAIIEETC 1016
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
713-1277 |
1.70e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 52.60 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 713 EAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERIdwtkqqeeLLSQLNVLEKQLQETQTK 792
Cdd:PRK01156 162 NSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSI--------TLKEIERLSIEYNNAMDD 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 793 NDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEK--EFNKLSERHMhvqlqldnlRLENEKLLESKACLQDSYD-- 868
Cdd:PRK01156 234 YNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKnnYYKELEERHM---------KIINDPVYKNRNYINDYFKyk 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 869 ----NLQEIMKFEIDQLSRNLQNFKK------------ENETLKSDLNNLMELLEAEKERNNKLSLQFEEDK---ENSSK 929
Cdd:PRK01156 305 ndieNKKQILSNIDAEINKYHAIIKKlsvlqkdyndyiKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKkkiEEYSK 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 930 EILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQEL----RTSVCEKTETI 1005
Cdd:PRK01156 385 NIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsVCPVCGTTLGE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1006 DTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRlRILSEDIER----DMLCEDLAHATE----QLNMLTE 1077
Cdd:PRK01156 465 EKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE-YLESEEINKsineYNKIESARADLEdikiKINELKD 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1078 ASKK-----------HSGLLQSAQEELTKKEALIQELQHKLNQK-KEEVEQKKNEYNFKMRQLEhvmdSAAEDPQS--PK 1143
Cdd:PRK01156 544 KHDKyeeiknrykslKLEDLDSKRTSWLNALAVISLIDIETNRSrSNEIKKQLNDLESRLQEIE----IGFPDDKSyiDK 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1144 TPPHFQTHlAKLLETQEQEIEDGRASKTSLEHLVTKLNEdrevknaEILRMKEQLREMENLRLESQQLIEKNWLLQGQLD 1223
Cdd:PRK01156 620 SIREIENE-ANNLNNKYNEIQENKILIEKLRGKIDNYKK-------QIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD 691
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 74752937 1224 DIKRQKENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSAL 1277
Cdd:PRK01156 692 DAKANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAF 745
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
849-1370 |
1.90e-06 |
|
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: 52.42 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 849 LRLENEKLLESKACLQDSYDNLQEiMKFEIDQLSRNLQ-------NFKKENETLKSDLNNLMELLEAEKERNNKLSLQFE 921
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQE-LQFENEKVSLKLEeeiqenkDLIKENNATRHLCNLLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 922 E------DKENSSKEILKVLEAVRQEKQKETA----KCEQQMAKVQKLEES----LLATEKVISSLEKSRDSDKKVVADL 987
Cdd:pfam05483 180 EtrqvymDLNNNIEKMILAFEELRVQAENARLemhfKLKEDHEKIQHLEEEykkeINDKEKQVSLLLIQITEKENKMKDL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 988 MNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLRI-----LSEDIERDMLC 1062
Cdd:pfam05483 260 TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticqLTEEKEAQMEE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1063 EDLAHATEQL--NMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQ 1140
Cdd:pfam05483 340 LNKAKAAHSFvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEK 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1141 SPKTPPHF----------QTHLAKLLETQEQEIEDgrasktsLEHLVTKLNEDREVKNAEILRMKEqlrEMENLRLESQQ 1210
Cdd:pfam05483 420 LLDEKKQFekiaeelkgkEQELIFLLQAREKEIHD-------LEIQLTAIKTSEEHYLKEVEDLKT---ELEKEKLKNIE 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1211 LIEKNWLLqgQLDDIKRQKENSDQnhpdNQQLKNEQEESIKERlaksKIVEEMLKMKADLEEVQSALYNkEMECLRmtde 1290
Cdd:pfam05483 490 LTAHCDKL--LLENKELTQEASDM----TLELKKHQEDIINCK----KQEERMLKQIENLEEKEMNLRD-ELESVR---- 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1291 vertqtleSKAFQEKEQLRSKLEEmyEERERTSQEMEMLRKQVECLAEENGKLVGHQNLHQKIQYVVRLKKENVRLAEET 1370
Cdd:pfam05483 555 --------EEFIQKGDEVKCKLDK--SEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKG 624
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
877-1298 |
2.32e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 52.38 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 877 EIDQLSRNLQNFKKENETLKSDLNnlmellEAEKERNNKLSLQfeEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKV 956
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELR------RIENRLDELSQEL--SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 957 QKLEESLLATEKvissleksrdsdkkvvadlmnQIQELRTSVCEKTETIDTLKQELKDINCKYNsalvdreESRVLIKKQ 1036
Cdd:TIGR02169 747 SSLEQEIENVKS---------------------ELKELEARIEELEEDLHKLEEALNDLEARLS-------HSRIPEIQA 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1037 EVDILDlKETLRLRILSEDIERDMlcedlaHATEQLNMLTEASKKHsglLQSAQEELTKKEALIQELQHKLNQKKEEVEQ 1116
Cdd:TIGR02169 799 ELSKLE-EEVSRIEARLREIEQKL------NRLTLEKEYLEKEIQE---LQEQRIDLKEQIKSIEKEIENLNGKKEELEE 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1117 KKNEYNFKMRQLEhvmdsaaedpqspktpphfqthlaKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKE 1196
Cdd:TIGR02169 869 ELEELEAALRDLE------------------------SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKA 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1197 QLREMEnlrlesQQLIEknwllqgqLDDIKRQKENSDQNHPDNQQLKNEQEEsIKERLAKSkiveEMLKMKA--DLEEVQ 1274
Cdd:TIGR02169 925 KLEALE------EELSE--------IEDPKGEDEEIPEEELSLEDVQAELQR-VEEEIRAL----EPVNMLAiqEYEEVL 985
|
410 420
....*....|....*....|....
gi 74752937 1275 SALynKEMECLRMTDEVERTQTLE 1298
Cdd:TIGR02169 986 KRL--DELKEKRAKLEEERKAILE 1007
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
713-1120 |
2.72e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.13 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 713 EAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHHST---QMQELFSSERIDWTKQQEELLSQLNVLEKQLQET 789
Cdd:pfam10174 292 DQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTakeQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 790 QTKNDFLKSEVHDLRVVLHSADKELSSVkleyssfktnqEKEFNKLSERHMHVQLQLDNLRlENEKLLESKACLQDS--- 866
Cdd:pfam10174 372 TEEKSTLAGEIRDLKDMLDVKERKINVL-----------QKKIENLQEQLRDKDKQLAGLK-ERVKSLQTDSSNTDTalt 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 867 ------------YDNLQEIMKFEIDQLSRNLQNFKKENETLKSDLNNLM-ELLEAEkerNNKLSLQFEEDKENSS----K 929
Cdd:pfam10174 440 tleealsekeriIERLKEQREREDRERLEELESLKKENKDLKEKVSALQpELTEKE---SSLIDLKEHASSLASSglkkD 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 930 EILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKV---ISSLEKS----RDSDKKVVAD---LMNQIQELRTSVC 999
Cdd:pfam10174 517 SKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEIndrIRLLEQEvaryKEESGKAQAEverLLGILREVENEKN 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1000 EKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDlkETLRLRILSEDIERDMLCEDLAHATEQLNMLTEAS 1079
Cdd:pfam10174 597 DKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLE--EARRREDNLADNSQQLQLEELMGALEKTRQELDAT 674
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 74752937 1080 KKHsglLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNE 1120
Cdd:pfam10174 675 KAR---LSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQE 712
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
932-1369 |
3.00e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 932 LKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVA--DLMNQIQELRTSVCEKTETIDTLK 1009
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1010 QELKDinckYNSALVDREESRVLIKKQEVDILDLKETLRLRILsedierdmlcEDLAHATEQLNMLTEASKKHSGLLQSA 1089
Cdd:COG4717 153 ERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATE----------EELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1090 QEELTKKEALIQELQHKLNQKKEEveQKKNEYNFKMRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRAS 1169
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALE--ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1170 KTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEKNWL-------LQGQLDDIKRQKENSDQNHPDNQQL 1242
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDrieelqeLLREAEELEEELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1243 KNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMEclrmtdevertqTLESKAFQEKEQLRSKLEEMYEERERT 1322
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGE------------LEELLEALDEEELEEELEELEEELEEL 444
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 74752937 1323 SQEMEMLRKQVECLAEENGKLVGHQNLHQKIQYVVRLKKENVRLAEE 1369
Cdd:COG4717 445 EEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
872-1339 |
3.35e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 872 EIMKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQ 951
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 952 QMA-KVQKLEESLLATEKVISSLEKSRDSDK-KVVADLMNQIQELRTSVCE--KTETIDTLKQELKDINCKYNSALVDRE 1027
Cdd:PTZ00121 1405 KKAdELKKAAAAKKKADEAKKKAEEKKKADEaKKKAEEAKKADEAKKKAEEakKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1028 ESRVLIKKQEVDildlKETLRLRILSEDIERdmlCEDLAHATE--QLNMLTEASKKHSGLLQSAQEELTKKEALIQELQH 1105
Cdd:PTZ00121 1485 ADEAKKKAEEAK----KKADEAKKAAEAKKK---ADEAKKAEEakKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1106 KLNQKKEEVEQKKNE---YNFKMRQLEhVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNE 1182
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAeedKNMALRKAE-EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1183 DREVKNAEILRMKEQLR-EMENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHpdnQQLKNEQEESIKERLAKSKIVE 1261
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA---EALKKEAEEAKKAEELKKKEAE 1713
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74752937 1262 EmlKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESKafqEKEQLRSKLEEMYEERERTSQEmemLRKQVECLAEE 1339
Cdd:PTZ00121 1714 E--KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK---KDEEEKKKIAHLKKEEEKKAEE---IRKEKEAVIEE 1783
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
773-1349 |
9.97e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 773 EELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYssfktnqeKEFNKLSERhmhvqlqLDNLRLE 852
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV--------KELEELKEE-------IEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 853 NEKLLESKACLQDsydnlqeimkfEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKE--RNNKLSLQFEEDKENSSKE 930
Cdd:PRK03918 247 LESLEGSKRKLEE-----------KIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 931 iLKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVAdLMNQIQELRTSvcEKTETIDTLKQ 1010
Cdd:PRK03918 316 -LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA-KKEELERLKKR--LTGLTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1011 ELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRL------------RILSEDIERDMLCE----------DLAHA 1068
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgRELTEEHRKELLEEytaelkriekELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1069 TEQLNMLTEASKKHSGLLQSAQEELTKKEAL--IQELQHKLNQ-KKEEVEQKKNEY---NFKMRQLEHVMDSAAEDPQSP 1142
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKELAeqLKELEEKLKKyNLEELEKKAEEYeklKEKLIKLKGEIKSLKKELEKL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1143 KTpphfqthLAKLLETQEQEIEDGRASKTSLEHlvtklnEDREVKNAEILRMKEQLREMENLRLESQQLIEKNWLLQGQL 1222
Cdd:PRK03918 552 EE-------LKKKLAELEKKLDELEEELAELLK------ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREE 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1223 DDIKRQKENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEmlkmkADLEEVQSALYNKEMECLRMTDEVERtqtLESKAF 1302
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE-----EEYEELREEYLELSRELAGLRAELEE---LEKRRE 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 74752937 1303 QEKEQLRsKLEEMYEERERTSQEMEMLRKQVECLAEENGKLVGHQNL 1349
Cdd:PRK03918 691 EIKKTLE-KLKEELEEREKAKKELEKLEKALERVEELREKVKKYKAL 736
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
704-1120 |
1.19e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 704 PPEMNEQAFEAISEELRTVQEQMSALQAKLDEEEhknlKLQQHVDKLEHHSTQMQElfSSERIDWTKQQEELLSQLNVLE 783
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELRE--ELEKLEKLLQLLPLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 784 KQLQETQTKNDFLKSEVHDLRvvlhsadkelssvkleyssfktNQEKEFNKLSERHMHVQLQLDnlRLENEKLLESKACL 863
Cdd:COG4717 139 AELAELPERLEELEERLEELR----------------------ELEEELEELEAELAELQEELE--ELLEQLSLATEEEL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 864 QDSYDNLQEIMKfEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNK-------------LSLQFEEDKENSSKE 930
Cdd:COG4717 195 QDLAEELEELQQ-RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLkearlllliaaalLALLGLGGSLLSLIL 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 931 --------ILKVLEAVRQEKQKETAKCEQQMAKVQKLEE----SLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSV 998
Cdd:COG4717 274 tiagvlflVLGLLALLFLLLAREKASLGKEAEELQALPAleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 999 CEKTETIDTLKQE--LKDINCKYNSALVDREESRVLIKKQEVDILDLKETL-----RLRILSEDIERDMLCEDLAHATEQ 1071
Cdd:COG4717 354 REAEELEEELQLEelEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELeeleeQLEELLGELEELLEALDEEELEEE 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 74752937 1072 LNMLTEASKKHSGLLQSAQEELTKKEALIQEL--QHKLNQKKEEVEQKKNE 1120
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQLeeDGELAELLQELEELKAE 484
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
879-1385 |
1.23e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 879 DQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAvrQEKQKETAKCEQQMAKVQK 958
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA--KKKADAAKKKAEEKKKADE 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 959 LEESLLATEKVISSLEKSRDSDKKVvadlmnqiQELRTSVCEKTETiDTLKQELKDINcKYNSALVDREESRvlikKQEV 1038
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKA--------DEAKKKAEEKKKA-DEAKKKAEEAK-KADEAKKKAEEAK----KAEE 1461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1039 DILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKK 1118
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK 1541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1119 NEYNFK---MRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMK 1195
Cdd:PTZ00121 1542 AEEKKKadeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1196 -EQLREMENLRLESQQLIEKNWLLQGQLDDIKRQKEnsdQNHPDNQQLKNEQEESIKErlakskiVEEMLKMKADLEEVQ 1274
Cdd:PTZ00121 1622 aEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE---ENKIKAAEEAKKAEEDKKK-------AEEAKKAEEDEKKAA 1691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1275 SALYNKEMEclrmTDEVERTQTLESKAFQEKEQLRSKleemYEERERTSQEMEMLRKQVECLAEENGKLVGHQNLHQKIQ 1354
Cdd:PTZ00121 1692 EALKKEAEE----AKKAEELKKKEAEEKKKAEELKKA----EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK 1763
|
490 500 510
....*....|....*....|....*....|.
gi 74752937 1355 YVVRLKKENVRlaEETEKLRAENVFLKEKKR 1385
Cdd:PTZ00121 1764 KEEEKKAEEIR--KEKEAVIEEELDEEDEKR 1792
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
579-922 |
1.45e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 579 ANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENL------LEATKACKRQEVSQLNKIH 652
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLeaeveqLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 653 AETLKIITTPTKAYQLHSRPVPKLSPEMGSFGSLYTQNSSILD--NDILNEpvppeMNEQAFEAiSEELRTVQEQMSALQ 730
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelRAELTL-----LNEEAANL-RERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 731 AKLDEEEHKNLKLQQHVDKLEHHSTQMQEL---FSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVL 807
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELieeLESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 808 HSADKELSSVKLEYSSFKTNQEKEFNKLSERHmhvqlqldnlRLENEKLLESKACLQDSYDNLQEimkfEIDQLSRNLQN 887
Cdd:TIGR02168 918 EELREKLAQLELRLEGLEVRIDNLQERLSEEY----------SLTLEEAEALENKIEDDEEEARR----RLKRLENKIKE 983
|
330 340 350
....*....|....*....|....*....|....*
gi 74752937 888 FKKENETlksdlnnLMELLEAEKERNNKLSLQFEE 922
Cdd:TIGR02168 984 LGPVNLA-------AIEEYEELKERYDFLTAQKED 1011
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
406-987 |
1.83e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.69 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 406 TRDKKKTNYMEYFQEAMLFFKKSEQEKKSLIEKVTQLEDLTLKKEKFI-------QSNKMI-VKFREDQIIRLEKLHKES 477
Cdd:COG5022 861 FSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIielkkslSSDLIEnLEFKTELIARLKKLLNNI 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 478 RGGFLPE---EQDRLLSELRNEIQTLREQIEHHPRVAKYA-------------MENH-----SLREENRRLRllEPVKRA 536
Cdd:COG5022 941 DLEEGPSieyVKLPELNKLHEVESKLKETSEEYEDLLKKStilvregnkanseLKNFkkelaELSKQYGALQ--ESTKQL 1018
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 537 QEMDAQtIAKLEKAFSEISGMEKSDKNQQGFS-PKAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYE----EFKELTRK 611
Cdd:COG5022 1019 KELPVE-VAELQSASKIISSESTELSILKPLQkLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQlestENLLKTIN 1097
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 612 RQLELESELQSLQKANLNLENLLEATKACKRQEVSQLNKIHAETLKIITTPTKAYQL---HSRPVPKLSPEMGSFGSLYT 688
Cdd:COG5022 1098 VKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLeldGLFWEANLEALPSPPPFAAL 1177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 689 QNSSILDNDILNEPvppemneqaFEAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQEL--FSSERI 766
Cdd:COG5022 1178 SEKRLYQSALYDEK---------SKLSSSEVNDLKNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLkgFNNLNK 1248
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 767 DWTKQQ----EELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERHMHV 842
Cdd:COG5022 1249 KFDTPAsmsnEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFNALRTKASSLRWKSATEVNYNSEELDDWCR 1328
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 843 QLQLDNLRLENEKLLESKACLQDSYDNLQEIMkfEIDQLSRNLQNFkkENETLKSDLNNLMELLEAEKERNNKLSLQFEE 922
Cdd:COG5022 1329 EFEISDVDEELEELIQAVKVLQLLKDDLNKLD--ELLDACYSLNPA--EIQNLKSRYDPADKENNLPKEILKKIEALLIK 1404
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74752937 923 DKENSSKEILKVLEAVRQEKQKETakceqqmAKVQKLEESLLATEKVISSLEKsrDSDKKVVADL 987
Cdd:COG5022 1405 QELQLSLEGKDETEVHLSEIFSEE-------KSLISLDRNSIYKEEVLSSLSA--LLTKEKIALL 1460
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
706-1342 |
1.87e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 706 EMNEQAFEAISEELRTVQEQMSALQAKLDEEEHKNLKLQ---QHVDKLEHHSTQMQElfSSERIDWTKQQEELLSQLNVL 782
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKkkaEEKKKADEAKKKAEE--DKKKADELKKAAAAKKKADEA 1423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 783 EKQLQETQtKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERHMhvqlqldnlrlENEKLLESKAC 862
Cdd:PTZ00121 1424 KKKAEEKK-KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE-----------EAKKADEAKKK 1491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 863 LQDSYDNLQEIMKFEidQLSRNLQNFKKENETLKSDlnnlmELLEAEKERNNKLSLQFEEDK---ENSSKEILKVLEAVR 939
Cdd:PTZ00121 1492 AEEAKKKADEAKKAA--EAKKKADEAKKAEEAKKAD-----EAKKAEEAKKADEAKKAEEKKkadELKKAEELKKAEEKK 1564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 940 QEKQKETAKCEQQMAkVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTsvceKTETIDTLKQELKDINCKY 1019
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMA-LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKI----KAEELKKAEEEKKKVEQLK 1639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1020 NSALVDREESRVLIKKQEVDILDLKETLRlrilsEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAqEELTKKEAl 1099
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAK-----KAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKA-EELKKKEA- 1712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1100 iqelqhKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLehlvtk 1179
Cdd:PTZ00121 1713 ------EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV------ 1780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1180 lnEDREVKNAEILRMKEQLREMENLRLESQQLIEKNWLLQGQLDDIKRQ----------KENSDQNHPD--NQQLKNEQE 1247
Cdd:PTZ00121 1781 --IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMedsaikevadSKNMQLEEADafEKHKFNKNN 1858
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1248 ESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMEclrmTDEVERTQTLESKAFQEKEQLRSKLE-EMYEER--ERTSQ 1324
Cdd:PTZ00121 1859 ENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKID----KDDIEREIPNNNMAGKNNDIIDDKLDkDEYIKRdaEETRE 1934
|
650
....*....|....*...
gi 74752937 1325 EMEMLRKQVECLAEENGK 1342
Cdd:PTZ00121 1935 EIIKISKKDMCINDFSSK 1952
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
378-1060 |
2.08e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 49.37 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 378 SQLQAEVKRLKEQLAELASGQTPPESFLTRDKKKTNYMEYFQEAMlffKKSEQEKKSLIEKVTQLEDLTLKKEKFIQSNK 457
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA---KKADEAKKKAEEAKKKADAAKKKAEEAKKAAE 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 458 MIVKFREDQIIRLEKLHKESRGGFLPEEQDRLLSElrnEIQTLREQIEHHPRVAKYAMENHSLREENRRLRllEPVKRAQ 537
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD---AAKKKAEEKKKADEAKKKAEEDKKKADELKKAA--AAKKKAD 1421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 538 EMD--AQTIAKLEKAFSEISGMEKSDKNQQGFSPKAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLE 615
Cdd:PTZ00121 1422 EAKkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE 1501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 616 LESELQSLQKANlNLENLLEATKACKRQEVSQLNKihAETLKIITTPTKAYQLHSRPVPKLSPEMGSfgslytqnssild 695
Cdd:PTZ00121 1502 AKKAAEAKKKAD-EAKKAEEAKKADEAKKAEEAKK--ADEAKKAEEKKKADELKKAEELKKAEEKKK------------- 1565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 696 ndiLNEPVPPEMNEQAFEAISEELRTVQEQMSALQAKLDEEEHKNlklqqhvdKLEHHSTQMQELFSSERIdwtKQQEEL 775
Cdd:PTZ00121 1566 ---AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKM--------KAEEAKKAEEAKIKAEEL---KKAEEE 1631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 776 LSQLNVLEKQLQETQTKNDFLKSEvhdlrvvlhsadKELSSVKLEYSSFKTNQEK----EFNKLSERHMHVQLQLDNLRL 851
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKA------------EEENKIKAAEEAKKAEEDKkkaeEAKKAEEDEKKAAEALKKEAE 1699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 852 ENEKLLESKACLQDSYDNLQEIMKFE------IDQLSRNLQNFKKENETLKSDlnnlmellEAEKERNNKLSLQFEEDKE 925
Cdd:PTZ00121 1700 EAKKAEELKKKEAEEKKKAEELKKAEeenkikAEEAKKEAEEDKKKAEEAKKD--------EEEKKKIAHLKKEEEKKAE 1771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 926 NSSKEILKVL-EAVRQEKQKETAKCEQQMAKVQKLEESLLATEK----VISSLEKSRDSDKKVVADLMNqiqelrtSVCE 1000
Cdd:PTZ00121 1772 EIRKEKEAVIeEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKegnlVINDSKEMEDSAIKEVADSKN-------MQLE 1844
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1001 KTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLRilSEDIERDM 1060
Cdd:PTZ00121 1845 EADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKID--KDDIEREI 1902
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
825-1334 |
2.86e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.48 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 825 KTNQEKEFNKLSERHMHV--QLQLDNLRLEN-EKLLESKACLQDSYDNLQEIMKFEIDQLSRNLQNFKKENETLKSDLNN 901
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENkkNIDKFLTEIKKkEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 902 LMELL---EAEKERNNKLSLQFEEdkensSKEILKVLEAVRQEKQKEtakceqqmakVQKLEESLLATEKVISSLEKSRD 978
Cdd:TIGR04523 199 LELLLsnlKKKIQKNKSLESQISE-----LKKQNNQLKDNIEKKQQE----------INEKTTEISNTQTQLNQLKDEQN 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 979 SDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLRILSEdier 1058
Cdd:TIGR04523 264 KIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQ---- 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1059 dmlcedlahATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAED 1138
Cdd:TIGR04523 340 ---------LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1139 PQSPKTPP-------HFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEI-----------LRMKEQLRE 1200
Cdd:TIGR04523 411 DEQIKKLQqekelleKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLkvlsrsinkikQNLEQKQKE 490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1201 MENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQQLKNEQE----------ESIKERLAKSKIVEEMLKMKADL 1270
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKEskisdledelNKDDFELKKENLEKEIDEKNKEI 570
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74752937 1271 EEV---QSALYNKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEERERTSQEMEMLRKQVE 1334
Cdd:TIGR04523 571 EELkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
356-919 |
2.90e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 356 FAQRAKLIKNKAVVNEDTQGNVSQLQAEVKRLKEQLAELASGQTPPESfltRDKKKTNYMEYFQEAMLFFKKSEQEKKSL 435
Cdd:PRK03918 202 LEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELES---LEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 436 IEKVTQLEDLTLKKEKFIQsnkmIVKFREDQIIRLEKLHKEsrggflpeeqdrlLSELRNEIQTLREQIEHHPRVAKYAM 515
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIK----LSEFYEEYLDELREIEKR-------------LSRLEEEINGIEERIKELEEKEERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 516 ENHSLREE-NRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQQGFSPKAQKEPcLFANTEKLKAQLLQIQTE 594
Cdd:PRK03918 342 ELKKKLKElEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE-IEEEISKITARIGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 595 LNNSKQEYEEFKELTRK-----RQLELESELQSLQKANLNLENLLEATKACK------RQEVSQLNKIHAETLKIITTPT 663
Cdd:PRK03918 421 IKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEekerklRKELRELEKVLKKESELIKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 664 KAYQLHSrpvpkLSPEMGSFGSlytqnssildndilnEPVppEMNEQAFEAISEELRTVQEQMSALQAKLDEEEHKNLKL 743
Cdd:PRK03918 501 LAEQLKE-----LEEKLKKYNL---------------EEL--EKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKL 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 744 QQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQLNVLE-------------KQLQETQTKNDFLKSEVHDLRVVLHSA 810
Cdd:PRK03918 559 AELEKKLDELEEELAELLKELEELGFESVEELEERLKELEpfyneylelkdaeKELEREEKELKKLEEELDKAFEELAET 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 811 DKELSSVKLEYSSFKTN-QEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEIMKfeidqlsrNLQNFK 889
Cdd:PRK03918 639 EKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELE--------EREKAK 710
|
570 580 590
....*....|....*....|....*....|
gi 74752937 890 KENETLKSDLNNLMELLEAEKERNNKLSLQ 919
Cdd:PRK03918 711 KELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
770-995 |
3.58e-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: 47.84 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 770 KQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSsfktNQEKEFNKLSERHMHVQLQLDNL 849
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 850 RLENEKLLeSKACLQDSYDNLQEIMKFE-IDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEdkenss 928
Cdd:COG4942 103 KEELAELL-RALYRLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE------ 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74752937 929 keilkvLEAVRQEKQKETAKCEQQMAKVQKLeesllatekvISSLEKSRDSDKKVVADLMNQIQELR 995
Cdd:COG4942 176 ------LEALLAELEEERAALEALKAERQKL----------LARLEKELAELAAELAELQQEAEELE 226
|
|
| HMMR_C |
pfam15908 |
Hyaluronan mediated motility receptor C-terminal; HMMR_C is the C-terminal region of ... |
1270-1376 |
3.73e-05 |
|
Hyaluronan mediated motility receptor C-terminal; HMMR_C is the C-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464934 [Multi-domain] Cd Length: 157 Bit Score: 45.29 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1270 LEEVQSALYNKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGKLVGHQNL 1349
Cdd:pfam15908 4 LEMEEQRKARLENTVDELTEEIKKWRNLYEELYNKTKPFQEQLDAFEAEKNALLNENGAAQEELNKLSDAYAKLLGHQNQ 83
|
90 100
....*....|....*....|....*..
gi 74752937 1350 HQKIQYVVRLKKENVRLAEETEKLRAE 1376
Cdd:pfam15908 84 KQKIKHVVKLKEENTQLKQEVSKLRSQ 110
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
719-1376 |
4.25e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 719 LRTVQEQMSALQAKLDEEEHKNLklqqhVDKLEHHSTQMQELFSS-ERIDWTKQQ-EELLSQLNVLEKQLQETQTKNDFL 796
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDL-----HERLNGLESELAELDEEiERYEEQREQaRETRDEADEVLEEHEERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 797 KSEVHDLRVVLHSADKELSSVKLEYSSfktnQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEimkf 876
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRD----LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD---- 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 877 EIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKeilkvleavRQEKQKE-TAKCEQQMAK 955
Cdd:PRK02224 329 RLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED---------RREEIEElEEEIEELRER 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 956 VQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLK-----QELKDinckynSALVDR-EES 1029
Cdd:PRK02224 400 FGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEG------SPHVETiEED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1030 RVLIKKQEVDILDLKETLRlrILSEDIERdmlCEDLAHATEQLNMLTEASKkhsgllqSAQEELTKKEALIQELQHKLNQ 1109
Cdd:PRK02224 474 RERVEELEAELEDLEEEVE--EVEERLER---AEDLVEAEDRIERLEERRE-------DLEELIAERRETIEEKRERAEE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1110 KKEEVEQkkneynfkmrqLEHVMDSAAEDPQspktpphfqthlaklleTQEQEIEDGRASKTSLEHLVTKLNEDREVKNa 1189
Cdd:PRK02224 542 LRERAAE-----------LEAEAEEKREAAA-----------------EAEEEAEEAREEVAELNSKLAELKERIESLE- 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1190 eilRMKEQLREMENLRlesqqlieknwllqgqlDDIKRQKENSDQnhpdnqqlKNEQEESIKERLAkskiveEMLKMKAD 1269
Cdd:PRK02224 593 ---RIRTLLAAIADAE-----------------DEIERLREKREA--------LAELNDERRERLA------EKRERKRE 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1270 LEEvqsalynkEMECLRMTDEVERTQTLEskafQEKEQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGKLVGHQNL 1349
Cdd:PRK02224 639 LEA--------EFDEARIEEAREDKERAE----EYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENR 706
|
650 660
....*....|....*....|....*...
gi 74752937 1350 HQKIQYVvrlkKENVRLAEET-EKLRAE 1376
Cdd:PRK02224 707 VEALEAL----YDEAEELESMyGDLRAE 730
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
484-1321 |
4.44e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 4.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 484 EEQDRLLSELRNEIQTLREQIEHhprvakyAMENHSLREENRRLRLLEPVKRAQEMDAQtiakLEKAFSEISGMEKSdkn 563
Cdd:TIGR02169 187 ERLDLIIDEKRQQLERLRREREK-------AERYQALLKEKREYEGYELLKEKEALERQ----KEAIERQLASLEEE--- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 564 qqgfspkaqkepclfanTEKLKAQLLQIQTELNNSKQEYEE----FKELTRKRQLELESELQSLQKANLNLENLLEATKA 639
Cdd:TIGR02169 253 -----------------LEKLTEEISELEKRLEEIEQLLEElnkkIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKER 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 640 CKRQEVSQLNKIHAETLKIITTptkayqlhsrpVPKLSPEMGSFGSLYTQNSSILDNDILNEpvppEMNEQAFEAISEEL 719
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAE-----------IEELEREIEEERKRRDKLTEEYAELKEEL----EDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 720 RTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQ--MQELFSSERIDWTKQQ--------EELLSQLNVLEKQLQET 789
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKREINELKRELDRLQEELQRlsEELADLNAAIAGIEAKineleeekEDKALEIKKQEWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 790 QTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQ-------------EKEFNKlSERHMHVQL-QLDNLRLENEK 855
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseervrggravEEVLKA-SIQGVHGTVaQLGSVGERYAT 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 856 LLESKA-------CLQDSYDNLQEIMKFEIDQLSR-------NLQNFKKENETLKSD--LNNLMELLEAEKERNNKLSLQ 919
Cdd:TIGR02169 540 AIEVAAgnrlnnvVVEDDAVAKEAIELLKRRKAGRatflplnKMRDERRDLSILSEDgvIGFAVDLVEFDPKYEPAFKYV 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 920 F---------EEDKENSSKEILKVLEAVRQEK------------------QKETAKCEQQMAKVQKLEESLLATEKVISS 972
Cdd:TIGR02169 620 FgdtlvvediEAARRLMGKYRMVTLEGELFEKsgamtggsraprggilfsRSEPAELQRLRERLEGLKRELSSLQSELRR 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 973 LEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETL-RLRI 1051
Cdd:TIGR02169 700 IENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhKLEE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1052 LSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEhv 1131
Cdd:TIGR02169 780 ALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE-- 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1132 mdsaaedpqspktpphfqtHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREvknaeilRMKEQLREMENLRLESQQL 1211
Cdd:TIGR02169 858 -------------------NLNGKKEELEEELEELEAALRDLESRLGDLKKERD-------ELEAQLRELERKIEELEAQ 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1212 IEKNWLLQGQLddiKRQKENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQS----ALYNKEMECLRM 1287
Cdd:TIGR02169 912 IEKKRKRLSEL---KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPvnmlAIQEYEEVLKRL 988
|
890 900 910
....*....|....*....|....*....|....
gi 74752937 1288 TDEVERTQTLEskafQEKEQLRsKLEEMYEERER 1321
Cdd:TIGR02169 989 DELKEKRAKLE----EERKAIL-ERIEEYEKKKR 1017
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
405-1121 |
4.99e-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: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 405 LTRDKKKTNYMEYFQEAML-------FFKKSEQEKKSLI------EKVTQLEDLTLKKEKFIQSNKMIVKFRedqiIRLE 471
Cdd:TIGR00618 131 VIHDLLKLDYKTFTRVVLLpqgefaqFLKAKSKEKKELLmnlfplDQYTQLALMEFAKKKSLHGKAELLTLR----SQLL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 472 KLHKESRGGFLPEEQDRLLSELRNEIQTLREQIEHHprvAKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAF 551
Cdd:TIGR00618 207 TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH---AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 552 SEISgmeksdknqqgFSPKAQKEPCLFANTEKLKAQLLQIQTELnnskQEYEEFKELTRKRQLELESELQSLQKANLNLE 631
Cdd:TIGR00618 284 ERIN-----------RARKAAPLAAHIKAVTQIEQQAQRIHTEL----QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQ 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 632 NLLEATKACKRQ-EVSQLNKIHAETLKIITTPTKAYQLHSRPVPKLSpemgsfgSLYTQNSSILDNdilnepvppEMNEQ 710
Cdd:TIGR00618 349 TLHSQEIHIRDAhEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKL-------QSLCKELDILQR---------EQATI 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 711 AFEAISEelRTVQEQMSALQAKLDEEEHKNLKLQQHVDKlEHHSTQMQELFSSERIDWTKQQEELLSQLNVLEKQLQETQ 790
Cdd:TIGR00618 413 DTRTSAF--RDLQGQLAHAKKQQELQQRYAELCAAAITC-TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKK 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 791 TkndflkseVHDLRVVLHSadkelssvkleyssfktNQEKEFNKlSERHMHVQLQLDNLRLENEKLLESkacLQDSYDNL 870
Cdd:TIGR00618 490 A--------VVLARLLELQ-----------------EEPCPLCG-SCIHPNPARQDIDNPGPLTRRMQR---GEQTYAQL 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 871 QEIMK---FEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLsLQFEED-----KENSSKEILKVLEAVRQEK 942
Cdd:TIGR00618 541 ETSEEdvyHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL-QNITVRlqdltEKLSEAEDMLACEQHALLR 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 943 QK-------ETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVAD---LMNQIQELRTSVCEKTETIDTLKQEL 1012
Cdd:TIGR00618 620 KLqpeqdlqDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLpkeLLASRQLALQKMQSEKEQLTYWKEML 699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1013 KDINCKYNSALVDREESRVLIKKQEVDILDLKETL--RLRILSEDI-----ERDMLCEDLAHATEQLNMLTEASKKHSGL 1085
Cdd:TIGR00618 700 AQCQTLLRELETHIEEYDREFNEIENASSSLGSDLaaREDALNQSLkelmhQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
730 740 750
....*....|....*....|....*....|....*.
gi 74752937 1086 LQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEY 1121
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD 815
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1087-1388 |
6.36e-05 |
|
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: 47.43 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1087 QSAQEELTKKEALIQELQHKLNQKKEEVEQKKNeynfKMRQLEHVMDS--AAEDPQSPKTPPHFQTHLAKLLETQEQEIE 1164
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKArqAEMDRQAAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1165 DgrasktslehlvtKLNEDREVKNAEILRMKEQLREMENLRLESQQlieKNWLLQGQLDDIKRQKensdqnhpdnqQLKN 1244
Cdd:pfam17380 357 E-------------RKRELERIRQEEIAMEISRMRELERLQMERQQ---KNERVRQELEAARKVK-----------ILEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1245 EQEESIKERLAkskiveEMLKMKADLEEVqsalynKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEERERTSQ 1324
Cdd:pfam17380 410 ERQRKIQQQKV------EMEQIRAEQEEA------RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKL 477
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74752937 1325 EMEMlRKQVECLAEENGKLVGHQNLHQKIQYVvrLKKENVRLAEETEKLRAENVFLKEKKRSES 1388
Cdd:pfam17380 478 ELEK-EKRDRKRAEEQRRKILEKELEERKQAM--IEEERKRKLLEKEMEERQKAIYEEERRREA 538
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
876-1376 |
6.95e-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: 47.66 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 876 FEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQ------------EKQ 943
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQtqqshayltqkrEAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 944 KETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKV---------VADLMNQIQEL-------------------- 994
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAaplaahikaVTQIEQQAQRIhtelqskmrsrakllmkraa 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 995 ----RTSVCEKTETIDTLKQELKDINCKYNSALVDREES------RVLIKKQEVDILDLKETLRL-------------RI 1051
Cdd:TIGR00618 333 hvkqQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIScqqhtlTQHIHTLQQQKTTLTQKLQSlckeldilqreqaTI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1052 LSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKN---EYNFKMRQL 1128
Cdd:TIGR00618 413 DTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlQETRKKAVV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1129 EHVMDSAAEDPQS-PKTPPHFQTHLAKLLETQ---------EQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQL 1198
Cdd:TIGR00618 493 LARLLELQEEPCPlCGSCIHPNPARQDIDNPGpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1199 REMENLRLESQQLIEKnwlLQGQLDDIKRQKENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKadlEEVQSALY 1278
Cdd:TIGR00618 573 SILTQCDNRSKEDIPN---LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS---QELALKLT 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1279 NKEMECLRMTDEVERTQTLESKAFQEK--EQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGKLVGHQNLHQKIQYV 1356
Cdd:TIGR00618 647 ALHALQLTLTQERVREHALSIRVLPKEllASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA 726
|
570 580
....*....|....*....|....*
gi 74752937 1357 VR-----LKKENVRLAEETEKLRAE 1376
Cdd:TIGR00618 727 SSslgsdLAAREDALNQSLKELMHQ 751
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
584-1015 |
1.04e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 46.66 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 584 LKAQLLQIQTELNNSKQEYE------EFKELTRKRQLELESE-LQSLQKANLNLENLlEATKACKRQEVSQLNKIHAETL 656
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKrarielEKKASALKRQLDRESDrNQELQKRIRLLEKR-EAEAEEALREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 657 KIITtptkayqlhsrpvpKLSPEMGSFGSLYTQNSSILDNDILNEPVPPEMNEQAFEAISEELRTVQEQMSALQAKLDEE 736
Cdd:pfam05557 86 EALN--------------KKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 737 EHKNLKLQQHVDKLEHHSTQMQELF---------------SSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVH 801
Cdd:pfam05557 152 EQLRQNLEKQQSSLAEAEQRIKELEfeiqsqeqdseivknSKSELARIPELEKELERLREHNKHLNENIENKLLLKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 802 DLRVVLHSADK---ELSSVKLEYSsfKTNQE-KEFNKLSERH-------MHVQLQLDNLRLENEKLLESKACLQDSYDNL 870
Cdd:pfam05557 232 DLKRKLEREEKyreEAATLELEKE--KLEQElQSWVKLAQDTglnlrspEDLSRRIEQLQQREIVLKEENSSLTSSARQL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 871 QEI---MKFEIDQLSRNLQNFKKENETLKSDLNNLM-ELLEAEKERNNKLSLQFEEDKE----NSSKEILKVLEAVRQEK 942
Cdd:pfam05557 310 EKArreLEQELAQYLKKIEDLNKKLKRHKALVRRLQrRVLLLTKERDGYRAILESYDKEltmsNYSPQLLERIEEAEDMT 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74752937 943 QKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKvvadlmnqiQELRTSVCEKTETIDTLKQELKDI 1015
Cdd:pfam05557 390 QKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQ---------QESLADPSYSKEEVDSLRRKLETL 453
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1080-1388 |
1.12e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1080 KKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQSPKTpphfqthLAKLLETQ 1159
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-------LKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1160 EQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEknwlLQGQLDDIKRQKENSDQNHPDN 1239
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK----LSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1240 QQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESK---------------AFQE 1304
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRltgltpeklekeleeLEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1305 KEQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGK-------LVGHQNLHQKIQY---VVRLKKENVRLAEETEKLR 1374
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEHRKELLEEYtaeLKRIEKELKEIEEKERKLR 479
|
330
....*....|....
gi 74752937 1375 AENVFLKEKKRSES 1388
Cdd:PRK03918 480 KELRELEKVLKKES 493
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
920-1334 |
1.12e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 920 FEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRT--S 997
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 998 VCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTE 1077
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1078 ASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEevEQKKNEYNFKMRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLE 1157
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAAL--EERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1158 TQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEKNWL-------LQGQLDDIKRQKE 1230
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDrieelqeLLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1231 NSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQtLESKAFQEKEQL-- 1308
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE-LEEELEELEEELee 443
|
410 420
....*....|....*....|....*..
gi 74752937 1309 -RSKLEEMYEERERTSQEMEMLRKQVE 1334
Cdd:COG4717 444 lEEELEELREELAELEAELEQLEEDGE 470
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
853-1329 |
1.24e-04 |
|
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: 46.58 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 853 NEKLLESKAcLQDSYDNLQEIMKF--EIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQfeEDKENSSKE 930
Cdd:TIGR00606 162 NWPLSEGKA-LKQKFDEIFSATRYikALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSK--EAQLESSRE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 931 ILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVisslEKSRDSDKKVVADLM-----------NQIQELRTSVC 999
Cdd:TIGR00606 239 IVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR----KKQMEKDNSELELKMekvfqgtdeqlNDLYHNHQRTV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1000 EKTE--------TIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILD---LKETLRLRILSEDIERDMLCE---DL 1065
Cdd:TIGR00606 315 REKErelvdcqrELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArdsLIQSLATRLELDGFERGPFSErqiKN 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1066 AHATEQLNMLTEASKKHSGL------LQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDP 1139
Cdd:TIGR00606 395 FHTLVIERQEDEAKTAAQLCadlqskERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1140 QSPKTPPHFQTHLAKL-----LETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEK 1214
Cdd:TIGR00606 475 ELDQELRKAERELSKAeknslTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1215 NW----LLQGQLDDIKRQKENSDQNHPdnqqlKNEQEESIKERLAKskiveeMLKMKADLEEVQSAlYNKEMECLRmtde 1290
Cdd:TIGR00606 555 KSrhsdELTSLLGYFPNKKQLEDWLHS-----KSKEINQTRDRLAK------LNKELASLEQNKNH-INNELESKE---- 618
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 74752937 1291 vERTQTLESKAFQ--EKEQLRSKLEEMYEERERTSQEMEML 1329
Cdd:TIGR00606 619 -EQLSSYEDKLFDvcGSQDEESDLERLKEEIEKSSKQRAML 658
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
960-1138 |
1.42e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.98 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 960 EESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINckynsalvdrEEsrvlIKKQEVD 1039
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ----------AE----IAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1040 ILDLKETLRLRI-----------------LSEDIErdmlceDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQE 1102
Cdd:COG3883 81 IEERREELGERAralyrsggsvsyldvllGSESFS------DFLDRLSALSKIADADADLLEELKADKAELEAKKAELEA 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 74752937 1103 LQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAED 1138
Cdd:COG3883 155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
484-1292 |
1.42e-04 |
|
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: 46.58 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 484 EEQDRLLSELRNEIQTLREQIehhprVAKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKN 563
Cdd:TIGR00606 206 QMELKYLKQYKEKACEIRDQI-----TSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 564 QQgfspkaqkepclfanteKLKAQLLQIQTELNNSKQEyeEFKELTRKRQLELESELQSLQKANLNLENLLEATKACKRQ 643
Cdd:TIGR00606 281 ME-----------------KDNSELELKMEKVFQGTDE--QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 644 EVSQLNKIHAETLKiittpTKAYQLHSRPVPKLSPEMGSFGSLytqnsSILDNDILNEPVPPEMNEQAFEAISEELRTVQ 723
Cdd:TIGR00606 342 KTELLVEQGRLQLQ-----ADRHQEHIRARDSLIQSLATRLEL-----DGFERGPFSERQIKNFHTLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 724 EQMSALQAKLDEEehknlklQQHVDKLEHHSTQMQELFSSERIDWTKQQEEL---LSQLNVLEKQLQETQTKNDFLKSEV 800
Cdd:TIGR00606 412 QLCADLQSKERLK-------QEQADEIRDEKKGLGRTIELKKEILEKKQEELkfvIKELQQLEGSSDRILELDQELRKAE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 801 HDLRVVLHSAD-----KELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEIMK 875
Cdd:TIGR00606 485 RELSKAEKNSLtetlkKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTS 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 876 FEID-----QLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKeilkvleavRQEKQKETAKCE 950
Cdd:TIGR00606 565 LLGYfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS---------YEDKLFDVCGSQ 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 951 QQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELrTSVCEKT-ETIDTLKQELKDINCKYNSALVDREES 1029
Cdd:TIGR00606 636 DEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSC-CPVCQRVfQTEAELQEFISDLQSKLRLAPDKLKST 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1030 RVLIKKQEVdildlketlrlrilsediERDMLCedlahateqlnmlteaskkhsGLLQSAQEELTKKEALIQELQHKLNQ 1109
Cdd:TIGR00606 715 ESELKKKEK------------------RRDEML---------------------GLAPGRQSIIDLKEKEIPELRNKLQK 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1110 KKEEVEQKKNEYNFKMRQLEHVM--DSAAEDPQSPKTP-PHFQTHLAKLLETQEQEIEDGRASktSLEHLVTKLNEDREV 1186
Cdd:TIGR00606 756 VNRDIQRLKNDIEEQETLLGTIMpeEESAKVCLTDVTImERFQMELKDVERKIAQQAAKLQGS--DLDRTVQQVNQEKQE 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1187 KNAEILRMKEQLREMENLRLESQQLIEKnwlLQGQLDDIKRQKENSDQNHPDNQQLKNEQEESIKE--------RLAKSK 1258
Cdd:TIGR00606 834 KQHELDTVVSKIELNRKLIQDQQEQIQH---LKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEvqslireiKDAKEQ 910
|
810 820 830
....*....|....*....|....*....|....
gi 74752937 1259 IVEEMLKMKADLEEVQSALYNKEMECLRMTDEVE 1292
Cdd:TIGR00606 911 DSPLETFLEKDQQEKEELISSKETSNKKAQDKVN 944
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
464-1044 |
1.47e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.65 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 464 EDQiirLEKLHKESRGG---FLPEEQDR---LLSELRNEIQTLREQIEHHPRVAKYAMENHSLREENRRLRLLEPVKRAQ 537
Cdd:pfam15921 244 EDQ---LEALKSESQNKielLLQQHQDRieqLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 538 EMDAqTIAKLEKAFSEISGMEKsDKnqqgfspkaqkepclfanTEKLKAQLLQIQTELNNSKQEYEEFKELT-------- 609
Cdd:pfam15921 321 DLES-TVSQLRSELREAKRMYE-DK------------------IEELEKQLVLANSELTEARTERDQFSQESgnlddqlq 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 610 --------RKRQLELESE-------------------LQSLQKANLN---LENLLEATKA-CKRQEVSQLNKIHA--ETL 656
Cdd:pfam15921 381 klladlhkREKELSLEKEqnkrlwdrdtgnsitidhlRRELDDRNMEvqrLEALLKAMKSeCQGQMERQMAAIQGknESL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 657 KIITTPTKAYQLHSRPVPKLSPEMGSfGSLYTQNSSILDNDIlnePVPPEMNEQAFEAISEELRTVQeqmSALQAKLDEE 736
Cdd:pfam15921 461 EKVSSLTAQLESTKEMLRKVVEELTA-KKMTLESSERTVSDL---TASLQEKERAIEATNAEITKLR---SRVDLKLQEL 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 737 EHknlkLQQHVDKLEHHSTQ-----MQELFSSERIDWTKQQEELLSQL---------NVLEKQLQETQTKNDfLKSEVHD 802
Cdd:pfam15921 534 QH----LKNEGDHLRNVQTEcealkLQMAEKDKVIEILRQQIENMTQLvgqhgrtagAMQVEKAQLEKEIND-RRLELQE 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 803 LRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERHMHVQlqldNLRLENEKLLESKACLQDSYDNLQEimkfEIDQLS 882
Cdd:pfam15921 609 FKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVK----DIKQERDQLLNEVKTSRNELNSLSE----DYEVLK 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 883 RNLQNFKKENETLKSDLNnlMELLEAEKE----RNNKLSLqfeedkENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQK 958
Cdd:pfam15921 681 RNFRNKSEEMETTTNKLK--MQLKSAQSEleqtRNTLKSM------EGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQF 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 959 LEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEV 1038
Cdd:pfam15921 753 LEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ 832
|
....*.
gi 74752937 1039 DILDLK 1044
Cdd:pfam15921 833 ESVRLK 838
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1086-1386 |
1.54e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1086 LQSAQEELTKKEALIQELQHKLNQKKEEVEqKKNEYNFKMRQLEHVMDSAaedpqspktpphfqthLAKLLETQEQEIED 1165
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELAL----------------LVLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1166 GRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMEnlrlESQQLIEKNWL-LQGQLDDIKRQKENSDQNHPDNQQLKN 1244
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELE----EEIEELQKELYaLANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1245 EQEESIKERLAKSKIVEEMLKMKAdlEEVQSALYNKEMECLRMTDEVERTQTLESK---AFQEKEQLRSKLEEMYE---- 1317
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELE--EKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQLELqias 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74752937 1318 ---ERERTSQEMEMLRKQVECLAEENGKLVGHQNLHQKIQYVVRLKKENVRLAEETEKLRAENVFLKEKKRS 1386
Cdd:TIGR02168 398 lnnEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
384-1048 |
2.08e-04 |
|
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: 46.19 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 384 VKRLKEQLAELASGQTPPESFLTRDKKKTNYMEYFQEAMLFFKKSEQEKKSLIEKVTQLEDLTLKK-EKFIQSNkmiVKF 462
Cdd:TIGR00606 240 VKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDlYHNHQRT---VRE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 463 REDQIIR----LEKLHKESRggflpeEQDRLLSELRNEIQTLREQIE-HHPRVAKYAMENHSLR-------------EEN 524
Cdd:TIGR00606 317 KERELVDcqreLEKLNKERR------LLNQEKTELLVEQGRLQLQADrHQEHIRARDSLIQSLAtrleldgfergpfSER 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 525 RRLRLLEPVKRAQEMDAQTIAKLEKAFSEisgmeKSDKNQQGFSPKAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYEE 604
Cdd:TIGR00606 391 QIKNFHTLVIERQEDEAKTAAQLCADLQS-----KERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQ 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 605 FkELTRKRQLELEselQSLQKANLNLENLLE-ATKACKRQEVSQLNKIHAETLKIITTPTKAYQLHSRPVPKLSPEMGSF 683
Cdd:TIGR00606 466 L-EGSSDRILELD---QELRKAERELSKAEKnSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLT 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 684 GSLYTQNSSILDN-----DILNEPVPPEMNEQAFEAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKlEHHSTQMQ 758
Cdd:TIGR00606 542 KDKMDKDEQIRKIksrhsDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINN-ELESKEEQ 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 759 ELFSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFL--KSEVHDlRVVLHSADKELSSVKLEYSSFKTnqEKEFNKLS 836
Cdd:TIGR00606 621 LSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLagATAVYS-QFITQLTDENQSCCPVCQRVFQT--EAELQEFI 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 837 ERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEIMKFEID-------QLSRNLQNFKKENETLKSDLNNLMELLEA- 908
Cdd:TIGR00606 698 SDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDlkekeipELRNKLQKVNRDIQRLKNDIEEQETLLGTi 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 909 -EKERNNKLSL-------QFEEDKENSSKEILKV---------------LEAVRQEKQKETAKCEQQMAKVQKLEE---- 961
Cdd:TIGR00606 778 mPEEESAKVCLtdvtimeRFQMELKDVERKIAQQaaklqgsdldrtvqqVNQEKQEKQHELDTVVSKIELNRKLIQdqqe 857
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 962 ---------SLLATEKV-ISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRv 1031
Cdd:TIGR00606 858 qiqhlksktNELKSEKLqIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSN- 936
|
730
....*....|....*..
gi 74752937 1032 liKKQEVDILDLKETLR 1048
Cdd:TIGR00606 937 --KKAQDKVNDIKEKVK 951
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1083-1339 |
2.11e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1083 SGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEdpqspktpphfqthLAKLLETQEQE 1162
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA--------------LARRIRALEQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1163 IEDGRASKTSLEHLVTKLNEDREVKNAEIlrmKEQLREMENLrleSQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQQL 1242
Cdd:COG4942 78 LAALEAELAELEKEIAELRAELEAQKEEL---AELLRALYRL---GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1243 KNEQEESIKE-RLAKSKIVEEMLKMKADLEEVQSALynkemecLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEERER 1321
Cdd:COG4942 152 AEELRADLAElAALRAELEAERAELEALLAELEEER-------AALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250
....*....|....*...
gi 74752937 1322 TSQEMEMLRKQVECLAEE 1339
Cdd:COG4942 225 LEALIARLEAEAAAAAER 242
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
436-1046 |
2.13e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.20 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 436 IEKVTQLEDLTLKKEKFIQSNKMIVKFREDQiirlEKLHKESRGGFLPEEQDRLLSE---LRNEIQTLREQIEHHPRvak 512
Cdd:TIGR01612 1060 IEKEIGKNIELLNKEILEEAEINITNFNEIK----EKLKHYNFDDFGKEENIKYADEinkIKDDIKNLDQKIDHHIK--- 1132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 513 yAMENHSLREENRrlrllepvkrAQEMDAQtIAKLEK-AFSEISG--MEKSDKNQQGFSPKAQKEPCLFANTEKLKAQLL 589
Cdd:TIGR01612 1133 -ALEEIKKKSENY----------IDEIKAQ-INDLEDvADKAISNddPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIA 1200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 590 QIQT------ELNNSKQEYEE-----FKELTRKRQLELESELQSLQKANLNLENLLEATKACKRQEVSQLN-KIHAETLK 657
Cdd:TIGR01612 1201 EIEKdktsleEVKGINLSYGKnlgklFLEKIDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDiKAEMETFN 1280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 658 IITTPTKAYQLHSRpvpklspemgsfgslyTQNSSIldNDILNEPVppemneQAFEAISEElRTVQEQMSALQAKLDEEE 737
Cdd:TIGR01612 1281 ISHDDDKDHHIISK----------------KHDENI--SDIREKSL------KIIEDFSEE-SDINDIKKELQKNLLDAQ 1335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 738 HKNLKLQQHVDKLehhsTQMQELFSSERI--------DWTKQQEE----LLSQLNVLEKqLQETQTKNDFLKSEVHDLRV 805
Cdd:TIGR01612 1336 KHNSDINLYLNEI----ANIYNILKLNKIkkiidevkEYTKEIEEnnknIKDELDKSEK-LIKKIKDDINLEECKSKIES 1410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 806 VLHSAD-----KELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQLDNLRLENEKlleSKACLQDSYDNLQEIMKFEIDQ 880
Cdd:TIGR01612 1411 TLDDKDideciKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKNIEMADNK---SQHILKIKKDNATNDHDFNINE 1487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 881 LSRNL---QNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEE--------DKENSSKEILKVLEAVRQEKQKETAKC 949
Cdd:TIGR01612 1488 LKEHIdksKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSAlaiknkfaKTKKDSEIIIKEIKDAHKKFILEAEKS 1567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 950 EQQMAKVQK----------------------------LEESLL-----------------ATEKVISSLE-KSRDSDKKV 983
Cdd:TIGR01612 1568 EQKIKEIKKekfrieddaakndksnkaaidiqlslenFENKFLkisdikkkindclketeSIEKKISSFSiDSQDTELKE 1647
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74752937 984 VADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRvliKKQEVDILD-LKET 1046
Cdd:TIGR01612 1648 NGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHK---KNYEIGIIEkIKEI 1708
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
782-997 |
4.56e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 782 LEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFnklserhmhVQLQLDNLRLENEKLLESKA 861
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKL---------LLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 862 CLQDSYDNLQEIMKFEIDQLSRNLQNfkKENETLKSDLNNLMELLEAEKERNN-------KLSLQFEEDKENSSKEILKV 934
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTpnhpdviALRAQIAALRAQLQQEAQRI 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74752937 935 LEAVRQEKQKETAKCEQQMAKVQKLEE---SLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTS 997
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEArlaELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
717-1308 |
5.25e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.68 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 717 EELRTVQEQMSALQAKLDEEehKNLKLQQHVdKLEHHSTQMQELFSS-----ERIDWTKQQE---ELLSQLNVLEKQLQE 788
Cdd:COG5022 810 KEYRSYLACIIKLQKTIKRE--KKLRETEEV-EFSLKAEVLIQKFGRslkakKRFSLLKKETiylQSAQRVELAERQLQE 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 789 TQTKNdflkSEVHDLRVVLHSADKELSSVKleySSFKTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLEskACLQDSYD 868
Cdd:COG5022 887 LKIDV----KSISSLKLVNLELESEIIELK---KSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIE--YVKLPELN 957
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 869 NLQEIMKfEIDQLSRNLQNFKKENETLKSDLNNLMELL-----EAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQ 943
Cdd:COG5022 958 KLHEVES-KLKETSEEYEDLLKKSTILVREGNKANSELknfkkELAELSKQYGALQESTKQLKELPVEVAELQSASKIIS 1036
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 944 KETAKcEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQI-QELRTSVCEKTETIDTLK------------- 1009
Cdd:COG5022 1037 SESTE-LSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLyQLESTENLLKTINVKDLEvtnrnlvkpanvl 1115
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1010 -----QELKDINCKYNSALVDREESRVLIKKQ--EVDILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKH 1082
Cdd:COG5022 1116 qfivaQMIKLNLLQEISKFLSQLVNTLEPVFQklSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKSKLS 1195
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1083 SGLLQSAQEEL--------------------TKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQSP 1142
Cdd:COG5022 1196 SSEVNDLKNELialfskifsgwprgdklkklISEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSY 1275
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1143 KTPPhfqTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREV-KNAEILRMKEQLREMENLRLESQQLIEKNWLLQGQ 1221
Cdd:COG5022 1276 KLEE---EVLPATINSLLQYINVGLFNALRTKASSLRWKSATEVnYNSEELDDWCREFEISDVDEELEELIQAVKVLQLL 1352
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1222 LDDIKRQKENSD----QNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLR--MTDEVERTQ 1295
Cdd:COG5022 1353 KDDLNKLDELLDacysLNPAEIQNLKSRYDPADKENNLPKEILKKIEALLIKQELQLSLEGKDETEVHLseIFSEEKSLI 1432
|
650
....*....|...
gi 74752937 1296 TLESKAFQEKEQL 1308
Cdd:COG5022 1433 SLDRNSIYKEEVL 1445
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
371-643 |
5.70e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.67 E-value: 5.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 371 EDTQGNVSQLQAEVKRLKEQLAELASGQTPPESFLTRDKKKTNYMEYfQEAMLFFKKSEQEKKSL------IEKVTQ--- 441
Cdd:TIGR02169 740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA-RLSHSRIPEIQAELSKLeeevsrIEARLReie 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 442 --LEDLTLKK---EKFIQSNKMIVKFREDQIIRLEKLHKESRGGFlpEEQDRLLSELRNEIQTLREQIEHHPRVAKyAME 516
Cdd:TIGR02169 819 qkLNRLTLEKeylEKEIQELQEQRIDLKEQIKSIEKEIENLNGKK--EELEEELEELEAALRDLESRLGDLKKERD-ELE 895
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 517 NHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQQGFSPKAQKEPCLFANTEKLKAQLLQIQTELN 596
Cdd:TIGR02169 896 AQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNM 975
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 74752937 597 NSKQEYEEfkelTRKRQLELESELQSLQKANLNLENLLEATKACKRQ 643
Cdd:TIGR02169 976 LAIQEYEE----VLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
706-1339 |
6.29e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 706 EMNEQAFEAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQE---LFSSERIDWTKQQEELLSQLNVL 782
Cdd:pfam01576 85 EEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEdilLLEDQNSKLSKERKLLEERISEF 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 783 EKQLQETQTKNDFL-------KSEVHDLRVVLHSADKelssVKLEYSSFKTNQEKEFNKLSERHMHVQLQLDNLRLENEK 855
Cdd:pfam01576 165 TSNLAEEEEKAKSLsklknkhEAMISDLEERLKKEEK----GRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 856 LLESKACLQDsydnlqeimKFEIDQLSRNlqNFKKENETLKSDLNNLMELLEAEKERNNKLslqfEEDKENSSKEilkvL 935
Cdd:pfam01576 241 KEEELQAALA---------RLEEETAQKN--NALKKIRELEAQISELQEDLESERAARNKA----EKQRRDLGEE----L 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 936 EAVRQE----------KQKETAKCEQQMAKVQK-LEESLLATEkviSSLEKSRDSDKKVVADLMNQIQELRTSVCEKTET 1004
Cdd:pfam01576 302 EALKTEledtldttaaQQELRSKREQEVTELKKaLEEETRSHE---AQLQEMRQKHTQALEELTEQLEQAKRNKANLEKA 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1005 IDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKetlrLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSG 1084
Cdd:pfam01576 379 KQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQ----ARLSESERQRAELAEKLSKLQSELESVSSLLNEAEG 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1085 LLQSAQEELTKKEALIQELQHKLnqkKEEVEQKKNeYNFKMRQLEH----VMDSAAEDPQSPKT-PPHFQTHLAKLLETQ 1159
Cdd:pfam01576 455 KNIKLSKDVSSLESQLQDTQELL---QEETRQKLN-LSTRLRQLEDernsLQEQLEEEEEAKRNvERQLSTLQAQLSDMK 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1160 EQeIEDGRASKTSLEHLVTKLNEDREVKNaeiLRMKEQLREMENLRLESQQlieknwlLQGQLDDIKRQKENSDQ--NHP 1237
Cdd:pfam01576 531 KK-LEEDAGTLEALEEGKKRLQRELEALT---QQLEEKAAAYDKLEKTKNR-------LQQELDDLLVDLDHQRQlvSNL 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1238 DNQQLKNEQEESiKERLAKSKIVEEMLKMKADLEEvqsalynKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEEMY- 1316
Cdd:pfam01576 600 EKKQKKFDQMLA-EEKAISARYAEERDRAEAEARE-------KETRALSLARALEEALEAKEELERTNKQLRAEMEDLVs 671
|
650 660 670
....*....|....*....|....*....|....*.
gi 74752937 1317 ---------EERERT----SQEMEMLRKQVECLAEE 1339
Cdd:pfam01576 672 skddvgknvHELERSkralEQQVEEMKTQLEELEDE 707
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
426-636 |
6.85e-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: 43.60 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 426 KKSEQEKKSLIEKVTQLEDLTLKKEKFIQSNKMIVKFREDQIIRLEKLHKESRGGFlpEEQDRLLSELRNEIQTLREQIE 505
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL--AALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 506 HHPR------VAKYAMENHSL-------REENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQQgfspkaq 572
Cdd:COG4942 101 AQKEelaellRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER------- 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74752937 573 kepclfANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEA 636
Cdd:COG4942 174 ------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
935-1185 |
6.93e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 935 LEAVRQEKQK---ETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKV------VADLMNQIQELRTSVCEktetI 1005
Cdd:COG4913 612 LAALEAELAEleeELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVasaereIAELEAELERLDASSDD----L 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1006 DTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETL-RLRILSEDIERDMLCEDLAHATEQLNMLTEAskkhsG 1084
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdELQDRLEAAEDLARLELRALLEERFAAALGD-----A 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1085 LLQSAQEELTKKealIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDpqspktPPHFQTHLAKL----LETQE 1160
Cdd:COG4913 763 VERELRENLEER---IDALRARLNRAEEELERAMRAFNREWPAETADLDADLES------LPEYLALLDRLeedgLPEYE 833
|
250 260
....*....|....*....|....*..
gi 74752937 1161 QEIED--GRASKTSLEHLVTKLNEDRE 1185
Cdd:COG4913 834 ERFKEllNENSIEFVADLLSKLRRAIR 860
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
708-1164 |
7.16e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 708 NEQAFEAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERidwtKQQEELLSQLNVLEKQLQ 787
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE----AELAEAEEELEELAEELL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 788 ETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSY 867
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 868 DNLQEIMKfEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQ--------FEEDKENSSKEILKVLEAVR 939
Cdd:COG1196 470 EEAALLEA-ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagavavLIGVEAAYEAALEAALAAAL 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 940 QEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKK----------VVADLMNQIQELRTSVCEKTETIDTLK 1009
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAAlargaigaavDLVASDLREADARYYVLGDTLLGRTLV 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1010 QELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLRILSEDIERDmlcEDLAHATEQLNMLTEASKKHSGLLQSA 1089
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAE---AELEELAERLAEEELELEEALLAEEEE 705
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74752937 1090 QEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVM-DSAAEDPQSPKTPPHFQTHLAKLletqEQEIE 1164
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLeEEALEELPEPPDLEELERELERL----EREIE 777
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
990-1200 |
7.48e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 990 QIQELRTSVCEKTETIDTLKQELKDINCKYNSAlvdREESRVLIKKQEVDildlketlrlrilSEDIERDMLCEDLAHAT 1069
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDAL---QERREALQRLAEYS-------------WDEIDVASAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1070 EQLNMLTEASKKhsglLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQSPKTPPHFQ 1149
Cdd:COG4913 675 AELERLDASSDD----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 74752937 1150 thlakLLETQEQEIEDGRASKtslehLVTKLNEDREVKNAEILRMKEQLRE 1200
Cdd:COG4913 751 -----LEERFAAALGDAVERE-----LRENLEERIDALRARLNRAEEELER 791
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
767-1155 |
1.16e-03 |
|
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: 43.67 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 767 DWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSsfktNQEKEFNKLSERHMHVQLQL 846
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALK----NARLDLRRLFDEKQSEKDKK 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 847 dnlrleNEKLLESKACLQDSYDNLQEimkfEIDQLSRNLQNFKKENETlksdlnnlmELLEAEKERNNKLsLQFEEDKEN 926
Cdd:pfam12128 670 ------NKALAERKDSANERLNSLEA----QLKQLDKKHQAWLEEQKE---------QKREARTEKQAYW-QVVEGALDA 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 927 SSKEILKVLEAVRQEKQKETAKCEQQMAKvqkleeSLlatekvissleKSRDSDKKVVADLMNQIQELRTSVcektETID 1006
Cdd:pfam12128 730 QLALLKAAIAARRSGAKAELKALETWYKR------DL-----------ASLGVDPDVIAKLKREIRTLERKI----ERIA 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1007 TLKQELKDINCKYNSALVDREESRVL-IKKQEVDILDLKEtlRLRILSEDIERDMlcedlahatEQLNMLTEASKKhsgL 1085
Cdd:pfam12128 789 VRRQEVLRYFDWYQETWLQRRPRLATqLSNIERAISELQQ--QLARLIADTKLRR---------AKLEMERKASEK---Q 854
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74752937 1086 LQSAQEELTKKEALIQELQH-KLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQspKTPPHFQTHLAKL 1155
Cdd:pfam12128 855 QVRLSENLRGLRCEMSKLATlKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVK--KYVEHFKNVIADH 923
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
706-1334 |
1.32e-03 |
|
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: 43.52 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 706 EMNEQAFEAISEELRTVQEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQElfsseridwtkQQEELLSQLNVLEKQ 785
Cdd:TIGR02169 276 ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA-----------EIDKLLAEIEELERE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 786 LQETQTKNDFLKSEV-------HDLRVVLHSADKELSSVKLEYSSFKTNQEK----------EFNKLSERHMHVQLQLDN 848
Cdd:TIGR02169 345 IEEERKRRDKLTEEYaelkeelEDLRAELEEVDKEFAETRDELKDYREKLEKlkreinelkrELDRLQEELQRLSEELAD 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 849 LRLENEKLLESKACLQDSYDNLQEimkfEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEE------ 922
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKAL----EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEaeaqar 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 923 ---DKENSSKEILKVLEA--------------VRQEKQK------------------ETAKCEQQMAKVQKL-EESLLAT 966
Cdd:TIGR02169 501 aseERVRGGRAVEEVLKAsiqgvhgtvaqlgsVGERYATaievaagnrlnnvvveddAVAKEAIELLKRRKAgRATFLPL 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 967 EKVISS-LEKSRDSDKKVVADLMNQI---QELR---------TSVCEKTET---------IDTLKQELKDinckyNSALV 1024
Cdd:TIGR02169 581 NKMRDErRDLSILSEDGVIGFAVDLVefdPKYEpafkyvfgdTLVVEDIEAarrlmgkyrMVTLEGELFE-----KSGAM 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1025 ----DREESRVLIKKQEVDILdlkETLRLRILSEDIERDMLCEDLAHATEQLNMLT----EASKKHSGL---LQSAQEEL 1093
Cdd:TIGR02169 656 tggsRAPRGGILFSRSEPAEL---QRLRERLEGLKRELSSLQSELRRIENRLDELSqelsDASRKIGEIekeIEQLEQEE 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1094 TKKEALIQELQHKLN---QKKEEVEQKKNEYNFKMRQLE---HVMDSAAEDPQSPKTPPHFQThLAKLLETQEQEIEDGR 1167
Cdd:TIGR02169 733 EKLKERLEELEEDLSsleQEIENVKSELKELEARIEELEedlHKLEEALNDLEARLSHSRIPE-IQAELSKLEEEVSRIE 811
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1168 ASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEKNWL------------------LQGQLDDIKRQK 1229
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGkkeeleeeleeleaalrdLESRLGDLKKER 891
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1230 ENSDQNHPDNQQLKNEQEESI-------KERLAKSKIVEEMLK----MKADLEEVQSALYNKE---MECLRMTDEVERTQ 1295
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIekkrkrlSELKAKLEALEEELSeiedPKGEDEEIPEEELSLEdvqAELQRVEEEIRALE 971
|
730 740 750
....*....|....*....|....*....|....*....
gi 74752937 1296 TLESKAFQEKEQLRSKLEEMYEERERTSQEMEMLRKQVE 1334
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIE 1010
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
710-978 |
1.42e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 710 QAFEAISEELRTVQEQMSALQAKLDEEEhknlklqqhvdklehhstqmqelfsseridwtKQQEELLSQLNVLEKQLQET 789
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALK--------------------------------KEEKALLKQLAALERRIAAL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 790 QTKndflkseVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERhmhVQLQLDNLRLENEKLLESKACLQDSYDN 869
Cdd:COG4942 68 ARR-------IRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 870 LQ------EIMKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLslqfeEDKENSSKEILKVLEAVRQEKQ 943
Cdd:COG4942 138 LQylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL-----EALKAERQKLLARLEKELAELA 212
|
250 260 270
....*....|....*....|....*....|....*
gi 74752937 944 KETAKCEQQMAKVQKLEESLLATEKVISSLEKSRD 978
Cdd:COG4942 213 AELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
484-875 |
1.60e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 484 EEQDRLLSELRNEIQTLREQIEHHPRVAKYAMENHSLREENRRLRLLE-------PVKRAQEMDAQTIAKLEKAFSEISg 556
Cdd:COG4717 105 EELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEerleelrELEEELEELEAELAELQEELEELL- 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 557 MEKSDKNQQGFSPKAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYEEFKEltrkrQLELESELQSLQKAN--LNLENLL 634
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN-----ELEAAALEERLKEARllLLIAAAL 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 635 EATKACKRQEVSQLNKIHAETLKIITTPTKAYQLHSRPVPKLSPEMGSFGSLYTQNS-------SILDNDILNEPVPPEM 707
Cdd:COG4717 259 LALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEleeeeleELLAALGLPPDLSPEE 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 708 NEQAFEAIsEELRTVQEQMSALQAKLD----EEEHKNLKLQQHVDKLEhhstqmqELFssERIDWTKQQEELLSQLNVLE 783
Cdd:COG4717 339 LLELLDRI-EELQELLREAEELEEELQleelEQEIAALLAEAGVEDEE-------ELR--AALEQAEEYQELKEELEELE 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 784 KQLQE---------TQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKtnQEKEFNKLSERHMHVQLQLDNLRLENE 854
Cdd:COG4717 409 EQLEEllgeleellEALDEEELEEELEELEEELEELEEELEELREELAELE--AELEQLEEDGELAELLQELEELKAELR 486
|
410 420
....*....|....*....|.
gi 74752937 855 KLLESKACLQDSYDNLQEIMK 875
Cdd:COG4717 487 ELAEEWAALKLALELLEEARE 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1156-1383 |
1.77e-03 |
|
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: 42.75 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1156 LETQEQEIEDGRASKTSLEHLVTKLNEDREvKNAEILRMKEQLREMEN--LRLESQQLIEKNWLLQGQLDDIKRQKENSD 1233
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRRERE-KAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1234 QNHPDNQQLKNEQEESIKERLAK--SKIVEEMLKMKADLEEVQS---------ALYNKEMEclRMTDEVERTQTLESKAF 1302
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKikDLGEEEQLRVKEKIGELEAeiaslersiAEKERELE--DAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1303 QEKEQLRSKLEEMYEERERTS-------QEMEMLRKQVECLAEENGKLVG-HQNLHQKIQYVVR----LKKENVRLAEET 1370
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTeeyaelkEELEDLRAELEEVDKEFAETRDeLKDYREKLEKLKReineLKRELDRLQEEL 415
|
250
....*....|...
gi 74752937 1371 EKLRAENVFLKEK 1383
Cdd:TIGR02169 416 QRLSEELADLNAA 428
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
943-1329 |
1.88e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.57 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 943 QKETAKCEQQMAKV-QKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINC---- 1017
Cdd:pfam07888 33 QNRLEECLQERAELlQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAssee 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1018 ---KYNSALVDREESRVLIKKQEVDIldlkETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELT 1094
Cdd:pfam07888 113 lseEKDALLAQRAAHEARIRELEEDI----KTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1095 KKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEdpqspktpphfqthlaklLETQEQEIEDGRASKTSLE 1174
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE------------------NEALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1175 HLVTKLNEDREVKNAEILRMKEqlrEMENLRLESQQLieknwllQGQLDDIKRQ-KENSDQNHPDNQQLKNEQEESiKER 1253
Cdd:pfam07888 251 RKVEGLGEELSSMAAQRDRTQA---ELHQARLQAAQL-------TLQLADASLAlREGRARWAQERETLQQSAEAD-KDR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1254 LAKskIVEEMLKMKADLEEVQSALYNKEMECLRMTDeVERTQTLESK------------AFQEKEQLRSKLEEMYEERER 1321
Cdd:pfam07888 320 IEK--LSAELQRLEERLQEERMEREKLEVELGREKD-CNRVQLSESRrelqelkaslrvAQKEKEQLQAEKQELLEYIRQ 396
|
....*...
gi 74752937 1322 TSQEMEML 1329
Cdd:pfam07888 397 LEQRLETV 404
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
870-1137 |
2.49e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 870 LQEIMKFEIDQLSRNLQNFKKEN-ETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAvrqekqketak 948
Cdd:PRK05771 25 LHELGVVHIEDLKEELSNERLRKlRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEE----------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 949 ceqqmaKVQKLEESLLATEKVISSLEksrdSDKKvvaDLMNQIQELrtsvcEKTETIDTlkqelkDINCKYNSALVDREE 1028
Cdd:PRK05771 94 ------ELEKIEKEIKELEEEISELE----NEIK---ELEQEIERL-----EPWGNFDL------DLSLLLGFKYVSVFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1029 SRVLIKKQEVDILDLKETLrLRILSEDIERDMLC-----EDLAHATEQLNMLtEASKKHSGLLQSAQEELTKKEALIQEL 1103
Cdd:PRK05771 150 GTVPEDKLEELKLESDVEN-VEYISTDKGYVYVVvvvlkELSDEVEEELKKL-GFERLELEEEGTPSELIREIKEELEEI 227
|
250 260 270
....*....|....*....|....*....|....
gi 74752937 1104 QHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAE 1137
Cdd:PRK05771 228 EKERESLLEELKELAKKYLEELLALYEYLEIELE 261
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
829-1301 |
2.52e-03 |
|
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: 42.52 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 829 EKEFNKLSERHMhvQLQLDNLRLENEKLLESKacLQDSYDNLQEIMKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEA 908
Cdd:pfam12128 247 QQEFNTLESAEL--RLSHLHFGYKSDETLIAS--RQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 909 EKERNNKLSLQFEEDKENSSKEILKVLEAVRQEkqketakCEQQMAKVQKLEESLLATEKVISSLEKSRDSD-KKVVADL 987
Cdd:pfam12128 323 ELEALEDQHGAFLDADIETAAADQEQLPSWQSE-------LENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 988 MNQIQELRtsvcektETIDTLKQELKDINCKYNSALVDREESRVL-IKKQEVDILDLKETLRLRILSEDIERDMLcEDLA 1066
Cdd:pfam12128 396 KDKLAKIR-------EARDRQLAVAEDDLQALESELREQLEAGKLeFNEEEYRLKSRLGELKLRLNQATATPELL-LQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1067 HATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEynfkMRQLEHVMDSAAEDPQS--PKT 1144
Cdd:pfam12128 468 NFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSA----LDELELQLFPQAGTLLHflRKE 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1145 PPHFQTHLAK------LLETQEQEIEDGRASKTSLEHLVTKLNEDReVKNAEILRMKEQLRE--------MENLRLESQQ 1210
Cdd:pfam12128 544 APDWEQSIGKvispelLHRTDLDPEVWDGSVGGELNLYGVKLDLKR-IDVPEWAASEEELRErldkaeeaLQSAREKQAA 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1211 LIEKNWLLQGQLDDIKRQKENSD---QNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKA--DLEEVQSALYNKEMECL 1285
Cdd:pfam12128 623 AEEQLVQANGELEKASREETFARtalKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERlnSLEAQLKQLDKKHQAWL 702
|
490
....*....|....*.
gi 74752937 1286 RMTDEVERTQTLESKA 1301
Cdd:pfam12128 703 EEQKEQKREARTEKQA 718
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
770-1202 |
2.58e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 770 KQQEELLSQLNVLEKQLQETQTKNDflksEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKefnklserhMHVQLQLDNL 849
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEK---------LEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 850 RLENEKLLESKACLQDSYDNLQEIMKfEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERnnklslQFEEDKENssk 929
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEE--- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 930 eilkvLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRD-SDKKVVADLMNQIQELRTSVCEKTETIDTL 1008
Cdd:COG4717 201 -----LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1009 KQELKDI-----------NCKYNSALVDREESRVLIKKQEVDILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTE 1077
Cdd:COG4717 276 AGVLFLVlgllallflllAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1078 ASKKHSGLLQSAQEEltKKEALIQ--------ELQHKLNQKKEEVEQKKneynfKMRQLEHVMDSAAEDPQSPKTPPHFQ 1149
Cdd:COG4717 356 AEELEEELQLEELEQ--EIAALLAeagvedeeELRAALEQAEEYQELKE-----ELEELEEQLEELLGELEELLEALDEE 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74752937 1150 THLAKLLETQEQ------EIEDGRASKTSLEHLVTKLNEDREV--KNAEILRMKEQLREME 1202
Cdd:COG4717 429 ELEEELEELEEEleeleeELEELREELAELEAELEQLEEDGELaeLLQELEELKAELRELA 489
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
485-768 |
2.64e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 485 EQDRLLSELRNEIQTLREQIEHhprvAKYAMEnhSLREENRRLRLLEP---VKRAQEMDAQtIAKLEKAFSEISGMEKSD 561
Cdd:PRK04863 848 ELERALADHESQEQQQRSQLEQ----AKEGLS--ALNRLLPRLNLLADetlADRVEEIREQ-LDEAEEAKRFVQQHGNAL 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 562 KNQQGFSPKAQKEPclfANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQ----------LELESELQSLQKANL-NL 630
Cdd:PRK04863 921 AQLEPIVSVLQSDP---EQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAhfsyedaaemLAKNSDLNEKLRQRLeQA 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 631 ENLLEATKACKRQEVSQLNKIHAETLKIITTPTKAYQLHSrpvpKLSPEMGSFGSlytqnssildndilnePVPPEMNEQ 710
Cdd:PRK04863 998 EQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQ----ELKQELQDLGV----------------PADSGAEER 1057
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74752937 711 AF---EAISEELRTVQEQMSALQAKLD--EEEHKNlkLQQHVDKLEHHSTQMQELFSSERIDW 768
Cdd:PRK04863 1058 ARarrDELHARLSANRSRRNQLEKQLTfcEAEMDN--LTKKLRKLERDYHEMREQVVNAKAGW 1118
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
105-304 |
3.15e-03 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 42.03 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 105 IFAYGQTGSGKTFTMMGPSESDNFShnlrgVIPRSFEYLFSLIDREKEKagagKSFlCKCSFIEIyNEQIYDLLDSASAG 184
Cdd:COG5059 385 IFAYMQSLKKETETLKSRIDLIMKS-----IISGTFERKKLLKEEGWKY----KST-LQFLRIEI-DRLLLLREEELSKK 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 185 LYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFT-ITIESMEKSNEIvnirtsLLNL 263
Cdd:COG5059 454 KTKIHKLNKLRHDLSSLLSSIPEETSDRVESEKASKLRSSASTKLNLRSSRSHSKFRdHLNGSNSSTKEL------SLNQ 527
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 74752937 264 VDLAGSERqKDTHAEGMRLKEAGNINRSLSCLGQVITALVD 304
Cdd:COG5059 528 VDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHALGS 567
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
975-1264 |
3.50e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 41.76 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 975 KSRDSDKKVVADLMNQIQELRTSVCEK------------TETIDTLKQElkdINCKYNSALVDRE-ESRVLIKKQEVDIL 1041
Cdd:PLN03229 422 KKREAVKTPVRELEGEVEKLKEQILKAkessskpselalNEMIEKLKKE---IDLEYTEAVIAMGlQERLENLREEFSKA 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1042 DLKETLRLRILSEDIER--DMLCEDLAHA------TEQLNMLTEASKKhsgllQSAQEELTKKEALIQELQHKLNQK--- 1110
Cdd:PLN03229 499 NSQDQLMHPVLMEKIEKlkDEFNKRLSRApnylslKYKLDMLNEFSRA-----KALSEKKSKAEKLKAEINKKFKEVmdr 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1111 -----------------------------KEEVEQKKNEYNFKMRQLEHVMD-------SAAEDPQSPKTPPHFQTHLAK 1154
Cdd:PLN03229 574 peikekmealkaevassgassgdeldddlKEKVEKMKKEIELELAGVLKSMGlevigvtKKNKDTAEQTPPPNLQEKIES 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1155 LLETQEQEIEDGRAS---KTSLEHL---VTKLNEDREVKNAE-ILRMKEQLREMENLRLESQQLIEKNWLLQGQLddikr 1227
Cdd:PLN03229 654 LNEEINKKIERVIRSsdlKSKIELLkleVAKASKTPDVTEKEkIEALEQQIKQKIAEALNSSELKEKFEELEAEL----- 728
|
330 340 350
....*....|....*....|....*....|....*..
gi 74752937 1228 qKENSDQNHPDNQQLKNeqeESIKERLAKSKIVEEML 1264
Cdd:PLN03229 729 -AAARETAAESNGSLKN---DDDKEEDSKEDGSRVEV 761
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
706-916 |
4.31e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 706 EMNEQAFEAISEELRTVQEQMSALQAKLDE--EEHKNLKLQQHVDKLehhSTQMQELfSSERIDWTKQQEELLSQLNVLE 783
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLL---LQQLSEL-ESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 784 KQLQETQTKNDFLksevhdlrvvlhSADKELSSVKLEYSSFKTNQEKEFNKLSERH---MHVQLQLDNLRlenEKLLESK 860
Cdd:COG3206 247 AQLGSGPDALPEL------------LQSPVIQQLRAQLAELEAELAELSARYTPNHpdvIALRAQIAALR---AQLQQEA 311
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 74752937 861 ACLQDSYDNLQEIMKFEIDQLSRNLQNFKKENETLKSDLNNLMElLEAEKERNNKL 916
Cdd:COG3206 312 QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR-LEREVEVAREL 366
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1160-1374 |
5.57e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 41.03 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1160 EQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLI-----EKNWLLQGQLDDIKRQKENSDQ 1234
Cdd:pfam07888 58 EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSeelseEKDALLAQRAAHEARIRELEED 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1235 NHPDNQ---------------------QLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVER 1293
Cdd:pfam07888 138 IKTLTQrvleretelermkerakkagaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1294 TQTLESKAFQEKEQLRSKLEEMYEERERtsqeMEMLRKQVECLAEENGKLVGHQNLHQKIQYVVRLK--KENVRLAEETE 1371
Cdd:pfam07888 218 LTQKLTTAHRKEAENEALLEELRSLQER----LNASERKVEGLGEELSSMAAQRDRTQAELHQARLQaaQLTLQLADASL 293
|
...
gi 74752937 1372 KLR 1374
Cdd:pfam07888 294 ALR 296
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
418-1267 |
7.08e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.80 E-value: 7.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 418 FQEAMLFFKKSEQEKKSLIEKVTQLEDLTLKKEKFIQSNKMIVKFREDQIIRLEKLHKESRGGFLP----EEQDRLLSEL 493
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKimklDNEIKALKSR 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 494 RNEIQTLREQIEHHpRVAKYAMENHSLRE-ENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQQG-FSPKA 571
Cdd:TIGR00606 278 KKQMEKDNSELELK-MEKVFQGTDEQLNDlYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGrLQLQA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 572 QKEPCLFANTEKLKaQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKACKRqevsQLNKI 651
Cdd:TIGR00606 357 DRHQEHIRARDSLI-QSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQE----QADEI 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 652 HAETLKIITTPTKAYQLHSRPVPKLSPEMGSFGSLYTQNSSILDNDILNEPVPPEMNEQAFEAISEELRTVQEQMSALQA 731
Cdd:TIGR00606 432 RDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 732 KLDEeehKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQE----------ELLSQLNVL--EKQLQETQTKndfLKSE 799
Cdd:TIGR00606 512 DLDR---KLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQirkiksrhsdELTSLLGYFpnKKQLEDWLHS---KSKE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 800 VHDLRVVLHSADKELSSV---KLEYSSFKTNQEKEFNKLSERHMHV------QLQLDNLRLENEK------LLESKACLQ 864
Cdd:TIGR00606 586 INQTRDRLAKLNKELASLeqnKNHINNELESKEEQLSSYEDKLFDVcgsqdeESDLERLKEEIEKsskqraMLAGATAVY 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 865 DSYDNLQEI--------------MKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKE--------RNNKLSLQFEE 922
Cdd:TIGR00606 666 SQFITQLTDenqsccpvcqrvfqTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDemlglapgRQSIIDLKEKE 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 923 DKE------NSSKEILKVLEAV-RQEKQKETAKCEQQMAKV--------QKLEESLLATEKVISSLEKSRDSdkkvvADL 987
Cdd:TIGR00606 746 IPElrnklqKVNRDIQRLKNDIeEQETLLGTIMPEEESAKVcltdvtimERFQMELKDVERKIAQQAAKLQG-----SDL 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 988 MNQIQELRTSVCEKTETIDTLKQELkdinckynsalvdrEESRVLIKKQEVDILDLKETL------RLRILSEDIERDML 1061
Cdd:TIGR00606 821 DRTVQQVNQEKQEKQHELDTVVSKI--------------ELNRKLIQDQQEQIQHLKSKTnelkseKLQIGTNLQRRQQF 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1062 CEDLAHATEQLNML----TEASKKHSGLLQSAQEELTKKEALI-------QELQHKLNQKKEEVEQKkneyNFKMRQLEH 1130
Cdd:TIGR00606 887 EEQLVELSTEVQSLireiKDAKEQDSPLETFLEKDQQEKEELIssketsnKKAQDKVNDIKEKVKNI----HGYMKDIEN 962
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1131 VMDSAAEDPQSPKTpPHFQTHLAKLLETQEQEI---EDGRASKTSLE-----HLVTKLNEDREVKNAEILRMKEQLREME 1202
Cdd:TIGR00606 963 KIQDGKDDYLKQKE-TELNTVNAQLEECEKHQEkinEDMRLMRQDIDtqkiqERWLQDNLTLRKRENELKEVEEELKQHL 1041
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1203 NLRLESQQLIEKNWL--LQGQLDDIKRQ--KENSDQNHPDNQQLKNEQEESIKE-RLAKSKIVEEMLKMK 1267
Cdd:TIGR00606 1042 KEMGQMQVLQMKQEHqkLEENIDLIKRNhvLALGRQKGYEKEIKHFKKELREPQfRDAEEKYREMMIVMR 1111
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1248-1382 |
9.27e-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: 9.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1248 ESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERtqtLESkafqEKEQLRSKLEEMYEERERTSQEME 1327
Cdd:COG2433 379 EEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVER---LEA----EVEELEAELEEKDERIERLERELS 451
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 74752937 1328 MLRKQVECLAEENGKLvghQNLHQKIQyvvRLKKENVRLAEETEKLRAENVFLKE 1382
Cdd:COG2433 452 EARSEERREIRKDREI---SRLDREIE---RLERELEEERERIEELKRKLERLKE 500
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1010-1376 |
9.65e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1010 QELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLriLSEDIERDMLCEDLAHATEQLNmlteaskkhsgLLQSA 1089
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEKLLQLLPLYQELEALEAELA-----------ELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1090 QEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQL----EHVMDSAAEDPQSPKTPphfQTHLAKLLETQEQEIED 1165
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLslatEEELQDLAEELEELQQR---LAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1166 GRASKTSLEHLVTKLNEDREVKNAEILRM---------------KEQLREMENLRLESQQLIEKNWLLQGQLDDIKRQKE 1230
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEARLLLLiaaallallglggslLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74752937 1231 NSDQNHPDNQQLKNEQEESIKERLAKSKI--VEEMLKMKADLEEVQSALYNKEMECLRMTDEV---ERTQTLESKAFQEK 1305
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDlsPEELLELLDRIEELQELLREAEELEEELQLEEleqEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74752937 1306 EQLRSKLEEmYEERERTSQEMEMLRKQVECLAEENGKLVGHQNLHQKIQYVVRLKKENVRLAEETEKLRAE 1376
Cdd:COG4717 385 EELRAALEQ-AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREE 454
|
|
| |
