|
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: 624.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 25 DAIKVFVRIRPPAERSGsaDGEQNLCLSVLSSTSLRLHSNPePKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGT 104
Cdd:cd01373 1 DAVKVFVRIRPPAEREG--DGEYGQCLKKLSSDTLVLHSKP-PKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 105 IFAYGQTGSGKTFTMMGPSESDN-FSHNLRGVIPRSFEYLFSLIDREKEKAGAGKSFLCKCSFIEIYNEQIYDLLDSASA 183
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDNeSPHGLRGVIPRIFEYLFSLIQREKEKAGEGKSFLCKCSFLEIYNEQIYDLLDPASR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 184 GLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVNIRTSLLNL 263
Cdd:cd01373 158 NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFVNIRTSRLNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 264 VDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDVGNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPG 343
Cdd:cd01373 238 VDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPS 317
|
330 340 350
....*....|....*....|....*....|
gi 767923891 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 |
3.01e-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: 467.12 E-value: 3.01e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 26 AIKVFVRIRPPAERSGSadgEQNLCLSVLSSTSLRLHSN----PEPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGY 101
Cdd:cd00106 1 NVRVAVRVRPLNGREAR---SAKSVISVDGGKSVVLDPPknrvAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 102 NGTIFAYGQTGSGKTFTMMGPSESDnfshnlRGVIPRSFEYLFSLIDREKEKagaGKSFLCKCSFIEIYNEQIYDLLDSA 181
Cdd:cd00106 78 NGTIFAYGQTGSGKTYTMLGPDPEQ------RGIIPRALEDIFERIDKRKET---KSSFSVSASYLEIYNEKIYDLLSPV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 182 -SAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVNIRTSL 260
Cdd:cd00106 149 pKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVTSSK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 261 LNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgnGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANV 340
Cdd:cd00106 229 LNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD---GQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACI 305
|
330 340
....*....|....*....|.
gi 767923891 341 HPGSRCFGETLSTLNFAQRAK 361
Cdd:cd00106 306 SPSSENFEETLSTLRFASRAK 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
26-370 |
7.04e-152 |
|
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: 461.27 E-value: 7.04e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 26 AIKVFVRIRPPAERSGSADGEQNLCLSVLSSTSLRLHSNPEP---KTFTFDHVADVDTTQESVFATVAKSIVESCMSGYN 102
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKNRqgeKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 103 GTIFAYGQTGSGKTFTMMGPSESdnfshnlRGVIPRSFEYLFSLIDREKEkagaGKSFLCKCSFIEIYNEQIYDLLDSAS 182
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIGTPDS-------PGIIPRALKDLFEKIDKREE----GWQFSVKVSYLEIYNEKIRDLLNPSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 183 AGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVNIRTSLLN 262
Cdd:smart00129 150 KKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 263 LVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHP 342
Cdd:smart00129 230 LVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQ--HSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSP 307
|
330 340
....*....|....*....|....*...
gi 767923891 343 GSRCFGETLSTLNFAQRAKLIKNKAVVN 370
Cdd:smart00129 308 SSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
32-363 |
7.39e-144 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 439.70 E-value: 7.39e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 32 RIRPPAERSGSADGEQNL-CLSVLSSTSLRLHSNP--EPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGTIFAY 108
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVsVESVDSETVESSHLTNknRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 109 GQTGSGKTFTMMGPSESdnfshnlRGVIPRSFEYLFSLIDREKEKagagKSFLCKCSFIEIYNEQIYDLLDSASA---GL 185
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQ-------PGIIPRALEDLFDRIQKTKER----SEFSVKVSYLEIYNEKIRDLLSPSNKnkrKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 186 YLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEI-VNIRTSLLNLV 264
Cdd:pfam00225 150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGeESVKTGKLNLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 265 DLAGSERQKDTH-AEGMRLKEAGNINRSLSCLGQVITALVDvgnGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPG 343
Cdd:pfam00225 230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD---KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPS 306
|
330 340
....*....|....*....|
gi 767923891 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 |
1.72e-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: 353.69 E-value: 1.72e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 25 DAIKVFVRIRPPAERSGSADGEQNLCLSVLSST-SLRlhsNPE------PKTFTFDHVADVDTTQESVFATVAKSIVESC 97
Cdd:cd01371 1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEKRGQvSVR---NPKatanepPKTFTFDAVFDPNSKQLDVYDETARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 98 MSGYNGTIFAYGQTGSGKTFTMMGPSESDnfshNLRGVIPRSFEYLFSLIDREKEKagagKSFLCKCSFIEIYNEQIYDL 177
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDP----ELRGIIPNSFAHIFGHIARSQNN----QQFLVRVSYLEIYNEEIRDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 178 L-DSASAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVN- 255
Cdd:cd01371 150 LgKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 256 IRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgnGKQRHVCYRDSKLTFLLRDSLGGNAKTA 335
Cdd:cd01371 230 IRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD---GKSTHIPYRDSKLTRLLQDSLGGNSKTV 306
|
330 340
....*....|....*....|....*...
gi 767923891 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 |
9.39e-111 |
|
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276825 [Multi-domain] Cd Length: 321 Bit Score: 351.25 E-value: 9.39e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 26 AIKVFVRIRPPAERSGSADGEqnlCLSVLSSTSLrLHSNPEPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGTI 105
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQ---VAWEIDNDTI-YLVEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 106 FAYGQTGSGKTFTMMGPSESDnfshnlrGVIPRSFEYLFSLIDREKEKAgagksFLCKCSFIEIYNEQIYDLLDSASAGL 185
Cdd:cd01374 77 FAYGQTSSGKTFTMSGDEDEP-------GIIPLAIRDIFSKIQDTPDRE-----FLLRVSYLEIYNEKINDLLSPTSQNL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 186 YLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVN-IRTSLLNLV 264
Cdd:cd01374 145 KIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGtVRVSTLNLI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 265 DLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALvdvGNGK-QRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPG 343
Cdd:cd01374 225 DLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKL---SEGKvGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPA 301
|
330 340
....*....|....*....|
gi 767923891 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 |
2.92e-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: 341.88 E-value: 2.92e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 27 IKVFVRIRPPaerSGSADGEQNLCLSVLSSTSLRLH---SNPEPKTFTFDHVADVDTTQESVFATVaKSIVESCMSGYNG 103
Cdd:cd01366 4 IRVFCRVRPL---LPSEENEDTSHITFPDEDGQTIEltsIGAKQKEFSFDKVFDPEASQEDVFEEV-SPLVQSALDGYNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 104 TIFAYGQTGSGKTFTMMGPSESDnfshnlrGVIPRSFEYLFSLIdreKEKAGAGKSFLCKCSFIEIYNEQIYDLLDSASA 183
Cdd:cd01366 80 CIFAYGQTGSGKTYTMEGPPESP-------GIIPRALQELFNTI---KELKEKGWSYTIKASMLEIYNETIRDLLAPGNA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 184 G---LYLR-EHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEivNIRTS 259
Cdd:cd01366 150 PqkkLEIRhDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTG--EISVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 260 LLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALvdvgNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIAN 339
Cdd:cd01366 228 KLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL----RQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVN 303
|
330 340
....*....|....*....|....*.
gi 767923891 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 |
6.83e-104 |
|
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: 333.14 E-value: 6.83e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 26 AIKVFVRIRP--PAERSgsaDGEQNlCLSVLSST-SLRLHSNpepKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYN 102
Cdd:cd01372 2 SVRVAVRVRPllPKEII---EGCRI-CVSFVPGEpQVTVGTD---KSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 103 GTIFAYGQTGSGKTFTMMGPSESDNFSHNLrGVIPRSFEYLFSLIDREKEkagaGKSFLCKCSFIEIYNEQIYDLLDSAS 182
Cdd:cd01372 75 ATVLAYGQTGSGKTYTMGTAYTAEEDEEQV-GIIPRAIQHIFKKIEKKKD----TFEFQLKVSFLEIYNEEIRDLLDPET 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 183 ---AGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIVNIR-- 257
Cdd:cd01372 150 dkkPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSad 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 258 ------TSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvGNGKQRHVCYRDSKLTFLLRDSLGGN 331
Cdd:cd01372 230 dknstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGD-ESKKGAHVPYRDSKLTRLLQDSLGGN 308
|
330 340 350
....*....|....*....|....*....|...
gi 767923891 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 |
3.05e-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: 328.13 E-value: 3.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 25 DAIKVFVRIRPPAERSGSADGEqnLCLSVLSSTSLRLHSNPEPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGT 104
Cdd:cd01369 2 CNIKVVCRFRPLNELEVLQGSK--SIVKFDPEDTVVIATSETGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 105 IFAYGQTGSGKTFTMMGPSESDnfshNLRGVIPRSFEYLFSLIdrekEKAGAGKSFLCKCSFIEIYNEQIYDLLDSASAG 184
Cdd:cd01369 80 IFAYGQTSSGKTYTMEGKLGDP----ESMGIIPRIVQDIFETI----YSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 185 LYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIEsmEKSNEIVNIRTSLLNLV 264
Cdd:cd01369 152 LSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVK--QENVETEKKKSGKLYLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 265 DLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgnGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPGS 344
Cdd:cd01369 230 DLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD---GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSS 306
|
330
....*....|....*....
gi 767923891 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 |
2.37e-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: 2.37e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 25 DAIKVFVRIRPPAERSGSADG-------EQNLCLSVLSSTSLRLHSNPE-PKTFTFDHVAD-VDT------TQESVFATV 89
Cdd:cd01365 1 ANVKVAVRVRPFNSREKERNSkcivqmsGKETTLKNPKQADKNNKATREvPKSFSFDYSYWsHDSedpnyaSQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 90 AKSIVESCMSGYNGTIFAYGQTGSGKTFTMMGPSESdnfshnlRGVIPRSFEYLFSLIDREKEKAgagKSFLCKCSFIEI 169
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQ-------PGIIPRLCEDLFSRIADTTNQN---MSYSVEVSYMEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 170 YNEQIYDLLDS----ASAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITI- 244
Cdd:cd01365 151 YNEKVRDLLNPkpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLt 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 245 -ESMEKSNEIVNIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDVGN----GKQRHVCYRDSK 319
Cdd:cd01365 231 qKRHDAETNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskKKSSFIPYRDSV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 767923891 320 LTFLLRDSLGGNAKTAIIANVHPGSRCFGETLSTLNFAQRAKLIKNKAVVN 370
Cdd:cd01365 311 LTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
27-400 |
1.26e-97 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 341.91 E-value: 1.26e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 27 IKVFVRIRPPaersgSADGEQNLCLSVLSSTSLRLHSnpepKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGTIF 106
Cdd:PLN03188 100 VKVIVRMKPL-----NKGEEGEMIVQKMSNDSLTING----QTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVF 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 107 AYGQTGSGKTFTMMGPSE---SDNFSHNLRGVIPRSFEYLFSLIDREKEK-AGAGKSFLCKCSFIEIYNEQIYDLLDSAS 182
Cdd:PLN03188 171 AYGQTGSGKTYTMWGPANgllEEHLSGDQQGLTPRVFERLFARINEEQIKhADRQLKYQCRCSFLEIYNEQITDLLDPSQ 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 183 AGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKS--NEIVNIRTSL 260
Cdd:PLN03188 251 KNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSvaDGLSSFKTSR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 261 LNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDVGN-GKQRHVCYRDSKLTFLLRDSLGGNAKTAIIAN 339
Cdd:PLN03188 331 INLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCA 410
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767923891 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 |
7.85e-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: 306.17 E-value: 7.85e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 27 IKVFVRIRP--PAERSGSADGEQNL---CLSVLSSTSLRLHSNPEpKTFTFDHVADVDTTQESVFATVAKSIVESCMSGY 101
Cdd:cd01364 4 IQVVVRCRPfnLRERKASSHSVVEVdpvRKEVSVRTGGLADKSST-KTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 102 NGTIFAYGQTGSGKTFTMMGpSESDNFSHNLR-----GVIPRSFEYLFSLIDREkekagaGKSFLCKCSFIEIYNEQIYD 176
Cdd:cd01364 83 NCTIFAYGQTGTGKTYTMEG-DRSPNEEYTWEldplaGIIPRTLHQLFEKLEDN------GTEYSVKVSYLEIYNEELFD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 177 LLDSAS-----AGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSN 251
Cdd:cd01364 156 LLSPSSdvserLRMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 252 EIVN-IRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgngKQRHVCYRDSKLTFLLRDSLGG 330
Cdd:cd01364 236 DGEElVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE----RAPHVPYRESKLTRLLQDSLGG 311
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 767923891 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 |
1.53e-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: 299.64 E-value: 1.53e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 27 IKVFVRIRPPAERSGSA------------------DGEQNLCLSVLSSTSLRLHSNPEPKTFTFDHVADVDTTQESVFAT 88
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEgfrrivkvmdnhmlvfdpKDEEDGFFHGGSNNRDRRKRRNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 89 VAKSIVESCMSGYNGTIFAYGQTGSGKTFTMMGPSESDnfshnlrGVIPRSFEYLFSLIDREKEKagagKSFLCKCSFIE 168
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP-------GLMVLTMKELFKRIESLKDE----KEFEVSMSYLE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 169 IYNEQIYDLLDSASAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESME 248
Cdd:cd01370 151 IYNETIRDLLNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 249 KSNEIV-NIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvGNGKQRHVCYRDSKLTFLLRDS 327
Cdd:cd01370 231 KTASINqQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD-PGKKNKHIPYRDSKLTRLLKDS 309
|
330 340 350
....*....|....*....|....*....|....*.
gi 767923891 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 |
3.17e-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: 278.69 E-value: 3.17e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 26 AIKVFVRIRPPAERSGS--ADGEQNLCLSVLSSTSLR---LHSNPEPKTFTFDHVADvDTTQESVFATVAKSIVESCMSG 100
Cdd:cd01375 1 KVQAFVRVRPTDDFAHEmiKYGEDGKSISIHLKKDLRrgvVNNQQEDWSFKFDGVLH-NASQELVYETVAKDVVSSALAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 101 YNGTIFAYGQTGSGKTFTMMGPSEsdNFSHnlRGVIPRSFEYLFSLIDREKEKAgagksFLCKCSFIEIYNEQIYDLLDS 180
Cdd:cd01375 80 YNGTIFAYGQTGAGKTFTMTGGTE--NYKH--RGIIPRALQQVFRMIEERPTKA-----YTVHVSYLEIYNEQLYDLLST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 181 ------ASAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIV 254
Cdd:cd01375 151 lpyvgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLSSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 255 NIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALvdvGNGKQRHVCYRDSKLTFLLRDSLGGNAKT 334
Cdd:cd01375 231 KYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIAL---SDKDRTHVPFRQSKLTHVLRDSLGGNCNT 307
|
330 340
....*....|....*....|....*..
gi 767923891 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 |
2.29e-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: 2.29e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 25 DAIKVFVRIRPPAERSGSADGEqnLCLSVLSSTSLRLHS------NPEPKT-------FTFDHVADVDTTQESVFATVAK 91
Cdd:cd01368 1 DPVKVYLRVRPLSKDELESEDE--GCIEVINSTTVVLHPpkgsaaNKSERNggqketkFSFSKVFGPNTTQKEFFQGTAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 92 SIVESCMSGYNGTIFAYGQTGSGKTFTMMGPSESdnfshnlRGVIPRSFEYLFSLIdrekekagagKSFLCKCSFIEIYN 171
Cdd:cd01368 79 PLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGD-------GGILPRSLDVIFNSI----------GGYSVFVSYIEIYN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 172 EQIYDLLDSAS-------AGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITI 244
Cdd:cd01368 142 EYIYDLLEPSPssptkkrQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 245 ------ESMEKSNEIVNIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITAL-VDVGNGKQRHVCYRD 317
Cdd:cd01368 222 vqapgdSDGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLrENQLQGTNKMVPFRD 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 767923891 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 |
8.79e-76 |
|
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: 8.79e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 27 IKVFVRIRPPAERSGSADGEQnlCLSVLSSTSLRLhSNP----EPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYN 102
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPS--CVSGIDSCSVEL-ADPrnhgETLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 103 GTIFAYGQTGSGKTFTMMGpsesdnfSHNLRGVIPRSFEYLFSLIDREKEKAGAgksflcKCSFIEIYNEQIYDLLDSAS 182
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLG-------SPEQPGLMPLTVMDLLQMTRKEAWALSF------TMSYLEIYQEKILDLLEPAS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 183 AGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEkSNEIVNIRTSLLN 262
Cdd:cd01376 146 KELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRE-RLAPFRQRTGKLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 263 LVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALvdvgNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHP 342
Cdd:cd01376 225 LIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL----NKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAP 300
|
330
....*....|....*....
gi 767923891 343 GSRCFGETLSTLNFAQRAK 361
Cdd:cd01376 301 ERTFYQDTLSTLNFAARSR 319
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
27-504 |
1.05e-72 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 253.89 E-value: 1.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 27 IKVFVRIRPpaersgsadGEQNLCLSVLSSTSLRLHSNPEPKTFTFDHVADVDTTQESVFATVAKSIVESCMSGYNGTIF 106
Cdd:COG5059 24 IKSTIRIIP---------GELGERLINTSKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 107 AYGQTGSGKTFTMMGpsesdnfSHNLRGVIPRSFEYLFSLIDREKekagAGKSFLCKCSFIEIYNEQIYDLLDSASAGLY 186
Cdd:COG5059 95 AYGQTGSGKTYTMSG-------TEEEPGIIPLSLKELFSKLEDLS----MTKDFAVSISYLEIYNEKIYDLLSPNEESLN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 187 LREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKSNEIvnIRTSLLNLVDL 266
Cdd:COG5059 164 IREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGT--SETSKLSLVDL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 267 AGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgNGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPGSRC 346
Cdd:COG5059 242 AGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGD--KKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 347 FGETLSTLNFAQRAKLIKNKAVVNedtqgNVSQLQAEVKRLKEQLAELASGQTPPESFLTRDKKKTNYMEYFQEAMLFFK 426
Cdd:COG5059 320 FEETINTLKFASRAKSIKNKIQVN-----SSSDSSREIEEIKFDLSEDRSEIEILVFREQSQLSQSSLSGIFAYMQSLKK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 427 KSEQEKKS--LIEKVTQL---EDLTLKKEKFiQSNKMIVKFREDQIIRLEKLHKESRggFLPEEQDRLLSELRNEIQTLR 501
Cdd:COG5059 395 ETETLKSRidLIMKSIISgtfERKKLLKEEG-WKYKSTLQFLRIEIDRLLLLREEEL--SKKKTKIHKLNKLRHDLSSLL 471
|
...
gi 767923891 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 |
2.51e-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: 2.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 27 IKVFVRIRP---PAERSGSAD---GEQNLCLSVLS-STSLRLHSNPEPKTFTFDHVADVDTTQESVFATVAKSIVESCMS 99
Cdd:cd01367 2 IKVCVRKRPlnkKEVAKKEIDvvsVPSKLTLIVHEpKLKVDLTKYIENHTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 100 GYNGTIFAYGQTGSGKTFTMMGpseSDNFSHNLRGVIPRSFEYLFSLIDREKEKAGAGKSflckCSFIEIYNEQIYDLLd 179
Cdd:cd01367 82 GGKATCFAYGQTGSGKTYTMGG---DFSGQEESKGIYALAARDVFRLLNKLPYKDNLGVT----VSFFEIYGGKVFDLL- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 180 SASAGLYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFTITIESMEKsneivNIRTS 259
Cdd:cd01367 154 NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGT-----NKLHG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 260 LLNLVDLAGSERQKDT-HAEGMRLKEAGNINRSLSCLGQVITALVDvgngKQRHVCYRDSKLTFLLRDSL-GGNAKTAII 337
Cdd:cd01367 229 KLSFVDLAGSERGADTsSADRQTRMEGAEINKSLLALKECIRALGQ----NKAHIPFRGSKLTQVLKDSFiGENSKTCMI 304
|
330 340
....*....|....*....|....
gi 767923891 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 |
2.53e-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: 2.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 29 VFVRIRPPaersgsadgeqnlclsvlsstsLRLHSNPEPKTFTFDHVADVDTTQESVFATVAKsIVESCMSGYNG-TIFA 107
Cdd:cd01363 1 VLVRVNPF----------------------KELPIYRDSKIIVFYRGFRRSESQPHVFAIADP-AYQSMLDGYNNqSIFA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 108 YGQTGSGKTFTMMgpsesdnfshnlrGVIPRSFEYLFSLIDREKEKAGAGKSFLCKCSfieiyNEQIYDLLDSasaglyl 187
Cdd:cd01363 58 YGESGAGKTETMK-------------GVIPYLASVAFNGINKGETEGWVYLTEITVTL-----EDQILQANPI------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 188 rehikkgvfvvgaveqvvtsaAEAYqvlsggwrnrRVASTSMNRESSRSHAVFTItiesmeksneivnirtsllnLVDLA 267
Cdd:cd01363 113 ---------------------LEAF----------GNAKTTRNENSSRFGKFIEI--------------------LLDIA 141
|
250 260 270
....*....|....*....|....*....|....
gi 767923891 268 GSERqkdthaegmrlkeagnINRSLSCLGQVITA 301
Cdd:cd01363 142 GFEI----------------INESLNTLMNVLRA 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
579-1310 |
1.68e-17 |
|
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: 88.96 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 579 ANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKACKRQevsqlnkihaetLKE 658
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI------------LRE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 659 QMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQElfsseridwtkQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLR 738
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEE-----------KLEELKEELESLEAELEELEAELEELESRLEELE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 739 VVLHSADKELSSVKLEYSSfktnQEKEFNKLSERHMHVQLQLDNLRLENEKLleskaclqdsydnLQEIMKFEIDQLSRN 818
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIAS----LNNEIERLEARLERLEDRRERLQQEIEEL-------------LKKLEEAELKELQAE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 819 LQNFKKENETLKSDLNNLMELLEAEKERNNKLS--LQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEES 896
Cdd:TIGR02168 442 LEELEEELEELQEELERLEEALEELREELEEAEqaLDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGI 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 897 LLATEKVISSLEKSRDSDKKVVADLMNQIqeLRTSVCEKTETIDTLKQ---------ELKDIncKYNSALVDREESRVLI 967
Cdd:TIGR02168 522 LGVLSELISVDEGYEAAIEAALGGRLQAV--VVENLNAAKKAIAFLKQnelgrvtflPLDSI--KGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 968 KKQEVDILDLKET-LRLRILSEDI-ERDMLCEDLAHATEQLNMLTE---------------------ASKKHSGLLQSAQ 1024
Cdd:TIGR02168 598 EGFLGVAKDLVKFdPKLRKALSYLlGGVLVVDDLDNALELAKKLRPgyrivtldgdlvrpggvitggSAKTNSSILERRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1025 E--ELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDpqspktpphfQTHLAKLLETQEQEIEDGRA 1102
Cdd:TIGR02168 678 EieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ----------ISALRKDLARLEAEVEQLEE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1103 SKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEKnwlLQGQLDDIKRQKENSdqnhpdNQQLKNEQEE 1182
Cdd:TIGR02168 748 RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ---LKEELKALREALDEL------RAELTLLNEE 818
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1183 SIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEERERTSQEMEM 1262
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 767923891 1263 LRKQVECLAEENGKLV-GHQNLHQKI-QYVVRLKKENVRLAEETEKLRAE 1310
Cdd:TIGR02168 899 LSEELRELESKRSELRrELEELREKLaQLELRLEGLEVRIDNLQERLSEE 948
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
27-178 |
2.32e-17 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 79.96 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 27 IKVFVRIRPPAERsgsadgeqNLCLSVLSSTSLRLHSNPEPKTFTFDHVADVDTTQESVFATVaKSIVESCMSGYNGTIF 106
Cdd:pfam16796 22 IRVFARVRPELLS--------EAQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIF 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767923891 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 ... |
489-1214 |
2.68e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.17 E-value: 2.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 489 LLSELRNEIQTLREQiehhprvAKYAMENHSLREENRRLRLLEPVKRAQEMDAqtiaKLEKAFSEISGMEKSDKNQQGFS 568
Cdd:TIGR02168 194 ILNELERQLKSLERQ-------AEKAERYKELKAELRELELALLVLRLEELRE----ELEELQEELKEAEEELEELTAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 569 PKAQKE-PCLFANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLlEATKACKRQEVSQ 647
Cdd:TIGR02168 263 QELEEKlEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL-ESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 648 LNKIhAETLKEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQmqelFSSERIDWTKQQEELLSQLNVLEKQLQETQTKN 727
Cdd:TIGR02168 342 LEEK-LEELKEELESLEAELEELEAELEELESRLEELEEQLET----LRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 728 DFLKSEVHDLRVVLHSADKELSSVKLEYSsfktnqEKEFNKLSERHMHVQLQLDNLRLENEKLLESkacLQDSYDNLQEI 807
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAELEEL------EEELEELQEELERLEEALEELREELEEAEQA---LDAAERELAQL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 808 mKFEIDQLSRNLQNFKKENETLKSDLNN----------LMELLEAEK-------------------ERNNKLSLQFEEDK 858
Cdd:TIGR02168 488 -QARLDSLERLQENLEGFSEGVKALLKNqsglsgilgvLSELISVDEgyeaaieaalggrlqavvvENLNAAKKAIAFLK 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 859 ENSS-------------KEILKVLEAVRQEK---QKETAKCEQQMAKVQKLEESLLATEKVISSL--------------- 907
Cdd:TIGR02168 567 QNELgrvtflpldsikgTEIQGNDREILKNIegfLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLdnalelakklrpgyr 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 908 ----------------------EKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRV 965
Cdd:TIGR02168 647 ivtldgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 966 LIKKQEVDILDLK---ETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQS-------AQEELTKKEALIQ 1035
Cdd:TIGR02168 727 QISALRKDLARLEaevEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEleaqieqLKEELKALREALD 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1036 ELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLN 1115
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1116 EDREVKNAEILRMKEQLREMENLRLESQQLIEKnwlLQGQLDDIKRQKensdqnhpdnQQLKNeQEESIKERLAKSKIV- 1194
Cdd:TIGR02168 887 EALALLRSELEELSEELRELESKRSELRRELEE---LREKLAQLELRL----------EGLEV-RIDNLQERLSEEYSLt 952
|
810 820
....*....|....*....|.
gi 767923891 1195 -EEMLKMKADLEEVQSALYNK 1214
Cdd:TIGR02168 953 lEEAEALENKIEDDEEEARRR 973
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
582-1254 |
5.11e-12 |
|
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: 70.92 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 582 EKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQ-----------KANLNLENL----------LEATKAC 640
Cdd:pfam15921 81 EEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQmerdamadirrRESQSQEDLrnqlqntvheLEAAKCL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 641 KRQ-------EVSQLNKI---HAETLKEQMSALqakLDEEEHKNLKLQQHVDKLEHH--------STQMQEL-----FSS 697
Cdd:pfam15921 161 KEDmledsntQIEQLRKMmlsHEGVLQEIRSIL---VDFEEASGKKIYEHDSMSTMHfrslgsaiSKILRELdteisYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 698 ERIDWTKQQEELL--SQLNVLEKQLQETQTKNDFLKSEvHDLRVVlhSADKELSSVKLEYSSFKTN------QEKEFNKL 769
Cdd:pfam15921 238 GRIFPVEDQLEALksESQNKIELLLQQHQDRIEQLISE-HEVEIT--GLTEKASSARSQANSIQSQleiiqeQARNQNSM 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 770 SERHM-HVQLQLDNLRLEnekLLESKACLQDSYDNLQEIM----------KFEIDQLSRNLQNFKKENETLKSDLNNLME 838
Cdd:pfam15921 315 YMRQLsDLESTVSQLRSE---LREAKRMYEDKIEELEKQLvlanselteaRTERDQFSQESGNLDDQLQKLLADLHKREK 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 839 LLEAEKERNNKL------------SLQFEEDKENSSKEILK-VLEAVRQEKQketAKCEQQMAKVQKLEESLLATEKVIS 905
Cdd:pfam15921 392 ELSLEKEQNKRLwdrdtgnsitidHLRRELDDRNMEVQRLEaLLKAMKSECQ---GQMERQMAAIQGKNESLEKVSSLTA 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 906 SLEKSRDSDKKVVADLMNQIQELRTSvcEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLK------- 978
Cdd:pfam15921 469 QLESTKEMLRKVVEELTAKKMTLESS--ERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhlrnv 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 979 ----ETLRLRIlsedIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELT------------------KKEALIQE 1036
Cdd:pfam15921 547 qtecEALKLQM----AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEkeindrrlelqefkilkdKKDAKIRE 622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1037 LQHKLNQKKEEveqKKNEYNFKMRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNE 1116
Cdd:pfam15921 623 LEARVSDLELE---KVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKM 699
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1117 DREVKNAEILRMKEQLREME-------NLRLESQQLIEKNwllQGQLDDIKRQ---KENSDQNHPDNQQLKNEQEESIKE 1186
Cdd:pfam15921 700 QLKSAQSELEQTRNTLKSMEgsdghamKVAMGMQKQITAK---RGQIDALQSKiqfLEEAMTNANKEKHFLKEEKNKLSQ 776
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767923891 1187 RLA-----KSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESKafQEKEQLRSKLEEMYEERE 1254
Cdd:pfam15921 777 ELStvateKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQR--QEQESVRLKLQHTLDVKE 847
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
615-1197 |
3.27e-11 |
|
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: 68.22 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 615 ELESELQSLQKANLNLENLLEATKACKRQEVSQLNKIH---------------------AETLKEQMSALQAKL----DE 669
Cdd:pfam15921 228 ELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHqdrieqliseheveitgltekASSARSQANSIQSQLeiiqEQ 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 670 EEHKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSE-------VHDLRVVLH 742
Cdd:pfam15921 308 ARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnlddqLQKLLADLH 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 743 SADKELSsvkleyssfktnQEKEFNK-LSERHMHVQLQLDNLRLEneklLESKACLQDSYDNLQEIMKFEID-QLSRNLQ 820
Cdd:pfam15921 388 KREKELS------------LEKEQNKrLWDRDTGNSITIDHLRRE----LDDRNMEVQRLEALLKAMKSECQgQMERQMA 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 821 NFKKENETLKSdLNNLMELLEAEKE---------RNNKLSLQFEE----DKENSSKEILKVLEAVRQEKQKETAKCEQQM 887
Cdd:pfam15921 452 AIQGKNESLEK-VSSLTAQLESTKEmlrkvveelTAKKMTLESSErtvsDLTASLQEKERAIEATNAEITKLRSRVDLKL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 888 AKVQKL---EESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESR 964
Cdd:pfam15921 531 QELQHLkneGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFK 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 965 VLIKKQEVDILDLKETL----------------RLRILsEDI--ERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEE 1026
Cdd:pfam15921 611 ILKDKKDAKIRELEARVsdlelekvklvnagseRLRAV-KDIkqERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEE 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1027 LtkkEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAaedpqspktpphfqTHLAKLLETQEQEIEDGRASKTS 1106
Cdd:pfam15921 690 M---ETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVA--------------MGMQKQITAKRGQIDALQSKIQF 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1107 LEHLVTKLNEDREVKNAEILRMKEQLR-----------EMENLRLESQQLIEKNWLLQGQLDdikrqkENSDQNHPDNQQ 1175
Cdd:pfam15921 753 LEEAMTNANKEKHFLKEEKNKLSQELStvateknkmagELEVLRSQERRLKEKVANMEVALD------KASLQFAECQDI 826
|
650 660
....*....|....*....|..
gi 767923891 1176 LKNEQEESIKERLAKSKIVEEM 1197
Cdd:pfam15921 827 IQRQEQESVRLKLQHTLDVKEL 848
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
978-1268 |
4.90e-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: 67.77 E-value: 4.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 978 KETLRLRILSEDIERdmLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNF 1057
Cdd:TIGR02168 222 LRELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1058 KMRQLEHVMDSAAEDPQSPKtpphfqtHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMEN 1137
Cdd:TIGR02168 300 LEQQKQILRERLANLERQLE-------ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1138 LRLESQQLIEKnwlLQGQLDDIKRQkENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEME 1217
Cdd:TIGR02168 373 RLEELEEQLET---LRSKVAQLELQ-IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE 448
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 767923891 1218 CLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEERERTSQEMEMLRKQVE 1268
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
582-1322 |
9.80e-11 |
|
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: 66.53 E-value: 9.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 582 EKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKACKRQEVSQLNKIHAETLKEQMS 661
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 662 ALQakldeEEHKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVL 741
Cdd:pfam02463 256 SKQ-----EIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 742 HSADKELSSVKLEYSSFKTNQEKEFNK---LSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEIMKFEIDQLSRN 818
Cdd:pfam02463 331 KKEKEEIEELEKELKELEIKREAEEEEeeeLEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLL 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 819 LQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQ------- 891
Cdd:pfam02463 411 LELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQeqlelll 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 892 ---KLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLK---------QELKDINCKYNSALVD 959
Cdd:pfam02463 491 srqKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIstavivevsATADEVEERQKLVRAL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 960 REESRVLIKKQEVDILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQH 1039
Cdd:pfam02463 571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRK 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1040 KLNQKKEEVEQKKNEYNF-KMRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHL---VTKLN 1115
Cdd:pfam02463 651 GVSLEEGLAEKSEVKASLsELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELladRVQEA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1116 EDREVKNAEILRMKEQLREMENLRLESQQLIEKNWLLQGQLDDIK---------------------------RQKENSDQ 1168
Cdd:pfam02463 731 QDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKElaeerekteklkveeekeeklkaqeeeLRALEEEL 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1169 NHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEE 1248
Cdd:pfam02463 811 KEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELES 890
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767923891 1249 MYEERERTSQEMEMLRKQVECLAEENGKLVGHQNLHQKIQYVVRLKKENVRLAEETEKLRAENVFLKEKKRSES 1322
Cdd:pfam02463 891 KEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKR 964
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
707-1310 |
1.51e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 707 EELLSQLNVLEKQLQETQtKNDFLKSEVHDLRV-----VLHSADKELSSVKLEYSSfktnQEKEFNKLSERHMHVQLQLD 781
Cdd:TIGR02168 196 NELERQLKSLERQAEKAE-RYKELKAELRELELallvlRLEELREELEELQEELKE----AEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 782 NLRLENEKLLESKACLQDSYDNLQEimkfEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLslqfeEDKENS 861
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALAN----EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL-----AEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 862 SKEILKVLEAVRQEKQKETAKCEqqmAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDT 941
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELE---AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 942 LKQELKDINCKYNSALVDREESRVLIKKQEVDILD--------LKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEAS 1013
Cdd:TIGR02168 419 LQQEIEELLKKLEEAELKELQAELEELEEELEELQeelerleeALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1014 KKHSGLLQSAQEELTKKE-------------------------ALIQELQH----KLNQKKEEVE-QKKNEYNFKMRQLE 1063
Cdd:TIGR02168 499 ENLEGFSEGVKALLKNQSglsgilgvlselisvdegyeaaieaALGGRLQAvvveNLNAAKKAIAfLKQNELGRVTFLPL 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1064 HVM---DSAAEDPQSPKTPPHFQThLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNA------------EILR- 1127
Cdd:TIGR02168 579 DSIkgtEIQGNDREILKNIEGFLG-VAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKlrpgyrivtldgDLVRp 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1128 --------------MKEQLREMENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQQLKNEQEESI---KERLAK 1190
Cdd:TIGR02168 658 ggvitggsaktnssILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIsalRKDLAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1191 SKIVEEMLKMKADLEEVQSALYNKEMECLRmtDEVERTQTLESKAFQEKEQLRSKLEEMYEERERTSQEMEMLRKQVECL 1270
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELE--ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 767923891 1271 AEENGKLVGHQNLHQKiqYVVRLKKENVRLAEETEKLRAE 1310
Cdd:TIGR02168 816 NEEAANLRERLESLER--RIAATERRLEDLEEQIEELSED 853
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
968-1268 |
4.28e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 60.91 E-value: 4.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 968 KKQEVDILDLKETLRLRILSEDIERDMlcedlahatEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEE 1047
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREV---------ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1048 VEQKKNEynfKMRQLEHVMDSaaedpQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLN-----------E 1116
Cdd:pfam17380 357 ERKRELE---RIRQEEIAMEI-----SRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQqqkvemeqiraE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1117 DREVKNAEILRMKEQ-LREMENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQQLKNEQEESIKERLA--KSKI 1193
Cdd:pfam17380 429 QEEARQREVRRLEEErAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEerKQAM 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1194 VEEMLKMK---ADLEEVQSALYNKEMEclRMTDEVERTQTLESKAFQEKEQL------RSKLEEMYEERERTSQEMEMLR 1264
Cdd:pfam17380 509 IEEERKRKlleKEMEERQKAIYEEERR--REAEEERRKQQEMEERRRIQEQMrkateeRSRLEAMEREREMMRQIVESEK 586
|
....
gi 767923891 1265 KQVE 1268
Cdd:pfam17380 587 ARAE 590
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
405-1055 |
5.04e-09 |
|
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: 61.14 E-value: 5.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 405 LTRDKKKTNYMEYFQEAML-------FFKKSEQEKKSLI------EKVTQLEDLTLKKEKFIQSNKMIVKFRedqiIRLE 471
Cdd:TIGR00618 131 VIHDLLKLDYKTFTRVVLLpqgefaqFLKAKSKEKKELLmnlfplDQYTQLALMEFAKKKSLHGKAELLTLR----SQLL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 472 KLHKESRGGFLPEEQDRLLSELRNEIQTLREQIEHHprvAKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAF 551
Cdd:TIGR00618 207 TLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH---AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 552 SEISGMEKSD------KNQQGFSPKAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQK 625
Cdd:TIGR00618 284 ERINRARKAAplaahiKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEV 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 626 ANLNLENLLEATKACKRQEVSQLNKIHAETLKEQMSALQAKLDEEEHKNLKLQQHVDKLEHH--STQMQELFSSERIDWT 703
Cdd:TIGR00618 364 ATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQlaHAKKQQELQQRYAELC 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 704 KQQEELLSQLNVLEK-QLQETQTKNDFLKSEVHDLRvVLHSADKELSSVKLEYSSFKTNQEKEFNKlSERHMHVQLQLDN 782
Cdd:TIGR00618 444 AAAITCTAQCEKLEKiHLQESAQSLKEREQQLQTKE-QIHLQETRKKAVVLARLLELQEEPCPLCG-SCIHPNPARQDID 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 783 LRLENEKLLESkacLQDSYDNLQEIMK---FEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLsLQFEED-- 857
Cdd:TIGR00618 522 NPGPLTRRMQR---GEQTYAQLETSEEdvyHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNL-QNITVRlq 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 858 ---KENSSKEILKVLEAVRQEKQK-------ETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVAD---LMNQ 924
Cdd:TIGR00618 598 dltEKLSEAEDMLACEQHALLRKLqpeqdlqDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLpkeLLAS 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 925 IQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETL--RLRILSEDI-----ERDMLCE 997
Cdd:TIGR00618 678 RQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLaaREDALNQSLkelmhQARTVLK 757
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 767923891 998 DLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEY 1055
Cdd:TIGR00618 758 ARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD 815
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
585-1169 |
6.31e-09 |
|
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: 60.42 E-value: 6.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 585 KAQLLQIQTELNNSKQEYEEFKELTRK---RQLELESELQSLQKANLNLENLLEATKACKRQEVSQLNKIHAE--TLKEQ 659
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQKKENKKNIDKfltEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNidKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 660 MSALQAKL---DEEEHKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLS---QLNVLEKQLQETQTKNDFLKSE 733
Cdd:TIGR04523 196 LLKLELLLsnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtqtQLNQLKDEQNKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 734 VHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSErhmhvqlqlDNLRLENEKLLESKACLQDSYDNLQEiMKFEID 813
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELK---------SELKNQEKKLEEIQNQISQNNKIISQ-LNEQIS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 814 QLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQKETakceqqmaKVQKL 893
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE--------QIKKL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 894 EESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVD 973
Cdd:TIGR04523 418 QQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKE 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 974 ILDLKEtlrlrilsediERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELqhKLNQKKEEVEQKKN 1053
Cdd:TIGR04523 498 LKKLNE-----------EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD--DFELKKENLEKEID 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1054 EYNFKMRQLEHVMDSAAEDpqspktpphfQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLR 1133
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKK----------QEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIK 634
|
570 580 590
....*....|....*....|....*....|....*.
gi 767923891 1134 EMENLRLESQQLIEknwLLQGQLDDIKRQKENSDQN 1169
Cdd:TIGR04523 635 NIKSKKNKLKQEVK---QIKETIKEIRNKWPEIIKK 667
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
356-928 |
2.40e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.54 E-value: 2.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 356 FAQRAKLIKNKAVVNEDTQGNVSQLQAEVKRLKEQLAELASGQTPPESfltRDKKKTNYMEYFQEAMLFFKKSEQEKKSL 435
Cdd:PRK03918 202 LEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELES---LEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 436 IEKVTQLEDLTLKKEKFIQsnkmIVKFREDQIIRLEKLHKEsrggflpeeqdrlLSELRNEIQTLREQIEHHPRVAKYAM 515
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIK----LSEFYEEYLDELREIEKR-------------LSRLEEEINGIEERIKELEEKEERLE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 516 ENHSLREE-NRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKsdknqqgfspkaqkepclfantEKLKAQLLqiqtE 594
Cdd:PRK03918 342 ELKKKLKElEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP----------------------EKLEKELE----E 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 595 LNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKACKRQEVSQLNKIHAETLKEQMSALQAKLDEEEHKN 674
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 675 LKLQQHVDKLEHHSTQMQELFSSERI-DWTKQQEELLSQLNVleKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKl 753
Cdd:PRK03918 476 RKLRKELRELEKVLKKESELIKLKELaEQLKELEEKLKKYNL--EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE- 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 754 EYSSFKTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKA-----------CLQDSYDNLQ------EIMKFEIDQLS 816
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLkelepfyneylELKDAEKELEreekelKKLEEELDKAF 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 817 RNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEES 896
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
570 580 590
....*....|....*....|....*....|....*.
gi 767923891 897 LLATEKVISSLEKSRDSDKKVVADL----MNQIQEL 928
Cdd:PRK03918 713 LEKLEKALERVEELREKVKKYKALLkeraLSKVGEI 748
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
615-1266 |
2.65e-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: 58.29 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 615 ELESELQSLQKANLNLenlleatkackRQEVSQLNKIHAETLKeqMSALQAKLDEEEHKNLKLQQHVDKLEhhsTQMQEL 694
Cdd:pfam10174 196 HLEVLLDQKEKENIHL-----------REELHRRNQLQPDPAK--TKALQTVIEMKDTKISSLERNIRDLE---DEVQML 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 695 FSSERIDWTKQQEELlsqlnvleKQLQETQTKNDFLKSEVHDLrvvlhsaDKELSSVKLEYSSFKTNQEKEFNKLSERHM 774
Cdd:pfam10174 260 KTNGLLHTEDREEEI--------KQMEVYKSHSKFMKNKIDQL-------KQELSKKESELLALQTKLETLTNQNSDCKQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 775 HVQLQLDNLRLENEKllesKACLQDSYDNLQ---EIMKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLS 851
Cdd:pfam10174 325 HIEVLKESLTAKEQR----AAILQTEVDALRlrlEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQ 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 852 LQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAkVQKLEESLLATEKVISSLEKSRDSDKKvvadlmnqiqelrts 931
Cdd:pfam10174 401 KKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTA-LTTLEEALSEKERIIERLKEQREREDR--------------- 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 932 vcEKTETIDTLKQELKDINCKYNSALVDREEsrvlikkQEVDILDLKEtlrlrilsedierdmlcedlaHATeqlNMLTE 1011
Cdd:pfam10174 465 --ERLEELESLKKENKDLKEKVSALQPELTE-------KESSLIDLKE---------------------HAS---SLASS 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1012 ASKKHSGLLQSAQEELTKKEALIQ-ELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDpqSPKTpphfQTHLAKLL 1090
Cdd:pfam10174 512 GLKKDSKLKSLEIAVEQKKEECSKlENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKEE--SGKA----QAEVERLL 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1091 ET-QEQEIEdgrasktslehlvtKLNEDREVKNAEIL---RMKEQLREMENLRLESQQLIEKNwllQGQLDDIKRQKENS 1166
Cdd:pfam10174 586 GIlREVENE--------------KNDKDKKIAELESLtlrQMKEQNKKVANIKHGQQEMKKKG---AQLLEEARRREDNL 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1167 DQNHpdnqqlKNEQEESIKERLAKSKivEEMLKMKADLEEVQSALYNKE--MECLRMTDEVERTQTLESK------AFQE 1238
Cdd:pfam10174 649 ADNS------QQLQLEELMGALEKTR--QELDATKARLSSTQQSLAEKDghLTNLRAERRKQLEEILEMKqeallaAISE 720
|
650 660
....*....|....*....|....*...
gi 767923891 1239 KEQLRSKLEEMYEERERTSQEMEMLRKQ 1266
Cdd:pfam10174 721 KDANIALLELSSSKKKKTQEEVMALKRE 748
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
424-1255 |
2.77e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.54 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 424 FFKKSEQEKKSLIEKVTQLEDLTLKKEKF----------IQSNKMIVKFREDQIIRL--EKLHKESRGGFLPEEQDRLLS 491
Cdd:TIGR02169 147 FISMSPVERRKIIDEIAGVAEFDRKKEKAleeleeveenIERLDLIIDEKRQQLERLrrEREKAERYQALLKEKREYEGY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 492 ELRNEIQTLREQIEHHPRvakyamENHSLREEnrrlrlLEPVKRAQEMDAQTIAKLEKAFSEISG--MEKSDKNQQGFSP 569
Cdd:TIGR02169 227 ELLKEKEALERQKEAIER------QLASLEEE------LEKLTEEISELEKRLEEIEQLLEELNKkiKDLGEEEQLRVKE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 570 KAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKA---CKRQEVS 646
Cdd:TIGR02169 295 KIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEeleDLRAELE 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 647 QLNKIHAETLKEQMSaLQAKLDEEEHKNLKLQQHVDKLEHHSTQ--MQELFSSERIDWTKQQ--------EELLSQLNVL 716
Cdd:TIGR02169 375 EVDKEFAETRDELKD-YREKLEKLKREINELKRELDRLQEELQRlsEELADLNAAIAGIEAKineleeekEDKALEIKKQ 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 717 EKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQ-------------EKEFNKlSERHMHVQL-QLDN 782
Cdd:TIGR02169 454 EWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQAraseervrggravEEVLKA-SIQGVHGTVaQLGS 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 783 LRLENEKLLESKA-------CLQDSYDNLQEIMKFEIDQLSR-------NLQNFKKENETLKSD--LNNLMELLEAEKER 846
Cdd:TIGR02169 533 VGERYATAIEVAAgnrlnnvVVEDDAVAKEAIELLKRRKAGRatflplnKMRDERRDLSILSEDgvIGFAVDLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 847 NNKLSLQF---------EEDKENSSKEILKVLEAVRQEK------------------QKETAKCEQQMAKVQKLEESLLA 899
Cdd:TIGR02169 613 EPAFKYVFgdtlvvediEAARRLMGKYRMVTLEGELFEKsgamtggsraprggilfsRSEPAELQRLRERLEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 900 TEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKE 979
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 980 TL-RLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFK 1058
Cdd:TIGR02169 773 DLhKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1059 MRQLEhvmdsaaedpqspktpphfqtHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREvknaeilRMKEQLREMENL 1138
Cdd:TIGR02169 853 EKEIE---------------------NLNGKKEELEEELEELEAALRDLESRLGDLKKERD-------ELEAQLRELERK 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1139 RLESQQLIEKNWLLQGQLddiKRQKENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQS----ALYNK 1214
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSEL---KAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPvnmlAIQEY 981
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 767923891 1215 EMECLRMTDEVERTQTLEskafQEKEQLRsKLEEMYEERER 1255
Cdd:TIGR02169 982 EEVLKRLDELKEKRAKLE----EERKAIL-ERIEEYEKKKR 1017
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
554-1279 |
3.48e-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: 58.06 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 554 ISGMEKSDKNQQGFSPKAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENL 633
Cdd:TIGR00618 169 LMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 634 LEATKA-CKRQEVSQLNKIHAETLKEQMSALqakldEEEHKNLKLQQHVDKLEHHSTQMQELfsseRIDWTKQQEELLSQ 712
Cdd:TIGR00618 249 REAQEEqLKKQQLLKQLRARIEELRAQEAVL-----EETQERINRARKAAPLAAHIKAVTQI----EQQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 713 LNVLEKQLQETQtkndflksevhdlrvvlhSADKELSSVKLEYSSFKTNQEKEfnklserhmhvqlqlDNLRLENEKLLE 792
Cdd:TIGR00618 320 MRSRAKLLMKRA------------------AHVKQQSSIEEQRRLLQTLHSQE---------------IHIRDAHEVATS 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 793 SKACLQDSYDNLQEIMKFE--IDQLSRNLQNFKKENETLKSDLNNLMELLEAEK-ERNNKLSLQFEEDKENSSKEILKVL 869
Cdd:TIGR00618 367 IREISCQQHTLTQHIHTLQqqKTTLTQKLQSLCKELDILQREQATIDTRTSAFRdLQGQLAHAKKQQELQQRYAELCAAA 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 870 EAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRdsdKKVVADLMNQIQELRTSVCEKTEtidTLKQELKDI 949
Cdd:TIGR00618 447 ITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRK---KAVVLARLLELQEEPCPLCGSCI---HPNPARQDI 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 950 -NCKYNSALVDREESRVLIKKQEVDILD---LKETLRLRILSEDIERdmLCEDLAHATEQLNMLTEASKKHSGLLQSAQ- 1024
Cdd:TIGR00618 521 dNPGPLTRRMQRGEQTYAQLETSEEDVYhqlTSERKQRASLKEQMQE--IQQSFSILTQCDNRSKEDIPNLQNITVRLQd 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1025 --EELTKKEALIQELQHKLNQKKEEV--EQKKNEYNFKMRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDG 1100
Cdd:TIGR00618 599 ltEKLSEAEDMLACEQHALLRKLQPEqdLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASR 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1101 RASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQ-----------LIEKNWLLQGQLDDIKRQKENSDQN 1169
Cdd:TIGR00618 679 QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEienassslgsdLAAREDALNQSLKELMHQARTVLKA 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1170 HPDNQQLKNEQEESIKERLAK-SKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQTLES-KAFQEKEQLRSKLE 1247
Cdd:TIGR00618 759 RTEAHFNNNEEVTAALQTGAElSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCeTLVQEEEQFLSRLE 838
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 767923891 1248 E----------MYEERERTSQEMEMLRKQVECLAEENGKLVG 1279
Cdd:TIGR00618 839 EksatlgeithQLLKYEECSKQLAQLTQEQAKIIQLSDKLNG 880
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
413-1255 |
4.72e-08 |
|
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: 57.67 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 413 NYMEYFQEAMLFFKKSEQEKKSLIEKVTQLEDLTLKKEKFIQsNKMIVKFREDQIIRLEKLHKESrggfLPEEQDRLLSE 492
Cdd:pfam02463 230 DYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVL-KENKEEEKEKKLQEEELKLLAK----EEEELKSELLK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 493 LRNEIQTLREQIEHHprvaKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQQGFSPKAQ 572
Cdd:pfam02463 305 LERRKVDDEEKLKES----EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 573 KEpclFANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKACKRQEVSQLNKIH 652
Cdd:pfam02463 381 LE---SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 653 AETLKEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKS 732
Cdd:pfam02463 458 LKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 733 EVHDLRVVLHSADKELSSVKLEYSSFKTNQekefnkLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEIMKFEI 812
Cdd:pfam02463 538 VENYKVAISTAVIVEVSATADEVEERQKLV------RALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 813 DQLSRNLQNFKKENEtLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQK 892
Cdd:pfam02463 612 TLEADEDDKRAKVVE-GILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 893 LEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEK-TETIDTLKQELKDINCKYNSALVDREESRVLIKKQE 971
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKiNEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 972 VDILDLKETLRLRIlsEDIERDMLCEDLAHATEQLNMLTEAsKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQK 1051
Cdd:pfam02463 771 LKEKELAEEREKTE--KLKVEEEKEEKLKAQEEELRALEEE-LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK 847
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1052 KNEYNFKMrqlehvmdsaaedpqspktpphfqthlaKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEiLRMKEQ 1131
Cdd:pfam02463 848 LEKLAEEE----------------------------LERLEEEITKEELLQELLLKEEELEEQKLKDELESKE-EKEKEE 898
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1132 LREMENLRLESQQLIEKNwllqgQLDDIKRQKENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSAL 1211
Cdd:pfam02463 899 KKELEEESQKLNLLEEKE-----NEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG 973
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 767923891 1212 YNKEMECLRMTDEVERTQTLESKaFQEKEQLRSKLEEMYEERER 1255
Cdd:pfam02463 974 KVNLMAIEEFEEKEERYNKDELE-KERLEEEKKKLIRAIIEETC 1016
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
656-1048 |
5.54e-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: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 656 LKEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMqelfSSERIDWTKQQEELLSQLNVLEKQLQEtqtkndfLKSEVH 735
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDEL----SQELSDASRKIGEIEKEIEQLEQEEEK-------LKERLE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 736 DLRVVLHSADKELssvkleyssfkTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLESkaclqDSYDNLQEIMKfEIDQL 815
Cdd:TIGR02169 741 ELEEDLSSLEQEI-----------ENVKSELKELEARIEELEEDLHKLEEALNDLEAR-----LSHSRIPEIQA-ELSKL 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 816 SRNLQNFKKENETLKSDLNNLMELLE-AEKERNNKLSLQfeEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLE 894
Cdd:TIGR02169 804 EEEVSRIEARLREIEQKLNRLTLEKEyLEKEIQELQEQR--IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 895 ESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINckynsALVDREESrvlIKKQEVDI 974
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE-----DPKGEDEE---IPEEELSL 953
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767923891 975 LDLKETLrlrilsEDIERDMlcedlaHATEQLNMLT----EASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEV 1048
Cdd:TIGR02169 954 EDVQAEL------QRVEEEI------RALEPVNMLAiqeyEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
816-1321 |
5.62e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 5.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 816 SRNLQNFKKENETLKSD-LNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLE 894
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADeAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 895 ESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRtsvceKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEvdi 974
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK-----KADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAE--- 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 975 ldlkETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKhsgllqsaQEELTKKEALIQELQHKlnQKKEEVEQKKNE 1054
Cdd:PTZ00121 1429 ----EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK--------AEEAKKADEAKKKAEEA--KKADEAKKKAEE 1494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1055 YNFKMRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDR---EVKNAEILRMKEQ 1131
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKkaeEKKKAEEAKKAEE 1574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1132 LREMENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQ------QLKNEQEESIKERLAKSKIVEEMLKMKADLE 1205
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaeELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1206 EVQSALYNKEMECLRMTDEVERTQTLESKAFQEK---EQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGKLVGHQN 1282
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKkaaEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEE 1734
|
490 500 510
....*....|....*....|....*....|....*....
gi 767923891 1283 LHQKIQYVVRlKKENVRLAEETEKLRAENVFLKEKKRSE 1321
Cdd:PTZ00121 1735 AKKEAEEDKK-KAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
600-1162 |
7.46e-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: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 600 QEYEEFKELTRKRQLEL--------ESELQSLQKANLNLENLLEATKACKRQEVSQLnkihaETLKEQMSALQAKLDEEE 671
Cdd:COG1196 213 ERYRELKEELKELEAELlllklrelEAELEELEAELEELEAELEELEAELAELEAEL-----EELRLELEELELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 672 HKNLKLQQHVDKLEhhstQMQELFSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSsv 751
Cdd:COG1196 288 AEEYELLAELARLE----QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA-- 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 752 kleyssfktNQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEimkfEIDQLSRNLQNFKKENETLKS 831
Cdd:COG1196 362 ---------EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE----AEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 832 DLNNLMELLEAEKERnnklsLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSR 911
Cdd:COG1196 429 ALAELEEEEEEEEEA-----LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 912 DSDKKVVADLMNQIQELRTSVCEKTETIDTLKQE----------LKDINCKYNSALVDREESRVLIKKQEVDILDLKETL 981
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEaaleaalaaaLQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIR 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 982 RLRILSEDIERDMLCEDLA------------------------HATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQEL 1037
Cdd:COG1196 584 ARAALAAALARGAIGAAVDlvasdlreadaryyvlgdtllgrtLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLT 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1038 QHKLNQKKEEVEQKKNEynfkMRQLEHVMDSAAEDpqspktpphfQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNED 1117
Cdd:COG1196 664 GGSRRELLAALLEAEAE----LEELAERLAEEELE----------LEEALLAEEEEERELAEAEEERLEEELEEEALEEQ 729
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 767923891 1118 REVKNAEILRMKEQLREMENLRLESQQLIEKNW-LLQGQLDDIKRQ 1162
Cdd:COG1196 730 LEAEREELLEELLEEEELLEEEALEELPEPPDLeELERELERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
582-1139 |
1.24e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 582 EKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKAcKRQEVSQLNKIHAEtLKEQMS 661
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE-LLAELARLEQDIAR-LEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 662 ALQAKLDEEEHKNLKLQQHvdkLEHHSTQMQELfSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVL 741
Cdd:COG1196 313 ELEERLEELEEELAELEEE---LEELEEELEEL-EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 742 HSADKELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEIMKfEIDQLSRNLQN 821
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EEEALLELLAE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 822 FKKENETLKSDLNNLMELLEAEKERNNKLslqfEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATE 901
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLLLL----LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 902 KVISSLEKSRDSDkkvvADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDRE---------ESRVLIKKQEV 972
Cdd:COG1196 544 LAAALQNIVVEDD----EVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAavdlvasdlREADARYYVLG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 973 DILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKK 1052
Cdd:COG1196 620 DTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1053 NEYNFKMRQLEHVMDSAAEdpqspktpphfQTHLAKLLETQEQEIEDGRASKTSLEHLVT--------KLNEDREVKNAE 1124
Cdd:COG1196 700 LAEEEEERELAEAEEERLE-----------EELEEEALEEQLEAEREELLEELLEEEELLeeealeelPEPPDLEELERE 768
|
570
....*....|....*..
gi 767923891 1125 ILRMKEQLREME--NLR 1139
Cdd:COG1196 769 LERLEREIEALGpvNLL 785
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
485-856 |
3.82e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 485 EQDRLLSELRNEIQTLREQI-EHHPRVAKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEiSGMEKSDKN 563
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 564 QQGFSPKAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYEEFKE---LTRKRQLELESELQSLQKANLNLEN---LLEAT 637
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEelkALREALDELRAELTLLNEEAANLRErleSLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 638 KACKRQEVSQLNKIHAEtLKEQMSALQAKLDEEEhknlklqqhvdklehhsTQMQELfSSERIDWTKQQEELLSQLNVLE 717
Cdd:TIGR02168 833 IAATERRLEDLEEQIEE-LSEDIESLAAEIEELE-----------------ELIEEL-ESELEALLNERASLEEALALLR 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 718 KQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERHmhvqlqldnlRLENEKLLESKACL 797
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEY----------SLTLEEAEALENKI 963
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 767923891 798 QDSYDNLQEimkfEIDQLSRNLQNFKKENETlksdlnnLMELLEAEKERNNKLSLQFEE 856
Cdd:TIGR02168 964 EDDEEEARR----RLKRLENKIKELGPVNLA-------AIEEYEELKERYDFLTAQKED 1011
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
762-1261 |
4.22e-07 |
|
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: 54.80 E-value: 4.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 762 QEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEIMKfEIDQLSRNLQNFKKENETLksdLNNLMELLE 841
Cdd:pfam01576 10 KEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCA-EAEEMRARLAARKQELEEI---LHELESRLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 842 AEKERNNKLSLQFEEDKENSS--KEILKVLEAVRQEKQKETAKCEqqmAKVQKLEESLLATEKVISSLEKSRDSDKKVVA 919
Cdd:pfam01576 86 EEEERSQQLQNEKKKMQQHIQdlEEQLDEEEAARQKLQLEKVTTE---AKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 920 DLMNQIQELRtsvcEKTETIDTLKQelkdincKYNSALVDREESRvliKKQEVDILDLkETLRLRILSEDIE-RDMLCED 998
Cdd:pfam01576 163 EFTSNLAEEE----EKAKSLSKLKN-------KHEAMISDLEERL---KKEEKGRQEL-EKAKRKLEGESTDlQEQIAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 999 LAHATEQLNMLTEASKKHSGLLQSAQEELTKKEAL---IQELQHKLNQKKEEVEQKKNEYNFKMRQ-------------- 1061
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAALARLEEETAQKNNAlkkIRELEAQISELQEDLESERAARNKAEKQrrdlgeelealkte 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1062 LEHVMDSAAEDPQSPKTPPHFQTHLAKLLEtqeqeiEDGRASKTSLEHLvtklnedREVKNAEILRMKEQL----REMEN 1137
Cdd:pfam01576 308 LEDTLDTTAAQQELRSKREQEVTELKKALE------EETRSHEAQLQEM-------RQKHTQALEELTEQLeqakRNKAN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1138 LRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPD-NQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEM 1216
Cdd:pfam01576 375 LEKAKQALESENAELQAELRTLQQAKQDSEHKRKKlEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEG 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 767923891 1217 ECLRMTDEV-------ERTQTLESKAFQEKEQLRSKLEEMYEERERTSQEME 1261
Cdd:pfam01576 455 KNIKLSKDVsslesqlQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLE 506
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
886-1119 |
4.35e-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: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 886 QMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRV 965
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 966 LIKKQEvdiLDLKETLRLRILSEDIERDML------CEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQH 1039
Cdd:COG4942 98 ELEAQK---EELAELLRALYRLGRQPPLALllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1040 KLNQKKEEVEQKKNEYNFKMRQLEHVMDSaaedpqspktpphfqthLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDRE 1119
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLAR-----------------LEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
466-1263 |
4.87e-07 |
|
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: 54.41 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 466 QIIRLEKLHKESRGGFLpEEQDRLLSELRNEIQTLREQIEHhpRVAKYAMEnhsLREENRRLRLLEPVKRAQE-MDAQTI 544
Cdd:pfam01576 120 QKLQLEKVTTEAKIKKL-EEDILLLEDQNSKLSKERKLLEE--RISEFTSN---LAEEEEKAKSLSKLKNKHEaMISDLE 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 545 AKLEKAFSEISGMEKSDKNQQGFSPKAQKEPC-LFANTEKLKAQLLQIQTELNNSKQEYEEfkELTRKRQLEleSELQSL 623
Cdd:pfam01576 194 ERLKKEEKGRQELEKAKRKLEGESTDLQEQIAeLQAQIAELRAQLAKKEEELQAALARLEE--ETAQKNNAL--KKIREL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 624 QKANLNLENLLEATKACKRQEVSQlnkihAETLKEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERIDWT 703
Cdd:pfam01576 270 EAQISELQEDLESERAARNKAEKQ-----RRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 704 KQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQLDNL 783
Cdd:pfam01576 345 AQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSES 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 784 RLENEKLLESKACLQDSYDNLQEIMkfeiDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFE--EDKENS 861
Cdd:pfam01576 425 ERQRAELAEKLSKLQSELESVSSLL----NEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRqlEDERNS 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 862 SKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATekvISSLEKSRDSDKKVVADLMNQIQElRTSVCEKTE-TID 940
Cdd:pfam01576 501 LQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT---LEALEEGKKRLQRELEALTQQLEE-KAAAYDKLEkTKN 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 941 TLKQELKDInckynsaLVDREESRVLI----KKQ---------EVDILDLKETLRLRILSEDIERDMLCEDLAHATEQLN 1007
Cdd:pfam01576 577 RLQQELDDL-------LVDLDHQRQLVsnleKKQkkfdqmlaeEKAISARYAEERDRAEAEAREKETRALSLARALEEAL 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1008 MLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMdSAAEDP--------QSPKTp 1079
Cdd:pfam01576 650 EAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDEL-QATEDAklrlevnmQALKA- 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1080 phfqTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKnAEILRMKEQLrEMENLRLESQ---------QLIEKNW 1150
Cdd:pfam01576 728 ----QFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQR-AQAVAAKKKL-ELDLKELEAQidaankgreEAVKQLK 801
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1151 LLQGQLDDIKRQKEnsdqnhpDNQQLKNEQEESIKERLAKSKIVE-EMLKMKADLEEVQSALYNKEMECLRMTDEVERTQ 1229
Cdd:pfam01576 802 KLQAQMKDLQRELE-------EARASRDEILAQSKESEKKLKNLEaELLQLQEDLAASERARRQAQQERDELADEIASGA 874
|
810 820 830
....*....|....*....|....*....|....
gi 767923891 1230 TLESKAFQEKEQLRSKLEEMYEERERTSQEMEML 1263
Cdd:pfam01576 875 SGKSALQDEKRRLEARIAQLEEELEEEQSNTELL 908
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
488-1055 |
5.39e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 488 RLLSELRNEIQTLREQIEhhprvAKYAMENHSL--REENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSdknqq 565
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIE-----EKEEKDLHERlnGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEER----- 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 566 gfspkaQKEpclfanTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQ---LELESELQSLqKANLNLENLLEATKACKR 642
Cdd:PRK02224 250 ------REE------LETLEAEIEDLRETIAETEREREELAEEVRDLRerlEELEEERDDL-LAEAGLDDADAEAVEARR 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 643 QEVSQLNKIHAETLKEQMSALQAKLDEEEhknlKLQQHVDKLEHHSTQMQElfsseridwtkQQEELLSQLNVLEKQLQE 722
Cdd:PRK02224 317 EELEDRDEELRDRLEECRVAAQAHNEEAE----SLREDADDLEERAEELRE-----------EAAELESELEEAREAVED 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 723 TQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQLDNLRlENEKLLESKAC------ 796
Cdd:PRK02224 382 RREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVE-EAEALLEAGKCpecgqp 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 797 LQDS--YDNLQEiMKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKER-----NNKLSLQFEEDKENSSKEILKVL 869
Cdd:PRK02224 461 VEGSphVETIEE-DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIerleeRREDLEELIAERRETIEEKRERA 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 870 EAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVaDLMNQIQELRTSVCEKTETIDTLKQELKDI 949
Cdd:PRK02224 540 EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKREAL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 950 NCKynsalvdREESRVLIKKQEVDILDLKETL---RLRILSEDIERdmLCEDLAHATEQLNMLTEASKKHSGLLQSAQEE 1026
Cdd:PRK02224 619 AEL-------NDERRERLAEKRERKRELEAEFdeaRIEEAREDKER--AEEYLEQVEEKLDELREERDDLQAEIGAVENE 689
|
570 580 590
....*....|....*....|....*....|....*
gi 767923891 1027 LTKKEALIQELQH------KLNQKKEEVEQKKNEY 1055
Cdd:PRK02224 690 LEELEELRERREAlenrveALEALYDEAEELESMY 724
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
653-1211 |
5.85e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.14 E-value: 5.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 653 AETLKEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERIdwtkqqeeLLSQLNVLEKQLQETQTKNDFLKS 732
Cdd:PRK01156 168 YDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSI--------TLKEIERLSIEYNNAMDDYNNLKS 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 733 EVHDLRVVLHSADKELSSVKLEYSSFKTNQEK--EFNKLSERHMhvqlqldnlRLENEKLLESKACLQDSYD------NL 804
Cdd:PRK01156 240 ALNELSSLEDMKNRYESEIKTAESDLSMELEKnnYYKELEERHM---------KIINDPVYKNRNYINDYFKykndieNK 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 805 QEIMKFEIDQLSRNLQNFKK------------ENETLKSDLNNLMELLEAEKERNNKLSLQFEEDK---ENSSKEILKVL 869
Cdd:PRK01156 311 KQILSNIDAEINKYHAIIKKlsvlqkdyndyiKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKkkiEEYSKNIERMS 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 870 EAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQEL----RTSVCEKTETIDTLKQE 945
Cdd:PRK01156 391 AFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLngqsVCPVCGTTLGEEKSNHI 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 946 LKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRlRILSEDIER----DMLCEDLAHATE----QLNMLTEASKK-- 1015
Cdd:PRK01156 471 INHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE-YLESEEINKsineYNKIESARADLEdikiKINELKDKHDKye 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1016 ---------HSGLLQSAQEELTKKEALIQELQHKLNQK-KEEVEQKKNEYNFKMRQLEhvmdSAAEDPQS--PKTPPHFQ 1083
Cdd:PRK01156 550 eiknrykslKLEDLDSKRTSWLNALAVISLIDIETNRSrSNEIKKQLNDLESRLQEIE----IGFPDDKSyiDKSIREIE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1084 THlAKLLETQEQEIEDGRASKTSLEHLVTKLNEdrevknaEILRMKEQLREMENLRLESQQLIEKNWLLQGQLDDIKRQK 1163
Cdd:PRK01156 626 NE-ANNLNNKYNEIQENKILIEKLRGKIDNYKK-------QIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANR 697
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 767923891 1164 ENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSAL 1211
Cdd:PRK01156 698 ARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAF 745
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
978-1192 |
7.42e-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: 53.23 E-value: 7.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 978 KETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNF 1057
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1058 KMRQLEHVMDSAAED----PQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLR 1133
Cdd:COG4942 109 LLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767923891 1134 EMENLRLESQQLIEKnwlLQGQLDDIKRQKENSDQNHPDNQQLKNEQEESIKERLAKSK 1192
Cdd:COG4942 189 ALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
797-1308 |
1.01e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 797 LQDSYDNLQEIMKfEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLS---LQFEEDKENSSKEiLKVLEAVR 873
Cdd:PRK03918 160 YENAYKNLGEVIK-EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISselPELREELEKLEKE-VKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 874 Q---EKQKETAKCEQQMAKvqkLEESLLATEKVISSLEKSRDSDKKVVADLmNQIQELRTSVCEKTETIDTLKQELKDIN 950
Cdd:PRK03918 238 EeieELEKELESLEGSKRK---LEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 951 CKYNSALVDREESRVLIKKQEVDILDLKETLR-----LRILSEDIERDMLCEDLAHATEQLNML-TEASKKHSGLLQSAQ 1024
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERLEELKKklkelEKRLEELEERHELYEEAKAKKEELERLkKRLTGLTPEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1025 EELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEhvmdsAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASK 1104
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK-----KAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1105 TSLEHLVTKL-NEDREVKNA-----EILRMKEQLREMENLRLESQQL----IEKNW----LLQGQLDDIKRQKENSDQNH 1170
Cdd:PRK03918 469 KEIEEKERKLrKELRELEKVlkkesELIKLKELAEQLKELEEKLKKYnleeLEKKAeeyeKLKEKLIKLKGEIKSLKKEL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1171 PDNQQLKNEQEE------SIKERLAK--SKIVEEMLKMKADLEEVQSAL---YNKEMECLRMTDEVERTQtleskafQEK 1239
Cdd:PRK03918 549 EKLEELKKKLAElekkldELEEELAEllKELEELGFESVEELEERLKELepfYNEYLELKDAEKELEREE-------KEL 621
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767923891 1240 EQLRSKLEEMYEERERTSQEMEMLRKQVeclaEENGKLVGHQNLHQKIQYVVRLKKENVRLAEETEKLR 1308
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKEL----EELEKKYSEEEYEELREEYLELSRELAGLRAELEELE 686
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1020-1321 |
1.13e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1020 LQSAQEELTKKEALIQELQHKLNQKKEEVEQ--KKNEYNFKMRQLEHVMDSAAEDpqspktpphfqtHLAKLLETQEQEI 1097
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERQAEKaeRYRELKEELKELEAELLLLKLR------------ELEAELEELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1098 EDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREM-ENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQQL 1176
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAqAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1177 KNE----QEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEE 1252
Cdd:COG1196 329 EEEleelEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767923891 1253 RERTSQEMEMLRKQVECLAEENGKLVghQNLHQKIQYVVRLKKENVRLAEETEKLRAENVFLKEKKRSE 1321
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELE--EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
582-1148 |
2.92e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 582 EKLKAQLLQIQTELNNSKQEYEEF-------KELTRKRQLELESELQSLQKANLNLENLleatkackRQEVSQLNKihae 654
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFikrteniEELIKEKEKELEEVLREINEISSELPEL--------REELEKLEK---- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 655 tLKEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQElfsseRIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEV 734
Cdd:PRK03918 229 -EVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEE-----RIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFY 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 735 HDLRVVLHSADKELSSVKLEYSSFK------TNQEKEFNKLSERHMHVQLQLDNLRlENEKLLESKACLQDSYDNLQEIM 808
Cdd:PRK03918 303 EEYLDELREIEKRLSRLEEEINGIEerikelEEKEERLEELKKKLKELEKRLEELE-ERHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 809 K-FEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEK----QKETAKC 883
Cdd:PRK03918 382 TgLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRkellEEYTAEL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 884 EQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVA--DLMNQIQELRTS--------VCEKTETIDTLKQELKDINCKY 953
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKlkELAEQLKELEEKlkkynleeLEKKAEEYEKLKEKLIKLKGEI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 954 NSALVDREESRVLIKKQEVDILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGL-------------L 1020
Cdd:PRK03918 542 KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELkdaekelereekeL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1021 QSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNF-KMRQLEHVMdsaaedpqspktpphfqTHLAKLLETQEQEIED 1099
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEeEYEELREEY-----------------LELSRELAGLRAELEE 684
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 767923891 1100 GRASKTSLEHLVTKLNEDREvknaEILRMKEQLREMENLRLESQQLIEK 1148
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELE----EREKAKKELEKLEKALERVEELREK 729
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
866-1303 |
7.12e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 866 LKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVA--DLMNQIQELRTSVCEKTETIDTLK 943
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 944 QELKDinckYNSALVDREESRVLIKKQEVDILDLKETLRLRILsedierdmlcEDLAHATEQLNMLTEASKKHSGLLQSA 1023
Cdd:COG4717 153 ERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATE----------EELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1024 QEELTKKEALIQELQHKLNQKKEEveQKKNEYNFKMRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRAS 1103
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALE--ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1104 KTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEKNWL-------LQGQLDDIKRQKENSDQNHPDNQQL 1176
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDrieelqeLLREAEELEEELQLEELEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1177 KNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMEclrmtdevertqTLESKAFQEKEQLRSKLEEMYEERERT 1256
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGE------------LEELLEALDEEELEEELEELEEELEEL 444
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 767923891 1257 SQEMEMLRKQVECLAEENGKLVGHQNLHQKIQYVVRLKKENVRLAEE 1303
Cdd:COG4717 445 EEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEE 491
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
806-1273 |
7.15e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.91 E-value: 7.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 806 EIMKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQ 885
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 886 QMA-KVQKLEESLLATEKVISSLEKSRDSDK-KVVADLMNQIQELRTSVCE--KTETIDTLKQELKDINCKYNSALVDRE 961
Cdd:PTZ00121 1405 KKAdELKKAAAAKKKADEAKKKAEEKKKADEaKKKAEEAKKADEAKKKAEEakKAEEAKKKAEEAKKADEAKKKAEEAKK 1484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 962 ESRVLIKKQEVDildlKETLRLRILSEDIERdmlCEDLAHATE--QLNMLTEASKKHSGLLQSAQEELTKKEALIQELQH 1039
Cdd:PTZ00121 1485 ADEAKKKAEEAK----KKADEAKKAAEAKKK---ADEAKKAEEakKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1040 KLNQKKEEVEQKKNE---YNFKMRQLEhVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNE 1116
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAeedKNMALRKAE-EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1117 DREVKNAEILRMKEQLR-EMENLRLESQQLIEKNWLLQGQLDDIKRQKENSDQNHpdnQQLKNEQEESIKERLAKSKIVE 1195
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAA---EALKKEAEEAKKAEELKKKEAE 1713
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767923891 1196 EmlKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESKafqEKEQLRSKLEEMYEERERTSQEmemLRKQVECLAEE 1273
Cdd:PTZ00121 1714 E--KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK---KDEEEKKKIAHLKKEEEKKAEE---IRKEKEAVIEE 1783
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
783-1304 |
7.23e-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: 50.49 E-value: 7.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 783 LRLENEKLLESKACLQDSYDNLQEiMKFEIDQLSRNLQ-------NFKKENETLKSDLNNLMELLEAEKERNNKLSLQFE 855
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQE-LQFENEKVSLKLEeeiqenkDLIKENNATRHLCNLLKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 856 E------DKENSSKEILKVLEAVRQEKQKETA----KCEQQMAKVQKLEES----LLATEKVISSLEKSRDSDKKVVADL 921
Cdd:pfam05483 180 EtrqvymDLNNNIEKMILAFEELRVQAENARLemhfKLKEDHEKIQHLEEEykkeINDKEKQVSLLLIQITEKENKMKDL 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 922 MNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLRI-----LSEDIERDMLC 996
Cdd:pfam05483 260 TFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATkticqLTEEKEAQMEE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 997 EDLAHATEQL--NMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQ 1074
Cdd:pfam05483 340 LNKAKAAHSFvvTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEK 419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1075 SPKTPPHF----------QTHLAKLLETQEQEIEDgrasktsLEHLVTKLNEDREVKNAEILRMKEqlrEMENLRLESQQ 1144
Cdd:pfam05483 420 LLDEKKQFekiaeelkgkEQELIFLLQAREKEIHD-------LEIQLTAIKTSEEHYLKEVEDLKT---ELEKEKLKNIE 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1145 LIEKNWLLqgQLDDIKRQKENSDQnhpdNQQLKNEQEESIKERlaksKIVEEMLKMKADLEEVQSALYNkEMECLRmtde 1224
Cdd:pfam05483 490 LTAHCDKL--LLENKELTQEASDM----TLELKKHQEDIINCK----KQEERMLKQIENLEEKEMNLRD-ELESVR---- 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1225 vertqtleSKAFQEKEQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGKLvgHQNLHQKIQYVVRLKKENVRLAEET 1304
Cdd:pfam05483 555 --------EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNL--KKQIENKNKNIEELHQENKALKKKG 624
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
381-994 |
9.06e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.52 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 381 QAEVKRLKEQLAELASGQTPPESFLTRDKKKTNYMEYFQEAMLFFKKSEQEKKSLIEKVTQLEDLTLKKEKFIQSNKMIV 460
Cdd:PTZ00121 1291 KADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 461 KFREDQIIRLEKLHKESRGGFLPEEQDRLLSELRNEIQTLREQIEHHPRVAKYAMENHSLREENRRLRLLEPVKRAQEM- 539
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAk 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 540 -DAQTIAKLEKAFSEISGMEKSDK-NQQGFSPKAQKEPCLFANTEKLKAQLLQIQTElnnSKQEYEEFKELTRKRQLELE 617
Cdd:PTZ00121 1451 kKAEEAKKAEEAKKKAEEAKKADEaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAE---AKKKADEAKKAEEAKKADEA 1527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 618 SELQSLQKANlnlenllEATKACKRQEVSQLNKIHAETLKEQMSALQAKLDEEEHKNLKL------QQHVDKLEHHSTQM 691
Cdd:PTZ00121 1528 KKAEEAKKAD-------EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALrkaeeaKKAEEARIEEVMKL 1600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 692 QELFSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLH-SADKELSSVKLEYSSFKTNQEK----EF 766
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEElKKAEEENKIKAAEEAKKAEEDKkkaeEA 1680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 767 NKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEIMKFE------IDQLSRNLQNFKKENETLKSDlnnlmell 840
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEeenkikAEEAKKEAEEDKKKAEEAKKD-------- 1752
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 841 EAEKERNNKLSLQFEEDKENSSKEILKVL-EAVRQEKQKETAKCEQQMAKVQKLEESLLATEK----VISSLEKSRDSDK 915
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAVIeEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKegnlVINDSKEMEDSAI 1832
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767923891 916 KVVADLMNqiqelrtSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLRilSEDIERDM 994
Cdd:PTZ00121 1833 KEVADSKN-------MQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKID--KDDIEREI 1902
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
469-792 |
1.07e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.30 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 469 RLEKLHKESrggfLPEEQDRLLS--------------ELRNEIQTLREQIEHHPRVAKYAMEN-HSLREEN-----RRLR 528
Cdd:PRK11281 44 QLDALNKQK----LLEAEDKLVQqdleqtlalldkidRQKEETEQLKQQLAQAPAKLRQAQAElEALKDDNdeetrETLS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 529 LLePVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQQGFSPKAQKEpcLFANTeklkAQLLQIQTELNNSKqeyEEFKEL 608
Cdd:PRK11281 120 TL-SLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAA--LYANS----QRLQQIRNLLKGGK---VGGKAL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 609 TRKRQLELESELQSLQKANLNLENLLEATkackrqevSQLnkihaetlkeqMSALQAKLDEeehKNLKLQQhvdkLEHHS 688
Cdd:PRK11281 190 RPSQRVLLQAEQALLNAQNDLQRKSLEGN--------TQL-----------QDLLQKQRDY---LTARIQR----LEHQL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 689 TQMQELFSSERIDWTKQQ-EELLSQlnvleKQLQETQTkNDFLKSEvhdlrvvlhsadkelSSVKLEYSSFKTNQEKEFN 767
Cdd:PRK11281 244 QLLQEAINSKRLTLSEKTvQEAQSQ-----DEAARIQA-NPLVAQE---------------LEINLQLSQRLLKATEKLN 302
|
330 340
....*....|....*....|....*
gi 767923891 768 KLSERHMHVQLQLDNLrLENEKLLE 792
Cdd:PRK11281 303 TLTQQNLRVKNWLDRL-TQSERNIK 326
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
484-833 |
2.32e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.92 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 484 EEQDRLLSELRNEIQTLREQIEHHPRVAKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKN 563
Cdd:COG5022 826 IKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELE 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 564 QQGFSPKAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQL-ELESELQSLQKANLNLENLLEATKACKR 642
Cdd:COG5022 906 SEIIELKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELnKLHEVESKLKETSEEYEDLLKKSTILVR 985
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 643 Q------EVSQLNKIHAETLKEQMSalqakldeeehknlkLQQHVDKLEHHSTQMQELFSSERIDwtKQQEELLSQLNVL 716
Cdd:COG5022 986 EgnkansELKNFKKELAELSKQYGA---------------LQESTKQLKELPVEVAELQSASKII--SSESTELSILKPL 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 717 EKqlqetQTKNDFLKSEVHDLRVVLHSADKELSsvkLEYSSFKTNQEKEFNKLSErhmhvqLQLDNLRLENEKLLESKAC 796
Cdd:COG5022 1049 QK-----LKGLLLLENNQLQARYKALKLRRENS---LLDDKQLYQLESTENLLKT------INVKDLEVTNRNLVKPANV 1114
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 767923891 797 L------QDSYDNLQEIMKFeidqLSRNLQNFKKENETLKSDL 833
Cdd:COG5022 1115 LqfivaqMIKLNLLQEISKF----LSQLVNTLEPVFQKLSVLQ 1153
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
492-1119 |
2.32e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 492 ELRNEIQTLREQIEHHprvakyaMENHS-LREENRRLRLLEPVKRAQEmdaqtiaKLEKAFSEISGMEKSDKNQQGFspK 570
Cdd:COG4913 222 DTFEAADALVEHFDDL-------ERAHEaLEDAREQIELLEPIRELAE-------RYAAARERLAELEYLRAALRLW--F 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 571 AQKEpclfanTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKACKRQEVSQLNK 650
Cdd:COG4913 286 AQRR------LELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERER 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 651 iHAETLKEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFL 730
Cdd:COG4913 360 -RRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNI 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 731 KSEVHDLRVVLHSADK----------ELSSVKLEYS-----------SFKTN------QEKEFNK-LSERHMHVQLQLDN 782
Cdd:COG4913 439 PARLLALRDALAEALGldeaelpfvgELIEVRPEEErwrgaiervlgGFALTllvppeHYAAALRwVNRLHLRGRLVYER 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 783 LRLENEKlleskaclqdsydnlQEIMKFEIDQLSRNLQnfKKENE---TLKSDLNNLMELL--EAEKE-RNNKLSL---- 852
Cdd:COG4913 519 VRTGLPD---------------PERPRLDPDSLAGKLD--FKPHPfraWLEAELGRRFDYVcvDSPEElRRHPRAItrag 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 853 -------QFEEDKEN----------SSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDK 915
Cdd:COG4913 582 qvkgngtRHEKDDRRrirsryvlgfDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 916 KV------VADLMNQIQELRTSVCEktetIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETL-RLRILSE 988
Cdd:COG4913 662 DVasaereIAELEAELERLDASSDD----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdELQDRLE 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 989 DIERDMLCEDLAHATEQLNMLTEAskkhsGLLQSAQEELTKKealIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDS 1068
Cdd:COG4913 738 AAEDLARLELRALLEERFAAALGD-----AVERELRENLEER---IDALRARLNRAEEELERAMRAFNREWPAETADLDA 809
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 767923891 1069 AAEDpqspktPPHFQTHLAKL----LETQEQEIED--GRASKTSLEHLVTKLNEDRE 1119
Cdd:COG4913 810 DLES------LPEYLALLDRLeedgLPEYEERFKEllNENSIEFVADLLSKLRRAIR 860
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
580-1005 |
2.33e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 580 NTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQlELESELQSLQKANLNLENLLEAtkaCKRQEVSQLNKIHAETLKEQ 659
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEK---LEKLLQLLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 660 MSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRV 739
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 740 VLHSADKELSSVKLEYSSFKTNQEKEFNK-----LSERHMHVQLQLDNLRLENE--------------------KLLESK 794
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARlllliAAALLALLGLGGSLLSLILTiagvlflvlgllallflllaREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 795 ACLQDSYDNLQEIMKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVL----- 869
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALlaeag 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 870 ---EAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDkkvvaDLMNQIQELRTSVCEKTETIDTLKQEL 946
Cdd:COG4717 381 vedEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE-----ELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 767923891 947 KDINCKYNSALVDREESRVLIKKQEvdildLKEtlRLRILSEDIERDMLCEDLAHATEQ 1005
Cdd:COG4717 456 AELEAELEQLEEDGELAELLQELEE-----LKA--ELRELAEEWAALKLALELLEEARE 507
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
813-1319 |
2.49e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.98 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 813 DQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAvrQEKQKETAKCEQQMAKVQK 892
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA--KKKADAAKKKAEEKKKADE 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 893 LEESLLATEKVISSLEKSRDSDKKVvadlmnqiQELRTSVCEKTETiDTLKQELKDINcKYNSALVDREESRvlikKQEV 972
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKA--------DEAKKKAEEKKKA-DEAKKKAEEAK-KADEAKKKAEEAK----KAEE 1461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 973 DILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKK 1052
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK 1541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1053 NEYNFK---MRQLEHVMDSAAEDPQSPKTPPHFQTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMK 1129
Cdd:PTZ00121 1542 AEEKKKadeLKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1130 -EQLREMENLRLESQQLIEKNWLLQGQLDDIKRQKEnsdQNHPDNQQLKNEQEESIKErlakskiVEEMLKMKADLEEVQ 1208
Cdd:PTZ00121 1622 aEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEE---ENKIKAAEEAKKAEEDKKK-------AEEAKKAEEDEKKAA 1691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1209 SALYNKEMEclrmTDEVERTQTLESKAFQEKEQLRSKleemYEERERTSQEMEMLRKQVECLAEENGKLVGHQNLHQKIQ 1288
Cdd:PTZ00121 1692 EALKKEAEE----AKKAEELKKKEAEEKKKAEELKKA----EEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLK 1763
|
490 500 510
....*....|....*....|....*....|.
gi 767923891 1289 YVVRLKKENVRlaEETEKLRAENVFLKEKKR 1319
Cdd:PTZ00121 1764 KEEEKKAEEIR--KEKEAVIEEELDEEDEKR 1792
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
707-1283 |
4.05e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 707 EELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYssfktnqeKEFNKLSERhmhvqlqLDNLRLE 786
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV--------KELEELKEE-------IEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 787 NEKLLESKACLQDsydnlqeimkfEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKE--RNNKLSLQFEEDKENSSKE 864
Cdd:PRK03918 247 LESLEGSKRKLEE-----------KIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 865 iLKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVAdLMNQIQELRTSvcEKTETIDTLKQ 944
Cdd:PRK03918 316 -LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA-KKEELERLKKR--LTGLTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 945 ELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRL------------RILSEDIERDMLCE----------DLAHA 1002
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgRELTEEHRKELLEEytaelkriekELKEI 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1003 TEQLNMLTEASKKHSGLLQSAQEELTKKEAL--IQELQHKLNQ-KKEEVEQKKNEY---NFKMRQLEHVMDSAAEDPQSP 1076
Cdd:PRK03918 472 EEKERKLRKELRELEKVLKKESELIKLKELAeqLKELEEKLKKyNLEELEKKAEEYeklKEKLIKLKGEIKSLKKELEKL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1077 KTpphfqthLAKLLETQEQEIEDGRASKTSLEHlvtklnEDREVKNAEILRMKEQLREMENLRLESQQLIEKNWLLQGQL 1156
Cdd:PRK03918 552 EE-------LKKKLAELEKKLDELEEELAELLK------ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREE 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1157 DDIKRQKENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEmlkmkADLEEVQSALYNKEMECLRMTDEVERtqtLESKAF 1236
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE-----EEYEELREEYLELSRELAGLRAELEE---LEKRRE 690
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 767923891 1237 QEKEQLRsKLEEMYEERERTSQEMEMLRKQVECLAEENGKLVGHQNL 1283
Cdd:PRK03918 691 EIKKTLE-KLKEELEEREKAKKELEKLEKALERVEELREKVKKYKAL 736
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
704-929 |
5.05e-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: 47.07 E-value: 5.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 704 KQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSsfktNQEKEFNKLSERHMHVQLQLDNL 783
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELA----ALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 784 RLENEKLLeSKACLQDSYDNLQEIMKFE-IDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEdkenss 862
Cdd:COG4942 103 KEELAELL-RALYRLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE------ 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767923891 863 keilkvLEAVRQEKQKETAKCEQQMAKVQKLeesllatekvISSLEKSRDSDKKVVADLMNQIQELR 929
Cdd:COG4942 176 ------LEALLAELEEERAALEALKAERQKL----------LARLEKELAELAAELAELQQEAEELE 226
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
554-1226 |
5.49e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 5.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 554 ISGMEKSDKNQQGFSPKAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENL 633
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 634 LEATKACKRQEVSQLNKihaETLKEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQL 713
Cdd:TIGR00606 265 MKLDNEIKALKSRKKQM---EKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 714 NV-LEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQL---------DNL 783
Cdd:TIGR00606 342 KTeLLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTaaqlcadlqSKE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 784 RLENEKLLEskacLQDSYDNLQEIMKFEIDQLSR---NLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQfeedKEN 860
Cdd:TIGR00606 422 RLKQEQADE----IRDEKKGLGRTIELKKEILEKkqeELKFVIKELQQLEGSSDRILELDQELRKAERELSKA----EKN 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 861 SSKEILKVLEAVRQEKQ--------KETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQI------Q 926
Cdd:TIGR00606 494 SLTETLKKEVKSLQNEKadldrklrKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLgyfpnkK 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 927 ELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLRILSEDIERDM--LCEDLAHATE 1004
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLerLKEEIEKSSK 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1005 QLNMLTEASKKHS---------------------------------------------------------------GLLQ 1021
Cdd:TIGR00606 654 QRAMLAGATAVYSqfitqltdenqsccpvcqrvfqteaelqefisdlqsklrlapdklksteselkkkekrrdemlGLAP 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1022 SAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVM--DSAAEDPQSPKTP-PHFQTHLAKLLETQEQEIE 1098
Cdd:TIGR00606 734 GRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMpeEESAKVCLTDVTImERFQMELKDVERKIAQQAA 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1099 DGRASktSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEKnwlLQGQLDDIKRQKENSDQNHPDNQQLKN 1178
Cdd:TIGR00606 814 KLQGS--DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQH---LKSKTNELKSEKLQIGTNLQRRQQFEE 888
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 767923891 1179 EQEESIKE--------RLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVE 1226
Cdd:TIGR00606 889 QLVELSTEvqslireiKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVN 944
|
|
| HMMR_C |
pfam15908 |
Hyaluronan mediated motility receptor C-terminal; HMMR_C is the C-terminal region of ... |
1204-1310 |
5.59e-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: 44.90 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1204 LEEVQSALYNKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGKLVGHQNL 1283
Cdd:pfam15908 4 LEMEEQRKARLENTVDELTEEIKKWRNLYEELYNKTKPFQEQLDAFEAEKNALLNENGAAQEELNKLSDAYAKLLGHQNQ 83
|
90 100
....*....|....*....|....*..
gi 767923891 1284 HQKIQYVVRLKKENVRLAEETEKLRAE 1310
Cdd:pfam15908 84 KQKIKHVVKLKEENTQLKQEVSKLRSQ 110
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1021-1322 |
8.45e-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: 47.04 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1021 QSAQEELTKKEALIQELQHKLNQKKEEVEQKKNeynfKMRQLEHVMDS--AAEDPQSPKTPPHFQTHLAKLLETQEQEIE 1098
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREVE----RRRKLEEAEKArqAEMDRQAAIYAEQERMAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1099 DgrasktslehlvtKLNEDREVKNAEILRMKEQLREMENLRLESQQlieKNWLLQGQLDDIKRQKensdqnhpdnqQLKN 1178
Cdd:pfam17380 357 E-------------RKRELERIRQEEIAMEISRMRELERLQMERQQ---KNERVRQELEAARKVK-----------ILEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1179 EQEESIKERLAkskiveEMLKMKADLEEVqsalynKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEERERTSQ 1258
Cdd:pfam17380 410 ERQRKIQQQKV------EMEQIRAEQEEA------RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKL 477
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767923891 1259 EMEMlRKQVECLAEENGKLVGHQNLHQKIQYVvrLKKENVRLAEETEKLRAENVFLKEKKRSES 1322
Cdd:pfam17380 478 ELEK-EKRDRKRAEEQRRKILEKELEERKQAM--IEEERKRKLLEKEMEERQKAIYEEERRREA 538
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
425-949 |
8.61e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 8.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 425 FKKSEQEKKSLIEKVTQLEDLTLKKEKFIQSNKMIVKFREDQIIRLE-----------------------KLHKESRGGF 481
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELReeleklekevkeleelkeeieelEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 482 LPEEQDRL------LSELRNEIQTLREQIEHHPRVAKYAMENHSLREENRRLR-LLEPVKRAQEMDAQTIAKLEKAFSEI 554
Cdd:PRK03918 254 KRKLEEKIreleerIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLdELREIEKRLSRLEEEINGIEERIKEL 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 555 SGMEKSDKNQQGFSPKAQKEPCLFANTEKLKAQLLQIQTELNNSKqeyeefKELTRKRQLELESELQSLQKANLNLE--- 631
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLK------KRLTGLTPEKLEKELEELEKAKEEIEeei 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 632 NLLEATKACKRQEVSQLNK--IHAETLKEQMSALQAKLDEEEHKNLklqqhvdkLEHHSTQMQELfSSERIDWTKQQEEL 709
Cdd:PRK03918 408 SKITARIGELKKEIKELKKaiEELKKAKGKCPVCGRELTEEHRKEL--------LEEYTAELKRI-EKELKEIEEKERKL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 710 LSQLNVLEKQLQETQTkndflKSEVHDLRVVLHSADKELSSVKLEYSSFKTnqeKEFNKLSERHMHVQLQLDNL--RLEN 787
Cdd:PRK03918 479 RKELRELEKVLKKESE-----LIKLKELAEQLKELEEKLKKYNLEELEKKA---EEYEKLKEKLIKLKGEIKSLkkELEK 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 788 EKLLESK-ACLQDSYDNLQEIMKFEIDQLS--------------RNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSL 852
Cdd:PRK03918 551 LEELKKKlAELEKKLDELEEELAELLKELEelgfesveeleerlKELEPFYNEYLELKDAEKELEREEKELKKLEEELDK 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 853 QFEE--DKENSSKEILKVLEAVRQEKQKETAkcEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRt 930
Cdd:PRK03918 631 AFEElaETEKRLEELRKELEELEKKYSEEEY--EELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE- 707
|
570
....*....|....*....
gi 767923891 931 svcEKTETIDTLKQELKDI 949
Cdd:PRK03918 708 ---KAKKELEKLEKALERV 723
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
615-1268 |
1.13e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.55 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 615 ELESELQSLQKANLNLENLLEATKACKRQEVSQLNKIHAE--TLKEQMSALQAKLDEEEHKnlklqqhVDKLEHHSTqmq 692
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKikILEQQIKDLNDKLKKNKDK-------INKLNSDLS--- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 693 eLFSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEyssfKTNQEKEFNKLSER 772
Cdd:TIGR04523 107 -KINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQ----KEELENELNLLEKE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 773 HMHVQLQLDNLRLENEKLLESKACLQdSYDNLQEIMKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSl 852
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSNLK-KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLK- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 853 qfeedkeNSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKvisslEKSRDSDKKVVADLMN---QIQELR 929
Cdd:TIGR04523 260 -------DEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN-----QKEQDWNKELKSELKNqekKLEEIQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 930 TSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLK---ETLRLRILSEDIERDMLCEDLAHATEQl 1006
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKkenQSYKQEIKNLESQINDLESKIQNQEKL- 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1007 nmlteaSKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHvmdsaaedpqspktpphfqthL 1086
Cdd:TIGR04523 407 ------NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN---------------------L 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1087 AKLLETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEKNWLLQGQLDDIKRQKENS 1166
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1167 DQNhpdnqqlKNEQEESIKERLAKSKIVEEMLKMKADLEEV---QSALYNKEMECLRMTDEVERTQTLESKAFQEKEQLR 1243
Cdd:TIGR04523 540 ISD-------LEDELNKDDFELKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKI 612
|
650 660
....*....|....*....|....*
gi 767923891 1244 SKLEEMYEERERTSQEMEMLRKQVE 1268
Cdd:TIGR04523 613 SSLEKELEKAKKENEKLSSIIKNIK 637
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
371-773 |
1.22e-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: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 371 EDTQGNVSQLQAEVKRLKEQLA-----ELASGQTPPESfLTRDKKKTNYMEYFQEAMLFFKKSEQEKKSLIEKVTQ-LED 444
Cdd:pfam15921 422 DDRNMEVQRLEALLKAMKSECQgqmerQMAAIQGKNES-LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERtVSD 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 445 LTL---KKEKFIQ-SNKMIVKFREDQIIRLEKL-HKESRGGFLPE-------------EQDRLLSELRNEIQTLREQIEH 506
Cdd:pfam15921 501 LTAslqEKERAIEaTNAEITKLRSRVDLKLQELqHLKNEGDHLRNvqtecealklqmaEKDKVIEILRQQIENMTQLVGQ 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 507 HPRVA-KYAMENHSLREE--NRRLRLLEPVKRAQEMDAQtIAKLEKAFSEISgMEKSDKNQQGfSPKAQKEPCLFANTEK 583
Cdd:pfam15921 581 HGRTAgAMQVEKAQLEKEinDRRLELQEFKILKDKKDAK-IRELEARVSDLE-LEKVKLVNAG-SERLRAVKDIKQERDQ 657
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 584 LKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATK-ACKRQEVSQLNKIH-AETLKEQMS 661
Cdd:pfam15921 658 LLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRnTLKSMEGSDGHAMKvAMGMQKQIT 737
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 662 ALQAKLDEEEHKnlklQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVL 741
Cdd:pfam15921 738 AKRGQIDALQSK----IQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVAL 813
|
410 420 430
....*....|....*....|....*....|..
gi 767923891 742 HSADKELSsvklEYSSFKTNQEKEFNKLSERH 773
Cdd:pfam15921 814 DKASLQFA----ECQDIIQRQEQESVRLKLQH 841
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
888-1274 |
1.71e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 888 AKVQKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRtsvcEKTETIDTLKQELKDINCKYNSALVDREESRVLI 967
Cdd:PRK02224 206 ERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHE----ERREELETLEAEIEDLRETIAETEREREELAEEV 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 968 KKQEVDILDLK-----------------ETLRLRI--LSEDIE--RDMLCE---DLAHATEQLNMLTEASKKHSGLLQSA 1023
Cdd:PRK02224 282 RDLRERLEELEeerddllaeaglddadaEAVEARReeLEDRDEelRDRLEEcrvAAQAHNEEAESLREDADDLEERAEEL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1024 QEELTKKEALIQELQHKLNQKKEEVEQKKNEynfkMRQLEHVMDSAAEDPQSpktpphFQTHLAKLLETQEQEIEDGRAS 1103
Cdd:PRK02224 362 REEAAELESELEEAREAVEDRREEIEELEEE----IEELRERFGDAPVDLGN------AEDFLEELREERDELREREAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1104 KTSLEHLVTKLNEDRE-------------VKNAEILRMKEQLRE-MENLRLESQQLIEKNWLLQGQLDDIK------RQK 1163
Cdd:PRK02224 432 EATLRTARERVEEAEAlleagkcpecgqpVEGSPHVETIEEDRErVEELEAELEDLEEEVEEVEERLERAEdlveaeDRI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1164 ENSDQNHPDNQQLKNEQEESIKERLAKskiVEEMLKMKADLE---EVQSALYNKEMEclRMTDEVERTQTLESKAFQEKE 1240
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEKRER---AEELRERAAELEaeaEEKREAAAEAEE--EAEEAREEVAELNSKLAELKE 586
|
410 420 430
....*....|....*....|....*....|....*.
gi 767923891 1241 QLRS--KLEEMYEERERTSQEMEMLRKQVECLAEEN 1274
Cdd:PRK02224 587 RIESleRIRTLLAAIADAEDEIERLREKREALAELN 622
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
919-1072 |
1.85e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 919 ADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKETLRLR--ILSEDIER---- 992
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERreELGERARAlyrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 993 -------DMLCE-----DLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMR 1060
Cdd:COG3883 99 ggsvsylDVLLGsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQA 178
|
170
....*....|..
gi 767923891 1061 QLEHVMDSAAED 1072
Cdd:COG3883 179 EQEALLAQLSAE 190
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
546-1273 |
1.92e-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: 45.94 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 546 KLEKAFSEISGMEKsdKNQQGFSPKA------QKEPCLFANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESE 619
Cdd:pfam01576 20 RQQKAESELKELEK--KHQQLCEEKNalqeqlQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERSQQLQNE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 620 LQSLQKANLNLENLLEATKACkRQEVsQLNKIHAEtlkeqmsalqAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSER 699
Cdd:pfam01576 98 KKKMQQHIQDLEEQLDEEEAA-RQKL-QLEKVTTE----------AKIKKLEEDILLLEDQNSKLSKERKLLEERISEFT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 700 IDWTKQQEELlsqlnvleKQLQETQTKNDFLKSEVHDLRvvlhsadKELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQ 779
Cdd:pfam01576 166 SNLAEEEEKA--------KSLSKLKNKHEAMISDLEERL-------KKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 780 LDNLRLENEKLLESKACLQDsydnlqeimKFEIDQLSRNlqNFKKENETLKSDLNNLMELLEAEKERNNKLslqfEEDKE 859
Cdd:pfam01576 231 IAELRAQLAKKEEELQAALA---------RLEEETAQKN--NALKKIRELEAQISELQEDLESERAARNKA----EKQRR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 860 NSSKEilkvLEAVRQE----------KQKETAKCEQQMAKVQK-LEESLLATEkviSSLEKSRDSDKKVVADLMNQIQEL 928
Cdd:pfam01576 296 DLGEE----LEALKTEledtldttaaQQELRSKREQEVTELKKaLEEETRSHE---AQLQEMRQKHTQALEELTEQLEQA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 929 RTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILDLKetlrLRILSEDIERDMLCEDLAHATEQLNM 1008
Cdd:pfam01576 369 KRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQ----ARLSESERQRAELAEKLSKLQSELES 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1009 LTEASKKHSGLLQSAQEELTKKEALIQELQHKLnqkKEEVEQKKNeYNFKMRQLEH----VMDSAAEDPQSPKT-PPHFQ 1083
Cdd:pfam01576 445 VSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL---QEETRQKLN-LSTRLRQLEDernsLQEQLEEEEEAKRNvERQLS 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1084 THLAKLLETQEQeIEDGRASKTSLEHLVTKLNEDREVKNaeiLRMKEQLREMENLRLESQQlieknwlLQGQLDDIKRQK 1163
Cdd:pfam01576 521 TLQAQLSDMKKK-LEEDAGTLEALEEGKKRLQRELEALT---QQLEEKAAAYDKLEKTKNR-------LQQELDDLLVDL 589
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1164 ENSDQ--NHPDNQQLKNEQEESiKERLAKSKIVEEMLKMKADLEEvqsalynKEMECLRMTDEVERTQTLESKAFQEKEQ 1241
Cdd:pfam01576 590 DHQRQlvSNLEKKQKKFDQMLA-EEKAISARYAEERDRAEAEARE-------KETRALSLARALEEALEAKEELERTNKQ 661
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 767923891 1242 LRSKLEEMY----------EERERT----SQEMEMLRKQVECLAEE 1273
Cdd:pfam01576 662 LRAEMEDLVsskddvgknvHELERSkralEQQVEEMKTQLEELEDE 707
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
582-890 |
2.18e-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: 45.83 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 582 EKLKAQLLQIQTELNNSKQEYEEFKEltrkRQLELESELQSLQKANLNLENLLEATKACKRQEVSQLNKIHAETLKEQMS 661
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKS----ELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVS 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 662 ALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQElfssERIDWT-------KQQEELLSQLNVLEKQLQETQTKNDFLKSEV 734
Cdd:TIGR02169 809 RIEARLREIEQKLNRLTLEKEYLEKEIQELQE----QRIDLKeqiksieKEIENLNGKKEELEEELEELEAALRDLESRL 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 735 HDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERhmhvQLQLDNLRLENEKLLESKACLQDSYDNLQEImkfeidq 814
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL----KAKLEALEEELSEIEDPKGEDEEIPEEELSL------- 953
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767923891 815 lsrnlqnfkkenETLKSDLNNLMELLEAEKERNNKLSLQFEEDKE--NSSKEILKVLEAVRQEKQKETAKCEQQMAKV 890
Cdd:TIGR02169 954 ------------EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKrlDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
810-1310 |
2.30e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 45.73 E-value: 2.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 810 FEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVRQ------------EKQ 877
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQtqqshayltqkrEAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 878 KETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKV---------VADLMNQIQEL-------------------- 928
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAaplaahikaVTQIEQQAQRIhtelqskmrsrakllmkraa 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 929 ----RTSVCEKTETIDTLKQELKDINCKYNSALVDREES------RVLIKKQEVDILDLKETLRL-------------RI 985
Cdd:TIGR00618 333 hvkqQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREIScqqhtlTQHIHTLQQQKTTLTQKLQSlckeldilqreqaTI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 986 LSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKN---EYNFKMRQL 1062
Cdd:TIGR00618 413 DTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihlQETRKKAVV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1063 EHVMDSAAEDPQS-PKTPPHFQTHLAKLLETQ---------EQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQL 1132
Cdd:TIGR00618 493 LARLLELQEEPCPlCGSCIHPNPARQDIDNPGpltrrmqrgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSF 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1133 REMENLRLESQQLIEKnwlLQGQLDDIKRQKENSDQNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKadlEEVQSALY 1212
Cdd:TIGR00618 573 SILTQCDNRSKEDIPN---LQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS---QELALKLT 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1213 NKEMECLRMTDEVERTQTLESKAFQEK--EQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGKLVGHQNLHQKIQYV 1290
Cdd:TIGR00618 647 ALHALQLTLTQERVREHALSIRVLPKEllASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA 726
|
570 580
....*....|....*....|....*
gi 767923891 1291 VR-----LKKENVRLAEETEKLRAE 1310
Cdd:TIGR00618 727 SSslgsdLAAREDALNQSLKELMHQ 751
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1014-1322 |
2.42e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1014 KKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQSPKTpphfqthLAKLLETQ 1093
Cdd:PRK03918 171 IKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEE-------LKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1094 EQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEknwlLQGQLDDIKRQKENSDQNHPDN 1173
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK----LSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1174 QQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVERTQTLESK---------------AFQE 1238
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRltgltpeklekeleeLEKA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1239 KEQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGK-------LVGHQNLHQKIQY---VVRLKKENVRLAEETEKLR 1308
Cdd:PRK03918 400 KEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgreLTEEHRKELLEEYtaeLKRIEKELKEIEEKERKLR 479
|
330
....*....|....
gi 767923891 1309 AENVFLKEKKRSES 1322
Cdd:PRK03918 480 KELRELEKVLKKES 493
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
418-1321 |
2.47e-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: 45.81 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 418 FQEAMLFFKKSEQEKKSLIEKVTQLEDLTLKKEKFIQSNKMIVKFREDQIIRLEKLHKESrggflpEEQDRLLSELRNEI 497
Cdd:TIGR00606 198 QGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEI------EHNLSKIMKLDNEI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 498 QTLREQiehhprvaKYAMENHSLREENRRlrllepVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQQGFSPKAQKEPCL 577
Cdd:TIGR00606 272 KALKSR--------KKQMEKDNSELELKM------EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRL 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 578 FaNTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKACKRQEVSQlnkihAETLK 657
Cdd:TIGR00606 338 L-NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDE-----AKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 658 EQMSALQAKLDEEehknlklQQHVDKLEHHSTQMQELFSSERIDWTKQQEEL---LSQLNVLEKQLQETQTKNDFLKSEV 734
Cdd:TIGR00606 412 QLCADLQSKERLK-------QEQADEIRDEKKGLGRTIELKKEILEKKQEELkfvIKELQQLEGSSDRILELDQELRKAE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 735 HDLRVVLHSAD-----KELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEIMK 809
Cdd:TIGR00606 485 RELSKAEKNSLtetlkKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTS 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 810 FEID-----QLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAVR-QEKQKETAKC 883
Cdd:TIGR00606 565 LLGYfpnkkQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGsQDEESDLERL 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 884 EQQMAKVQKLEESLLATEKVISS-LEKSRDSDK----------KVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCK 952
Cdd:TIGR00606 645 KEEIEKSSKQRAMLAGATAVYSQfITQLTDENQsccpvcqrvfQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKR 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 953 YNSALVDREESRVLIKKQEVDILDLKEtlRLRILSEDIERdmLCEDLAHATEQLNM------LTEASKKHSGLLQSAQEE 1026
Cdd:TIGR00606 725 RDEMLGLAPGRQSIIDLKEKEIPELRN--KLQKVNRDIQR--LKNDIEEQETLLGTimpeeeSAKVCLTDVTIMERFQME 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1027 LTKKEALIQELQHKLN---------QKKEEVEQKKNEYNFKMRQLEhVMDSAAEDPQspKTPPHFQTHLAKLLETQEQEI 1097
Cdd:TIGR00606 801 LKDVERKIAQQAAKLQgsdldrtvqQVNQEKQEKQHELDTVVSKIE-LNRKLIQDQQ--EQIQHLKSKTNELKSEKLQIG 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1098 EDGRASKTSLEHLVTKLNEDREVkNAEILRMKEQLREMENLRLESQQLIE-----KNWLLQGQLDDIKRQKENSDQNHPD 1172
Cdd:TIGR00606 878 TNLQRRQQFEEQLVELSTEVQSL-IREIKDAKEQDSPLETFLEKDQQEKEelissKETSNKKAQDKVNDIKEKVKNIHGY 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1173 NQQLKNEQEESiKERLAKSKiVEEMLKMKADLEEVQS--ALYNKEMECLRMTDEVERTQTLESKAFQEKEQLRSKLEEMY 1250
Cdd:TIGR00606 957 MKDIENKIQDG-KDDYLKQK-ETELNTVNAQLEECEKhqEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVE 1034
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767923891 1251 EERERTSQEMEMLRkqveclaeengkLVGHQNLHQKIQYVVRLKKENVRLAEETEKLRAENVFLKEKKRSE 1321
Cdd:TIGR00606 1035 EELKQHLKEMGQMQ------------VLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE 1093
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1020-1320 |
2.66e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1020 LQSAQEELTKKEALIQELQHKLNQKKEEVEqKKNEYNFKMRQLEHVMDSAaedpqspktpphfqthLAKLLETQEQEIED 1099
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELAL----------------LVLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1100 GRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMEnlrlESQQLIEKNWL-LQGQLDDIKRQKENSDQNHPDNQQLKN 1178
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELE----EEIEELQKELYaLANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1179 EQEESIKERLAKSKIVEEMLKMKAdlEEVQSALYNKEMECLRMTDEVERTQTLESK---AFQEKEQLRSKLEEMYE---- 1251
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELE--EKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQLELqias 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767923891 1252 ---ERERTSQEMEMLRKQVECLAEENGKLVGHQNLHQKIQYVVRLKKENVRLAEETEKLRAENVFLKEKKRS 1320
Cdd:TIGR02168 398 lnnEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
658-1054 |
2.83e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.14 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 658 EQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELfsseridwTKQQEELLSQLNVLEKQLQetqtkNDFLKSEVHDL 737
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEEL--------EAELEELREELEKLEKLLQ-----LLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 738 RVVLHSADKELSSVKLEYSSFKtNQEKEFNKLSERHMHVQLQLDnlRLENEKLLESKACLQDSYDNLQEIMKfEIDQLSR 817
Cdd:COG4717 138 EAELAELPERLEELEERLEELR-ELEEELEELEAELAELQEELE--ELLEQLSLATEEELQDLAEELEELQQ-RLAELEE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 818 NLQNFKKENETLKSDLNNLMELLEAEKERNNK-------------LSLQFEEDKENSSKE--------ILKVLEAVRQEK 876
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEERLkearlllliaaalLALLGLGGSLLSLILtiagvlflVLGLLALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 877 QKETAKCEQQMAKVQKLEE----SLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQE--LKDIN 950
Cdd:COG4717 294 AREKASLGKEAEELQALPAleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEelEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 951 CKYNSALVDREESRVLIKKQEVDILDLKETL-----RLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQE 1025
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAEEYQELKEELeeleeQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELRE 453
|
410 420 430
....*....|....*....|....*....|.
gi 767923891 1026 ELTKKEALIQEL--QHKLNQKKEEVEQKKNE 1054
Cdd:COG4717 454 ELAELEAELEQLeeDGELAELLQELEELKAE 484
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
609-1242 |
2.85e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 609 TRKRQLELESELQSLQKanlnlenllEATKACK-RQEVSQLNKIHAETLKEQMS-ALQAKLD-EEEHKNLKLQQHVDKLE 685
Cdd:COG5022 808 SRKEYRSYLACIIKLQK---------TIKREKKlRETEEVEFSLKAEVLIQKFGrSLKAKKRfSLLKKETIYLQSAQRVE 878
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 686 HHSTQMQEL-FSSERIDWTKQQ-EELLSQLNVLEKQLQETQTKNDFLKSEvhdlrvvlhsadkelSSVKLEyssfKTNQE 763
Cdd:COG5022 879 LAERQLQELkIDVKSISSLKLVnLELESEIIELKKSLSSDLIENLEFKTE---------------LIARLK----KLLNN 939
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 764 KEFNKLSERHMHVQLQLDNLRLENEKLLESkaclQDSYDNLQEIMKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEAE 843
Cdd:COG5022 940 IDLEEGPSIEYVKLPELNKLHEVESKLKET----SEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQEST 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 844 KERNNK----LSLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQ---QMAKVQKLEESLLATEKVISSLEKSRDSDKK 916
Cdd:COG5022 1016 KQLKELpvevAELQSASKIISSESTELSILKPLQKLKGLLLLENNQlqaRYKALKLRRENSLLDDKQLYQLESTENLLKT 1095
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 917 VVADlmnQIQELRTSVCEKTETIDTLK-QELKDINCKYNSALVDREESRVLIKKQ--EVDILDLKETLRLRILSEDIERD 993
Cdd:COG5022 1096 INVK---DLEVTNRNLVKPANVLQFIVaQMIKLNLLQEISKFLSQLVNTLEPVFQklSVLQLELDGLFWEANLEALPSPP 1172
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 994 MLCEDLAHATEQLNMLTEASKKHSGLLQSAQEEL--------------------TKKEALIQELQHKLNQKKEEVEQKKN 1053
Cdd:COG5022 1173 PFAALSEKRLYQSALYDEKSKLSSSEVNDLKNELialfskifsgwprgdklkklISEGWVPTEYSTSLKGFNNLNKKFDT 1252
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1054 EYNFKMRQLEHVMDSAAEDPQSPKTPPhfqTHLAKLLETQEQEIEDGRASKTSLEHLVTKLNEDREV-KNAEILRMKEQL 1132
Cdd:COG5022 1253 PASMSNEKLLSLLNSIDNLLSSYKLEE---EVLPATINSLLQYINVGLFNALRTKASSLRWKSATEVnYNSEELDDWCRE 1329
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1133 REMENLRLESQQLIEKNWLLQGQLDDIKRQKENSD----QNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQ 1208
Cdd:COG5022 1330 FEISDVDEELEELIQAVKVLQLLKDDLNKLDELLDacysLNPAEIQNLKSRYDPADKENNLPKEILKKIEALLIKQELQL 1409
|
650 660 670
....*....|....*....|....*....|....*.
gi 767923891 1209 SALYNKEMECLR--MTDEVERTQTLESKAFQEKEQL 1242
Cdd:COG5022 1410 SLEGKDETEVHLseIFSEEKSLISLDRNSIYKEEVL 1445
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1017-1273 |
3.35e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1017 SGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEdpqspktpphfqthLAKLLETQEQE 1096
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA--------------LARRIRALEQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1097 IEDGRASKTSLEHLVTKLNEDREVKNAEIlrmKEQLREMENLrleSQQLIEKNWLLQGQLDDIKRQKENSDQNHPDNQQL 1176
Cdd:COG4942 78 LAALEAELAELEKEIAELRAELEAQKEEL---AELLRALYRL---GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1177 KNEQEESIKE-RLAKSKIVEEMLKMKADLEEVQSALynkemecLRMTDEVERTQTLESKAFQEKEQLRSKLEEMYEERER 1255
Cdd:COG4942 152 AEELRADLAElAALRAELEAERAELEALLAELEEER-------AALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250
....*....|....*...
gi 767923891 1256 TSQEMEMLRKQVECLAEE 1273
Cdd:COG4942 225 LEALIARLEAEAAAAAER 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
787-1263 |
3.46e-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: 45.04 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 787 NEKLLESKAcLQDSYDNLQEIMKF--EIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQfeEDKENSSKE 864
Cdd:TIGR00606 162 NWPLSEGKA-LKQKFDEIFSATRYikALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSK--EAQLESSRE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 865 ILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVisslEKSRDSDKKVVADLM-----------NQIQELRTSVC 933
Cdd:TIGR00606 239 IVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR----KKQMEKDNSELELKMekvfqgtdeqlNDLYHNHQRTV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 934 EKTE--------TIDTLKQELKDINCKYNSALVDREESRVLIKKQEVDILD---LKETLRLRILSEDIERDMLCE---DL 999
Cdd:TIGR00606 315 REKErelvdcqrELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRArdsLIQSLATRLELDGFERGPFSErqiKN 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1000 AHATEQLNMLTEASKKHSGL------LQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDP 1073
Cdd:TIGR00606 395 FHTLVIERQEDEAKTAAQLCadlqskERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRIL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1074 QSPKTPPHFQTHLAKL-----LETQEQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLIEK 1148
Cdd:TIGR00606 475 ELDQELRKAERELSKAeknslTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKI 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1149 NW----LLQGQLDDIKRQKENSDQNHPdnqqlKNEQEESIKERLAKskiveeMLKMKADLEEVQSAlYNKEMECLRmtde 1224
Cdd:TIGR00606 555 KSrhsdELTSLLGYFPNKKQLEDWLHS-----KSKEINQTRDRLAK------LNKELASLEQNKNH-INNELESKE---- 618
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 767923891 1225 vERTQTLESKAFQ--EKEQLRSKLEEMYEERERTSQEMEML 1263
Cdd:TIGR00606 619 -EQLSSYEDKLFDvcGSQDEESDLERLKEEIEKSSKQRAML 658
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
484-754 |
3.88e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 484 EEQDRLLSELRNEIQTLREQIEHHpRVAKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKN 563
Cdd:COG1196 235 RELEAELEELEAELEELEAELEEL-EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 564 QQgfspkaqkepclfANTEKLKAQLLQIQTELNNSKQEYEEfkelTRKRQLELESELQSLQKANLNLENLLEATKAcKRQ 643
Cdd:COG1196 314 LE-------------ERLEELEEELAELEEELEELEEELEE----LEEELEEAEEELEEAEAELAEAEEALLEAEA-ELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 644 EVSQLNKIHAETLKEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQLNVLEKQLQET 723
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
250 260 270
....*....|....*....|....*....|.
gi 767923891 724 QTKNDfLKSEVHDLRVVLHSADKELSSVKLE 754
Cdd:COG1196 456 EEEEA-LLELLAELLEEAALLEAALAELLEE 485
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
485-1104 |
4.52e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 485 EQDRLLSELRNEIQTLREQIEHHPRVAKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQ 564
Cdd:PTZ00121 1299 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKK 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 565 QGFSPKAQKEpclfantEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKACKRQE 644
Cdd:PTZ00121 1379 KADAAKKKAE-------EKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 645 VSQlNKIHAETLKEQmsALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQelfssERIDWTKQQEELLSQLNVLEKQlQETQ 724
Cdd:PTZ00121 1452 KAE-EAKKAEEAKKK--AEEAKKADEAKKKAEEAKKADEAKKKAEEAK-----KKADEAKKAAEAKKKADEAKKA-EEAK 1522
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 725 TKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSfKTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNL 804
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 805 QEIMKFEIDQLSrnlqnfKKENETLKSDlnnlmELLEAEKERNNKLSLQFEEDKE-NSSKEILKVLEAVRQEKQKETAKC 883
Cdd:PTZ00121 1602 EEEKKMKAEEAK------KAEEAKIKAE-----ELKKAEEEKKKVEQLKKKEAEEkKKAEELKKAEEENKIKAAEEAKKA 1670
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 884 EQQMAKVQKL----EESLLATEKVISSLEKSRDSD--KKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINCKYNSAL 957
Cdd:PTZ00121 1671 EEDKKKAEEAkkaeEDEKKAAEALKKEAEEAKKAEelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 958 VDREESRvliKKQEVDILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQEL 1037
Cdd:PTZ00121 1751 KDEEEKK---KIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEM 1827
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767923891 1038 QhkLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQSPKTPPHFQTHlAKLLETQEQEIEDGRASK 1104
Cdd:PTZ00121 1828 E--DSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKE-KDLKEDDEEEIEEADEIE 1891
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
716-931 |
5.16e-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: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 716 LEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFnklserhmhVQLQLDNLRLENEKLLESKA 795
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEEAKL---------LLQQLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 796 CLQDSYDNLQEIMKFEIDQLSRNLQNfkKENETLKSDLNNLMELLEAEKERNN-------KLSLQFEEDKENSSKEILKV 868
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSARYTpnhpdviALRAQIAALRAQLQQEAQRI 314
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767923891 869 LEAVRQEKQKETAKCEQQMAKVQKLEE---SLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTS 931
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEArlaELPELEAELRRLEREVEVARELYESLLQRLEEARLA 380
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
582-949 |
5.29e-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: 44.35 E-value: 5.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 582 EKLKAQLLQIQTELNNSKQEYEEfkeLTRKRQLELESELQSLQKANLNLEN-LLEATKACKRQEVSQLNKIHA-ETLKEQ 659
Cdd:pfam05557 64 EAEAEEALREQAELNRLKKKYLE---ALNKKLNEKESQLADAREVISCLKNeLSELRRQIQRAELELQSTNSElEELQER 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 660 MSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELF---------------SSERIDWTKQQEELLSQLNVLEKQLQETQ 724
Cdd:pfam05557 141 LDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEfeiqsqeqdseivknSKSELARIPELEKELERLREHNKHLNENI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 725 TKNDFLKSEVHDLRVVLHSADK-ELSSVKLEYSSFKTNQE-KEFNKLSERH-------MHVQLQLDNLRLENEKLLESKA 795
Cdd:pfam05557 221 ENKLLLKEEVEDLKRKLEREEKyREEAATLELEKEKLEQElQSWVKLAQDTglnlrspEDLSRRIEQLQQREIVLKEENS 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 796 CLQDSYDNLQEI---MKFEIDQLSRNLQNFKKENETLKSDLNNLM-ELLEAEKERNNKLSLQFEEDKE----NSSKEILK 867
Cdd:pfam05557 301 SLTSSARQLEKArreLEQELAQYLKKIEDLNKKLKRHKALVRRLQrRVLLLTKERDGYRAILESYDKEltmsNYSPQLLE 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 868 VLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRDSDKKvvadlmnqiQELRTSVCEKTETIDTLKQELK 947
Cdd:pfam05557 381 RIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQ---------QESLADPSYSKEEVDSLRRKLE 451
|
..
gi 767923891 948 DI 949
Cdd:pfam05557 452 TL 453
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
657-1310 |
7.11e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 657 KEQMSALQAKLDEEEHKNLklqqhVDKLEHHSTQMQELFSS-ERIDWTKQQ-EELLSQLNVLEKQLQETQTKNDFLKSEV 734
Cdd:PRK02224 186 RGSLDQLKAQIEEKEEKDL-----HERLNGLESELAELDEEiERYEEQREQaRETRDEADEVLEEHEERREELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 735 HDLRVVLHSADKELSSVKLEYSSfktnQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQEimkfEIDQ 814
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRD----LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD----RLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 815 LSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKeilkvleavRQEKQKE-TAKCEQQMAKVQKL 893
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED---------RREEIEElEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 894 EESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLK-----QELKDinckynSALVDR-EESRVLI 967
Cdd:PRK02224 404 PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgQPVEG------SPHVETiEEDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 968 KKQEVDILDLKETLRlrILSEDIERdmlCEDLAHATEQLNMLTEASKkhsgllqSAQEELTKKEALIQELQHKLNQKKEE 1047
Cdd:PRK02224 478 EELEAELEDLEEEVE--EVEERLER---AEDLVEAEDRIERLEERRE-------DLEELIAERRETIEEKRERAEELRER 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1048 VEQkkneynfkmrqLEHVMDSAAEDPQspktpphfqthlaklleTQEQEIEDGRASKTSLEHLVTKLNEDREVKNaeilR 1127
Cdd:PRK02224 546 AAE-----------LEAEAEEKREAAA-----------------EAEEEAEEAREEVAELNSKLAELKERIESLE----R 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1128 MKEQLREMENLRlesqqlieknwllqgqlDDIKRQKENSDQnhpdnqqlKNEQEESIKERLAkskiveEMLKMKADLEEv 1207
Cdd:PRK02224 594 IRTLLAAIADAE-----------------DEIERLREKREA--------LAELNDERRERLA------EKRERKRELEA- 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1208 qsalynkEMECLRMTDEVERTQTLEskafQEKEQLRSKLEEMYEERERTSQEMEMLRKQVECLAEENGKLVGHQNLHQKI 1287
Cdd:PRK02224 642 -------EFDEARIEEAREDKERAE----EYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEAL 710
|
650 660
....*....|....*....|....
gi 767923891 1288 QYVvrlkKENVRLAEET-EKLRAE 1310
Cdd:PRK02224 711 EAL----YDEAEELESMyGDLRAE 730
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
426-636 |
9.49e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 9.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 426 KKSEQEKKSLIEKVTQLEDLTLKKEKFIQSNKMIVKFREDQIIRLEKLHKESRGGFlpEEQDRLLSELRNEIQTLREQIE 505
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL--AALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 506 HHPR------VAKYAMENHSL-------REENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQQgfspkaq 572
Cdd:COG4942 101 AQKEelaellRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER------- 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767923891 573 kepclfANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEA 636
Cdd:COG4942 174 ------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
484-895 |
9.85e-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: 43.58 E-value: 9.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 484 EEQDRLLSELRNEIQTLREQI--------EHHPRVAKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEIS 555
Cdd:pfam05557 121 QRAELELQSTNSELEELQERLdllkakasEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIP 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 556 GMEKSDKNQQGFSPK--AQKEPCLFANT------------EKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLE------ 615
Cdd:pfam05557 201 ELEKELERLREHNKHlnENIENKLLLKEevedlkrklereEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNlrsped 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 616 LESELQSLQKANLNLENLLEATKACKRQEVSQLNKIHAETLKEQMSALQAKLDEEEHKNLK--LQQHVDKLEHHSTQMQE 693
Cdd:pfam05557 281 LSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVrrLQRRVLLLTKERDGYRA 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 694 LFSSERIDWT--KQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQE-KEFNKLS 770
Cdd:pfam05557 361 ILESYDKELTmsNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESlADPSYSK 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 771 ERHMHVQLQLDNLRLENEKLLESKACLQdsydnlQEIMKFEIDQLSrNLQNFK----KENETLKSD--LNNLMELLEAEK 844
Cdd:pfam05557 441 EEVDSLRRKLETLELERQRLREQKNELE------MELERRCLQGDY-DPKKTKvlhlSMNPAAEAYqqRKNQLEKLQAEI 513
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 767923891 845 ERNNKLSLQFEEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEE 895
Cdd:pfam05557 514 ERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQRLKE 564
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
924-1134 |
1.06e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 924 QIQELRTSVCEKTETIDTLKQELKDINCKYNSAlvdREESRVLIKKQEVDildlketlrlrilSEDIERDMLCEDLAHAT 1003
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDAL---QERREALQRLAEYS-------------WDEIDVASAEREIAELE 674
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1004 EQLNMLTEASKKhsglLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQSPKTPPHFQ 1083
Cdd:COG4913 675 AELERLDASSDD----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767923891 1084 thlakLLETQEQEIEDGRASKtslehLVTKLNEDREVKNAEILRMKEQLRE 1134
Cdd:COG4913 751 -----LEERFAAALGDAVERE-----LRENLEERIDALRARLNRAEEELER 791
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
581-793 |
1.22e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 581 TEKLKAQLlQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKA-------NLNLENLLEATKacKRQEVSQLNKIHA 653
Cdd:COG3096 360 TERLEEQE-EVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQAldvqqtrAIQYQQAVQALE--KARALCGLPDLTP 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 654 ETLKEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSS--------ERIDWTKQQEELLSQLNVLEKQLQETQT 725
Cdd:COG3096 437 ENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELvckiagevERSQAWQTARELLRRYRSQQALAQRLQQ 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767923891 726 kndfLKSEVHDLRVVLHSADKelssvkleyssfKTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLES 793
Cdd:COG3096 517 ----LRAQLAELEQRLRQQQN------------AERLLEEFCQRIGQQLDAAEELEELLAELEAQLEE 568
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
582-859 |
1.23e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 582 EKLKAQLLQIQTELNNSKQEYEEFKELTRKRQLELE------SELQSLQKANLNLENLLEATKACKRQEVSQLN------ 649
Cdd:pfam05483 373 EKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEelkkilAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQarekei 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 650 ----------KIHAETLKEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQLNVLEKQ 719
Cdd:pfam05483 453 hdleiqltaiKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 720 LQETQTkndfLKSEVHDLRvvlhsadKELSSVKLEYSSFKTNQEKEFNKLSERHMHVQlqldnlrLENEKLLESKACLQD 799
Cdd:pfam05483 533 LKQIEN----LEEKEMNLR-------DELESVREEFIQKGDEVKCKLDKSEENARSIE-------YEVLKKEKQMKILEN 594
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 800 SYDNLQEimkfEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKLSLQFEEDKE 859
Cdd:pfam05483 595 KCNNLKK----QIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQ 650
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
438-700 |
1.25e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.38 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 438 KVTQLEDLTLKKEKFIQSNKMIVKFREDQIIRLEKLHKesrgGFLPEEQ--DRLLSELRNEIQTLREQIEHHPRVAKYAM 515
Cdd:PLN03188 892 EITQLNRLVQQYKHERECNAIIGQTREDKIIRLESLMD----GVLSKEDflEEELASLMHEHKLLKEKYENHPEVLRTKI 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 516 ENHSLREENRRLR----------LLEPVkraQEMDAQTIAKLEKafSEISGMEKSDKNQQGFSPKAQKEPCLFANTEklk 585
Cdd:PLN03188 968 ELKRVQDELEHYRnfydmgerevLLEEI---QDLRSQLQYYIDS--SLPSARKRNSLLKLTYSCEPSQAPPLNTIPE--- 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 586 aqllqiqtelnNSKQEYEEFKELTRKRQLELESELQSLQKanlNLENLLEATKACKRQEVSQLN--KIHAETLKEQMsal 663
Cdd:PLN03188 1040 -----------STDESPEKKLEQERLRWTEAESKWISLAE---ELRTELDASRALAEKQKHELDteKRCAEELKEAM--- 1102
|
250 260 270
....*....|....*....|....*....|....*..
gi 767923891 664 qaKLDEEEHKNLkLQQHVDKLEHHstqMQELFSSERI 700
Cdd:PLN03188 1103 --QMAMEGHARM-LEQYADLEEKH---IQLLARHRRI 1133
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
701-1089 |
2.10e-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: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 701 DWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSsfktNQEKEFNKLSERHMHVQLQL 780
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALK----NARLDLRRLFDEKQSEKDKK 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 781 dnlrleNEKLLESKACLQDSYDNLQEimkfEIDQLSRNLQNFKKENETlksdlnnlmELLEAEKERNNKLsLQFEEDKEN 860
Cdd:pfam12128 670 ------NKALAERKDSANERLNSLEA----QLKQLDKKHQAWLEEQKE---------QKREARTEKQAYW-QVVEGALDA 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 861 SSKEILKVLEAVRQEKQKETAKCEQQMAKvqkleeSLlatekvissleKSRDSDKKVVADLMNQIQELRTSVcektETID 940
Cdd:pfam12128 730 QLALLKAAIAARRSGAKAELKALETWYKR------DL-----------ASLGVDPDVIAKLKREIRTLERKI----ERIA 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 941 TLKQELKDINCKYNSALVDREESRVL-IKKQEVDILDLKEtlRLRILSEDIERDMlcedlahatEQLNMLTEASKKhsgL 1019
Cdd:pfam12128 789 VRRQEVLRYFDWYQETWLQRRPRLATqLSNIERAISELQQ--QLARLIADTKLRR---------AKLEMERKASEK---Q 854
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767923891 1020 LQSAQEELTKKEALIQELQH-KLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEDPQspKTPPHFQTHLAKL 1089
Cdd:pfam12128 855 QVRLSENLRGLRCEMSKLATlKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVK--KYVEHFKNVIADH 923
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
662-912 |
2.14e-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: 42.06 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 662 ALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQelfsSERIDWTKQQEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVL 741
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALK----KEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 742 HSADKELSSVKLEYSSFktnqekefnkLSERHMHVQLQLDNLRLENEKLLESKACLQdSYDNLQEIMKFEIDQLSRNLQN 821
Cdd:COG4942 93 AELRAELEAQKEELAEL----------LRALYRLGRQPPLALLLSPEDFLDAVRRLQ-YLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 822 FKKENETLKSDLNNLMELLEAEKERNNKLslqfeEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQKLEESLLATE 901
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAAL-----EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
250
....*....|.
gi 767923891 902 KVISSLEKSRD 912
Cdd:COG4942 237 AAAAERTPAAG 247
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
804-1071 |
2.41e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.22 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 804 LQEIMKFEIDQLSRNLQNFKKEN-ETLKSDLNNLMELLEAEKERNNKLSLQFEEDKENSSKEILKVLEAvrqekqketak 882
Cdd:PRK05771 25 LHELGVVHIEDLKEELSNERLRKlRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEE----------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 883 ceqqmaKVQKLEESLLATEKVISSLEksrdSDKKvvaDLMNQIQELrtsvcEKTETIDTlkqelkDINCKYNSALVDREE 962
Cdd:PRK05771 94 ------ELEKIEKEIKELEEEISELE----NEIK---ELEQEIERL-----EPWGNFDL------DLSLLLGFKYVSVFV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 963 SRVLIKKQEVDILDLKETLrLRILSEDIERDMLC-----EDLAHATEQLNMLtEASKKHSGLLQSAQEELTKKEALIQEL 1037
Cdd:PRK05771 150 GTVPEDKLEELKLESDVEN-VEYISTDKGYVYVVvvvlkELSDEVEEELKKL-GFERLELEEEGTPSELIREIKEELEEI 227
|
250 260 270
....*....|....*....|....*....|....
gi 767923891 1038 QHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAE 1071
Cdd:PRK05771 228 EKERESLLEELKELAKKYLEELLALYEYLEIELE 261
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1090-1317 |
2.88e-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: 41.98 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1090 LETQEQEIEDGRASKTSLEHLVTKLNEDREvKNAEILRMKEQLREMEN--LRLESQQLIEKNWLLQGQLDDIKRQKENSD 1167
Cdd:TIGR02169 179 LEEVEENIERLDLIIDEKRQQLERLRRERE-KAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1168 QNHPDNQQLKNEQEESIKERLAK--SKIVEEMLKMKADLEEVQS---------ALYNKEMEclRMTDEVERTQTLESKAF 1236
Cdd:TIGR02169 258 EEISELEKRLEEIEQLLEELNKKikDLGEEEQLRVKEKIGELEAeiaslersiAEKERELE--DAEERLAKLEAEIDKLL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1237 QEKEQLRSKLEEMYEERERTS-------QEMEMLRKQVECLAEENGKL-VGHQNLHQKIQYVVR----LKKENVRLAEET 1304
Cdd:TIGR02169 336 AEIEELEREIEEERKRRDKLTeeyaelkEELEDLRAELEEVDKEFAETrDELKDYREKLEKLKReineLKRELDRLQEEL 415
|
250
....*....|...
gi 767923891 1305 EKLRAENVFLKEK 1317
Cdd:TIGR02169 416 QRLSEELADLNAA 428
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
357-805 |
3.16e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.05 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 357 AQRAKLIKNKAvvNEDTQGNVSQLQAEVKRLKEQLAELASGQTPPESFLTRDKKKTNYMEYFQEAMLFFKKSEQEKKSLI 436
Cdd:PTZ00121 1443 AKKADEAKKKA--EEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE 1520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 437 EKVTQLEDLTLKKEKFIQSNKMIVKFREDQIIRLEKLHKESRGGFLPE----EQDRLLSELRNEIQTLREQIEHHPRVAK 512
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEakkaEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 513 YAMENHSLREENRRlrllEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQQGFSPKAQKEPCLFANTEKLKAQLLQIQ 592
Cdd:PTZ00121 1601 YEEEKKMKAEEAKK----AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 593 TELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNlenllEATKACKRQEVSQLNKIHAETLK-----EQMSALQAKL 667
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE-----EKKKAEELKKAEEENKIKAEEAKkeaeeDKKKAEEAKK 1751
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 668 DEEEHKNL-KLQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQ----------LNVLEKQLQETQTKNDFLKSEVHD 736
Cdd:PTZ00121 1752 DEEEKKKIaHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDkkikdifdnfANIIEGGKEGNLVINDSKEMEDSA 1831
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767923891 737 LRVVLHSADKELSSVKlEYSSFKTNQEKEFNKLSERHMHVQLQLDNLRLENEKLLESKACLQDSYDNLQ 805
Cdd:PTZ00121 1832 IKEVADSKNMQLEEAD-AFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIE 1899
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
617-1043 |
3.35e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 41.82 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 617 ESELQSlQKANLNLENLLEATKACKRQEVSQ----LNKIhaETLKEQMSALQAKLDEEEHKNLKLQQHVDKL-EHHSTQM 691
Cdd:PRK11281 38 EADVQA-QLDALNKQKLLEAEDKLVQQDLEQtlalLDKI--DRQKEETEQLKQQLAQAPAKLRQAQAELEALkDDNDEET 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 692 QELFSSERIdwtkqqEELLSQLNVLEKQLQETQTKNDFLKSEVHDLRVVLHSADKELSS-----VKLEYSSFKTNQEKEF 766
Cdd:PRK11281 115 RETLSTLSL------RQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYAnsqrlQQIRNLLKGGKVGGKA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 767 NKLSERHM-HVQLQLDNLRLE-NEKLLESKACLQDSYDNLQEIMKFEIDQLSRNLQNF-------------KKENETLKS 831
Cdd:PRK11281 189 LRPSQRVLlQAEQALLNAQNDlQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLqeainskrltlseKTVQEAQSQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 832 DLNNLME---LLEAEKERNNKLS--LQFEEDKENS-SKEILKVLEAVRQEKQKETAKCEQqmakVQKLEESLLATeKVIS 905
Cdd:PRK11281 269 DEAARIQanpLVAQELEINLQLSqrLLKATEKLNTlTQQNLRVKNWLDRLTQSERNIKEQ----ISVLKGSLLLS-RILY 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 906 SLEKSRDSDkKVVADLMNQIQELRTSVCEKTETIDTLKQelkdinckyNSALVDREESRvliKKQEVDIlDLKETLrLRI 985
Cdd:PRK11281 344 QQQQALPSA-DLIEGLADRIADLRLEQFEINQQRDALFQ---------PDAYIDKLEAG---HKSEVTD-EVRDAL-LQL 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 767923891 986 LsedIERDMLCEDLAHateQLN-MLTEASKkhsglLQSAQEELTkkeALIQELQHKLNQ 1043
Cdd:PRK11281 409 L---DERRELLDQLNK---QLNnQLNLAIN-----LQLNQQQLL---SVSDSLQSTLTQ 453
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
353-759 |
3.46e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 353 TLNFAQRAKLIKNKAVVnEDTQGNVSQLQAEVKRLKEQLAELasgqtppESFLTRDKKKTNYMEYFQEAMLFFKKSEQEK 432
Cdd:COG4717 67 ELNLKELKELEEELKEA-EEKEEEYAELQEELEELEEELEEL-------EAELEELREELEKLEKLLQLLPLYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 433 KSLIEKVTQLEDLtLKKEKFIQSNKMIVKFREDQIIRLEKLHKESRGGFLPEEQDRL------LSELRNEIQTLREQIEH 506
Cdd:COG4717 139 AELAELPERLEEL-EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELqdlaeeLEELQQRLAELEEELEE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 507 hprvAKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQQGFSPKAQKE-----PCLFANT 581
Cdd:COG4717 218 ----AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLvlgllALLFLLL 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 582 EKLKAQLLQIQTELNNSKQ----EYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKACKRQEvSQLNKIHAETLK 657
Cdd:COG4717 294 AREKASLGKEAEELQALPAleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-EELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 658 EQMSALQAKLDEEE-----HKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQ-EELLSQLNVLEKQLQETQTKNDFLK 731
Cdd:COG4717 373 AALLAEAGVEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEELLEALDeEELEEELEELEEELEELEEELEELR 452
|
410 420 430
....*....|....*....|....*....|
gi 767923891 732 SEVHDLRVVLHSA--DKELSSVKLEYSSFK 759
Cdd:COG4717 453 EELAELEAELEQLeeDGELAELLQELEELK 482
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
877-1263 |
3.98e-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: 41.42 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 877 QKETAKCEQQMAKV-QKLEESLLATEKVISSLEKSRDSDKKVVADLMNQIQELRTSVCEKTETIDTLKQELKDINC---- 951
Cdd:pfam07888 33 QNRLEECLQERAELlQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAssee 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 952 ---KYNSALVDREESRVLIKKQEVDIldlkETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELT 1028
Cdd:pfam07888 113 lseEKDALLAQRAAHEARIRELEEDI----KTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1029 KKEALIQELQHKLNQKKEEVEQKKNEYNFKMRQLEHVMDSAAEdpqspktpphfqthlaklLETQEQEIEDGRASKTSLE 1108
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE------------------NEALLEELRSLQERLNASE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1109 HLVTKLNEDREVKNAEILRMKEqlrEMENLRLESQQlieknwlLQGQLDDIKRQ-KENSDQNHPDNQQLKNEQEESiKER 1187
Cdd:pfam07888 251 RKVEGLGEELSSMAAQRDRTQA---ELHQARLQAAQ-------LTLQLADASLAlREGRARWAQERETLQQSAEAD-KDR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1188 LAksKIVEEMLKMKADLEEVQSALYNKEMECLRMTDeVERTQTLESK------------AFQEKEQLRSKLEEMYEERER 1255
Cdd:pfam07888 320 IE--KLSAELQRLEERLQEERMEREKLEVELGREKD-CNRVQLSESRrelqelkaslrvAQKEKEQLQAEKQELLEYIRQ 396
|
....*...
gi 767923891 1256 TSQEMEML 1263
Cdd:pfam07888 397 LEQRLETV 404
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
105-304 |
4.19e-03 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 41.26 E-value: 4.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 105 IFAYGQTGSGKTFTMMGPSESDNFShnlrgVIPRSFEYLFSLIDREKEKagagKSFlCKCSFIEIyNEQIYDLLDSASAG 184
Cdd:COG5059 385 IFAYMQSLKKETETLKSRIDLIMKS-----IISGTFERKKLLKEEGWKY----KST-LQFLRIEI-DRLLLLREEELSKK 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 185 LYLREHIKKGVFVVGAVEQVVTSAAEAYQVLSGGWRNRRVASTSMNRESSRSHAVFT-ITIESMEKSNEIvnirtsLLNL 263
Cdd:COG5059 454 KTKIHKLNKLRHDLSSLLSSIPEETSDRVESEKASKLRSSASTKLNLRSSRSHSKFRdHLNGSNSSTKEL------SLNQ 527
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767923891 264 VDLAGSERqKDTHAEGMRLKEAGNINRSLSCLGQVITALVD 304
Cdd:COG5059 528 VDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHALGS 567
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
909-1198 |
4.39e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 41.38 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 909 KSRDSDKKVVADLMNQIQELRTSVCEK------------TETIDTLKQElkdINCKYNSALVDRE-ESRVLIKKQEVDIL 975
Cdd:PLN03229 422 KKREAVKTPVRELEGEVEKLKEQILKAkessskpselalNEMIEKLKKE---IDLEYTEAVIAMGlQERLENLREEFSKA 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 976 DLKETLRLRILSEDIER--DMLCEDLAHA------TEQLNMLTEASKKhsgllQSAQEELTKKEALIQELQHKLNQK--- 1044
Cdd:PLN03229 499 NSQDQLMHPVLMEKIEKlkDEFNKRLSRApnylslKYKLDMLNEFSRA-----KALSEKKSKAEKLKAEINKKFKEVmdr 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1045 -----------------------------KEEVEQKKNEYNFKMRQLEHVMD-------SAAEDPQSPKTPPHFQTHLAK 1088
Cdd:PLN03229 574 peikekmealkaevassgassgdeldddlKEKVEKMKKEIELELAGVLKSMGlevigvtKKNKDTAEQTPPPNLQEKIES 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1089 LLETQEQEIEDGRAS---KTSLEHL---VTKLNEDREVKNAE-ILRMKEQLREMENLRLESQQLIEKNWLLQGQLddikr 1161
Cdd:PLN03229 654 LNEEINKKIERVIRSsdlKSKIELLkleVAKASKTPDVTEKEkIEALEQQIKQKIAEALNSSELKEKFEELEAEL----- 728
|
330 340 350
....*....|....*....|....*....|....*..
gi 767923891 1162 qKENSDQNHPDNQQLKNeqeESIKERLAKSKIVEEML 1198
Cdd:PLN03229 729 -AAARETAAESNGSLKN---DDDKEEDSKEDGSRVEV 761
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
489-892 |
4.83e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 489 LLSELRNEIQTLreqieHHPRVAKYAMENHSLREENRRLRLLEPVKRAQEMDAQTIAKLEKAFSEISGMEKSDKNQQGFS 568
Cdd:COG4717 47 LLERLEKEADEL-----FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 569 PKAQKEPCLFANTEKLKAQLLQIQTELNNSKQEYEEFKELTRKRQlELESELQSLQKAnlnLENLLEATKACKRQEVSQL 648
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE-ELEAELAELQEE---LEELLEQLSLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 649 nkihAETLKEQMSALQAKLDEEEHKNLKLQQHVDKLEHHSTQMQELFSSERIDWTKQQEELLSQLNVLEKQ--------- 719
Cdd:COG4717 198 ----AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLggsllslil 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 720 -------------------LQETQTKNDFLKSEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKEFNKLSERHMHVQLQL 780
Cdd:COG4717 274 tiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 781 DNLRLENEKLLeskacLQDSYDNLQEIMKF----------EIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERNNKL 850
Cdd:COG4717 354 REAEELEEELQ-----LEELEQEIAALLAEagvedeeelrAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEE 428
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 767923891 851 SLqfeEDKENSSKEILKVLEAVRQEKQKETAKCEQQMAKVQK 892
Cdd:COG4717 429 EL---EEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
763-1235 |
4.93e-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: 41.36 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 763 EKEFNKLSERHMhvQLQLDNLRLENEKLLESKacLQDSYDNLQEIMKFEIDQLSRNLQNFKKENETLKSDLNNLMELLEA 842
Cdd:pfam12128 247 QQEFNTLESAEL--RLSHLHFGYKSDETLIAS--RQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 843 EKERNNKLSLQFEEDKENSSKEILKVLEAVRQEkqketakCEQQMAKVQKLEESLLATEKVISSLEKSRDSD-KKVVADL 921
Cdd:pfam12128 323 ELEALEDQHGAFLDADIETAAADQEQLPSWQSE-------LENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGI 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 922 MNQIQELRtsvcektETIDTLKQELKDINCKYNSALVDREESRVL-IKKQEVDILDLKETLRLRILSEDIERDMLcEDLA 1000
Cdd:pfam12128 396 KDKLAKIR-------EARDRQLAVAEDDLQALESELREQLEAGKLeFNEEEYRLKSRLGELKLRLNQATATPELL-LQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1001 HATEQLNMLTEASKKHSGLLQSAQEELTKKEALIQELQHKLNQKKEEVEQKKNEynfkMRQLEHVMDSAAEDPQS--PKT 1078
Cdd:pfam12128 468 NFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSA----LDELELQLFPQAGTLLHflRKE 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1079 PPHFQTHLAKLLETQE------QEIEDGRASKTSLEHLVTKLNEDReVKNAEILRMKEQLRE--------MENLRLESQQ 1144
Cdd:pfam12128 544 APDWEQSIGKVISPELlhrtdlDPEVWDGSVGGELNLYGVKLDLKR-IDVPEWAASEEELRErldkaeeaLQSAREKQAA 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1145 LIEKNWLLQGQLDDIKRQKENSD---QNHPDNQQLKNEQEESIKERLAKSKIVEEMLKMKA--DLEEVQSALYNKEMECL 1219
Cdd:pfam12128 623 AEEQLVQANGELEKASREETFARtalKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERlnSLEAQLKQLDKKHQAWL 702
|
490
....*....|....*.
gi 767923891 1220 RMTDEVERTQTLESKA 1235
Cdd:pfam12128 703 EEQKEQKREARTEKQA 718
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
584-726 |
5.00e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 5.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 584 LKAQLLQIQTELNNSKQEYEEFKE------------LTRKRQLELESELQSLQKANLNLENLLEATKACKRQEVSQLNKI 651
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEEFRQknglvdlseeakLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 652 HA----ETLKEQMSALQAKLDE------EEHKNLK-LQQHVDKLEhhsTQMQELFSSERIDWTKQQEELLSQLNVLEKQL 720
Cdd:COG3206 260 LQspviQQLRAQLAELEAELAElsarytPNHPDVIaLRAQIAALR---AQLQQEAQRILASLEAELEALQAREASLQAQL 336
|
....*.
gi 767923891 721 QETQTK 726
Cdd:COG3206 337 AQLEAR 342
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
704-1136 |
7.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 704 KQQEELLSQLNVLEKQLQETQTKNDflksEVHDLRVVLHSADKELSSVKLEYSSFKTNQEKefnklserhMHVQLQLDNL 783
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEE----EYAELQEELEELEEELEELEAELEELREELEK---------LEKLLQLLPL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 784 RLENEKLLESKACLQDSYDNLQEIMKfEIDQLSRNLQNFKKENETLKSDLNNLMELLEAEKERnnklslQFEEDKENssk 863
Cdd:COG4717 131 YQELEALEAELAELPERLEELEERLE-ELRELEEELEELEAELAELQEELEELLEQLSLATEE------ELQDLAEE--- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 864 eilkvLEAVRQEKQKETAKCEQQMAKVQKLEESLLATEKVISSLEKSRD-SDKKVVADLMNQIQELRTSVCEKTETIDTL 942
Cdd:COG4717 201 -----LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERlKEARLLLLIAAALLALLGLGGSLLSLILTI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 943 KQELKDI-----------NCKYNSALVDREESRVLIKKQEVDILDLKETLRLRILSEDIERDMLCEDLAHATEQLNMLTE 1011
Cdd:COG4717 276 AGVLFLVlgllallflllAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1012 ASKKHSGLLQSAQEEltKKEALIQ--------ELQHKLNQKKEEVEQKKneynfKMRQLEHVMDSAAEDPQSPKTPPHFQ 1083
Cdd:COG4717 356 AEELEEELQLEELEQ--EIAALLAeagvedeeELRAALEQAEEYQELKE-----ELEELEEQLEELLGELEELLEALDEE 428
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767923891 1084 THLAKLLETQEQ------EIEDGRASKTSLEHLVTKLNEDREV--KNAEILRMKEQLREME 1136
Cdd:COG4717 429 ELEEELEELEEEleeleeELEELREELAELEAELEQLEEDGELaeLLQELEELKAELRELA 489
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
431-1162 |
8.04e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 40.81 E-value: 8.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 431 EKKSLIEKVTQLEDLTLKKEKFIQSNKMIVK-FREDQIIRLEKLHK-ESRGGFLPEEQDRllSELRNEIQTLREQIEHHP 508
Cdd:TIGR01612 1487 ELKEHIDKSKGCKDEADKNAKAIEKNKELFEqYKKDVTELLNKYSAlAIKNKFAKTKKDS--EIIIKEIKDAHKKFILEA 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 509 RVAKYAMEnhslREENRRLRLLEPVKRAQE-----MDAQT-IAKLEKAFSEISGMEKSDKNQQGFSPKAQKEPCLFA-NT 581
Cdd:TIGR01612 1565 EKSEQKIK----EIKKEKFRIEDDAAKNDKsnkaaIDIQLsLENFENKFLKISDIKKKINDCLKETESIEKKISSFSiDS 1640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 582 EKLKaqlLQIQTELNNSKQEYEEFKELTRKRQLELESELQSLQKANLNLENLLEATKAC-------KRQEVSQLNKIHAE 654
Cdd:TIGR01612 1641 QDTE---LKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNyeigiieKIKEIAIANKEEIE 1717
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 655 TLKEQMSALQAKLDEEEHKN-LKLQQHVDKLEHHSTQMQELFsseridwtkqqEELLSQLNVLEKQLqETQTKNDFLKSE 733
Cdd:TIGR01612 1718 SIKELIEPTIENLISSFNTNdLEGIDPNEKLEEYNTEIGDIY-----------EEFIELYNIIAGCL-ETVSKEPITYDE 1785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 734 VHDLRVVLHSADKELSSVKLEYSSFKTNQE-KEFNKLSErhmHVQLQLDNLrleNEKLLESKACLQDSYDNLqeimkfei 812
Cdd:TIGR01612 1786 IKNTRINAQNEFLKIIEIEKKSKSYLDDIEaKEFDRIIN---HFKKKLDHV---NDKFTKEYSKINEGFDDI-------- 1851
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 813 dqlSRNLQNFKKEnetlkSDLNNLMELLEAEKERN----NKLSLQFEEDKENSSKEILKVLEAVRQEKQKETAkceqqma 888
Cdd:TIGR01612 1852 ---SKSIENVKNS-----TDENLLFDILNKTKDAYagiiGKKYYSYKDEAEKIFINISKLANSINIQIQNNSG------- 1916
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 889 kVQKLEESLLAtekVISSLEKSRDSDKKVVADLMNQiQELRTSVCEKTETIDTLKQELKDINCKYNSALVDREESRVLIK 968
Cdd:TIGR01612 1917 -IDLFDNINIA---ILSSLDSEKEDTLKFIPSPEKE-PEIYTKIRDSYDTLLDIFKKSQDLHKKEQDTLNIIFENQQLYE 1991
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 969 KQEVDIlDLKETLR-LRILSEDIERDMlcEDLAHATEQLNMLTEASKKHSGLLQSAQeeltkkealiqelQHKLNQKKEE 1047
Cdd:TIGR01612 1992 KIQASN-ELKDTLSdLKYKKEKILNDV--KLLLHKFDELNKLSCDSQNYDTILELSK-------------QDKIKEKIDN 2055
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1048 VEQKKNEY--NFKMRQLEHVMDSAAEDPQSpktpphfqthlaklLETQEQEIEdgrasktslehlvtKLNEDREVKNAEI 1125
Cdd:TIGR01612 2056 YEKEKEKFgiDFDVKAMEEKFDNDIKDIEK--------------FENNYKHSE--------------KDNHDFSEEKDNI 2107
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 767923891 1126 LRMKEQLREMENL-----RLESQQLIEKNWLLQgQLDDIKRQ 1162
Cdd:TIGR01612 2108 IQSKKKLKELTEAfnteiKIIEDKIIEKNDLID-KLIEMRKE 2148
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1094-1308 |
9.06e-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: 40.26 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1094 EQEIEDGRASKTSLEHLVTKLNEDREVKNAEILRMKEQLREMENLRLESQQLI-----EKNWLLQGQLDDIKRQKENSDQ 1168
Cdd:pfam07888 58 EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSeelseEKDALLAQRAAHEARIRELEED 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1169 NHPDNQ---------------------QLKNEQEESIKERLAKSKIVEEMLKMKADLEEVQSALYNKEMECLRMTDEVER 1227
Cdd:pfam07888 138 IKTLTQrvleretelermkerakkagaQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767923891 1228 TQTLESKAFQEKEQLRSKLEEMYEERERtsqeMEMLRKQVECLAEENGKLVGHQNLHQKIQYVVRLK--KENVRLAEETE 1305
Cdd:pfam07888 218 LTQKLTTAHRKEAENEALLEELRSLQER----LNASERKVEGLGEELSSMAAQRDRTQAELHQARLQaaQLTLQLADASL 293
|
...
gi 767923891 1306 KLR 1308
Cdd:pfam07888 294 ALR 296
|
|
| |
