|
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: 602.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 25 DAIKVFVRIRPAEEgaRSADGEQSFCLSVLSQTTLRLHSNPdPKTFVFDYVAGMDTTQESVFSTVAKSIVESCMSGYNGT 104
Cdd:cd01373 1 DAVKVFVRIRPPAE--REGDGEYGQCLKKLSSDTLVLHSKP-PKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 105 IFAYGQTGSGKTFTMMGPSDSDN-FSHNLRGIIPRSFEYLFSLIDREKEKAGAGKSFLCKCSFIEVYNEQIYDLLDSASV 183
Cdd:cd01373 78 IFAYGQTGSGKTYTMWGPSESDNeSPHGLRGVIPRIFEYLFSLIQREKEKAGEGKSFLCKCSFLEIYNEQIYDLLDPASR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 184 GLYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEKSSETVNIRTSLLNL 263
Cdd:cd01373 158 NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACFVNIRTSRLNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 264 VDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDVGNGKQRHICYRDSKLTFLLRDSLGGNAKTAIIANVHPG 343
Cdd:cd01373 238 VDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPS 317
|
330 340 350
....*....|....*....|....*....|
gi 39930325 344 SRCFGETLSTLNFAQRAKLIKNKAVVNEDT 373
Cdd:cd01373 318 SKCFGETLSTLRFAQRAKLIKNKAVVNEDT 347
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
26-370 |
8.20e-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: 462.43 E-value: 8.20e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 26 AIKVFVRIRPAEEGARSADGEQSFCLSVLSQTTLRLHSNPDP---KTFVFDYVAGMDTTQESVFSTVAKSIVESCMSGYN 102
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTVRSPKNRqgeKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 103 GTIFAYGQTGSGKTFTMMGPSDSdnfshnlRGIIPRSFEYLFSLIDREKEkagaGKSFLCKCSFIEVYNEQIYDLLDSAS 182
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIGTPDS-------PGIIPRALKDLFEKIDKREE----GWQFSVKVSYLEIYNEKIRDLLNPSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 183 VGLYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEKSSETVNIRTSLLN 262
Cdd:smart00129 150 KKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 263 LVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgNGKQRHICYRDSKLTFLLRDSLGGNAKTAIIANVHP 342
Cdd:smart00129 230 LVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQ--HSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSP 307
|
330 340
....*....|....*....|....*...
gi 39930325 343 GSRCFGETLSTLNFAQRAKLIKNKAVVN 370
Cdd:smart00129 308 SSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
26-361 |
3.02e-149 |
|
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: 455.18 E-value: 3.02e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 26 AIKVFVRIRPAEEgaRSADGEQSfCLSVLSQTTLRLHSNPD----PKTFVFDYVAGMDTTQESVFSTVAKSIVESCMSGY 101
Cdd:cd00106 1 NVRVAVRVRPLNG--REARSAKS-VISVDGGKSVVLDPPKNrvapPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 102 NGTIFAYGQTGSGKTFTMMGPSDSDnfshnlRGIIPRSFEYLFSLIDREKEKagaGKSFLCKCSFIEVYNEQIYDLLDSA 181
Cdd:cd00106 78 NGTIFAYGQTGSGKTYTMLGPDPEQ------RGIIPRALEDIFERIDKRKET---KSSFSVSASYLEIYNEKIYDLLSPV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 182 -SVGLYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEKSSETVNIRTSL 260
Cdd:cd00106 149 pKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVTSSK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 261 LNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgnGKQRHICYRDSKLTFLLRDSLGGNAKTAIIANV 340
Cdd:cd00106 229 LNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALAD---GQNKHIPYRDSKLTRLLQDSLGGNSKTIMIACI 305
|
330 340
....*....|....*....|.
gi 39930325 341 HPGSRCFGETLSTLNFAQRAK 361
Cdd:cd00106 306 SPSSENFEETLSTLRFASRAK 326
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
32-363 |
3.94e-139 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 428.53 E-value: 3.94e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 32 RIRPAEEGARSADGEQ-SFCLSVLSQTTLRLHSNPD--PKTFVFDYVAGMDTTQESVFSTVAKSIVESCMSGYNGTIFAY 108
Cdd:pfam00225 1 RVRPLNEREKERGSSViVSVESVDSETVESSHLTNKnrTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 109 GQTGSGKTFTMMGPSDSdnfshnlRGIIPRSFEYLFSLIDREKEKagagKSFLCKCSFIEVYNEQIYDLLDSA---SVGL 185
Cdd:pfam00225 81 GQTGSGKTYTMEGSDEQ-------PGIIPRALEDLFDRIQKTKER----SEFSVKVSYLEIYNEKIRDLLSPSnknKRKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 186 YLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEKSSET-VNIRTSLLNLV 264
Cdd:pfam00225 150 RIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGeESVKTGKLNLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 265 DLAGSERQKDTH-AEGMRLKEAGNINRSLSCLGQVITALVDvgnGKQRHICYRDSKLTFLLRDSLGGNAKTAIIANVHPG 343
Cdd:pfam00225 230 DLAGSERASKTGaAGGQRLKEAANINKSLSALGNVISALAD---KKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPS 306
|
330 340
....*....|....*....|
gi 39930325 344 SRCFGETLSTLNFAQRAKLI 363
Cdd:pfam00225 307 SSNYEETLSTLRFASRAKNI 326
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
26-363 |
1.03e-110 |
|
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276825 [Multi-domain] Cd Length: 321 Bit Score: 352.02 E-value: 1.03e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 26 AIKVFVRIRPAEEGARSADGEqsfCLSVLSQTTLrLHSNPDPKTFVFDYVAGMDTTQESVFSTVAKSIVESCMSGYNGTI 105
Cdd:cd01374 1 KITVTVRVRPLNSREIGINEQ---VAWEIDNDTI-YLVEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 106 FAYGQTGSGKTFTMMGPSDSDnfshnlrGIIPRSFEYLFSLIDREKEKAgagksFLCKCSFIEVYNEQIYDLLDSASVGL 185
Cdd:cd01374 77 FAYGQTSSGKTFTMSGDEDEP-------GIIPLAIRDIFSKIQDTPDRE-----FLLRVSYLEIYNEKINDLLSPTSQNL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 186 YLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEKS-SETVNIRTSLLNLV 264
Cdd:cd01374 145 KIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGeLEEGTVRVSTLNLI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 265 DLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALvdvGNGK-QRHICYRDSKLTFLLRDSLGGNAKTAIIANVHPG 343
Cdd:cd01374 225 DLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKL---SEGKvGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPA 301
|
330 340
....*....|....*....|
gi 39930325 344 SRCFGETLSTLNFAQRAKLI 363
Cdd:cd01374 302 ESHVEETLNTLKFASRAKKI 321
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
25-363 |
4.29e-110 |
|
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: 350.61 E-value: 4.29e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 25 DAIKVFVRIRPAEEGARSADGEQSFCLSV-LSQTTLRlhsNPD------PKTFVFDYVAGMDTTQESVFSTVAKSIVESC 97
Cdd:cd01371 1 ENVKVVVRCRPLNGKEKAAGALQIVDVDEkRGQVSVR---NPKatanepPKTFTFDAVFDPNSKQLDVYDETARPLVDSV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 98 MSGYNGTIFAYGQTGSGKTFTMMGPSDSDnfshNLRGIIPRSFEYLFSLIDREKEKagagKSFLCKCSFIEVYNEQIYDL 177
Cdd:cd01371 78 LEGYNGTIFAYGQTGTGKTYTMEGKREDP----ELRGIIPNSFAHIFGHIARSQNN----QQFLVRVSYLEIYNEEIRDL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 178 L-DSASVGLYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEKSSETVN- 255
Cdd:cd01371 150 LgKDQTKRLELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENh 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 256 IRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgnGKQRHICYRDSKLTFLLRDSLGGNAKTA 335
Cdd:cd01371 230 IRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVD---GKSTHIPYRDSKLTRLLQDSLGGNSKTV 306
|
330 340
....*....|....*....|....*...
gi 39930325 336 IIANVHPGSRCFGETLSTLNFAQRAKLI 363
Cdd:cd01371 307 MCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
27-365 |
7.33e-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: 341.50 E-value: 7.33e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 27 IKVFVRIRPAEEGARSADGEqsfCLSVLSQTTLRLH---SNPDPKTFVFDYVAGMDTTQESVFSTVaKSIVESCMSGYNG 103
Cdd:cd01366 4 IRVFCRVRPLLPSEENEDTS---HITFPDEDGQTIEltsIGAKQKEFSFDKVFDPEASQEDVFEEV-SPLVQSALDGYNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 104 TIFAYGQTGSGKTFTMMGPSDSDnfshnlrGIIPRSFEYLFSLIdreKEKAGAGKSFLCKCSFIEVYNEQIYDLLDSASV 183
Cdd:cd01366 80 CIFAYGQTGSGKTYTMEGPPESP-------GIIPRALQELFNTI---KELKEKGWSYTIKASMLEIYNETIRDLLAPGNA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 184 G---LYLR-EHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESmeKSSETVNIRTS 259
Cdd:cd01366 150 PqkkLEIRhDSEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISG--RNLQTGEISVG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 260 LLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALvdvgNGKQRHICYRDSKLTFLLRDSLGGNAKTAIIAN 339
Cdd:cd01366 228 KLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL----RQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVN 303
|
330 340
....*....|....*....|....*.
gi 39930325 340 VHPGSRCFGETLSTLNFAQRAKLIKN 365
Cdd:cd01366 304 ISPAESNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
25-363 |
4.21e-104 |
|
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: 333.91 E-value: 4.21e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 25 DAIKVFVRIRPaEEGARSADGEQsFCLSVLSQTTLRLHSNPDPKTFVFDYVAGMDTTQESVFSTVAKSIVESCMSGYNGT 104
Cdd:cd01369 2 CNIKVVCRFRP-LNELEVLQGSK-SIVKFDPEDTVVIATSETGKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 105 IFAYGQTGSGKTFTMMGPSDSDnfshNLRGIIPRSFEYLFSLIdrekEKAGAGKSFLCKCSFIEVYNEQIYDLLDSASVG 184
Cdd:cd01369 80 IFAYGQTSSGKTYTMEGKLGDP----ESMGIIPRIVQDIFETI----YSMDENLEFHVKVSYFEIYMEKIRDLLDVSKTN 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 185 LYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIEsmEKSSETVNIRTSLLNLV 264
Cdd:cd01369 152 LSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVK--QENVETEKKKSGKLYLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 265 DLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgnGKQRHICYRDSKLTFLLRDSLGGNAKTAIIANVHPGS 344
Cdd:cd01369 230 DLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD---GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPSS 306
|
330
....*....|....*....
gi 39930325 345 RCFGETLSTLNFAQRAKLI 363
Cdd:cd01369 307 YNESETLSTLRFGQRAKTI 325
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
26-364 |
1.59e-102 |
|
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: 330.45 E-value: 1.59e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 26 AIKVFVRIRPAEegARSADGEQSFCLSVLSQTTlRLHSNPDpKTFVFDYVAGMDTTQESVFSTVAKSIVESCMSGYNGTI 105
Cdd:cd01372 2 SVRVAVRVRPLL--PKEIIEGCRICVSFVPGEP-QVTVGTD-KSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 106 FAYGQTGSGKTFTMMGPSDSDNFSHNLrGIIPRSFEYLFSLIDREKEkagaGKSFLCKCSFIEVYNEQIYDLLDSASVG- 184
Cdd:cd01372 78 LAYGQTGSGKTYTMGTAYTAEEDEEQV-GIIPRAIQHIFKKIEKKKD----TFEFQLKVSFLEIYNEEIRDLLDPETDKk 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 185 --LYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEKSSETVNIR----- 257
Cdd:cd01372 153 ptISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSaddkn 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 258 ---TSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvGNGKQRHICYRDSKLTFLLRDSLGGNAKT 334
Cdd:cd01372 233 stfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGD-ESKKGAHVPYRDSKLTRLLQDSLGGNSHT 311
|
330 340 350
....*....|....*....|....*....|
gi 39930325 335 AIIANVHPGSRCFGETLSTLNFAQRAKLIK 364
Cdd:cd01372 312 LMIACVSPADSNFEETLNTLKYANRARNIK 341
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
25-370 |
4.15e-97 |
|
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: 316.22 E-value: 4.15e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 25 DAIKVFVRIRP-----AEEGAR---SADGEQSFCLSVLSQTTLRLHSNPDPKTFVFDY----VAGMD---TTQESVFSTV 89
Cdd:cd01365 1 ANVKVAVRVRPfnsreKERNSKcivQMSGKETTLKNPKQADKNNKATREVPKSFSFDYsywsHDSEDpnyASQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 90 AKSIVESCMSGYNGTIFAYGQTGSGKTFTMMGPSDSdnfshnlRGIIPRSFEYLFSLIDREKEKAgagKSFLCKCSFIEV 169
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQ-------PGIIPRLCEDLFSRIADTTNQN---MSYSVEVSYMEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 170 YNEQIYDLLDS----ASVGLYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITI- 244
Cdd:cd01365 151 YNEKVRDLLNPkpkkNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLt 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 245 -ESMEKSSETVNIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDVGN----GKQRHICYRDSK 319
Cdd:cd01365 231 qKRHDAETNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskKKSSFIPYRDSV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 39930325 320 LTFLLRDSLGGNAKTAIIANVHPGSRCFGETLSTLNFAQRAKLIKNKAVVN 370
Cdd:cd01365 311 LTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
27-372 |
7.09e-95 |
|
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: 309.64 E-value: 7.09e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 27 IKVFVRIRPAEEGARSADGEQ-----SFCLSVLSQTTLRLHSNPDpKTFVFDYVAGMDTTQESVFSTVAKSIVESCMSGY 101
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSvvevdPVRKEVSVRTGGLADKSST-KTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 102 NGTIFAYGQTGSGKTFTMMGPSDSDNFSH----NLRGIIPRSFEYLFSLIDREkekagaGKSFLCKCSFIEVYNEQIYDL 177
Cdd:cd01364 83 NCTIFAYGQTGTGKTYTMEGDRSPNEEYTweldPLAGIIPRTLHQLFEKLEDN------GTEYSVKVSYLEIYNEELFDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 178 LDSAS-VGLYLREH----IKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEKSSE 252
Cdd:cd01364 157 LSPSSdVSERLRMFddprNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTID 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 253 TVN-IRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgngKQRHICYRDSKLTFLLRDSLGGN 331
Cdd:cd01364 237 GEElVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE----RAPHVPYRESKLTRLLQDSLGGR 312
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 39930325 332 AKTAIIANVHPGSRCFGETLSTLNFAQRAKLIKNKAVVNED 372
Cdd:cd01364 313 TKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVNQK 353
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
27-391 |
7.48e-95 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 334.60 E-value: 7.48e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 27 IKVFVRIRP---AEEGARSADGEQSFCLSVLSQTtlrlhsnpdpktFVFDYVAGMDTTQESVFSTVAKSIVESCMSGYNG 103
Cdd:PLN03188 100 VKVIVRMKPlnkGEEGEMIVQKMSNDSLTINGQT------------FTFDSIADPESTQEDIFQLVGAPLVENCLAGFNS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 104 TIFAYGQTGSGKTFTMMGPSD---SDNFSHNLRGIIPRSFEYLFSLIDREKEK-AGAGKSFLCKCSFIEVYNEQIYDLLD 179
Cdd:PLN03188 168 SVFAYGQTGSGKTYTMWGPANgllEEHLSGDQQGLTPRVFERLFARINEEQIKhADRQLKYQCRCSFLEIYNEQITDLLD 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 180 SASVGLYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEKSSE--TVNIR 257
Cdd:PLN03188 248 PSQKNLQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVAdgLSSFK 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 258 TSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDVGN-GKQRHICYRDSKLTFLLRDSLGGNAKTAI 336
Cdd:PLN03188 328 TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtGKQRHIPYRDSRLTFLLQESLGGNAKLAM 407
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 39930325 337 IANVHPGSRCFGETLSTLNFAQRAKLIKNKAVVNEDTQGNVSQLQAEVKRLKEQL 391
Cdd:PLN03188 408 VCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDDVNFLREVIRQLRDEL 462
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
27-363 |
1.67e-92 |
|
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: 302.73 E-value: 1.67e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 27 IKVFVRIRP-----AEEGARS--------------ADGEQSFCLSVLSQTTLRLHSNPDpKTFVFDYVAGMDTTQESVFS 87
Cdd:cd01370 2 LTVAVRVRPfsekeKNEGFRRivkvmdnhmlvfdpKDEEDGFFHGGSNNRDRRKRRNKE-LKYVFDRVFDETSTQEEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 88 TVAKSIVESCMSGYNGTIFAYGQTGSGKTFTMMGPSDSDnfshnlrGIIPRSFEYLFSLIDREKEKagagKSFLCKCSFI 167
Cdd:cd01370 81 ETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEP-------GLMVLTMKELFKRIESLKDE----KEFEVSMSYL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 168 EVYNEQIYDLLDSASVGLYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESM 247
Cdd:cd01370 150 EIYNETIRDLLNPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 248 EK-SSETVNIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvGNGKQRHICYRDSKLTFLLRD 326
Cdd:cd01370 230 DKtASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALAD-PGKKNKHIPYRDSKLTRLLKD 308
|
330 340 350
....*....|....*....|....*....|....*..
gi 39930325 327 SLGGNAKTAIIANVHPGSRCFGETLSTLNFAQRAKLI 363
Cdd:cd01370 309 SLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
26-361 |
6.17e-81 |
|
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: 269.84 E-value: 6.17e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 26 AIKVFVRIRP----AEEGARSADGEQSfcLSVLSQTTLR---LHSNPDPKTFVFDYVAGmDTTQESVFSTVAKSIVESCM 98
Cdd:cd01375 1 KVQAFVRVRPtddfAHEMIKYGEDGKS--ISIHLKKDLRrgvVNNQQEDWSFKFDGVLH-NASQELVYETVAKDVVSSAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 99 SGYNGTIFAYGQTGSGKTFTMMGpsDSDNFSHnlRGIIPRSFEYLFSLIDREKEKAgagksFLCKCSFIEVYNEQIYDLL 178
Cdd:cd01375 78 AGYNGTIFAYGQTGAGKTFTMTG--GTENYKH--RGIIPRALQQVFRMIEERPTKA-----YTVHVSYLEIYNEQLYDLL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 179 DS------ASVGLYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEKSSE 252
Cdd:cd01375 149 STlpyvgpSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 253 TVNIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALvdvGNGKQRHICYRDSKLTFLLRDSLGGNA 332
Cdd:cd01375 229 SEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIAL---SDKDRTHVPFRQSKLTHVLRDSLGGNC 305
|
330 340
....*....|....*....|....*....
gi 39930325 333 KTAIIANVHPGSRCFGETLSTLNFAQRAK 361
Cdd:cd01375 306 NTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
25-361 |
1.28e-77 |
|
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: 260.79 E-value: 1.28e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 25 DAIKVFVRIRPAeeGARSADGEQSFCLSVLSQTTLRLH-------------SNPDPKTFVFDYVAGMDTTQESVFSTVAK 91
Cdd:cd01368 1 DPVKVYLRVRPL--SKDELESEDEGCIEVINSTTVVLHppkgsaanksernGGQKETKFSFSKVFGPNTTQKEFFQGTAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 92 SIVESCMSGYNGTIFAYGQTGSGKTFTMMGPSDSdnfshnlRGIIPRSFEYLFSLIdrekekagagKSFLCKCSFIEVYN 171
Cdd:cd01368 79 PLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGD-------GGILPRSLDVIFNSI----------GGYSVFVSYIEIYN 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 172 EQIYDLLDSASVG-------LYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITI 244
Cdd:cd01368 142 EYIYDLLEPSPSSptkkrqsLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 245 ESMEKSS------ETVNIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITAL-VDVGNGKQRHICYRD 317
Cdd:cd01368 222 VQAPGDSdgdvdqDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLrENQLQGTNKMVPFRD 301
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 39930325 318 SKLTFLLRDSLGGNAKTAIIANVHPGSRCFGETLSTLNFAQRAK 361
Cdd:cd01368 302 SKLTHLFQNYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
11-500 |
4.02e-76 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 264.29 E-value: 4.02e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 11 NVTNSHSNQPSNEGDAIKVFVRIRPAEEGARSADGEQSfcLSVLSQTTlrlhsnpDPKTFVFDYVAGMDTTQESVFSTVA 90
Cdd:COG5059 8 PLKSRLSSRNEKSVSDIKSTIRIIPGELGERLINTSKK--SHVSLEKS-------KEGTYAFDKVFGPSATQEDVYEETI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 91 KSIVESCMSGYNGTIFAYGQTGSGKTFTMMGpsdsdnfSHNLRGIIPRSFEYLFSLIDREKekagAGKSFLCKCSFIEVY 170
Cdd:COG5059 79 KPLIDSLLLGYNCTVFAYGQTGSGKTYTMSG-------TEEEPGIIPLSLKELFSKLEDLS----MTKDFAVSISYLEIY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 171 NEQIYDLLDSASVGLYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEKS 250
Cdd:COG5059 148 NEKIYDLLSPNEESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 251 SETvnIRTSLLNLVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALVDvgNGKQRHICYRDSKLTFLLRDSLGG 330
Cdd:COG5059 228 SGT--SETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGD--KKKSGHIPYRESKLTRLLQDSLGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 331 NAKTAIIANVHPGSRCFGETLSTLNFAQRAKLIKNKAVVNedtqgNVSQLQAEVKRLKEQLSQFTSGQITPESLLARDKE 410
Cdd:COG5059 304 NCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVN-----SSSDSSREIEEIKFDLSEDRSEIEILVFREQSQLS 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 411 KTNYIEYFlEAMLFFKKSEQEKKSLIEKITQL------EDLTLKKEKFiQSNKMIVKFREDQIMRLERLHKEGRGSflPE 484
Cdd:COG5059 379 QSSLSGIF-AYMQSLKKETETLKSRIDLIMKSiisgtfERKKLLKEEG-WKYKSTLQFLRIEIDRLLLLREEELSK--KK 454
|
490
....*....|....*.
gi 39930325 485 EQDRLLSELRDEVQTL 500
Cdd:COG5059 455 TKIHKLNKLRHDLSSL 470
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
27-361 |
1.62e-75 |
|
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. Members of this group might play a role in regulating chromosomal movement along microtubules in mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276827 [Multi-domain] Cd Length: 319 Bit Score: 253.58 E-value: 1.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 27 IKVFVRIRPAEEGARSADGeqSFCLSVLSQTTLRLhSNPD----PKTFVFDYVAGMDTTQESVFSTVAKSIVESCMSGYN 102
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASD--PSCVSGIDSCSVEL-ADPRnhgeTLKYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 103 GTIFAYGQTGSGKTFTMMGpsdsdnfSHNLRGIIPRSFEYLFSLIDREKEKAGAgksflcKCSFIEVYNEQIYDLLDSAS 182
Cdd:cd01376 79 ATVFAYGSTGAGKTFTMLG-------SPEQPGLMPLTVMDLLQMTRKEAWALSF------TMSYLEIYQEKILDLLEPAS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 183 VGLYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEkSSETVNIRTSLLN 262
Cdd:cd01376 146 KELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRE-RLAPFRQRTGKLN 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 263 LVDLAGSERQKDTHAEGMRLKEAGNINRSLSCLGQVITALvdvgNGKQRHICYRDSKLTFLLRDSLGGNAKTAIIANVHP 342
Cdd:cd01376 225 LIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNAL----NKNLPRIPYRDSKLTRLLQDSLGGGSRCIMVANIAP 300
|
330
....*....|....*....
gi 39930325 343 GSRCFGETLSTLNFAQRAK 361
Cdd:cd01376 301 ERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
27-361 |
2.18e-64 |
|
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: 222.17 E-value: 2.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 27 IKVFVRIRPAEEGARSA------DGEQSFCLSVLS-QTTLRLHSNPDPKTFVFDYVAGMDTTQESVFSTVAKSIVESCMS 99
Cdd:cd01367 2 IKVCVRKRPLNKKEVAKkeidvvSVPSKLTLIVHEpKLKVDLTKYIENHTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 100 GYNGTIFAYGQTGSGKTFTMMGpsdSDNFSHNLRGIIPRSFEYLFSLIDREKEKAGAGKSflckCSFIEVYNEQIYDLLd 179
Cdd:cd01367 82 GGKATCFAYGQTGSGKTYTMGG---DFSGQEESKGIYALAARDVFRLLNKLPYKDNLGVT----VSFFEIYGGKVFDLL- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 180 SASVGLYLREHIKKGVFVVGAVEQAVTSAAETYQVLSRGWRNRRVASTSMNRESSRSHAVFTITIESMEKssetvNIRTS 259
Cdd:cd01367 154 NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGT-----NKLHG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 260 LLNLVDLAGSERQKDT-HAEGMRLKEAGNINRSLSCLGQVITALVDvgngKQRHICYRDSKLTFLLRDSL-GGNAKTAII 337
Cdd:cd01367 229 KLSFVDLAGSERGADTsSADRQTRMEGAEINKSLLALKECIRALGQ----NKAHIPFRGSKLTQVLKDSFiGENSKTCMI 304
|
330 340
....*....|....*....|....
gi 39930325 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 |
6.93e-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: 93.95 E-value: 6.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 29 VFVRIRPAeegarsadgeqsfclsvlsqttLRLHSNPDPKTFVFDYVAGMDTTQESVFSTVAKsIVESCMSGYNG-TIFA 107
Cdd:cd01363 1 VLVRVNPF----------------------KELPIYRDSKIIVFYRGFRRSESQPHVFAIADP-AYQSMLDGYNNqSIFA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 108 YGQTGSGKTFTMMgpsdsdnfshnlrGIIPRSFEYLFSLIDREKEKagagksFLCKCSFIEVYNE-QIYDLLDSasvgly 186
Cdd:cd01363 58 YGESGAGKTETMK-------------GVIPYLASVAFNGINKGETE------GWVYLTEITVTLEdQILQANPI------ 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 187 lrehikkgvfvvgaveqavtsaAETYqvlsrgwrnrRVASTSMNRESSRSHAVFTItiesmekssetvnirtsllnLVDL 266
Cdd:cd01363 113 ----------------------LEAF----------GNAKTTRNENSSRFGKFIEI--------------------LLDI 140
|
250 260 270
....*....|....*....|....*....|....*
gi 39930325 267 AGSERqkdthaegmrlkeagnINRSLSCLGQVITA 301
Cdd:cd01363 141 AGFEI----------------INESLNTLMNVLRA 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
520-1339 |
1.66e-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: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 520 LREENRRLKLLapvkraheidaQSIARLEKAFAEVSSTETN-DKGLQGFSPKALKESSFFTNTEKLKAQllQIQTELNNS 598
Cdd:TIGR02168 195 LNELERQLKSL-----------ERQAEKAERYKELKAELRElELALLVLRLEELREELEELQEELKEAE--EELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 599 KQEYEEFKELTRKKQLELESELQSLQKANLNLENLLEATKVCKRQEVSQLNKLHAEtlkiittptkayqlcsrlvpkssp 678
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ------------------------ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 679 evgsfgflctesSSRLDNDILNEpvppemsEQALEAVSEELRTVQEQLSVLQVKLDEEERKNLKLQQNVDKLEHHSTQMQ 758
Cdd:TIGR02168 318 ------------LEELEAQLEEL-------ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 759 EL---FSSERSDWTKQQQEHVTQLSDLEKQLQDAQTKNEFLKCEVHDLRIVLNSADKElslvklEYSTFKENHEKELSQL 835
Cdd:TIGR02168 379 EQletLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK------ELQAELEELEEELEEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 836 SERHVQVQLQLDNARLENEKLLESQACLQDSYDNLQ------EVMKFEIDQLSKNLQNCKQENETLKSDLHNLVELFEAE 909
Cdd:TIGR02168 453 QEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVD 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 910 KERNNKLSLQFEE-------DKENSSKEILKVLETVRQEKQKEMAKCEKQMAKIQKLEESLLATEN----VISSLEKSRE 978
Cdd:TIGR02168 533 EGYEAAIEAALGGrlqavvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgflgVAKDLVKFDP 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 979 SDKELVTNLMNQI---------QELRISIGEKsETIATLKQELqdINCKYNASLAD-KEESKELIRRQEVDILELK-ETL 1047
Cdd:TIGR02168 613 KLRKALSYLLGGVlvvddldnaLELAKKLRPG-YRIVTLDGDL--VRPGGVITGGSaKTNSSILERRREIEELEEKiEEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1048 RLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQHKLNQEKEEVEQKKNEFSLKMRQ 1127
Cdd:TIGR02168 690 EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1128 LEhvmgsateypqspKTPPHFQAHLAKlLETQEQEIEDgraSKTSLQHLVTKLNEDREVKNAEILRMKDQLCEMENLRLE 1207
Cdd:TIGR02168 770 LE-------------EAEEELAEAEAE-IEELEAQIEQ---LKEELKALREALDELRAELTLLNEEAANLRERLESLERR 832
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1208 SQQLREKNWLLQRQLDDVKRQQESGDQSHPDSQQLKNEHEEIIKERL-AKNKLIEEMLKMKTNLEEVQSALHSKEKACHR 1286
Cdd:TIGR02168 833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLnERASLEEALALLRSELEELSEELRELESKRSE 912
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 39930325 1287 MSEEIERTRTLESRAFQEKEQLRSKLEEMYEE-RERTFLEMEMLKKQLEFLAEE 1339
Cdd:TIGR02168 913 LRRELEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDD 966
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
27-178 |
5.22e-15 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 73.41 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 27 IKVFVRIRPAEEgarsadgeQSFCLSVLSQTTLRLHSNPDPKTFVFDYVAGMDTTQESVFSTVaKSIVESCMSGYNGTIF 106
Cdd:pfam16796 22 IRVFARVRPELL--------SEAQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIF 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930325 107 AYGQTGSGKTFTMmgpsdsdnfshnlrgiIPRSFEYLFSLIdrekEKAGAGKSFLCKCSFIEVYNEQIYDLL 178
Cdd:pfam16796 93 AYGQTGSGSNDGM----------------IPRAREQIFRFI----SSLKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
570-1320 |
3.29e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 74.77 E-value: 3.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 570 KALKESSFFTNTEK--LKAQLLQIQTELNNSKQEYEEFKELTRKK---QLELESELQS----LQKANLNLENLLEATKVc 640
Cdd:pfam15921 92 RRLNESNELHEKQKfyLRQSVIDLQTKLQEMQMERDAMADIRRREsqsQEDLRNQLQNtvheLEAAKCLKEDMLEDSNT- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 641 krqEVSQLNKL---HAETLKIITTPTKAYQLCSrlvPKSSPEVGSFGFLCTESSSRLDNDILNEpvppemSEQALEAVSE 717
Cdd:pfam15921 171 ---QIEQLRKMmlsHEGVLQEIRSILVDFEEAS---GKKIYEHDSMSTMHFRSLGSAISKILRE------LDTEISYLKG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 718 ELRTVQEQLSVLqvKLDEEERKNLKLQQNVDKLEH----HSTQMQELfsSERSDWTKQQQEHVTqlSDLEKQLQDAQTKN 793
Cdd:pfam15921 239 RIFPVEDQLEAL--KSESQNKIELLLQQHQDRIEQliseHEVEITGL--TEKASSARSQANSIQ--SQLEIIQEQARNQN 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 794 EFLKCEVHDLRIVLNSADKELSLVKLEYSTFKENHEKELSqlserhvqvqlqldnarLENEKLLESQAclqdsydnlqev 873
Cdd:pfam15921 313 SMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLV-----------------LANSELTEART------------ 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 874 mkfEIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKL------------SLQFEEDKENSSKEILK-VLETVRQ 940
Cdd:pfam15921 364 ---ERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidHLRRELDDRNMEVQRLEaLLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 941 EKQKEMakcEKQMAKIQKLEESLlateNVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQDincKYN 1020
Cdd:pfam15921 441 ECQGQM---ERQMAAIQGKNESL----EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQE---KER 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1021 ASLADKEESKELIRRQEVDILELK----------------ETLRLRIlsedIERDMLCEDLAHATEQLNMLTEASKKHSG 1084
Cdd:pfam15921 511 AIEATNAEITKLRSRVDLKLQELQhlknegdhlrnvqtecEALKLQM----AEKDKVIEILRQQIENMTQLVGQHGRTAG 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1085 LLQSAQEELT------------------RKEALIQELQHKLNQEKEEVEQKKNEFSLKMRQLEHVMGSATEYPQSPKTPp 1146
Cdd:pfam15921 587 AMQVEKAQLEkeindrrlelqefkilkdKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTS- 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1147 hfQAHLAKLLETQEQEIEDGRASKTSLQHLVTKLNEDREVKNAEILRMKDQLCEMENLRLESQQL---REKNWLLQR-QL 1222
Cdd:pfam15921 666 --RNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVamgMQKQITAKRgQI 743
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1223 DDVKRQ----QESGDQSHPDSQQLKNEHEEIIKE----RLAKNKLIEEMLKMKTNLEEVQSALHSKEKACHRMSEEIERT 1294
Cdd:pfam15921 744 DALQSKiqflEEAMTNANKEKHFLKEEKNKLSQElstvATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAEC 823
|
810 820
....*....|....*....|....*.
gi 39930325 1295 RTLESRafQEKEQLRSKLEEMYEERE 1320
Cdd:pfam15921 824 QDIIQR--QEQESVRLKLQHTLDVKE 847
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
712-1340 |
6.09e-11 |
|
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: 67.40 E-value: 6.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 712 LEAVSEELRTVQEQLSVLQVKLDEEERKNLKLQQNVDKLEHHSTQMQELFSSERSDWTKQQQEHVT-------QLSDLEK 784
Cdd:TIGR02169 172 KEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERqkeaierQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 785 QLQDAQTKNEFLKCEVHDLRIVLNSADKELS-LVKLEYSTFKEN-----------------HEKELSQLSERHVQVQLQL 846
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEIEQLLEELNKKIKdLGEEEQLRVKEKigeleaeiaslersiaeKERELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 847 DNARLENEKLLESQ-------ACLQDSYDNLQEVM-----------------KFEIDQLSKNLQNCKQENETLKSDLHNL 902
Cdd:TIGR02169 332 DKLLAEIEELEREIeeerkrrDKLTEEYAELKEELedlraeleevdkefaetRDELKDYREKLEKLKREINELKRELDRL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 903 VELFEAEKER----NNKLS------LQFEEDKENSSKEILKV---LETVRQEKQKEMAKCEKQMAKIQKLEESLLATENV 969
Cdd:TIGR02169 412 QEELQRLSEEladlNAAIAgieakiNELEEEKEDKALEIKKQewkLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 970 ISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQ---------ELQDINCKYNASLADKEESKELI------- 1033
Cdd:TIGR02169 492 LAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSvgeryataiEVAAGNRLNNVVVEDDAVAKEAIellkrrk 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1034 ------------RRQEVDILELKETLRLRILSEDIERD--------------MLCEDLAHATEQL---NMLT-------- 1076
Cdd:TIGR02169 572 agratflplnkmRDERRDLSILSEDGVIGFAVDLVEFDpkyepafkyvfgdtLVVEDIEAARRLMgkyRMVTlegelfek 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1077 --------EASKKHSGLLQSAQEELTRKEALIQELQHKLN---QEKEEVEQKKNEFSLKMRQLEHVMGSATEYPQSPKTP 1145
Cdd:TIGR02169 652 sgamtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSslqSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1146 PHFQAHLAKLLETQEQEIEDGRAS-KTSLQHLVTKLNEDREVKNAEilrmKDQLCEMENlRLESQQLREKNWLLQRQLDD 1224
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENvKSELKELEARIEELEEDLHKL----EEALNDLEA-RLSHSRIPEIQAELSKLEEE 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1225 VKRQQ---ESGDQSHPDSQQLKNEHEEIIKERLAKNKLIEEMLKM--------KTNLEEVQSALHSKEKACHRMSEEIER 1293
Cdd:TIGR02169 807 VSRIEarlREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSiekeienlNGKKEELEEELEELEAALRDLESRLGD 886
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 39930325 1294 TRTLESRAFQEKEQLRSKLEEMYEERERTFLEMEMLKKQLEFLAEEN 1340
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
762-1043 |
2.35e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 762 SSERSDWTKQQQEHVTQLSDLEKQLQDAQTKNEFLKCEVHDLRIVLNSADKELSLVKLEYSTFKENHEKELSQLSERHVQ 841
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 842 VQLQLDNARLENEKLLESQACLQDSYDNLQEV------MKFEIDQLSKNLQNCKQENETLKSDLHNLVELFE-------A 908
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELeaqieqLKEELKALREALDELRAELTLLNEEAANLRERLEslerriaA 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 909 EKERNNKLSLQFEEDKE---------NSSKEILKVLETVRQEKQKEMAKCEKQMAKI----QKLEESLLATENVISSLEK 975
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEdieslaaeiEELEELIEELESELEALLNERASLEEALALLrselEELSEELRELESKRSELRR 915
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39930325 976 SRESDKELVTNLMNQIQELRISIGEKSETIATLKQ-ELQDINCKYNASLADKEESKELIRRQEVDILEL 1043
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSlTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1027-1334 |
2.82e-09 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 61.68 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1027 EESKELIRRQEVDILELKETLRLRILSEDIERDMlcedlahatEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQHK 1106
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREV---------ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1107 LN-----QEKEEVEQ-KKNEFSL---KMRQLEHVMGSATEYPQSPKTPPHfQAHLAKLLETQEQeiedgRASKTSLQHLV 1177
Cdd:pfam17380 350 LErirqeERKRELERiRQEEIAMeisRMRELERLQMERQQKNERVRQELE-AARKVKILEEERQ-----RKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1178 TKLNEDREVKNAEILRMKDQLC-EMENLRLESQQLREKNWLLQRQLDDVKRQQESGDQSHPDSQQLKNEHEEIIKERLAK 1256
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERArEMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1257 NK--LIEEMLKMK---TNLEEVQSALHSKEKacHRMSEEIERTR--TLESRAFQEK----EQLRSKLEEMYEERE--RTF 1323
Cdd:pfam17380 504 RKqaMIEEERKRKlleKEMEERQKAIYEEER--RREAEEERRKQqeMEERRRIQEQmrkaTEERSRLEAMEREREmmRQI 581
|
330
....*....|.
gi 39930325 1324 LEMEMLKKQLE 1334
Cdd:pfam17380 582 VESEKARAEYE 592
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
872-1188 |
3.55e-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: 61.61 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 872 EVMKFEIDQLSKNLQNCKQENETLKSDLHNLvelfEAEKERNNKLSLQFEEDKENSSKEILKVLETVRQ---EKQKEMAK 948
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQL----RKELEELSRQISALRKDLARLEAEVEQLEERIAQlskELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 949 CEKQMAKIQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQDinckYNASLADKEE 1028
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES----LERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1029 SKELIRRQEVDILELKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEEL-------TRKEALIQ 1101
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELreleskrSELRRELE 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1102 ELQHKLNQEKEEVEQKKNEF-SLKMRQLEHVMGSA----TEYPQSPKTPPHFQAHLAKL--------------------- 1155
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIdNLQERLSEEYSLTLeeaeALENKIEDDEEEARRRLKRLenkikelgpvnlaaieeyeel 998
|
330 340 350
....*....|....*....|....*....|....*.
gi 39930325 1156 ---LETQEQEIEDGRASKTSLQHLVTKLneDREVKN 1188
Cdd:TIGR02168 999 kerYDFLTAQKEDLTEAKETLEEAIEEI--DREARE 1032
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
710-1387 |
9.78e-09 |
|
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: 59.99 E-value: 9.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 710 QALEAVSEELRTVQEQLSVLQVKLDEEERKNLKLQ-QNVDKLEHHSTQMQELFSSERSDWTKQQQEHVTQLSDLEKQLQD 788
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKeQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 789 AQTKNEFLKCE----------VHDLRIVLNSADKELSLVKLEYSTFKENHEKELSQLSERHVQVQLQLDNARLENEKLLE 858
Cdd:pfam02463 249 EQEEIESSKQEiekeeeklaqVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 859 SQACLQDSYDNLQEVMKFEIDQLSKNL---QNCKQENETLKSDLHNLVELFEAEKERNNKLSLQFEEDKENSSKEILKVL 935
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEeeeEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 936 ETVRQEKQKEMAKCEKQMAKIQKLEESLLATENVISSLEKSRESDKEL-VTNLMNQIQELRISIGEKSETIATLKQELQD 1014
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQeLKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1015 INCKYNASLADKEESKELIRRQEVDIL-ELKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKH--SGLLQSAQE 1091
Cdd:pfam02463 489 LLSRQKLEERSQKESKARSGLKVLLALiKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAdeVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1092 ELTRKEALIQELQHKLNQEKEEVEQKKNEFSLKMRQLEHVMGSATEYPQSPKTPPHFQAHLAKLLETQEQEIEDGRASKT 1171
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1172 SLQHLVTKLNEDREVKNAEILRMKDQLCEMENLRLESQQLREKNWLLQRQLDDVKRQQESGDQSHPDSQQLKNEHEEIIK 1251
Cdd:pfam02463 649 RKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQ 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1252 ERLAKNKLIEEMLKMKTNLEEVQSALHSKEKACHRMSEEIERTRTLESRAFQEKEQLRSKLEEMYEERERTFLEMEMLKK 1331
Cdd:pfam02463 729 EAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEE 808
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 39930325 1332 QLEFLAEENGKLVGHQNLHQKIQyvVRLKKENIRLTEETEKLRAENLFLKEKKKEF 1387
Cdd:pfam02463 809 ELKEEAELLEEEQLLIEQEEKIK--EEELEELALELKEEQKLEKLAEEELERLEEE 862
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
904-1385 |
1.35e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 904 ELFEAEKERNNKLSLQFEEDKENSSKEILKVLETVRQEKQKEMAKCE--KQMAKIQKLEESLLATE--------NVISSL 973
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEekKKADEAKKAEEKKKADEakkkaeeaKKADEA 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 974 EKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQDINCKYNASLADKEESKELIRRQEVDILELKETLRLRILS 1053
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1054 EDIERDmlCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQHKLNQEKEEVEQ--KKNEFSLKMRQLEHV 1131
Cdd:PTZ00121 1401 EEDKKK--ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEakKKAEEAKKADEAKKK 1478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1132 MGSATEYPQSPKTPPHFQAHLAKLLETQEQEIEDGRASKTSLQHLVTKLNEDREVKNAEILRMKDQLCEMENLRlESQQL 1211
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK-KAEEL 1557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1212 REKNWllQRQLDDVKRQQESGDQSHPDSQQLKNEHEEIIKERLaknKLIEEMLKMKTnlEEVQSALHSKEKACHRMSEEI 1291
Cdd:PTZ00121 1558 KKAEE--KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM---KLYEEEKKMKA--EEAKKAEEAKIKAEELKKAEE 1630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1292 ERTRTLESRAFQEKEqlRSKLEEMYEERERTFLEMEMLKKQLEFLAEENGKLVGHQNLHQKIQYVVRLKKENIRLTEETE 1371
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEE--KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELK 1708
|
490
....*....|....
gi 39930325 1372 KLRAEnlflkEKKK 1385
Cdd:PTZ00121 1709 KKEAE-----EKKK 1717
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
878-1386 |
2.33e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 878 IDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKLSLQfEEDKENSSKEIlKVLETVRQEKQKEMAKCEKQMAKIQ 957
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEK-EKELEEVLREI-NEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 958 KLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKqELQDINCKYNASLADKEESKELIRRQE 1037
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1038 VDILELKETLR--LRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQ----HKLNQEK 1111
Cdd:PRK03918 314 KRLSRLEEEINgiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgltpEKLEKEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1112 EEVEQKKNEFSLKMRQLEHVMGS----------ATEYPQSPKTP------PHFQAHLAKLLETQEQEIEDGRASKTSLQH 1175
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGElkkeikelkkAIEELKKAKGKcpvcgrELTEEHRKELLEEYTAELKRIEKELKEIEE 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1176 LVTKL-NEDREVKNA-----EILRMKDQLCEMENLRLESQQLR----EKNW----LLQRQLDDVKRQQESGDQSHPDSQQ 1241
Cdd:PRK03918 474 KERKLrKELRELEKVlkkesELIKLKELAEQLKELEEKLKKYNleelEKKAeeyeKLKEKLIKLKGEIKSLKKELEKLEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1242 LKNEHEEIIKERLAKNKLIEEMLKMKTNL-----EEVQSALHSKEKACHRMSEEIERTRTLESRAfQEKEQLRSKLEEMY 1316
Cdd:PRK03918 554 LKKKLAELEKKLDELEEELAELLKELEELgfesvEELEERLKELEPFYNEYLELKDAEKELEREE-KELKKLEEELDKAF 632
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930325 1317 EERERTFLEMEMLKKQLeflaEENGKLVGHQNLHQKIQYVVRLKKENIRLTEETEKLR------AENL-FLKEKKKE 1386
Cdd:PRK03918 633 EELAETEKRLEELRKEL----EELEKKYSEEEYEELREEYLELSRELAGLRAELEELEkrreeiKKTLeKLKEELEE 705
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
952-1185 |
2.51e-08 |
|
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: 57.85 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 952 QMAKIQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQDInckyNASLAD-KEESK 1030
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL----EAELAElEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1031 ELIRRQEVDILELKETLRLRILSEDIERDML------CEDLAHATEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQ 1104
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1105 HKLNQEKEEVEQKKNEFSLKMRQLEHVMgsateypqspktpphfqAHLAKLLETQEQEIEDGRASKTSLQHLVTKLNEDR 1184
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLL-----------------ARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
.
gi 39930325 1185 E 1185
Cdd:COG4942 237 A 237
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
709-1263 |
2.86e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 709 EQALEAVSEELRTVQEQLSVLQVKLDEEERKNLKLQQNVDKLEHHSTQMQELF---SSERSDWTKQQQEHVTQLSDLEKQ 785
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyelLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 786 LQDAQTKNEFLKCEVHDLRIVLNSADKELSLVKLEYSTFKE---NHEKELSQLSERHVQVQLQLDNARLENEKLLESQAC 862
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAelaEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 863 LQDSYDNLQEVMKFEIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKLSLQFEEDKEnsskeilkvLETVRQEK 942
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA---------LLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 943 QKEMAKCEKQMAKIQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRISiGEKSETIATLKQELQDINCKYNAS 1022
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA-GAVAVLIGVEAAYEAALEAALAAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1023 LADKEESKELIRRQEVDILELKETLRLRILSEDIERDmlcEDLAHATEQLNMLTEASKKHSGLLQSAQEELTR-KEALIQ 1101
Cdd:COG1196 548 LQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRA---RAALAAALARGAIGAAVDLVASDLREADARYYVlGDTLLG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1102 ELQHKLNQEKEEVEQKKNEFSLKMRQLEHVMGSAteypqspkTPPHFQAHLAKLLETQEQEIEDGRASKTSLQHLVTKLN 1181
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA--------GGSLTGGSRRELLAALLEAEAELEELAERLAEEELELE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1182 EDREVKNAEILRMKDQLCEMENLRLESQQLREKNWLLQRQLDDVKRQQESGDQSHPDSQQLKNEHEEIIKERLAK-NKLI 1260
Cdd:COG1196 697 EALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERlEREI 776
|
...
gi 39930325 1261 EEM 1263
Cdd:COG1196 777 EAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
780-1349 |
1.64e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 780 SDLEKQLQDAQTKNEFLKCEVHDLRIVLNSADKELSLVKLEYSTFKENHEKelsqlserhvqvqlqLDNARLENEKLLES 859
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE---------------IEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 860 QACLQDsydnlqevmkfEIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKE--RNNKLSLQFEEDKENSSKEiLKVLET 937
Cdd:PRK03918 254 KRKLEE-----------KIRELEERIEELKKEIEELEEKVKELKELKEKAEEyiKLSEFYEEYLDELREIEKR-LSRLEE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 938 VRQEKQKEMAKCEKQMAKIQKLEESLLATENVISSLEKSRESdKELVTNLMNQIQELR-----ISIGEKSETIATLKQEL 1012
Cdd:PRK03918 322 EINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHEL-YEEAKAKKEELERLKkrltgLTPEKLEKELEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1013 QDINCKYNASLADKEESKELIRRQEVDILELKETLRL-----RILSEDIERDMLCEdlahATEQLNMLTEASKKHSGLLQ 1087
Cdd:PRK03918 401 EEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEE----YTAELKRIEKELKEIEEKER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1088 SAQEELTRKEALIQElQHKLNQEKEEVEQKKN-EFSLKMRQLEHVMGSATEYPQSPKTPPHFQAHLaKLLETQEQEIEDG 1166
Cdd:PRK03918 477 KLRKELRELEKVLKK-ESELIKLKELAEQLKElEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEEL 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1167 RASKTSLQHLVTKLNEDREVKNAEILRMKDQLCEMENLRLESQQLREKNWL--------LQRQLDDVKRQQESGDQSHPD 1238
Cdd:PRK03918 555 KKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLelkdaekeLEREEKELKKLEEELDKAFEE 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1239 SQQLKNEHEEIIKERLAKNKLIEEmlkmkTNLEEVQSALHSKEKACHRMSEEIERtrtLESRAFQEKEQLRsKLEEMYEE 1318
Cdd:PRK03918 635 LAETEKRLEELRKELEELEKKYSE-----EEYEELREEYLELSRELAGLRAELEE---LEKRREEIKKTLE-KLKEELEE 705
|
570 580 590
....*....|....*....|....*....|.
gi 39930325 1319 RERTFLEMEMLKKQLEFLAEENGKLVGHQNL 1349
Cdd:PRK03918 706 REKAKKELEKLEKALERVEELREKVKKYKAL 736
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
904-1195 |
2.40e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 904 ELFEAEKERNNKLSLQFEEDKENSSKEiLKVLETVRQEKQKEMAKCEKQMAKIQKLEESLLATenvISSLEKSRESDKEL 983
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELEEAQAEEYELLAE---LARLEQDIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 984 VTNLMNQIQELRISIGEKSETIATLKQELQDINCKYNASLADKEESKELIRRQEVDILELKETLRLRILSEDIERDMLCE 1063
Cdd:COG1196 311 RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1064 DLAHATEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQHKLNQEKEEVEQKKNEFSLKMRQLEHVMGSATEYPQspk 1143
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE--- 467
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 39930325 1144 tpphfQAHLAKLLETQEQEIEDGRASKTSLQHLVTKLNEDREVKNAEILRMK 1195
Cdd:COG1196 468 -----LLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1086-1386 |
2.46e-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: 55.45 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1086 LQSAQEELTRKEALIQELQHKLNQEKEEVEqKKNEFSLKMRQLEHVMGSAteypqspktpphfqahLAKLLETQEQEIED 1165
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAE-KAERYKELKAELRELELAL----------------LVLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1166 GRASKTSLQHLVTKLNEDREVKNAEILRMKDQLCEMENlrlESQQLREKNWLLQRQLDDVKRQQESGDQS-HPDSQQLKN 1244
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEE---EIEELQKELYALANEISRLEQQKQILRERlANLERQLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1245 EHEEIIKERLAKNKLIEEMLKMKTNLEEVQSALHSKEKACHRMSEEIERTRTLESRAFQEKEQLRSKLEEMYEERERTFL 1324
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930325 1325 EMEMLKKQLEFLAEENGKLVGHQNLHQKIQYVVRLKKENIRLTE---ETEKLRAENLFLKEKKKE 1386
Cdd:TIGR02168 401 EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEleeELEELQEELERLEEALEE 465
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
661-1343 |
3.22e-07 |
|
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: 54.97 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 661 TPTKAYQLCSRLVPKSSPEVGSFGFLCTESSSRLDNDILNEPVPPEMSEQALEAVSEELRTVQEQLSVLQVKLdeeerkn 740
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYL------- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 741 lklqqnvdklehhsTQMQELfSSERSDWTKQQQEHVTQLSDLEKQLQDAQTKNEFLKCEVHDLRIVLNSA-----DKELS 815
Cdd:TIGR00618 246 --------------TQKREA-QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKavtqiEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 816 LVKLEYSTFKENHEKELSQLSERHVQVQLQLDNARLENEklLESQACLQDSYDNLQEVMKFEIDQLSKNLQNCKQENETL 895
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT--LHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 896 KSDLHNLVELF-EAEKERNNKLSLQFEEDKENSSKEILKVLETVRQEKQKEMAKCEKQMAK---IQKLEESLlatenvis 971
Cdd:TIGR00618 389 TTLTQKLQSLCkELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCtaqCEKLEKIH-------- 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 972 sLEKSRESDKELvTNLMNQIQELRISIGEKSETIATLKQELQDINC-------KYNASLADKEESKELIRRQEVDILELK 1044
Cdd:TIGR00618 461 -LQESAQSLKER-EQQLQTKEQIHLQETRKKAVVLARLLELQEEPCplcgsciHPNPARQDIDNPGPLTRRMQRGEQTYA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1045 ---------------ETLRLRILSEDIERdmLCEDLAHATEQLNMLTEASKKHSGLLQSAQ---EELTRKEALIQELQHK 1106
Cdd:TIGR00618 539 qletseedvyhqltsERKQRASLKEQMQE--IQQSFSILTQCDNRSKEDIPNLQNITVRLQdltEKLSEAEDMLACEQHA 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1107 LNQEKEEvEQKKNEFSLKMRQLE--------HVMGSATEYPQSPKTpphfqAHLAKLLETQEQEIEDGRASKTSLQHLVT 1178
Cdd:TIGR00618 617 LLRKLQP-EQDLQDVRLHLQQCSqelalkltALHALQLTLTQERVR-----EHALSIRVLPKELLASRQLALQKMQSEKE 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1179 KLNEDREVKNAEILRMKDQLCEMENLRLESQQ-----------LREKNWLLQRQLDDVKRQQESGDQSHPDSQQLKNEHE 1247
Cdd:TIGR00618 691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEienassslgsdLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEV 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1248 EIIKERLAK-NKLIEEMLKMKTNLEEVQSALHSKEKAC--HRMSEEIERTRTLESRAfQEKEQLRSKLEEMYE---ERER 1321
Cdd:TIGR00618 771 TAALQTGAElSHLAAEIQFFNRLREEDTHLLKTLEAEIgqEIPSDEDILNLQCETLV-QEEEQFLSRLEEKSAtlgEITH 849
|
730 740
....*....|....*....|..
gi 39930325 1322 TFLEMEMLKKQLEFLAEENGKL 1343
Cdd:TIGR00618 850 QLLKYEECSKQLAQLTQEQAKI 871
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
775-1314 |
5.78e-07 |
|
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: 54.06 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 775 HVTQLSDLEKQLQDAQTKNEFLKCEVHDLRIVLNSADKELSLVKLEYSTFKENHEKelsqlSERHVQVQLQLDNARLENE 854
Cdd:pfam10174 266 HTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSD-----CKQHIEVLKESLTAKEQRA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 855 KLLESQAclqDSYDNLQEVMKFEIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKLSlqfeedkenssKEILKV 934
Cdd:pfam10174 341 AILQTEV---DALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQ-----------KKIENL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 935 LETVRqEKQKEMAKCEKQMAKIQK-----------LEESLLATENVISSLEKSRESDKElvtnlmnqiqelrisigEKSE 1003
Cdd:pfam10174 407 QEQLR-DKDKQLAGLKERVKSLQTdssntdtalttLEEALSEKERIIERLKEQREREDR-----------------ERLE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1004 TIATLKQELQDINCKYNASLADKEEskelirrQEVDILELKEtlrlrilsedierdmlcedlaHATeqlNMLTEASKKHS 1083
Cdd:pfam10174 469 ELESLKKENKDLKEKVSALQPELTE-------KESSLIDLKE---------------------HAS---SLASSGLKKDS 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1084 GLLQSAQEELTRKEALIQ-ELQHKLNQEKEEVEQKKNEFSLKMRQLEHVMGSATEypQSPKTpphfQAHLAKLLET-QEQ 1161
Cdd:pfam10174 518 KLKSLEIAVEQKKEECSKlENQLKKAHNAEEAVRTNPEINDRIRLLEQEVARYKE--ESGKA----QAEVERLLGIlREV 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1162 EIEdgrasktslqhlvtKLNEDREVKNAEIL---RMKDQLCEMENLRLESQQLREKNwllQRQLDDVKRQQESGDQSHPD 1238
Cdd:pfam10174 592 ENE--------------KNDKDKKIAELESLtlrQMKEQNKKVANIKHGQQEMKKKG---AQLLEEARRREDNLADNSQQ 654
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930325 1239 SQQlknehEEIIKErLAKNKliEEMLKMKTNLEEVQSALHSKEKacHRMSEEIERTRTLESRAFQEKEQLRSKLEE 1314
Cdd:pfam10174 655 LQL-----EELMGA-LEKTR--QELDATKARLSSTQQSLAEKDG--HLTNLRAERRKQLEEILEMKQEALLAAISE 720
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1086-1383 |
9.95e-07 |
|
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: 9.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1086 LQSAQEELTRKEALIQELQHKLNQEKEEVEQ--KKNEFSLKMRQLEHVMGSAteypqspktppHFQAHLAKLlETQEQEI 1163
Cdd:COG1196 181 LEATEENLERLEDILGELERQLEPLERQAEKaeRYRELKEELKELEAELLLL-----------KLRELEAEL-EELEAEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1164 EDGRASKTSLQHLVTKLNEDREVKNAEILRMKDQLCEM-ENLRLESQQL----REKNWLLQRQLDDVKRQQESGDQSHPD 1238
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAqAEEYELLAELarleQDIARLEERRRELEERLEELEEELAEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1239 SQQLKNEHEEIIKERLAKNKLIEEMLKMKTNLEEVQSALHSKEKACHRMSEEIERTRTLESRAFQEKEQLRSKLEEMYEE 1318
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1319 RERTFLEMEMLKKQL-----EFLAEENGKLVGHQNLHQKIQYVVRLKKENIRLTEETEKLRAENLFLKEK 1383
Cdd:COG1196 409 EEALLERLERLEEELeeleeALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
921-1340 |
1.03e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 921 EEDKENSSKEILKVlETVRQEKQKEMAKCEKQMAKIQK---------LEESLLATENVISSLEKSRESDKELVTNLMNQI 991
Cdd:PRK02224 165 EEYRERASDARLGV-ERVLSDQRGSLDQLKAQIEEKEEkdlherlngLESELAELDEEIERYEEQREQARETRDEADEVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 992 QELRisigEKSETIATLKQELQDINCKYNASLADKEESKELIRRQEVDILELK-----------------ETLRLRI--L 1052
Cdd:PRK02224 244 EEHE----ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEeerddllaeaglddadaEAVEARReeL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1053 SEDIE--RDMLCE---DLAHATEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQHKLNQEKEEVEQKKNEfslkMRQ 1127
Cdd:PRK02224 320 EDRDEelRDRLEEcrvAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEE----IEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1128 LEHVMGSAteypqsPKTPPHFQAHLAKLLETQEQEIEDGRASKTSLQHLVTKLNEDRE-------------VKNAEIL-R 1193
Cdd:PRK02224 396 LRERFGDA------PVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpVEGSPHVeT 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1194 MKDQLCEMENLRLESQQLREKNWLLQRQLDDVK------RQQESGDQSHPDSQQLKNEHEEIIKERLAKnklIEEMLKMK 1267
Cdd:PRK02224 470 IEEDRERVEELEAELEDLEEEVEEVEERLERAEdlveaeDRIERLEERREDLEELIAERRETIEEKRER---AEELRERA 546
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39930325 1268 TNLE-EVQSALHSKEKACHRMSEEIERTRTLESRAFQEKEQLRS--KLEEMYEERERTFLEMEMLKKQLEFLAEEN 1340
Cdd:PRK02224 547 AELEaEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLREKREALAELN 622
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
872-1369 |
1.14e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 872 EVMKFEIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKLSLQFEEDKENSSKEILKVLETVRQEKQKEMAKCEK 951
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDK 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 952 QMA-KIQKLEESLLATENVISSLEKSRESDKelvtnLMNQIQELRISIGEKSETIATLKQElqdiNCKYNASLADKEEsk 1030
Cdd:PTZ00121 1405 KKAdELKKAAAAKKKADEAKKKAEEKKKADE-----AKKKAEEAKKADEAKKKAEEAKKAE----EAKKKAEEAKKAD-- 1473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1031 ELIRRQEvdilELKETLRLRILSEDIERDmlCEDLAHATEQlnmlteasKKHSGLLQSAQEELTRKEALIQELQHKLNQE 1110
Cdd:PTZ00121 1474 EAKKKAE----EAKKADEAKKKAEEAKKK--ADEAKKAAEA--------KKKADEAKKAEEAKKADEAKKAEEAKKADEA 1539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1111 KEEVEQKKNEfslKMRQLEHVMGSATEYPQSPKTPPHFQAHLAKLLETQEQEIEDGRASKTSLQHLVTKLNEDREVKNAE 1190
Cdd:PTZ00121 1540 KKAEEKKKAD---ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAE 1616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1191 ILRMKdqlceMENLRLESQQLREKNWLLQRQLDDVKRqqesgdqshpdSQQLKNEhEEIIKERLAKNKLIEEMLKMKTnl 1270
Cdd:PTZ00121 1617 EAKIK-----AEELKKAEEEKKKVEQLKKKEAEEKKK-----------AEELKKA-EEENKIKAAEEAKKAEEDKKKA-- 1677
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1271 EEVQSALHSKEKACHRMSEEIERTRTLESRAFQEKEQLRsKLEEMYEERERTFLEMEMLKKQLE---FLAEENGKLVGHQ 1347
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKK-KAEELKKAEEENKIKAEEAKKEAEedkKKAEEAKKDEEEK 1756
|
490 500
....*....|....*....|..
gi 39930325 1348 NLHQKIQYVVRLKKENIRLTEE 1369
Cdd:PTZ00121 1757 KKIAHLKKEEEKKAEEIRKEKE 1778
|
|
| HMMR_C |
pfam15908 |
Hyaluronan mediated motility receptor C-terminal; HMMR_C is the C-terminal region of ... |
1270-1387 |
1.20e-06 |
|
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: 49.91 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1270 LEEVQSALHSKEKACHRMSEEIERTRTLESRAFQEKEQLRSKLEEMYEERERTFLEMEMLKKQLEFLAEENGKLVGHQNL 1349
Cdd:pfam15908 4 LEMEEQRKARLENTVDELTEEIKKWRNLYEELYNKTKPFQEQLDAFEAEKNALLNENGAAQEELNKLSDAYAKLLGHQNQ 83
|
90 100 110
....*....|....*....|....*....|....*...
gi 39930325 1350 HQKIQYVVRLKKENIRLTEETEKLRAENLFLKEKKKEF 1387
Cdd:pfam15908 84 KQKIKHVVKLKEENTQLKQEVSKLRSQLAKEKQVQKKL 121
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
408-1328 |
1.56e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.05 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 408 DKEKTNYIEYFLEAmLFFKKSEQEKKSLIEKITQLEDLTLKKEKFIQSNKMIVKFREDQIMRLERLHKEGRgsflpEEQD 487
Cdd:pfam02463 152 PERRLEIEEEAAGS-RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLEL-----EEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 488 RLLSELRDEVQTlREHVEHHPRLAKYAMENHSLREENRRLKLLAPVKRAHEIDAQSI-------ARLEKAFAEVSSTETN 560
Cdd:pfam02463 226 LLYLDYLKLNEE-RIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKklqeeelKLLAKEEEELKSELLK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 561 DKGLQGFSPKALKESSffTNTEKLKAQLLQIQTELNNSKQEYEEfKELTRKKQLELESELQSLQKANLNLENLLEATKVC 640
Cdd:pfam02463 305 LERRKVDDEEKLKESE--KEKKKAEKELKKEKEEIEELEKELKE-LEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 641 KRQEVSQLNKLHAETLKIITTPTKAYQLCSRLVPKSSpevgsfgflctESSSRLDNDILNEPVPPEMSEQALEAVSEELR 720
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLE-----------DLLKEEKKEELEILEEEEESIELKQGKLTEEK 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 721 TVQEQLSVLQVKLDEEERKNLKLQQNVDKLEHHSTQMQELFSSERSDWTKQQQEHVTQLSDLEKQLQD---AQTKNEFLK 797
Cdd:pfam02463 451 EELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDgvgGRIISAHGR 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 798 CEVHDLRIVLNSADKELSLVKLEYSTFKENHEKELSQLSERHVQVQLQLDNARLENEKLLESQACLQDSYDNLQEVMKFE 877
Cdd:pfam02463 531 LGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 878 IDqLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKLSLQFEEDKENSSKEILKVLETVRQEKQKEMAKcekqmaKIQ 957
Cdd:pfam02463 611 AT-LEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQE------LQE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 958 KLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQDINCKYNASLADKEESKELIRRQE 1037
Cdd:pfam02463 684 KAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKE 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1038 VDILELKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASK----KHSGLLQSAQEELTRKEALIQELQHKLNQEKEE 1113
Cdd:pfam02463 764 EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALeeelKEEAELLEEEQLLIEQEEKIKEEELEELALELK 843
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1114 VEQKknefslkmrqlehvmgsateypqspktpphfqahLAKLLETQEQEIEDGRASKTSLQHLVTKLNEDREVKNAEILR 1193
Cdd:pfam02463 844 EEQK----------------------------------LEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELE 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1194 MKDQLCEMENLRLESQQLREKNWLLQRQLDDVKRQQESGDQSHPDSQQLKNEHEEIIKERLAKNKLIEEMLKMKTNLEEV 1273
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAK 969
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 39930325 1274 QSALHSKEKACHRMSEEIERTRTLESRaFQEKEQLRSKLEEMYEERERTFLEMEM 1328
Cdd:pfam02463 970 EELGKVNLMAIEEFEEKEERYNKDELE-KERLEEEKKKLIRAIIEETCQRLKEFL 1023
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
707-1120 |
2.49e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 707 MSEQALEAVSEELRTVQ--------EQLSVLQVKLDEEERKNLKLQQNVDKLEHHSTQMQELfssersdwTKQQQEHVTQ 778
Cdd:COG4717 46 MLLERLEKEADELFKPQgrkpelnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL--------EAELEELREE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 779 LSDLEKQLQDAQTKNEFlkcevHDLRIVLNSADKELSLVKLEYSTFKENHEkELSQLSERHVQVQLQLDnaRLENEKLLE 858
Cdd:COG4717 118 LEKLEKLLQLLPLYQEL-----EALEAELAELPERLEELEERLEELRELEE-ELEELEAELAELQEELE--ELLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 859 SQACLQDSYDNLQEVMKfEIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNK-------------LSLQFEEDKE 925
Cdd:COG4717 190 TEEELQDLAEELEELQQ-RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLkearlllliaaalLALLGLGGSL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 926 NSSKE--------ILKVLETVRQEKQKEMAKCEKQMAKIQKLEE----SLLATENVISSLEKSRESDKELVTNLMNQIQE 993
Cdd:COG4717 269 LSLILtiagvlflVLGLLALLFLLLAREKASLGKEAEELQALPAleelEEEELEELLAALGLPPDLSPEELLELLDRIEE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 994 LRISIGEKSETIATLKQELQDINCKYNASLADKEESKELIRR-----QEVDILELKETLRLRILSE--DIERDMLCEDLA 1066
Cdd:COG4717 349 LQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAAleqaeEYQELKEELEELEEQLEELlgELEELLEALDEE 428
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 39930325 1067 HATEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQ-----HKLNQEKEEVEQKKNE 1120
Cdd:COG4717 429 ELEEELEELEEELEELEEELEELREELAELEAELEQLEedgelAELLQELEELKAELRE 487
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
820-1122 |
4.57e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 820 EYSTFKENHEKELSQLSERHVQVQL-------QLDNARLENEKLLESQACLQDSYD-------NLQEVMKFEIDQLSKNL 885
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLiidekrqQLERLRREREKAERYQALLKEKREyegyellKEKEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 886 QNCKQENETLKSDLHNLVELFEAEKERNNKLSLQFEEDKENSSKEILKVLETVRQEK---QKEMAKCEKQM----AKIQK 958
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIaslERSIAEKERELedaeERLAK 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 959 LEESLLATENVISSLEKSRESDKELVTNLMNQIQELRisigeksETIATLKQELQDINCKYNASladKEESKELIRRQEV 1038
Cdd:TIGR02169 327 LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK-------EELEDLRAELEEVDKEFAET---RDELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1039 DILELKETLR-LRILSEDIERdmLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQHKLNQEKEEVEQK 1117
Cdd:TIGR02169 397 LKREINELKReLDRLQEELQR--LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDL 474
|
....*
gi 39930325 1118 KNEFS 1122
Cdd:TIGR02169 475 KEEYD 479
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
484-1114 |
9.45e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 484 EEQDRLLSELRDEVQTLREhvehhpRLAKYAMENHSLREENRRLKLLAPVKRAHEIDA-QSIARLEKAFAEVSsTETNDK 562
Cdd:TIGR02169 374 EEVDKEFAETRDELKDYRE------KLEKLKREINELKRELDRLQEELQRLSEELADLnAAIAGIEAKINELE-EEKEDK 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 563 GLqgfspkALKESSffTNTEKLKAQLLQIQTELNNSKQEYEEFKELTRKKQLELE------SELQSLQKANLNLENLLEA 636
Cdd:TIGR02169 447 AL------EIKKQE--WKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAeaeaqaRASEERVRGGRAVEEVLKA 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 637 TKVCKRQEVSQLNKLHAETLKIITTPTKAyQLCSRLVPKSSPEVGSFGFLCTESSSRLD----NDILNEPVPPEMSEQ-- 710
Cdd:TIGR02169 519 SIQGVHGTVAQLGSVGERYATAIEVAAGN-RLNNVVVEDDAVAKEAIELLKRRKAGRATflplNKMRDERRDLSILSEdg 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 711 ----ALEAVSEELRTVQEQLSVLQVKL---DEEERKNLKLQQNVDKLE----HHSTQMQELFSSERSDW--TKQQQEHVT 777
Cdd:TIGR02169 598 vigfAVDLVEFDPKYEPAFKYVFGDTLvveDIEAARRLMGKYRMVTLEgelfEKSGAMTGGSRAPRGGIlfSRSEPAELQ 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 778 QLSD----LEKQLQDAQTKNEFLKCEVHDLRIVLNSADKELSLVKLEYSTFKENHEKELSQLSERHVQVQlQLDNARLEN 853
Cdd:TIGR02169 678 RLRErlegLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS-SLEQEIENV 756
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 854 EkllesqaclqdsyDNLQEVMKfEIDQLSKNLQNCKQENETLKSDL-HNLVELFEAEKE------RNNKLSLQFEEDKEN 926
Cdd:TIGR02169 757 K-------------SELKELEA-RIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSkleeevSRIEARLREIEQKLN 822
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 927 SSKEILKVLETVRQEKQKEMAKCEKQM-----------AKIQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELR 995
Cdd:TIGR02169 823 RLTLEKEYLEKEIQELQEQRIDLKEQIksiekeienlnGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 996 ISIGEKSETIATLKQELQDINCKYNASladKEESKELIRRQEVDILELKETLRLRILSEDIERdmlCEDLAHATEQLNML 1075
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEAL---EEELSEIEDPKGEDEEIPEEELSLEDVQAELQR---VEEEIRALEPVNML 976
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 39930325 1076 T----EASKKHSGLLQSAQEELTRKEALIQELQHKLNQEKEEV 1114
Cdd:TIGR02169 977 AiqeyEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
920-1340 |
9.73e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 9.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 920 FEEDKENSSKEILKVLETVRQEKQKEMAKCEKQMAKIQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELR--IS 997
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEklLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 998 IGEKSETIATLKQELQDINCKYNASLADKEESKELIRRQEVDILELKETLRLRILSEDIERDMLCEDLAHATEQLNMLTE 1077
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1078 ASKKHSGLLQSAQEELTRKEALIQELQHKLNQEKEEVEQKKNEFSLK---------------MRQLEHVMGSATEYPQSP 1142
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLiaaallallglggslLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1143 KTPPHFQAHLAKLLETQEQEIEDGRA----SKTSLQHLVTKLNEDREVKNAEILRMKDQLCEMENLRLESQQLREKnWLL 1218
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPAleelEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE-LQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1219 QRQLDDVKRQQESGDQSHPDS-----------QQLKNEHEEIIKERLAKNKLIEEMLK------MKTNLEEVQSALHSKE 1281
Cdd:COG4717 366 EELEQEIAALLAEAGVEDEEElraaleqaeeyQELKEELEELEEQLEELLGELEELLEaldeeeLEEELEELEEELEELE 445
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930325 1282 KACHRMSEEI----ERTRTLE-----SRAFQEKEQLRSKLEEMYEERERTFLEMEMLKKQLEFLAEEN 1340
Cdd:COG4717 446 EELEELREELaeleAELEQLEedgelAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
347-937 |
1.16e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.08 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 347 FGETLSTLNfaqRAKLIKNKAVVnEDTQGNVSQLQAEVKRLKEQLSQFTSGQITPESLLARDKEKTNYieyfleamlfFK 426
Cdd:COG5022 851 FGRSLKAKK---RFSLLKKETIY-LQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKKS----------LS 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 427 KSEQEK-KSLIEKITQLEDLTLKKEKFIQSNKMIVKFREdqimrLERLH-KEGRGSFLPEEQDRLL---SELRDEVQTLR 501
Cdd:COG5022 917 SDLIENlEFKTELIARLKKLLNNIDLEEGPSIEYVKLPE-----LNKLHeVESKLKETSEEYEDLLkksTILVREGNKAN 991
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 502 EHVEHHPR-LAKYAMENHSLREENRRLKllapvKRAHEIdaQSIARLEKAFAEVSSTETNDKGLQGfsPKALKESSFFTN 580
Cdd:COG5022 992 SELKNFKKeLAELSKQYGALQESTKQLK-----ELPVEV--AELQSASKIISSESTELSILKPLQK--LKGLLLLENNQL 1062
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 581 TEKLKAQLLQIQTELNNSKQEYE----EFKELTRKKQLELESELQSLQKANLNLENLLEATKVCKRQEVSQLNKLHAETL 656
Cdd:COG5022 1063 QARYKALKLRRENSLLDDKQLYQlestENLLKTINVKDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTL 1142
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 657 KIITTPTKAYQL---CSRLVPKSSPEVGSFGFLCTESSSRLDNDILNEPvppemseqaLEAVSEELRTVQEQLSVLQVKL 733
Cdd:COG5022 1143 EPVFQKLSVLQLeldGLFWEANLEALPSPPPFAALSEKRLYQSALYDEK---------SKLSSSEVNDLKNELIALFSKI 1213
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 734 DEEERKNLKLQQNVDKLEHHSTQMQELFSSERSDWTKQQQ------EHVTQLSDLEKQLQDAQTKNEFLKCEVHDLRIVL 807
Cdd:COG5022 1214 FSGWPRGDKLKKLISEGWVPTEYSTSLKGFNNLNKKFDTPasmsneKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYI 1293
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 808 NSADKEL-----SLVKLEYSTFKENHEKELSQLSERHvqvqlQLDNARLENEKLLESQACLQDSYDNL----------QE 872
Cdd:COG5022 1294 NVGLFNAlrtkaSSLRWKSATEVNYNSEELDDWCREF-----EISDVDEELEELIQAVKVLQLLKDDLnkldelldacYS 1368
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930325 873 VMKFEIDQLSKNLQNCKQENETLKSDLHNLVEL---FEAEKERNNKLSLQFEEDKENSSKEILKVLET 937
Cdd:COG5022 1369 LNPAEIQNLKSRYDPADKENNLPKEILKKIEALlikQELQLSLEGKDETEVHLSEIFSEEKSLISLDR 1436
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
863-1329 |
2.05e-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: 49.27 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 863 LQDSYDNLQEVMKF--EIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKLSLQfeEDKENSSKEILKVLETVRQ 940
Cdd:TIGR00606 171 LKQKFDEIFSATRYikALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSK--EAQLESSREIVKSYENELD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 941 EKQKEMAKCEKQMAKIQKLEESLLA-------TENVISSLEKSRESDKELVTNLMNQIQELRISIG-EKSETIATLKQEL 1012
Cdd:TIGR00606 249 PLKNRLKEIEHNLSKIMKLDNEIKAlksrkkqMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVrEKERELVDCQREL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1013 QDINCKYNASLADKEE--------------SKELIRRQEVDILELKETLRLRILSEDIERDMLCEDlAHATEQLNMLTEA 1078
Cdd:TIGR00606 329 EKLNKERRLLNQEKTEllveqgrlqlqadrHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKN-FHTLVIERQEDEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1079 SKKHSGL------LQSAQEELTRKEALIQELQHKLNQEKEEVEQKKNEFSLKMRQLEHVMGSATEYPQSPKTPPHFQAHL 1152
Cdd:TIGR00606 408 KTAAQLCadlqskERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1153 AKL-----LETQEQEIEDGRASKTSLQHLVTKLNEDREVKNAEILRMKDQLCEMENLRLESQQLREKNW----LLQRQLD 1223
Cdd:TIGR00606 488 SKAeknslTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSrhsdELTSLLG 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1224 DVKRQQESGDQSHPDSQQLKneheeIIKERLAknKLIEEMLKMKTNLEEVQSALHSKEKACHRMSEEIertrtLESRAFQ 1303
Cdd:TIGR00606 568 YFPNKKQLEDWLHSKSKEIN-----QTRDRLA--KLNKELASLEQNKNHINNELESKEEQLSSYEDKL-----FDVCGSQ 635
|
490 500
....*....|....*....|....*.
gi 39930325 1304 EKEqlrSKLEEMYEERERTFLEMEML 1329
Cdd:TIGR00606 636 DEE---SDLERLKEEIEKSSKQRAML 658
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1085-1386 |
2.07e-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: 48.97 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1085 LLQSAQEELTRKEALIQELQHKLNQEKeeVEQKKNEFSLKMRQLEHVMGSATEYPQSPKTPPHFQAHLAKLLETQEQEIE 1164
Cdd:pfam17380 274 LLHIVQHQKAVSERQQQEKFEKMEQER--LRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1165 DGRASKtslqhlvtKLNEDREVKNAEILRMKDQLCEMENLRLESQQlreKNWLLQRQLDDVKRQQESGDQSHPDSQQLKN 1244
Cdd:pfam17380 352 RIRQEE--------RKRELERIRQEEIAMEISRMRELERLQMERQQ---KNERVRQELEAARKVKILEEERQRKIQQQKV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1245 EHEEIIKERlaknkliEEMLKmktnlEEVQSALHSKEKACHRM-SEEIERTRTLESRAFQEKEQLRSKLEEMYEERERTF 1323
Cdd:pfam17380 421 EMEQIRAEQ-------EEARQ-----REVRRLEEERAREMERVrLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKR 488
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930325 1324 LEmEMLKKQLEFLAEENGKLVGHQNLHQKIQYVVRLKKENIrLTEETEKLRAENLFLKEKKKE 1386
Cdd:pfam17380 489 AE-EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKA-IYEEERRREAEEERRKQQEME 549
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
777-1356 |
2.75e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 777 TQLSDLEKQLQDAQTKneflkcevhDLRIVLNSADKELSLVKLEYSTFKENHEkelsqlserhvQVQLQLDNARLENEKL 856
Cdd:PRK02224 187 GSLDQLKAQIEEKEEK---------DLHERLNGLESELAELDEEIERYEEQRE-----------QARETRDEADEVLEEH 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 857 LESQACLqdsydnlqEVMKFEIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKL--SLQFEEDKENSSKEILKV 934
Cdd:PRK02224 247 EERREEL--------ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLlaEAGLDDADAEAVEARREE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 935 LETVRQEKQKEMAKCEKQMAKIQKLEESLlaTENvISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQD 1014
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAHNEEAESL--RED-ADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1015 INCKYNASLADKEESKELIRrqevDILELKETLRLRILSEDIERDMLCEDLAHATEqlnmLTEASK--------KHSGLL 1086
Cdd:PRK02224 396 LRERFGDAPVDLGNAEDFLE----ELREERDELREREAELEATLRTARERVEEAEA----LLEAGKcpecgqpvEGSPHV 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1087 QSAQEELTRKEaliqelqhKLNQEKEEVEQKKNEFSLKMRQLEHVMGSATEYPQSPKTpphfQAHLAKLLETQEQEIEDG 1166
Cdd:PRK02224 468 ETIEEDRERVE--------ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEER----REDLEELIAERRETIEEK 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1167 RASKTSLQHLVTKLNEDREVKNAEilrmkdqlceMENLRLESQQLREKNWLLQRQLDDVKRQQESGDQSHpDSQQLKNEH 1246
Cdd:PRK02224 536 RERAEELRERAAELEAEAEEKREA----------AAEAEEEAEEAREEVAELNSKLAELKERIESLERIR-TLLAAIADA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1247 EEIIKERLAKNKLIEEMlkmktNLEevqsalhSKEkachRMSEEIERTRTLES---------------RAFQEKEQLRSK 1311
Cdd:PRK02224 605 EDEIERLREKREALAEL-----NDE-------RRE----RLAEKRERKRELEAefdearieearedkeRAEEYLEQVEEK 668
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 39930325 1312 LEEMYEERERTFLEMEMLKKQLEFLAEENGKLVGHQNLHQKIQYV 1356
Cdd:PRK02224 669 LDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEAL 713
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
921-1318 |
3.06e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 921 EEDKENSSKEILKVLETVRQEKQKEMAKCEKQM----AKIQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRI 996
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLdelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 997 SIGEKSETIATLKQELQDINCKYNASLADKEESKELIRRQEVDIL-----ELKETL-RLRILSEDIERDMlcedlaHATE 1070
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIqaelsKLEEEVsRIEARLREIEQKL------NRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1071 QLNMLTEASKKHsglLQSAQEELTRKEALIQELQHKLNQEKEEVEQKKNEFSLKMRQLEhvmgsateypqspktpphfqa 1150
Cdd:TIGR02169 826 LEKEYLEKEIQE---LQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLE--------------------- 881
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1151 hlaKLLETQEQEIEDGRASKTSLQHLVTKLNEDREVKNaeiLRMKDQLCEMENLrleSQQLREknwllqrqLDDVKRQQE 1230
Cdd:TIGR02169 882 ---SRLGDLKKERDELEAQLRELERKIEELEAQIEKKR---KRLSELKAKLEAL---EEELSE--------IEDPKGEDE 944
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1231 SGDQSHPDSQQLKNEHEEIIKERLA----KNKLIEEMLKMKTNLEEVQSALHSKEKACHRMSEEIERTRTLESRAFQEK- 1305
Cdd:TIGR02169 945 EIPEEELSLEDVQAELQRVEEEIRAlepvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAf 1024
|
410
....*....|...
gi 39930325 1306 EQLRSKLEEMYEE 1318
Cdd:TIGR02169 1025 EAINENFNEIFAE 1037
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
712-1120 |
3.14e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 712 LEAVSEELRTVQEQLSVLQVKLDEEERK----NLKLQQNVDKLEHHSTQMQELFSseRSDWTKQQQEHvtqLSDLEKQLQ 787
Cdd:pfam15921 470 LESTKEMLRKVVEELTAKKMTLESSERTvsdlTASLQEKERAIEATNAEITKLRS--RVDLKLQELQH---LKNEGDHLR 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 788 DAQTkneflKCEVhdLRIVLNSADKELSLVKLEYSTFKE---NHEKELSQLSERHVQVQLQLDNARLE-----------N 853
Cdd:pfam15921 545 NVQT-----ECEA--LKLQMAEKDKVIEILRQQIENMTQlvgQHGRTAGAMQVEKAQLEKEINDRRLElqefkilkdkkD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 854 EKLLESQACLQD-----------SYDNLQEV--MKFEIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKER----NNKL 916
Cdd:pfam15921 618 AKIRELEARVSDlelekvklvnaGSERLRAVkdIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEmettTNKL 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 917 SLQFE--EDKENSSKEILKVLETVRQEKQKEMAKCEKQM----AKIQKLEESLLATENVISSLEKSRESDKELVTNLMnq 990
Cdd:pfam15921 698 KMQLKsaQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQItakrGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS-- 775
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 991 iQELRISIGEKSETIAT----------LKQELQDINCKYNASLADKEESKELIRRQEVDI--LELKETLRLRIL------ 1052
Cdd:pfam15921 776 -QELSTVATEKNKMAGElevlrsqerrLKEKVANMEVALDKASLQFAECQDIIQRQEQESvrLKLQHTLDVKELqgpgyt 854
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39930325 1053 SEDIERDMLCEDLAHATEQLNMLTEAS-----KKHSGLLQSAQEELTRK-EALIQELQHKLNQEKEEVEQKKNE 1120
Cdd:pfam15921 855 SNSSMKPRLLQPASFTRTHSNVPSSQStasflSHHSRKTNALKEDPTRDlKQLLQELRSVINEEPTVQLSKAED 928
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
424-1334 |
3.75e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 424 FFKKSEQEKKSLIEKITQLEDLTLKKEKfiqsnkmivkfredqimRLERLHKEGRGSflpEEQDRLLSELRDEVQTLREH 503
Cdd:TIGR02169 147 FISMSPVERRKIIDEIAGVAEFDRKKEK-----------------ALEELEEVEENI---ERLDLIIDEKRQQLERLRRE 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 504 VEHhprlakyAMENHSLREENRRLKLLAPVKRAHEIDAQsiarLEKAFAEVSSTETNDKGLQGFSPKALKESsfftntek 583
Cdd:TIGR02169 207 REK-------AERYQALLKEKREYEGYELLKEKEALERQ----KEAIERQLASLEEELEKLTEEISELEKRL-------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 584 lkAQLLQIQTELNnskqeyEEFKELTRKKQLELESELQSLQKANLNLENLLEATKVCKRQEVSQLNKLHAETLKIITTpt 663
Cdd:TIGR02169 268 --EEIEQLLEELN------KKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE-- 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 664 kayqlcsrlVPKSSPEVGSFGFLCTESSSRLDNDILNEpvppEMSEQALEAVSEELRTVQEQLSVLQVKLDEEERKNLKL 743
Cdd:TIGR02169 338 ---------IEELEREIEEERKRRDKLTEEYAELKEEL----EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 744 QQNVDKLEHHSTQMqelfSSERSDWTKQQQEHVTQLSDLEKQLQDAQTKNEFLKCEVHDLRIVLNSADKELSLVKLEYST 823
Cdd:TIGR02169 405 KRELDRLQEELQRL----SEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 824 FkenhEKELSQLSERHVQVQLQLDNARLE------NEKLLESQacLQDSYDNLQEVMKFEID-------QLSKNLQNCKQ 890
Cdd:TIGR02169 481 V----EKELSKLQRELAEAEAQARASEERvrggraVEEVLKAS--IQGVHGTVAQLGSVGERyataievAAGNRLNNVVV 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 891 ENETLKsdlhnlVELFEAEKERN---------NKLSlQFEEDKENSSKE--ILKVLETVRQEKQKE-------------- 945
Cdd:TIGR02169 555 EDDAVA------KEAIELLKRRKagratflplNKMR-DERRDLSILSEDgvIGFAVDLVEFDPKYEpafkyvfgdtlvve 627
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 946 -MAKCEKQMAKIQ------------------------------KLEESLLATENVISSLEKSRESDKELVTNLMNQIQEL 994
Cdd:TIGR02169 628 dIEAARRLMGKYRmvtlegelfeksgamtggsraprggilfsrSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDEL 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 995 RISIGEKSETIATLKQELQDINCKYNASLADKEESKELIRRQEVDILELKEtlRLRILSEDIERdmLCEDLAHATEQLNM 1074
Cdd:TIGR02169 708 SQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS--ELKELEARIEE--LEEDLHKLEEALND 783
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1075 LtEASKKHSGlLQSAQEELTRKEALIQELQHKLNqekeEVEQKKNEFSLKMRQLEhvmgsateypqspktpphfqahlaK 1154
Cdd:TIGR02169 784 L-EARLSHSR-IPEIQAELSKLEEEVSRIEARLR----EIEQKLNRLTLEKEYLE------------------------K 833
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1155 LLETQEQEIEDGRASKTSLQHLVTKLNEDREVKNAEIlrmkdqlcemENLRLESQQLREKNWLLQRQLDDVK---RQQES 1231
Cdd:TIGR02169 834 EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL----------EELEAALRDLESRLGDLKKERDELEaqlRELER 903
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1232 GDQSHPDSQQLKNEHEEIIKERL-AKNKLIEEMLKMKTNLEEVQSALHSKEK---ACHRMSEEIERTRTLESRAFQEKEQ 1307
Cdd:TIGR02169 904 KIEELEAQIEKKRKRLSELKAKLeALEEELSEIEDPKGEDEEIPEEELSLEDvqaELQRVEEEIRALEPVNMLAIQEYEE 983
|
970 980
....*....|....*....|....*..
gi 39930325 1308 LRSKLEEMYEERERTFLEMEMLKKQLE 1334
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEERKAILERIE 1010
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
378-1060 |
4.83e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 378 SQLQAEVKRLKEQLSQFTSGQITPESLLARDKEKTNYIEYFLEAMlffKKSEQEKKSLIEKITQLEDLTLKKEKFIQSNK 457
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA---KKADEAKKKAEEAKKKADAAKKKAEEAKKAAE 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 458 MIVKFREDQIMRLERLHKEGRGSFLPEEQDRllsELRDEVQTLREHVEHHPRLAKYAMENHSLREENRrlKLLAPVKRAH 537
Cdd:PTZ00121 1347 AAKAEAEAAADEAEAAEEKAEAAEKKKEEAK---KKADAAKKKAEEKKKADEAKKKAEEDKKKADELK--KAAAAKKKAD 1421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 538 EID--AQSIARLEKAFAEVSSTETNDKGLQGFSPKALKESSFFTNTEKLKAQLLQIQTELNNSKQEYEEFKELTRKKQLE 615
Cdd:PTZ00121 1422 EAKkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE 1501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 616 LESELQSLQKAnlnlENLLEATKVCKRQEVSQL-NKLHAETLKIITTPTKAYQLCSRLVPKSSPEVGSfgflcTESSSRL 694
Cdd:PTZ00121 1502 AKKAAEAKKKA----DEAKKAEEAKKADEAKKAeEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK-----AEEAKKA 1572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 695 DNDILNEPVPPEMSEQALEAVSEELRTVQEQLSVL---QVKLDEEER---KNLKLQQNVDKLEHHSTQMQELFSSERSDW 768
Cdd:PTZ00121 1573 EEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkaeEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEKKKAEEL 1652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 769 TKQQQEHVTQLSDLEKQLQDAQTKNEFLKCEVHDLRivlnsadkelslVKLEYSTFKENHEKELSQLSERHVQVQLQLDN 848
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK------------KAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 849 ARLEnekllesqaclqdsydnlQEVMKFEIDQLSKNLQNCKQENETLKSDlhnlvelfEAEKERNNKLSLQFEEDKENSS 928
Cdd:PTZ00121 1721 LKKA------------------EEENKIKAEEAKKEAEEDKKKAEEAKKD--------EEEKKKIAHLKKEEEKKAEEIR 1774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 929 KEILKVL-ETVRQEKQKEMAKCEKqmakiqKLEESLLATENVISSLEKSR---ESDKELVTNLMNQIQELRISIGEKSET 1004
Cdd:PTZ00121 1775 KEKEAVIeEELDEEDEKRRMEVDK------KIKDIFDNFANIIEGGKEGNlviNDSKEMEDSAIKEVADSKNMQLEEADA 1848
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 39930325 1005 IATLKQELQDINCKYNASLADKEESKELIRRQEVDILELKETLRLRilSEDIERDM 1060
Cdd:PTZ00121 1849 FEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKID--KDDIEREI 1902
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
825-1045 |
5.33e-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: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 825 KENHEKELSQLSERHVQVQLQLDNARLENEKLLESQACLQDSYDNLQE---VMKFEIDQLSKNLQNCKQENETLKSDLHN 901
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 902 LVELFEA------EKERNNKLSLQFEEDKENSSKEILKVLETVRQEKQKEMAKCEKQMAKIQKLEESLlatenvisslEK 975
Cdd:COG4942 102 QKEELAEllralyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL----------EA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 976 SRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQDINCKYNASLADKEESKELIRRQEVDILELKE 1045
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
714-1343 |
5.65e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 5.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 714 AVSEELRTVQEQ-LSVLQVKLDEEERKnlklqqnvdklehHSTQMQELfssersdwtkqQQEHVTQLSDLEKQLQDAQTK 792
Cdd:pfam01576 316 AAQQELRSKREQeVTELKKALEEETRS-------------HEAQLQEM-----------RQKHTQALEELTEQLEQAKRN 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 793 neflKCEVHDLRIVLNSADKELSLVKLEYSTFKENHEKELSQLSERHVQVQLQLDNARLENEKLLESQACLQDSYDNLQE 872
Cdd:pfam01576 372 ----KANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSS 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 873 VMkfeiDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKLSLQFE--EDKENSSKEILKVLETVRQEKQKEMAKCE 950
Cdd:pfam01576 448 LL----NEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRqlEDERNSLQEQLEEEEEAKRNVERQLSTLQ 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 951 KQMAKIQKLEESLLATenvISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQDI-----NCKYNASLAD 1025
Cdd:pfam01576 524 AQLSDMKKKLEEDAGT---LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLlvdldHQRQLVSNLE 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1026 KEESK-ELIRRQEVDILELKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQ 1104
Cdd:pfam01576 601 KKQKKfDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNV 680
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1105 HKLNQEKEEVEQKKNEFSLKMRQLEHVMGSATEypQSPKTPPHFQAHLAK----LLETQEQEIEDGRASKTSLQHLVTKL 1180
Cdd:pfam01576 681 HELERSKRALEQQVEEMKTQLEELEDELQATED--AKLRLEVNMQALKAQferdLQARDEQGEEKRRQLVKQVRELEAEL 758
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1181 NEDREVKnAEILRMKDQLcEMENLRLESQ-------------QLREknwlLQRQLDDVKRQQESGDQSHPDSQQLKNEHE 1247
Cdd:pfam01576 759 EDERKQR-AQAVAAKKKL-ELDLKELEAQidaankgreeavkQLKK----LQAQMKDLQRELEEARASRDEILAQSKESE 832
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1248 EIIKERLAknklieEMLKMKTNLEEVQSALHSKEKACHRMSEEIERTRTLESRAFQEKEQLRSKLEEMYEERERTFLEME 1327
Cdd:pfam01576 833 KKLKNLEA------ELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTE 906
|
650
....*....|....*.
gi 39930325 1328 MLKKQLEFLAEENGKL 1343
Cdd:pfam01576 907 LLNDRLRKSTLQVEQL 922
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
932-1386 |
7.16e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 932 LKVLETVRQEKQKEMAKcekqmaKIQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQE 1011
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEK------KLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1012 LQDINCKYNASLADKEESKELIRRQEVDILELKETLRlrilsedierdmlcEDLAHATEQLNMLTEASKKHSGLLQSAQE 1091
Cdd:TIGR04523 98 INKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKK--------------ENKKNIDKFLTEIKKKEKELEKLNNKYND 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1092 ELTRKEALIQELqHKLNQEKEEVEQKKNEFSLKMRQLEHVMGSATEYPQSPKtpphfqahlaklleTQEQEIEDGRASKT 1171
Cdd:TIGR04523 164 LKKQKEELENEL-NLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNK--------------SLESQISELKKQNN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1172 SLQHLVTKLNEDREVKNAEILRMKDQLcemenLRLESQQLREKNWLLQRQLdDVKRQQESGDQSHPDSQQLKNEHEEIIK 1251
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQL-----NQLKDEQNKIKKQLSEKQK-ELEQNNKKIKELEKQLNQLKSEISDLNN 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1252 ERLAK--NKLIEEMLKMKTNLEEVQSALHSKEKACHRMSEEIERTRT----LESRAFQEKEQLR---SKLEEMYEERERT 1322
Cdd:TIGR04523 303 QKEQDwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKeltnSESENSEKQRELEekqNEIEKLKKENQSY 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930325 1323 FLEMEMLKKQLEFLaeeNGKLVGHQNLHQKIQYVVR-LKKENIRLTEETEKLRAENLFLKEKKKE 1386
Cdd:TIGR04523 383 KQEIKNLESQINDL---ESKIQNQEKLNQQKDEQIKkLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
708-1343 |
7.44e-05 |
|
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: 47.41 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 708 SEQALEAVSEELRTVQEQLSVLQVKLDEEER-KNLKLQQNVDKLEHHSTQMQEL-FSSERSdwTKQQQEHVTQLSDLEKQ 785
Cdd:pfam05483 72 NSEGLSRLYSKLYKEAEKIKKWKVSIEAELKqKENKLQENRKIIEAQRKAIQELqFENEKV--SLKLEEEIQENKDLIKE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 786 LQDAQTKNEFLKCEVHDLRIVLNSADKELSLVKLEYSTFKENHEKELSQLSERHVQVQlqldNARLENE-KLLESQACLQ 864
Cdd:pfam05483 150 NNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAE----NARLEMHfKLKEDHEKIQ 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 865 dsydNLQEVMKFEIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKLSLQFEEDKENSsKEILKVLETVRQEKQK 944
Cdd:pfam05483 226 ----HLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENL-KELIEKKDHLTKELED 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 945 EMAKCEKQMAKIQKLEESLLATENVISSLEKSRESDKE-----------LVTNLMNQIQELRISIGEKSETIATLKQELQ 1013
Cdd:pfam05483 301 IKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEelnkakaahsfVVTEFEATTCSLEELLRTEQQRLEKNEDQLK 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1014 DINCKYNASLADKEESKELIRRQEVDILELKETL--RLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQ---- 1087
Cdd:pfam05483 381 IITMELQKKSSELEEMTKFKNNKEVELEELKKILaeDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqlt 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1088 ----SAQEELTRKEALIQELQH-------------KLNQEKEEVEQKKNEFSLKMR-QLEHVMGSATEYPQSPKTPPHFQ 1149
Cdd:pfam05483 461 aiktSEEHYLKEVEDLKTELEKeklknieltahcdKLLLENKELTQEASDMTLELKkHQEDIINCKKQEERMLKQIENLE 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1150 AHLAKLLETQEQEIEDGRASKTSLQHLVTKLNEDREVKNAEILRMKDQLCEMEN------------------LRLESQQL 1211
Cdd:pfam05483 541 EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENkcnnlkkqienknknieeLHQENKAL 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1212 REKNWLLQRQLDDV-----KRQQESGDQSHPDSQQLKNEHEEIIKERLAKNKLIEEMLKMKTNLEEVQSALHSKEKAC-H 1285
Cdd:pfam05483 621 KKKGSAENKQLNAYeikvnKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCqH 700
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930325 1286 RMSE-------------EIERTRTLESRAFQEKEQLRSKLEEMYE-ERERTFLEMEMLKKQLEFLAEENGKL 1343
Cdd:pfam05483 701 KIAEmvalmekhkhqydKIIEERDSELGLYKNKEQEQSSAKAALEiELSNIKAELLSLKKQLEIEKEEKEKL 772
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
834-1027 |
7.53e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 47.15 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 834 QLSERHVQVQLQLDNARLenekllesQACLQDSYDNLQEvMKFEIDQLS---KNLQNC----KQENETLKSDLHNLVElf 906
Cdd:pfam09726 390 QLSKPDALVRLEQDIKKL--------KAELQASRQTEQE-LRSQISSLTsleRSLKSElgqlRQENDLLQTKLHNAVS-- 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 907 eaekernnklslQFEEDKENSSKeilkvLETVRQEKQKEMAKCEKQMA---KIQKLEESLL--ATENVISSLEKSRESDK 981
Cdd:pfam09726 459 ------------AKQKDKQTVQQ-----LEKRLKAEQEARASAEKQLAeekKRKKEEEATAarAVALAAASRGECTESLK 521
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 39930325 982 ELVTNLMNQIQELRISIGEKSETIATLKQELQDINcKYNASLADKE 1027
Cdd:pfam09726 522 QRKRELESEIKKLTHDIKLKEEQIRELEIKVQELR-KYKESEKDTE 566
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
883-1386 |
7.80e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 7.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 883 KNLQNCKQENETLKSDLHNLVELFEA-EKERNNKLSLqfEEDKENSSKEILKVLETVRQEKQKEMAKCEKQMAK----IQ 957
Cdd:TIGR04523 57 KNLDKNLNKDEEKINNSNNKIKILEQqIKDLNDKLKK--NKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKlekqKK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 958 KLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQDINCKYNA---SLADKEESKELIR 1034
Cdd:TIGR04523 135 ENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKlelLLSNLKKKIQKNK 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1035 RQEVDILELKE---TLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQHKLNQEK 1111
Cdd:TIGR04523 215 SLESQISELKKqnnQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1112 EEVEQKKNEfslkmrqlehvmgsateypqspktpphFQAHLAKLLETQEQEIEDgraSKTSLQHLVTKLNEDREVKNAEI 1191
Cdd:TIGR04523 295 SEISDLNNQ---------------------------KEQDWNKELKSELKNQEK---KLEEIQNQISQNNKIISQLNEQI 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1192 LRMKDQLCEMENLRLESQ-QLREKnwllQRQLDDVKRQQESGDQSHPDSQQLKNEHEEIIKERLAKNKLIEEmlkmktNL 1270
Cdd:TIGR04523 345 SQLKKELTNSESENSEKQrELEEK----QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDE------QI 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1271 EEVQSALHSKEKACHRMSEEIERTRTLESRAFQEKEQLRSKLEEMYEERERTFLEMEMLKKQLEFLAEENGKLVghQNLH 1350
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ--KELK 492
|
490 500 510
....*....|....*....|....*....|....*.
gi 39930325 1351 QKIQYVVRLKKENIRLTEETEKLRAENLFLKEKKKE 1386
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK 528
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
829-1313 |
8.84e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.09 E-value: 8.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 829 EKELSQLSERHVQVQLQLDNARLENEKLLESQACLQDSYDNLQEVMKfEIDQLSKNLQNCKQENETLksdLHNLVELFEA 908
Cdd:pfam01576 11 EEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCA-EAEEMRARLAARKQELEEI---LHELESRLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 909 EKERNNKL--------------------------SLQFE------------------EDKENSSKEILKVLE-------- 936
Cdd:pfam01576 87 EEERSQQLqnekkkmqqhiqdleeqldeeeaarqKLQLEkvtteakikkleedilllEDQNSKLSKERKLLEerisefts 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 937 --TVRQEKQKEMAKCE-KQMAKIQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQ 1013
Cdd:pfam01576 167 nlAEEEEKAKSLSKLKnKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQ 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1014 DINCKYNASLADKEESKELIRRQEVDILELKETLRL------------RILSEDIE--RDMLCEDLAHATEQLNMLTEAS 1079
Cdd:pfam01576 247 AALARLEEETAQKNNALKKIRELEAQISELQEDLESeraarnkaekqrRDLGEELEalKTELEDTLDTTAAQQELRSKRE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1080 KKHSGLLQSAQEELTRKEALIQELQHKLNQEKEeveqkknEFSLKMRQLEHVMGSATEYPQSPKTPPHFQAHLAKLLETQ 1159
Cdd:pfam01576 327 QEVTELKKALEEETRSHEAQLQEMRQKHTQALE-------ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQA 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1160 EQEIEDGRASKTS-LQHLVTKLNEDREVKNAEILRMKDQLCEMENLRLESQQLREKNWLLQRQLDDVKRQ--------QE 1230
Cdd:pfam01576 400 KQDSEHKRKKLEGqLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQlqdtqellQE 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1231 SGDQSHPDSQQLKN------------EHEEIIKERLAK--NKLIEEMLKMKTNLEEVQSALHSKEKACHRMSEEIERTrt 1296
Cdd:pfam01576 480 ETRQKLNLSTRLRQledernslqeqlEEEEEAKRNVERqlSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAL-- 557
|
570
....*....|....*..
gi 39930325 1297 leSRAFQEKEQLRSKLE 1313
Cdd:pfam01576 558 --TQQLEEKAAAYDKLE 572
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
780-1005 |
9.37e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 780 SDLEKQLQDAQTKNEFLKCEVHDLRIVLNSADKELSlvkleysTFKENH-----EKELSQLSERHVQVQLQLDNARLEne 854
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALE-------EFRQKNglvdlSEEAKLLLQQLSELESQLAEARAE-- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 855 kllesQACLQDSYDNLQEVMKFEIDQL-----SKNLQNCKQENETLKSDLHNLVELFEAE----KERNNKLSlQFEEDKE 925
Cdd:COG3206 235 -----LAEAEARLAALRAQLGSGPDALpellqSPVIQQLRAQLAELEAELAELSARYTPNhpdvIALRAQIA-ALRAQLQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 926 NSSKEILKVLETVRQEKQKEMAKCEKQMAKIQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETI 1005
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
727-1231 |
9.59e-05 |
|
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: 47.04 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 727 SVLQVKLDEEERKNLKLQQNVDKLEHHSTQMQELFSS--ERSDWTKQQQEHVTQ-LSDLEKQLQDAQTKNEFLKCEVHDL 803
Cdd:pfam05557 37 SALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREqaELNRLKKKYLEALNKkLNEKESQLADAREVISCLKNELSEL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 804 RIVLNSADKELSLVKLEYSTFKENHE---KELSQLSERHVQVQLQLDNARLENEKL--LESQACLQDSYDNLQEVMKFE- 877
Cdd:pfam05557 117 RRQIQRAELELQSTNSELEELQERLDllkAKASEAEQLRQNLEKQQSSLAEAEQRIkeLEFEIQSQEQDSEIVKNSKSEl 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 878 --IDQLSKNLQNCKQENETLKSDLHNlVELFEAEKErnnklSLQFEEDKENSSKEILKVLETVRQEKQKEMAKCEKQMAK 955
Cdd:pfam05557 197 arIPELEKELERLREHNKHLNENIEN-KLLLKEEVE-----DLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQD 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 956 IQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQDINCKynasladKEESKELIRR 1035
Cdd:pfam05557 271 TGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKK-------LKRHKALVRR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1036 qevdilelketLRLRILSEDIERDMLCEDLAHATEQLNMlTEASKKHSGLLQSAQEELTRKEALIQELQHKLNQEKEEVE 1115
Cdd:pfam05557 344 -----------LQRRVLLLTKERDGYRAILESYDKELTM-SNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1116 QKKNEFSLKMRQLEhvMGSATEYPQSPKTPPHFQAHLAKLLETQEQEIEDGRASKTSLQHLVTKLN--EDREVKNAEILR 1193
Cdd:pfam05557 412 GYKQQAQTLERELQ--ALRQQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRClqGDYDPKKTKVLH 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 39930325 1194 MKD---------QLCEMENLRLESQQLREKNWLLQRQLDDVKRQQES 1231
Cdd:pfam05557 490 LSMnpaaeayqqRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPET 536
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
706-1363 |
1.19e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 706 EMSEQALEAVSEELRTVQEQLSVLQVKLDEEER----KNLKLQQNVDKLEHHSTQMQELFSSERsDWTKQQQEHVTQLSD 781
Cdd:TIGR00606 408 KTAAQLCADLQSKERLKQEQADEIRDEKKGLGRtielKKEILEKKQEELKFVIKELQQLEGSSD-RILELDQELRKAERE 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 782 LEKQLQDAQTknEFLKCEVHDLRivLNSADKELSLVKLEYSTFKENHEKE----LSQLSERHVQVQLQLDNARLENEKLL 857
Cdd:TIGR00606 487 LSKAEKNSLT--ETLKKEVKSLQ--NEKADLDRKLRKLDQEMEQLNHHTTtrtqMEMLTKDKMDKDEQIRKIKSRHSDEL 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 858 ESQA-------CLQDSYDNLQEVMKFEIDQLSKnLQNCKQENETLKSDLHNLVELFEAE--KERNNKLSLQFEEDKENSS 928
Cdd:TIGR00606 563 TSLLgyfpnkkQLEDWLHSKSKEINQTRDRLAK-LNKELASLEQNKNHINNELESKEEQlsSYEDKLFDVCGSQDEESDL 641
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 929 KEILKVLETVRQEKQKEMAKCEKQMAKIQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATL 1008
Cdd:TIGR00606 642 ERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKK 721
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1009 KQELQDInckynasLADKEESKELIRRQEVDILELKEtlRLRILSEDIERdmLCEDLAHATEQLNM------LTEASKKH 1082
Cdd:TIGR00606 722 EKRRDEM-------LGLAPGRQSIIDLKEKEIPELRN--KLQKVNRDIQR--LKNDIEEQETLLGTimpeeeSAKVCLTD 790
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1083 SGLLQSAQEELTRKEALIQELQHK------------LNQEKEEVEQKKNEFSLKMRQLEHVMGSATEYPQspktppHFQA 1150
Cdd:TIGR00606 791 VTIMERFQMELKDVERKIAQQAAKlqgsdldrtvqqVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQ------HLKS 864
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1151 HLAKLLETQEQEIEDGRASKTSLQHLVTKLNEDREVkNAEILRMKDQLCEMEnlrlesqQLREKnwLLQRQLDDVKRQQE 1230
Cdd:TIGR00606 865 KTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSL-IREIKDAKEQDSPLE-------TFLEK--DQQEKEELISSKET 934
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1231 SGDQSHPDSQQLKNEHEEIIKERLAKNKLIEE-----MLKMKTNLEEVQSALHSKEKACHRMSEEIERTRTLESRAFQEK 1305
Cdd:TIGR00606 935 SNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgkddyLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQE 1014
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 39930325 1306 EQLRSKLEEMYEERERTFLEmEMLKKQLEFLAEEngKLVGHQNLHQKIQYVVRLKKEN 1363
Cdd:TIGR00606 1015 RWLQDNLTLRKRENELKEVE-EELKQHLKEMGQM--QVLQMKQEHQKLEENIDLIKRN 1069
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
730-1386 |
1.51e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 730 QVKLDEEERKNLKLQQNVDKLEHHSTQMQELFSSERSDWTKQQQEHVT---QLSDLEKQLQDAQTKNEFLKCEVHDLRIV 806
Cdd:TIGR00606 362 HIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTaaqLCADLQSKERLKQEQADEIRDEKKGLGRT 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 807 LnsadkELSLVKLEYSTFKENHEKELSQLSERHVQVQLQLDNARLENEKLLESQACLQDSYDNLQEVMKFEIDQLSKNLQ 886
Cdd:TIGR00606 442 I-----ELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRK 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 887 NCK--QENETLKSDLHNLVELFEAEKERNNKLSlQFEEDKENSSKEIL---------KVLETVRQEKQKEMAKCEKQMAK 955
Cdd:TIGR00606 517 LRKldQEMEQLNHHTTTRTQMEMLTKDKMDKDE-QIRKIKSRHSDELTsllgyfpnkKQLEDWLHSKSKEINQTRDRLAK 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 956 IQKLEESLLATENVISSLEKSREsdkELVTNLMNQIQELRISIGEKSEtIATLKQELQDINcKYNASLADKEESKELIRR 1035
Cdd:TIGR00606 596 LNKELASLEQNKNHINNELESKE---EQLSSYEDKLFDVCGSQDEESD-LERLKEEIEKSS-KQRAMLAGATAVYSQFIT 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1036 QEVDILELKETLRLRILSEDIERDMLCEDLAHA-----TEQLNMLTEASKKHS------GLLQSAQEELTRKEALIQELQ 1104
Cdd:TIGR00606 671 QLTDENQSCCPVCQRVFQTEAELQEFISDLQSKlrlapDKLKSTESELKKKEKrrdemlGLAPGRQSIIDLKEKEIPELR 750
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1105 HKLNQEKEEVEQKKNEFSLKMRQLEHVMgSATEYPQSPKTPPHFQAHLAKLLETQEQEIED--GRASKTSLQHLVTKLNE 1182
Cdd:TIGR00606 751 NKLQKVNRDIQRLKNDIEEQETLLGTIM-PEEESAKVCLTDVTIMERFQMELKDVERKIAQqaAKLQGSDLDRTVQQVNQ 829
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1183 DREVKNAEILRMKDqlcEMENLRLESQQLREKNWLLQRQLDDVKRQQESGDQSHPDSQQLKNEHEEIIKERLAKNKLIee 1262
Cdd:TIGR00606 830 EKQEKQHELDTVVS---KIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREI-- 904
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1263 mlkmKTNLEEVQSALHSKEKACHRMSEEIERTRTLESRAFQEKEQLRSKLEEMYEERERTFLEME-----MLKKQLEFLA 1337
Cdd:TIGR00606 905 ----KDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQdgkddYLKQKETELN 980
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 39930325 1338 EENGKLVGHQNLHQKIQYVVRLKKENIRLTEETEKLRAENLFLKEKKKE 1386
Cdd:TIGR00606 981 TVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENE 1029
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
584-1057 |
1.70e-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: 45.89 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 584 LKAQLLQIQTELNNSKQEYE------EFKELTRKKQLELESE-LQSLQKANLNLENLlEATKVCKRQEVSQLNKLHAETL 656
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKrarielEKKASALKRQLDRESDrNQELQKRIRLLEKR-EAEAEEALREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 657 KIITTPTKAyqlcsrlvpKSSPEVGSfgflcTESSSRLDNDILNEPVPPEMSEQALEAVSEELRTVQEQLSVLQVKLDEE 736
Cdd:pfam05557 86 EALNKKLNE---------KESQLADA-----REVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 737 ERKNLKLQQNVDKLEHHSTQMQELFS--SERSDW---TKQQQEHVTQLSDLEKQLQDAQTKNEF----------LKCEVH 801
Cdd:pfam05557 152 EQLRQNLEKQQSSLAEAEQRIKELEFeiQSQEQDseiVKNSKSELARIPELEKELERLREHNKHlnenienkllLKEEVE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 802 DLRIVL----NSADKELSL-VKLEYSTFKENHEKELSQ-----------LSERHVQVQlQLDNARLENEKLLESQAclqD 865
Cdd:pfam05557 232 DLKRKLereeKYREEAATLeLEKEKLEQELQSWVKLAQdtglnlrspedLSRRIEQLQ-QREIVLKEENSSLTSSA---R 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 866 SYDNLQEVMKFEIDQLSKNLQNCKQENETLKSDLHNLV-ELFEAEKERNNKLSLQFEEDKE----NSSKEILKVLETVRQ 940
Cdd:pfam05557 308 QLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQrRVLLLTKERDGYRAILESYDKEltmsNYSPQLLERIEEAED 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 941 EKQKEMAKCEKQMAKIQKLEESLLATENVISSLEKS------------RESDKELVTNLMNQIQELRISIGEKSETIATL 1008
Cdd:pfam05557 388 MTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERElqalrqqesladPSYSKEEVDSLRRKLETLELERQRLREQKNEL 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 39930325 1009 KQEL------QDINCK--------YNASLADKEESKELIRRQEVDILELKEtlRLRILSEDIE 1057
Cdd:pfam05557 468 EMELerrclqGDYDPKktkvlhlsMNPAAEAYQQRKNQLEKLQAEIERLKR--LLKKLEDDLE 528
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
582-1117 |
1.81e-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: 46.17 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 582 EKLKAQLLQIQTELNNSKQEYEEFKELTRKKqlelESELQSLQKANLNLENLLEATKVCKRQEVSQLNKLHAETLKIITT 661
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKD----EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 662 PTKAYQLCSRLVPKSSPEVGSfgflcTESSSRLDNDILNEpvpPEMSEQALEAVSEELRTVQEQLSVLQVKLDEEERKNL 741
Cdd:TIGR04523 112 IKNDKEQKNKLEVELNKLEKQ-----KKENKKNIDKFLTE---IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 742 KLQQNVDKLEHHSTQMQELFSSERSdWTKQQQEHVTQLSDLEKQLQDAQTKNEFLKCEVHDLRIVLNSADKELslvkley 821
Cdd:TIGR04523 184 NIQKNIDKIKNKLLKLELLLSNLKK-KIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQL------- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 822 STFKENHEKELSQLSERhvqvQLQLDNArleNEKLLESQACLQDSYDNLQEVMKFEIDQLSKNLQNCKQENETLKSDLHN 901
Cdd:TIGR04523 256 NQLKDEQNKIKKQLSEK----QKELEQN---NKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 902 lvelfeaEKERNNKLSLQFEEDKENSSKEiLKVLETVRQEKQKEMAKCEKQMAKIQKLEESLLAT----ENVISSLEKSR 977
Cdd:TIGR04523 329 -------QISQNNKIISQLNEQISQLKKE-LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEiknlESQINDLESKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 978 ESDKELVTNLMNQIQELRISIGEKSETIATLKQELQDINcKYNASLADKEESKELIRR---QEVDILELK-ETLRLRILS 1053
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNN-SEIKDLTNQDSVKELIIKnldNTRESLETQlKVLSRSINK 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39930325 1054 EDIERDMLCEDLAHATEQLNMLTEASKKhsglLQSAQEELTRKEALIQELQHKLNQEKEEVEQK 1117
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKLNEEKKE----LEEKVKDLTKKISSLKEKIEKLESEKKEKESK 539
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
826-1383 |
2.36e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 826 ENHEKELSQLSERHVQVQLQLDNARLENEKLLESQACLQDSYDNLQEVMKFEIDQLSK---NLQNCKQENETLKSDLHNL 902
Cdd:pfam05483 116 EAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKyeyEREETRQVYMDLNNNIEKM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 903 VELFEAEK--ERNNKLSLQFEedkensSKEILKVLETVRQEKQKEMAKCEKQMAKIQ-KLEESLLATENVISSLEKSRES 979
Cdd:pfam05483 196 ILAFEELRvqAENARLEMHFK------LKEDHEKIQHLEEEYKKEINDKEKQVSLLLiQITEKENKMKDLTFLLEESRDK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 980 DKELVTNLMNQIQELRISIGEKSEtiatLKQELQDINCKYNASLADKEESKELIRRQEVDILELketlrlrilSEDIERD 1059
Cdd:pfam05483 270 ANQLEEKTKLQDENLKELIEKKDH----LTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL---------TEEKEAQ 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1060 MLCEDLAHATEQL--NMLTEASKKHSGLLQSAQEELTRKE----ALIQELQHKlNQEKEEVEQKKNEFSLKMRQLEHVMG 1133
Cdd:pfam05483 337 MEELNKAKAAHSFvvTEFEATTCSLEELLRTEQQRLEKNEdqlkIITMELQKK-SSELEEMTKFKNNKEVELEELKKILA 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1134 SAT----EYPQSPKTPPHFQA---HLAKLLETQEQEIEDgraskTSLQHLVTKLNEDREVKNAEILRMkdqlcEMENLRL 1206
Cdd:pfam05483 416 EDEklldEKKQFEKIAEELKGkeqELIFLLQAREKEIHD-----LEIQLTAIKTSEEHYLKEVEDLKT-----ELEKEKL 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1207 ESQQLreknwllqrqlddvkrqqesgdQSHPDSQQLKNEheeiikerlaknKLIEEMLKMKTNLEEVQSALHSKEKACHR 1286
Cdd:pfam05483 486 KNIEL----------------------TAHCDKLLLENK------------ELTQEASDMTLELKKHQEDIINCKKQEER 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1287 MSEEIErtrTLESRAFQEKEQLRSKLEEMYEERERTFLEMEMlkkqleflAEENGKLVGHQNLHQKIQYVV------RLK 1360
Cdd:pfam05483 532 MLKQIE---NLEEKEMNLRDELESVREEFIQKGDEVKCKLDK--------SEENARSIEYEVLKKEKQMKIlenkcnNLK 600
|
570 580
....*....|....*....|...
gi 39930325 1361 KENIRLTEETEKLRAENLFLKEK 1383
Cdd:pfam05483 601 KQIENKNKNIEELHQENKALKKK 623
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
820-1384 |
2.65e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.49 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 820 EYSTFKENHEKELSQLSERHVQVQLQLDNARLENEKLLESQACLQDSYDNLQEVMKFEIDQLSKNLQNCKQENETLKSDL 899
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 900 HNLVELFEAEKERNNKLSLQfeedKENSSKEILKVLETVRQEKQKEMAKCEKQmakiqkleeSLLATENVISSLEKS-RE 978
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKMMLS----HEGVLQEIRSILVDFEEASGKKIYEHDSM---------STMHFRSLGSAISKIlRE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 979 SDKElvtnlmnqIQELRISIGEKSETIATLKQELQDinckynasladkeeSKELIRRQEVDILElketlrlRILSE-DIE 1057
Cdd:pfam15921 229 LDTE--------ISYLKGRIFPVEDQLEALKSESQN--------------KIELLLQQHQDRIE-------QLISEhEVE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1058 RDMLCEDLAHATEQLNMLTEAskkhsglLQSAQEELTRKEAL----IQELQHKLNQEKEEVEQKKNEFSLKMRQLEHVMG 1133
Cdd:pfam15921 280 ITGLTEKASSARSQANSIQSQ-------LEIIQEQARNQNSMymrqLSDLESTVSQLRSELREAKRMYEDKIEELEKQLV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1134 SA--------TEYPQSPKTPPHFQAHLAKLLETQEQeiedgRASKTSLQHLVTKLNEDREVKNA---EILRMKDQLCEME 1202
Cdd:pfam15921 353 LAnseltearTERDQFSQESGNLDDQLQKLLADLHK-----REKELSLEKEQNKRLWDRDTGNSitiDHLRRELDDRNME 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1203 NLRLES---QQLREKNWLLQRQLDDVKRQQESGDQSHPDSQQLKNEHEEIikerlakNKLIEEMLKMKTNLE-------E 1272
Cdd:pfam15921 428 VQRLEAllkAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEML-------RKVVEELTAKKMTLEssertvsD 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1273 VQSALHSKEKACHRMSEEIERTRTLESRAFQEKEQLRSK---LEEMYEERERTFLEMEMLKKQLEFLAEENGKLVGHQNL 1349
Cdd:pfam15921 501 LTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ 580
|
570 580 590
....*....|....*....|....*....|....*.
gi 39930325 1350 HQKIQYVVRLKKENIRLTEETEKLRAENL-FLKEKK 1384
Cdd:pfam15921 581 HGRTAGAMQVEKAQLEKEINDRRLELQEFkILKDKK 616
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
875-1387 |
3.39e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 875 KFEIDQLSKNL-QNCKQENETLK--SDLHNLVELFEAEKERNNKLSLQFEEDKENSSKEILKVLETVRQEKQKEMAKcEK 951
Cdd:TIGR04523 123 EVELNKLEKQKkENKKNIDKFLTeiKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL-EL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 952 QMAKIQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQDINCKYNASLADKEESKE 1031
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1032 LIRRQEVDILELKETLrlrilsedierdmlcEDLAHATEQ--LNMLTEASKKHSGLLQSAQEELTRKEALIQELQHKLNQ 1109
Cdd:TIGR04523 282 KIKELEKQLNQLKSEI---------------SDLNNQKEQdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1110 EKEEVEQKKNEFSLKMRQLEHVmgsateypqspktpphfQAHLAKLLETQEQEIEDGRASKTSLQHLVTKLNEDREVKNA 1189
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEK-----------------QNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQ 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1190 EILRMKDQLCEMENLRLESQQLREKNWLLQRQLDDVKRQQESGDQSHPDSQQLKNEHEEIIKERLAKNKlieemlKMKTN 1269
Cdd:TIGR04523 410 KDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSIN------KIKQN 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1270 LEEVQSALHSKEKACHRMSEEIERTRTLESRAFQEKEQLRSKLEEMYEERERTFLEMEMLKKQLEFLAEENGKlvghqnl 1349
Cdd:TIGR04523 484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK------- 556
|
490 500 510
....*....|....*....|....*....|....*...
gi 39930325 1350 hqkiqyvVRLKKENIRLTEETEKLRAENLFLKEKKKEF 1387
Cdd:TIGR04523 557 -------ENLEKEIDEKNKEIEELKQTQKSLKKKQEEK 587
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
829-1307 |
4.52e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.83 E-value: 4.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 829 EKELSQLSERHVQVQLqLDNARLENEKLLESQaclQDSYDNLQEVMKFEIDQLSKNLQNCKQENETLKSDLHNLVELFEA 908
Cdd:pfam12128 247 QQEFNTLESAELRLSH-LHFGYKSDETLIASR---QEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 909 EKERNNKLSLQFEEDKENSSKEILKVLETVRQEKQKEMAKCEKQMAKIQKLEESLLATENVISSLEKSRESDKElvTNLM 988
Cdd:pfam12128 323 ELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIK--DKLA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 989 NQIQELRISIGEKSETIATLKQELQDINCKYNASLadKEESKELIRRQEvdilelkeTLRLRILSEDIERDMLcEDLAHA 1068
Cdd:pfam12128 401 KIREARDRQLAVAEDDLQALESELREQLEAGKLEF--NEEEYRLKSRLG--------ELKLRLNQATATPELL-LQLENF 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1069 TEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQHKLNQEKEEVEQKKNEFSLKMRQLEHVMGSATEYPQspKTPPHF 1148
Cdd:pfam12128 470 DERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLR--KEAPDW 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1149 QAHLAK------LLETQEQEIEDGRASKTSLQHLVTKLNEDReVKNAEILRMKDQLCE--------MENLRLESQQLREK 1214
Cdd:pfam12128 548 EQSIGKvispelLHRTDLDPEVWDGSVGGELNLYGVKLDLKR-IDVPEWAASEEELRErldkaeeaLQSAREKQAAAEEQ 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1215 NWLLQRQLDDVKRQQESG----DQSHPDSQQLKNEHEEiikERLAKNKLIEEMLKMK----TNLEEVQSALHSKEKAchr 1286
Cdd:pfam12128 627 LVQANGELEKASREETFArtalKNARLDLRRLFDEKQS---EKDKKNKALAERKDSAnerlNSLEAQLKQLDKKHQA--- 700
|
490 500
....*....|....*....|.
gi 39930325 1287 MSEEIERTRTLESRAFQEKEQ 1307
Cdd:pfam12128 701 WLEEQKEQKREARTEKQAYWQ 721
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
960-1137 |
5.16e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 960 EESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQDInckyNASLADKEEskELIRRQEvd 1039
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----QAEIAEAEA--EIEERRE-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1040 ilELKETLR-----------LRIL--SEDIerdmlcEDLAHATEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQHK 1106
Cdd:COG3883 87 --ELGERARalyrsggsvsyLDVLlgSESF------SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE 158
|
170 180 190
....*....|....*....|....*....|.
gi 39930325 1107 LNQEKEEVEQKKNEFSLKMRQLEHVMGSATE 1137
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
708-928 |
7.11e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 708 SEQALEAVSEELRTVQEQLSVLQVKLDEEERKNLKLQQNVDKLEhhsTQMQELfsseRSDWTKQQQEHVTQLSDLEKQLQ 787
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ---AEIDKL----QAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 788 DAQTKNEFLKcevhDLRIVLNSADKELSLVKLEY-STFKENHEKELSQLSerhvQVQLQLDNARLENEKLLESQACLQDS 866
Cdd:COG3883 94 ALYRSGGSVS----YLDVLLGSESFSDFLDRLSAlSKIADADADLLEELK----ADKAELEAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39930325 867 YDNLQEVMKFEIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKLSLQFEEDKENSS 928
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
708-967 |
7.66e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 7.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 708 SEQALEAVSEELRTVQEQLSVLQVKLDEEERKNLKLQQNVDKLEhhstqmqelfssersdwtkqqqehvTQLSDLEKQLQ 787
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALE-------------------------RRIAALARRIR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 788 DAQTKneflkcevhdlrivLNSADKELSLVKLEYSTFKENHEKELSQLSERHVQVQLqldNARLENEKLLESQACLQDSY 867
Cdd:COG4942 73 ALEQE--------------LAALEAELAELEKEIAELRAELEAQKEELAELLRALYR---LGRQPPLALLLSPEDFLDAV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 868 DNLQ------EVMKFEIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKLslqfeEDKENSSKEILKVLETVRQE 941
Cdd:COG4942 136 RRLQylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL-----EALKAERQKLLARLEKELAE 210
|
250 260
....*....|....*....|....*.
gi 39930325 942 KQKEMAKCEKQMAKIQKLEESLLATE 967
Cdd:COG4942 211 LAAELAELQQEAEELEALIARLEAEA 236
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
545-860 |
8.05e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 545 ARLEKAfAEVSSTETNDKGLQGFSPKALkesSFFTNTEKLKAQLLQIQTELNNSKQEYEEF-KELTRKKQLELESELQSL 623
Cdd:PRK11281 43 AQLDAL-NKQKLLEAEDKLVQQDLEQTL---ALLDKIDRQKEETEQLKQQLAQAPAKLRQAqAELEALKDDNDEETRETL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 624 QKANL-NLENLLEATkvckrqeVSQLNKLHAETLkiittptkayQLCSRLVP-KSSPE-VGSfgfLCTESSSRLD--NDI 698
Cdd:PRK11281 119 STLSLrQLESRLAQT-------LDQLQNAQNDLA----------EYNSQLVSlQTQPErAQA---ALYANSQRLQqiRNL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 699 LN------EPVPPEM-----SEQA-LEAVSEELRTVQEQLSVLQVkLDEEERKNLKLQQNVdkLEHHSTQMQELFSSERs 766
Cdd:PRK11281 179 LKggkvggKALRPSQrvllqAEQAlLNAQNDLQRKSLEGNTQLQD-LLQKQRDYLTARIQR--LEHQLQLLQEAINSKR- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 767 dwTKQQQEHVTQLSDLEKqLQDAQTkNEFLKCEvhdlrivlNSADKELS--LVKleySTfkenheKELSQLSERHVQVQL 844
Cdd:PRK11281 255 --LTLSEKTVQEAQSQDE-AARIQA-NPLVAQE--------LEINLQLSqrLLK---AT------EKLNTLTQQNLRVKN 313
|
330
....*....|....*.
gi 39930325 845 QLDNArLENEKLLESQ 860
Cdd:PRK11281 314 WLDRL-TQSERNIKEQ 328
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
767-1103 |
8.46e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.06 E-value: 8.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 767 DWTKQQQEHVTQLSDLEKQLQDAQTKNEFLKCEVHDLRIVLNSADKELSLVKLEYstfkENHEKELSQLSERHVQVQLQL 846
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTAL----KNARLDLRRLFDEKQSEKDKK 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 847 DNARLENEKLLESQAclqDSYDNLQEVMKFEIDQLSKNLQNCKQENETLKsdlhnLVELFEAEKERNNKLSL--QFEEDK 924
Cdd:pfam12128 670 NKALAERKDSANERL---NSLEAQLKQLDKKHQAWLEEQKEQKREARTEK-----QAYWQVVEGALDAQLALlkAAIAAR 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 925 ENSSKEILKVLETVRQEKQKEMAKCEKQMAKIQKLEESLLAT-ENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSE 1003
Cdd:pfam12128 742 RSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKiERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIER 821
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1004 TIATLKQELQDINCKYNASLADKEESKELIRRQEVDILELKETLRLRILS-EDIERDMLCEDLAH-ATEQLNMLTEASKK 1081
Cdd:pfam12128 822 AISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKlATLKEDANSEQAQGsIGERLAQLEDLKLK 901
|
330 340
....*....|....*....|..
gi 39930325 1082 HSGLLQSAQEELTRKEALIQEL 1103
Cdd:pfam12128 902 RDYLSESVKKYVEHFKNVIADH 923
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1005-1326 |
9.47e-04 |
|
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: 9.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1005 IATLKQELQDINckynASLADKEESKELIRRQEVDILELKETLR--LRILSEDIERDMLCEDLAHATEQLNMLTEASKKh 1082
Cdd:COG4913 612 LAALEAELAELE----EELAEAEERLEALEAELDALQERREALQrlAEYSWDEIDVASAEREIAELEAELERLDASSDD- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1083 sglLQSAQEELTRKEALIQELQHKLNQEKEEVEQKKNEFSLKMRQLEHVMGSATEYPQSPKTPPHFQahlakLLETQEQE 1162
Cdd:COG4913 687 ---LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-----LEERFAAA 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1163 IEDGRASKtslqhLVTKLNEDREVKNAEIlrmkdqlcemenlrlesQQLREKnwlLQRQLDDVKRQQESGDQSHPDS--- 1239
Cdd:COG4913 759 LGDAVERE-----LRENLEERIDALRARL-----------------NRAEEE---LERAMRAFNREWPAETADLDADles 813
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1240 --------QQLKN----EHEEIIKERLAKNklieemlkMKTNLEEVQSALhskEKACHRMSEEIER-TRTLESRAFQEKE 1306
Cdd:COG4913 814 lpeylallDRLEEdglpEYEERFKELLNEN--------SIEFVADLLSKL---RRAIREIKERIDPlNDSLKRIPFGPGR 882
|
330 340
....*....|....*....|
gi 39930325 1307 QLRSKLEEMYEERERTFLEM 1326
Cdd:COG4913 883 YLRLEARPRPDPEVREFRQE 902
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
807-1214 |
1.22e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 807 LNSADKELSLVKLEYSTFKENhEKELSQLSERHVQVQLQLDNARLENEKLlESQACLQDSYDNLQEVmKFEIDQLSKNLQ 886
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAEL-QEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEAL-EAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 887 NCKQENETLKSDLHNLVELFEAEKERNNKLSLQFEED---KENSSKEILKVLETVRQEKQKEMAKCEKQMAKIQKLEESL 963
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 964 LATENVISSLEKSRESDKE----LVTNLMNQIQELRISIGEKSETIATLKQ--------ELQDINCKYNASLADKEESKE 1031
Cdd:COG4717 230 EQLENELEAAALEERLKEArlllLIAAALLALLGLGGSLLSLILTIAGVLFlvlgllalLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1032 LIRRQEVDILELKETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEEltRKEALIQ--------EL 1103
Cdd:COG4717 310 LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ--EIAALLAeagvedeeEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1104 QHKLNQeKEEVEQKKNEFSLKMRQLEHVMGSATEYPQSPKtpphfqahlaklLETQEQEIEDGRASKTSLQHLVTKLNED 1183
Cdd:COG4717 388 RAALEQ-AEEYQELKEELEELEEQLEELLGELEELLEALD------------EEELEEELEELEEELEELEEELEELREE 454
|
410 420 430
....*....|....*....|....*....|.
gi 39930325 1184 REVKNAEILRMKDQLcEMENLRLESQQLREK 1214
Cdd:COG4717 455 LAELEAELEQLEEDG-ELAELLQELEELKAE 484
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
710-1071 |
1.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 710 QALEAVSEELRTVQEQLSVLQVKLDEEERKNLKLQQNVDKLEHHSTQMQELFSSERSDWTKQQQEHVTQLSDLEKQLQDA 789
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 790 QTKNEFLKCEVHDLRIVLNSADKELSlvKLEYSTFKENHEKELSQLSER------------------------------- 838
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELE--QLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflv 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 839 ---HVQVQLQLDNARLENEKLLESQACLQDSYDNLQEVMKFEIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNK 915
Cdd:COG4717 283 lglLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 916 LSLQFEEdkenssKEILKVLETVRQEKQKEMAKCEKQMAKIQKLEESLLATENVISSLEKSRESDKELVT--NLMNQIQE 993
Cdd:COG4717 363 LQLEELE------QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEE 436
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39930325 994 LRISIGEKSETIATLKQELQDInckyNASLADKEESKELiRRQEVDILELKEtlRLRILSEDIERDMLCEDLAHATEQ 1071
Cdd:COG4717 437 LEEELEELEEELEELREELAEL----EAELEQLEEDGEL-AELLQELEELKA--ELRELAEEWAALKLALELLEEARE 507
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
420-1157 |
1.41e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.42 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 420 EAMLFFKKSEQEKKSLIEKITQLEDLT-LKKEKFIQSNKMIVKF-REDQIMRLERLHKEGRGSFLPEE---QDRLLSELR 494
Cdd:TIGR00618 153 EFAQFLKAKSKEKKELLMNLFPLDQYTqLALMEFAKKKSLHGKAeLLTLRSQLLTLCTPCMPDTYHERkqvLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 495 DEVQTLREhvehhpRLAKYAMENHSLREENRRLKLLAPVKRAHEIDAQSIARLEKAFAEVSstetndkglqgFSPKALKE 574
Cdd:TIGR00618 233 EALQQTQQ------SHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN-----------RARKAAPL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 575 SSFFTNTEKLKAQLLQIQTELNNSKQEYEEF---KELTRKKQLELESELQSLQKANLNLENLLEATKVCKR------QEV 645
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLlmkRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSireiscQQH 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 646 SQLNKLHAETlKIITTPTKAYQLCSRLVPKSSPEVGSFGFLCTESS------SRLDNDILNEPVPPEMSEQALEAVSEEL 719
Cdd:TIGR00618 376 TLTQHIHTLQ-QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRdlqgqlAHAKKQQELQQRYAELCAAAITCTAQCE 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 720 RTVQEQLSVLQVKLDEEERKnLKLQQNVDKLEHHSTQMQElfssersdwtKQQQEHVTQLSDLEKQLQDAQTKNEFLKCE 799
Cdd:TIGR00618 455 KLEKIHLQESAQSLKEREQQ-LQTKEQIHLQETRKKAVVL----------ARLLELQEEPCPLCGSCIHPNPARQDIDNP 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 800 VHDLRIVLNSADKELSLVKLEystfkENHEKELSQLSERHVQVQLQLDNARLENEKLLESQACLQDSYDNLQEVMKFEID 879
Cdd:TIGR00618 524 GPLTRRMQRGEQTYAQLETSE-----EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQD 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 880 QLSKNLQNCKQENETLKSDLHNLVElfEAEKERNNKLSLQFEEDKENSSKEILKVLETVRQEKQKEMAKCEKQMAKiqKL 959
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHALLRKLQP--EQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPK--EL 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 960 EESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQDINCKYNASLADKEESKELIRRQEVD 1039
Cdd:TIGR00618 675 LASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQART 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1040 ILELKETLRLRILSE---DIERDMLCEDLAHATEQLNMLTEASKKHSGLLQSAQEELTRKEALIQELQ-HKLNQEKEEVE 1115
Cdd:TIGR00618 755 VLKARTEAHFNNNEEvtaALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQcETLVQEEEQFL 834
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 39930325 1116 QKKNEFSLKMRQLEHVMGSATEYPQSPKTPPHFQAHLAKLLE 1157
Cdd:TIGR00618 835 SRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSD 876
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
702-884 |
1.48e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.12 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 702 PVPPEMSEQALEavseelrtvQEqlsVLQV--KLDEEERKnlkLQQNVDKLEHHSTQMQELfssersdwTKQQQEHVTQL 779
Cdd:PRK10929 97 SVPPNMSTDALE---------QE---ILQVssQLLEKSRQ---AQQEQDRAREISDSLSQL--------PQQQTEARRQL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 780 SDLEKQLQD--------AQTKNEFLKCEVHDLRIVLNsadkELSLVKLEystfkENHEKELSQL-----SERHVQVQLQL 846
Cdd:PRK10929 154 NEIERRLQTlgtpntplAQAQLTALQAESAALKALVD----ELELAQLS-----ANNRQELARLrselaKKRSQQLDAYL 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 39930325 847 DNAR--------LENEKLLESQACLQDSYDNLQEVMkfeIDQLSKN 884
Cdd:PRK10929 225 QALRnqlnsqrqREAERALESTELLAEQSGDLPKSI---VAQFKIN 267
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
719-945 |
2.04e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-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: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 719 LRTVQEQLSVLQVKLDEEERKNLKLQQNVDKLEHH---STQMQELFSSERSDWTKQQ--QEHVTQLSDLEKQLqDAQTKN 793
Cdd:pfam15905 96 LQALEEELEKVEAKLNAAVREKTSLSASVASLEKQlleLTRVNELLKAKFSEDGTQKkmSSLSMELMKLRNKL-EAKMKE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 794 EFLKCEvhDLRIVLNSADKELslvkleystfkENHEKELSQLSERHVQVQLQLDNARLENEKLLESQACLQDSYDNLqEV 873
Cdd:pfam15905 175 VMAKQE--GMEGKLQVTQKNL-----------EHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQV-EK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 874 MKFEIDQLSKNLQNCKQENETLKSDLH-NLVELFEAEKERNNKLSL----------QFEEDKENSSKEILKVLETVRQEK 942
Cdd:pfam15905 241 YKLDIAQLEELLKEKNDEIESLKQSLEeKEQELSKQIKDLNEKCKLlesekeellrEYEEKEQTLNAELEELKEKLTLEE 320
|
...
gi 39930325 943 QKE 945
Cdd:pfam15905 321 QEH 323
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
27-304 |
2.31e-03 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 42.42 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 27 IKVFVRIRPA-----------EEGARSADGEQSFCLSVLSQTTLRLHSnpdpktFVFDYVAGMDTTQESVFStVAKSIVE 95
Cdd:COG5059 307 TRVICTISPSsnsfeetintlKFASRAKSIKNKIQVNSSSDSSREIEE------IKFDLSEDRSEIEILVFR-EQSQLSQ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 96 SCMSGyngtIFAYGQTGSGKTFTMMGPSDSDNFShnlrgIIPRSFEYLFSLIDREKEKagagKSFlCKCSFIEvyneQIY 175
Cdd:COG5059 380 SSLSG----IFAYMQSLKKETETLKSRIDLIMKS-----IISGTFERKKLLKEEGWKY----KST-LQFLRIE----IDR 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 176 DLLDSASVGLYLREHIKKGVFVVGAVEQAVTSAAET---YQVLSRGWRNRRVASTSMNRESSRSHAVFT-ITIESMEKSS 251
Cdd:COG5059 442 LLLLREEELSKKKTKIHKLNKLRHDLSSLLSSIPEEtsdRVESEKASKLRSSASTKLNLRSSRSHSKFRdHLNGSNSSTK 521
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 39930325 252 ETvnirtsLLNLVDLAGSERqKDTHAEGMRLKEAGNINRSLSCLGQVITALVD 304
Cdd:COG5059 522 EL------SLNQVDLAGSER-KVSQSVGELLRETQSLNKSLSSLGDVIHALGS 567
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1010-1376 |
2.90e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1010 QELQDINCKYNASLADKEESKELIRRQEVDILELKETLRLriLSEDIERDMLCEDLAHATEQLNMLTEASKKhsglLQSA 1089
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEKLLQLLPLYQELEALEAELAELPERLEE----LEER 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1090 QEELTRKEALIQELQHKLNQEKEEVEQKKNEFSLKMRQleHVMGSATEYPQSPKTpphfQAHLAKLLETQEQEIEDGRAS 1169
Cdd:COG4717 155 LEELRELEEELEELEAELAELQEELEELLEQLSLATEE--ELQDLAEELEELQQR----LAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1170 KTSLQHLVTKLNEDREVKNAEILRM-----------KDQLCEMENLRLESQQLR------EKNWLLQRQLDDVKRQQESG 1232
Cdd:COG4717 229 LEQLENELEAAALEERLKEARLLLLiaaallallglGGSLLSLILTIAGVLFLVlgllalLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1233 DQSHPDSQQLKNEHEEIIKERLAKNKLIEEMLKMKTNLEEVQSALHSKEKACHRM---SEEIERTRTLESRAFQEKEQLR 1309
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELqleELEQEIAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39930325 1310 SKLEEmYEERERTFLEMEMLKKQLEFLAEENGKLVGHQNLHQKIQYVVRLKKENIRLTEETEKLRAE 1376
Cdd:COG4717 389 AALEQ-AEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREE 454
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
425-983 |
3.23e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 425 FKKSEQEKKSLIEKITQLEDLTLKKEK------------------------FIQSNKMIVKFREDQIMRLERLHKEGRGS 480
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEELIKEKEKeleevlreineisselpelreeleKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 481 FLPEEQD-----RLLSELRDEVQTLREHVEHHPRLAKYAMENHSLREE-NRRLKLLAPVKRAHEIDAQSIARLEKAFAEV 554
Cdd:PRK03918 254 KRKLEEKireleERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFyEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 555 SSTETNDKGLQGFSPKALKESSFFTNTEKLKAQLLQIQTELNNSKqeyeefKELTRKKQLELESELQSLQKANLNLENLL 634
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLK------KRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 635 EATkvckRQEVSQLNKLHAETLKIITTPTKAYQLCSrlVPKSSPEVGSFGFLCTESSSRLdNDILNEPVPPEMSEQALEA 714
Cdd:PRK03918 408 SKI----TARIGELKKEIKELKKAIEELKKAKGKCP--VCGRELTEEHRKELLEEYTAEL-KRIEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 715 VSEELRTV---QEQLSVLQVKLDEEERKNLKLQQ-NVDKLEHHSTQMQELfsSERSDWTKQQQEHVtqLSDLEKqLQDAQ 790
Cdd:PRK03918 481 ELRELEKVlkkESELIKLKELAEQLKELEEKLKKyNLEELEKKAEEYEKL--KEKLIKLKGEIKSL--KKELEK-LEELK 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 791 TKNEFLKCEVHDLRIVLNSADKELSlvKLEYSTFKENhEKELSQLSERHVQVqLQLDNARLENEKLLESQACLQDsydnl 870
Cdd:PRK03918 556 KKLAELEKKLDELEEELAELLKELE--ELGFESVEEL-EERLKELEPFYNEY-LELKDAEKELEREEKELKKLEE----- 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 871 qevmkfEIDQLSKNLQNCKQENETLKSDLHNLVELFEAEKERNNKLSLQFEEDKENSSKEILKVLETVRQEKQKEMAKCE 950
Cdd:PRK03918 627 ------ELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
570 580 590
....*....|....*....|....*....|...
gi 39930325 951 KQMAKIQKLEESLLATENVISSLEKSRESDKEL 983
Cdd:PRK03918 701 EELEEREKAKKELEKLEKALERVEELREKVKKY 733
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
934-1329 |
3.66e-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: 3.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 934 VLETVRQEKQKEMAKCekqmakIQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRISIGEKSETIATLKQELQ 1013
Cdd:pfam07888 31 LLQNRLEECLQERAEL------LQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1014 DINC-------KYNASLADKEESKELIRRQEVDIlelkETLRLRILSEDIERDMLCEDLAHATEQLNMLTEASKKHSGLL 1086
Cdd:pfam07888 105 ELSAsseelseEKDALLAQRAAHEARIRELEEDI----KTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1087 QSAQEELTRKEALIQELQHKLNQEKEEVEQKKNEFSlkmrQLEHVMGSAteypqspktpphfQAHLAKLlETQEQEIEDG 1166
Cdd:pfam07888 181 QQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTIT----TLTQKLTTA-------------HRKEAEN-EALLEELRSL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1167 RASKTSLQHLVTKLNEDRevknAEILRMKDQ-LCEMENLRLESQQLreknwllQRQLDDVKRQQESGDQSHPDSQQLKNE 1245
Cdd:pfam07888 243 QERLNASERKVEGLGEEL----SSMAAQRDRtQAELHQARLQAAQL-------TLQLADASLALREGRARWAQERETLQQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1246 HEEIIKERLAKnkLIEEMLKMKTNLEEVQSalhSKEKACHRMSEEIERTRTLESRAFQEKEQLRSKLEEMYEERERTFLE 1325
Cdd:pfam07888 312 SAEADKDRIEK--LSAELQRLEERLQEERM---EREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAE 386
|
....
gi 39930325 1326 MEML 1329
Cdd:pfam07888 387 KQEL 390
|
|
| MPS2 |
pfam17060 |
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component ... |
1129-1278 |
3.74e-03 |
|
Monopolar spindle protein 2; Is a fungal transmembrane protein which is part of the component of the spindle pole body (SPB) required for the insertion of the nascent SPB into the nuclear envelope and for the proper execution of spindle pole body (SPB) duplication. It seems that Mps2-Spc24 interaction may contribute to the localization of Spc24 and other kinetochore components to the inner plaque of the SPB.
Pssm-ID: 407228 [Multi-domain] Cd Length: 340 Bit Score: 41.11 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1129 EHVMGSATEYPQSPKTPphFQAHLAKLLETQEQEIEDGRASK--TSLQHLVTKLNEDREVKNaEILRMKDQlcEMENLRL 1206
Cdd:pfam17060 108 EDVKSSPRSEADSLGTP--IKVDLLRNLKPQESPETPRRINRkyKSLELRVESMKDELEFKD-ETIMEKDR--ELTELTS 182
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39930325 1207 ESQQLREKNWLLQRQLDDVKRQQESGdqsHPDSQQLKNEHEEIIKErlAKNKLIEEML---KMKTNLEEVQSALH 1278
Cdd:pfam17060 183 TISKLKDKYDFLSREFEFYKQHHEHG---GNNSIKTATKHEFIISE--LKRKLQEQNRlirILQEQIQFDPGALH 252
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
709-891 |
5.10e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 709 EQALEAVSEELRTVQEQLSVLQVKLDEEERknlKLQQNVDKLEHHstQMQELFSSERSDWtkqqQEHVTQLSDLEKQLQD 788
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEA---ELDALQERREAL--QRLAEYSWDEIDV----ASAEREIAELEAELER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 789 AQTKN---EFLKCEVHDLRIVLNSADKELSLVKLEYSTfkenHEKELSQLSERHVQVQLQLDNARLENEKLLES------ 859
Cdd:COG4913 680 LDASSddlAALEEQLEELEAELEELEEELDELKGEIGR----LEKELEQAEEELDELQDRLEAAEDLARLELRAlleerf 755
|
170 180 190
....*....|....*....|....*....|...
gi 39930325 860 -QACLQDSYDNLQEVMKFEIDQLSKNLQNCKQE 891
Cdd:COG4913 756 aAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
612-1012 |
5.28e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 41.20 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 612 KQLELESELQSLQKANLNLENLlEATKVCKRQEVSQLNKLHAETL------KIITTPTKAYQLCSRLVPKSSPEVgsfgf 685
Cdd:pfam13166 94 IQEKIAKLKKEIKDHEEKLDAA-EANLQKLDKEKEKLEADFLDECwkkikrKKNSALSEALNGFKYEANFKSRLL----- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 686 lcTESSSRLDNDilNEPVPPEMSEQALEAVSEELRTVQEQLSVLQVKLDEEERKNLKLQQNVDKlehhSTQMQELFSS-E 764
Cdd:pfam13166 168 --REIEKDNFNA--GVLLSDEDRKAALATVFSDNKPEIAPLTFNVIDFDALEKAEILIQKVIGK----SSAIEELIKNpD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 765 RSDWTKQQQEHVTQLSDlekqlqdaqtKNEFLKCEVHDLRIVLNSA--DKElslVKLEYSTFKENHEKELSQLSERHVQV 842
Cdd:pfam13166 240 LADWVEQGLELHKAHLD----------TCPFCGQPLPAERKAALEAhfDDE---FTEFQNRLQKLIEKVESAISSLLAQL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 843 QLQLDNARL-----ENEKLLESQA-CLQDSYDNLQEVMKFEIDQLSKNLQNCKQENETLKsdLHNLVELFEAEKERNNKL 916
Cdd:pfam13166 307 PAVSDLASLlsafeLDVEDIESEAeVLNSQLDGLRRALEAKRKDPFKSIELDSVDAKIES--INDLVASINELIAKHNEI 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 917 SLQFEEDKENSSKEilkvLETVRQEKQKEMakcekqmakIQKLEESLLATENVISSLEKSRESDKELVTNLMNQIQELRI 996
Cdd:pfam13166 385 TDNFEEEKNKAKKK----LRLHLVEEFKSE---------IDEYKDKYAGLEKAINSLEKEIKNLEAEIKKLREEIKELEA 451
|
410
....*....|....*.
gi 39930325 997 SIGEKSETIATLKQEL 1012
Cdd:pfam13166 452 QLRDHKPGADEINKLL 467
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
746-1338 |
5.33e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 746 NVDKLEHHSTQMQELFSSERSDwtkqqqehVTQLSDLEKQLQDAQTKNEFLKCEVHDLRIVLNSADKELSLVKLEYstfk 825
Cdd:PRK01156 160 EINSLERNYDKLKDVIDMLRAE--------ISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEY---- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 826 ENHEKELSQLSERHVQVQLQLDNARLENEKLLESQACLQDSYDNL-------QEVMKFEIDQLSKNlQNCKQENETLKSD 898
Cdd:PRK01156 228 NNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNnyykeleERHMKIINDPVYKN-RNYINDYFKYKND 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 899 LHNLVELFEAEKERNNKLslqfeedKENSSKeiLKVLETVRQE---KQKEMAKCEKQMAKIQKLEESLLATENVISSLEK 975
Cdd:PRK01156 307 IENKKQILSNIDAEINKY-------HAIIKK--LSVLQKDYNDyikKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKK 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 976 SRESDKELVTNLMNQIQELrisIGEKSETIATLKQELQDINCK---YNASLADKEESKELIRRQEVDILELKETLRLRIL 1052
Cdd:PRK01156 378 KIEEYSKNIERMSAFISEI---LKIQEIDPDAIKKELNEINVKlqdISSKVSSLNQRIRALRENLDELSRNMEMLNGQSV 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1053 SEDIERDMLCEDLAHATEQLNmlteaskkhsgllqsaqEELTRKEALIQELQHKLNQEKEE-VEQKKNEFSLKMRQLEHv 1131
Cdd:PRK01156 455 CPVCGTTLGEEKSNHIINHYN-----------------EKKSRLEEKIREIEIEVKDIDEKiVDLKKRKEYLESEEINK- 516
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1132 mgSATEYpqspktpphfqahlaKLLETQEQEIEDGRASKTSLQHLVTKLNEDREVKNA---EILRMKDQ-----LCEMEN 1203
Cdd:PRK01156 517 --SINEY---------------NKIESARADLEDIKIKINELKDKHDKYEEIKNRYKSlklEDLDSKRTswlnaLAVISL 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1204 LRLESQQLREKNwlLQRQLDDV-KRQQESGDQSHPDSQQLKNEHEEIIKERLAKNKLIEEMLKMKTNLEEVQSALHSKEK 1282
Cdd:PRK01156 580 IDIETNRSRSNE--IKKQLNDLeSRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKK 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1283 ACHRMSEEIERTRTLESRAFQEKEQLR---------------------------SKLEEMYEERERTFLEMEMLKKQLEF 1335
Cdd:PRK01156 658 QIAEIDSIIPDLKEITSRINDIEDNLKksrkalddakanrarlestieilrtriNELSDRINDINETLESMKKIKKAIGD 737
|
...
gi 39930325 1336 LAE 1338
Cdd:PRK01156 738 LKR 740
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1083-1321 |
5.33e-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: 40.90 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1083 SGLLQSAQEELTRKEALIQELQHKLNQEKEEVEQKKNEFSLKMRQLEHVMGSAteypqspktpphfqAHLAKLLETQEQE 1162
Cdd:COG4942 12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI--------------AALARRIRALEQE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1163 IEDGRASKTSLQHLVTKLNEDREVKNAEILRMKDQLCEMenlrleSQQLREKNWLLQRQLDDVKRQQESGDQSHPDSQQ- 1241
Cdd:COG4942 78 LAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL------GRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39930325 1242 ---LKNEHEEIIKERLAKNKLIEEMLKMKTNLEEVQSALHSKEKACHRMSEEIERTRTLESRAFQEKEQLRSKLEEMYEE 1318
Cdd:COG4942 152 aeeLRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
...
gi 39930325 1319 RER 1321
Cdd:COG4942 232 LEA 234
|
|
| |
