|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
8-310 |
2.05e-105 |
|
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: 340.08 E-value: 2.05e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 8 SIQVCIKVRPCEPGLT-----SLWQVkEGRSIQLADSHAEPYVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGTIFAY 82
Cdd:cd01374 1 KITVTVRVRPLNSREIgineqVAWEI-DNDTIYLVEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 83 GQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISSETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHE-SGNGIVNVNC 161
Cdd:cd01374 80 GQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDdVEKGVYVAGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 162 KESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIFRIIIESRKSDHSDNDTVKQSVLSLVDLAGSEQVDPADHAS 241
Cdd:cd01374 160 TEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTVRVSTLNLIDLAGSERAAQTGAAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 242 -----------SLMIFRNLVKSLSESVDSKPNSFRDSKLPRIMLPSLGGNVLTSIICTITP--SFVEESSSTISFGTCAK 308
Cdd:cd01374 240 vrrkegshinkSLLTLGTVISKLSEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPaeSHVEETLNTLKFASRAK 319
|
..
gi 78706884 309 KI 310
Cdd:cd01374 320 KI 321
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
44-310 |
1.30e-90 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 297.95 E-value: 1.30e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 44 YVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISSETERD-F 122
Cdd:pfam00225 42 FTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSeF 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 123 LLRVGYIEIYNEKIYDLLNKKNQD---LKIHESGNGIVNV-NCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSH 198
Cdd:pfam00225 122 SVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKKGVYVkGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSH 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 199 AIFRIIIESRKSDHSDNDTVKQSVLSLVDLAGSEQVDPADHAS------------SLMIFRNLVKSLSESVDSK-PnsFR 265
Cdd:pfam00225 202 AIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSERASKTGAAGgqrlkeaaninkSLSALGNVISALADKKSKHiP--YR 279
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 78706884 266 DSKLPRIMLPSLGGNVLTSIICTITPS--FVEESSSTISFGTCAKKI 310
Cdd:pfam00225 280 DSKLTRLLQDSLGGNSKTLMIANISPSssNYEETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
8-316 |
2.96e-90 |
|
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: 297.18 E-value: 2.96e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 8 SIQVCIKVRP-----CEPGLTSLWQV--KEGRSIQLADSHAEP----YVFDYVFDEGASNQEVFDRMAKHIVHACMQGSN 76
Cdd:smart00129 1 NIRVVVRVRPlnkreKSRKSPSVVPFpdKVGKTLTVRSPKNRQgekkFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 77 GTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISS-ETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNG 155
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKrEEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIREDEKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 156 IVNV-NCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIFRIIIESRKSDhSDNDTVKQSVLSLVDLAGSEQV 234
Cdd:smart00129 161 GVYVkGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN-SSSGSGKASKLNLVDLAGSERA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 235 DPADHAS-----------SLMIFRNLVKSLSESVDSKPNSFRDSKLPRIMLPSLGGNVLTSIICTITPS--FVEESSSTI 301
Cdd:smart00129 240 KKTGAEGdrlkeagninkSLSALGNVINALAQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSssNLEETLSTL 319
|
330
....*....|....*
gi 78706884 302 SFGTCAKKIRCKPQV 316
Cdd:smart00129 320 RFASRAKEIKNKPIV 334
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
8-308 |
3.16e-84 |
|
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: 279.53 E-value: 3.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 8 SIQVCIKVRP----CEPGLTSLWQVKEGRSIQL---ADSHAEP--YVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGT 78
Cdd:cd00106 1 NVRVAVRVRPlngrEARSAKSVISVDGGKSVVLdppKNRVAPPktFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 79 IFAYGQTSSGKTYTMMGDEQN-PGVMVLAAKEIFQQISS--ETERDFLLRVGYIEIYNEKIYDLLNKKNQ-DLKIHESGN 154
Cdd:cd00106 81 IFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERIDKrkETKSSFSVSASYLEIYNEKIYDLLSPVPKkPLSLREDPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 155 -GIVNVNCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIFRIIIESRKSDhSDNDTVKQSVLSLVDLAGSEQ 233
Cdd:cd00106 161 rGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNRE-KSGESVTSSKLNLVDLAGSER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 234 VDPADHAS-----------SLMIFRNLVKSLsesVDSKPN--SFRDSKLPRIMLPSLGGNVLTSIICTITPS--FVEESS 298
Cdd:cd00106 240 AKKTGAEGdrlkeggninkSLSALGKVISAL---ADGQNKhiPYRDSKLTRLLQDSLGGNSKTIMIACISPSseNFEETL 316
|
330
....*....|
gi 78706884 299 STISFGTCAK 308
Cdd:cd00106 317 STLRFASRAK 326
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
7-310 |
2.15e-73 |
|
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: 248.40 E-value: 2.15e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 7 SSIQVCIKVRPcEPGLT------SLWQVKEGRSIQLADSHAE-PYVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGTI 79
Cdd:cd01369 2 CNIKVVCRFRP-LNELEvlqgskSIVKFDPEDTVVIATSETGkTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 80 FAYGQTSSGKTYTMMG---DEQNPGVMVLAAKEIFQQISSETERD-FLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNG 155
Cdd:cd01369 81 FAYGQTSSGKTYTMEGklgDPESMGIIPRIVQDIFETIYSMDENLeFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 156 IVNV-NCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIFRIIIESRksdHSDNDTVKQSVLSLVDLAGSEQV 234
Cdd:cd01369 161 GPYVkGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE---NVETEKKKSGKLYLVDLAGSEKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 235 DPA-------DHA----SSLMIFRNLVKSLSesvDSKPNS--FRDSKLPRIMLPSLGGNVLTSIICTITPSFVEESS--S 299
Cdd:cd01369 238 SKTgaegavlDEAkkinKSLSALGNVINALT---DGKKTHipYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESEtlS 314
|
330
....*....|.
gi 78706884 300 TISFGTCAKKI 310
Cdd:cd01369 315 TLRFGQRAKTI 325
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
44-310 |
1.25e-65 |
|
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: 226.84 E-value: 1.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 44 YVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISS-ETERDF 122
Cdd:cd01370 63 YVFDRVFDETSTQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESlKDEKEF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 123 LLRVGYIEIYNEKIYDLLNKKNQDLKIHE-SGNGIVNVNCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIF 201
Cdd:cd01370 143 EVSMSYLEIYNETIRDLLNPSSGPLELREdAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 202 RIIIESRKSDHSDNDTVKQSVLSLVDLAGSEQ-----------VDPADHASSLMIFRNLVKSLSESvDSKPN--SFRDSK 268
Cdd:cd01370 223 QITVRQQDKTASINQQVRQGKLSLIDLAGSERasatnnrgqrlKEGANINRSLLALGNCINALADP-GKKNKhiPYRDSK 301
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 78706884 269 LPRIMLPSLGGNVLTSIICTITPS--FVEESSSTISFGTCAKKI 310
Cdd:cd01370 302 LTRLLKDSLGGNCRTVMIANISPSssSYEETHNTLKYANRAKNI 345
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
7-311 |
5.59e-65 |
|
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: 224.90 E-value: 5.59e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 7 SSIQVCIKVRP------CEPGLTSLWQVKEGRSIQLADSHAepYVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGTIF 80
Cdd:cd01372 1 SSVRVAVRVRPllpkeiIEGCRICVSFVPGEPQVTVGTDKS--FTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 81 AYGQTSSGKTYTMMG------DEQNPGVMVLAAKEIFQQIS-SETERDFLLRVGYIEIYNEKIYDLLN---KKNQDLKIH 150
Cdd:cd01372 79 AYGQTGSGKTYTMGTaytaeeDEEQVGIIPRAIQHIFKKIEkKKDTFEFQLKVSFLEIYNEEIRDLLDpetDKKPTISIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 151 ESGNG-IVNVNCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIFRIIIESRK---SDHSDNDTVKQSV---- 222
Cdd:cd01372 159 EDSKGgITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKkngPIAPMSADDKNSTftsk 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 223 LSLVDLAGSEQV-------DPADHA----SSLMIFRNLVKSL-SESVDSKPNSFRDSKLPRIMLPSLGGNVLTSIICTIT 290
Cdd:cd01372 239 FHFVDLAGSERLkrtgatgDRLKEGisinSGLLALGNVISALgDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVS 318
|
330 340
....*....|....*....|...
gi 78706884 291 PS--FVEESSSTISFGTCAKKIR 311
Cdd:cd01372 319 PAdsNFEETLNTLKYANRARNIK 341
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
9-319 |
5.22e-62 |
|
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: 215.92 E-value: 5.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 9 IQVCIKVRPCEPGLT----SLWQVKE--GRSIQLADSHAEPYVF--DYVFDEGASNQEVFdRMAKHIVHACMQGSNGTIF 80
Cdd:cd01366 4 IRVFCRVRPLLPSEEnedtSHITFPDedGQTIELTSIGAKQKEFsfDKVFDPEASQEDVF-EEVSPLVQSALDGYNVCIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 81 AYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISSETERD--FLLRVGYIEIYNEKIYDLLNK---KNQDLKI-HESGN 154
Cdd:cd01366 83 AYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGwsYTIKASMLEIYNETIRDLLAPgnaPQKKLEIrHDSEK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 155 GIVNV-NCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIFRIIIESRksdHSDNDTVKQSVLSLVDLAGSEQ 233
Cdd:cd01366 163 GDTTVtNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGR---NLQTGEISVGKLNLVDLAGSER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 234 VDPADHASS-LMIFRNLVKSLSESVD-----SKPNS---FRDSKLPRIMLPSLGGNVLTSIICTITP--SFVEESSSTIS 302
Cdd:cd01366 240 LNKSGATGDrLKETQAINKSLSALGDvisalRQKQShipYRNSKLTYLLQDSLGGNSKTLMFVNISPaeSNLNETLNSLR 319
|
330
....*....|....*..
gi 78706884 303 FgtcAKKIRCkpqvCKI 319
Cdd:cd01366 320 F---ASKVNS----CEL 329
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
7-316 |
8.00e-62 |
|
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: 216.45 E-value: 8.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 7 SSIQVCIKVRP-----CEPGLTSLWQVKEGRSIQLADSHAE-----------PYVFDYVFDE-------GASNQEVFDRM 63
Cdd:cd01365 1 ANVKVAVRVRPfnsreKERNSKCIVQMSGKETTLKNPKQADknnkatrevpkSFSFDYSYWShdsedpnYASQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 64 AKHIVHACMQGSNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQI--SSETERDFLLRVGYIEIYNEKIYDLLN 141
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIadTTNQNMSYSVEVSYMEIYNEKVRDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 142 KKN----QDLKIHES-GNGIVNVNCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIFRIIIESRKSD-HSDN 215
Cdd:cd01365 161 PKPkknkGNLKVREHpVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDaETNL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 216 DTVKQSVLSLVDLAGSEQVDPAdHAS------------SLMIFRNLVKSLSES---VDSKPNSF---RDSKLPRIMLPSL 277
Cdd:cd01365 241 TTEKVSKISLVDLAGSERASST-GATgdrlkeganinkSLTTLGKVISALADMssgKSKKKSSFipyRDSVLTWLLKENL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 78706884 278 GGNVLTSIICTITPSFV--EESSSTISFGTCAKKIRCKPQV 316
Cdd:cd01365 320 GGNSKTAMIAAISPADInyEETLSTLRYADRAKKIVNRAVV 360
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
8-310 |
1.32e-60 |
|
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: 211.94 E-value: 1.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 8 SIQVCIKVRPC-----EPGLTSLWQVKEGR-SIQL----ADSHAEP--YVFDYVFDEGASNQEVFDRMAKHIVHACMQGS 75
Cdd:cd01371 2 NVKVVVRCRPLngkekAAGALQIVDVDEKRgQVSVrnpkATANEPPktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 76 NGTIFAYGQTSSGKTYTMMG---DEQNPGVMVLAAKEIFQQISSETE-RDFLLRVGYIEIYNEKIYDLLNK-KNQDLKIH 150
Cdd:cd01371 82 NGTIFAYGQTGTGKTYTMEGkreDPELRGIIPNSFAHIFGHIARSQNnQQFLVRVSYLEIYNEEIRDLLGKdQTKRLELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 151 ES-GNGIVNVNCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIFRIIIESRKSDHSDNDTVKQSVLSLVDLA 229
Cdd:cd01371 162 ERpDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 230 GSEQVDPADHAS-----------SLMIFRNLVKSLsesVDSKPN--SFRDSKLPRIMLPSLGGNVLTSIICTITP--SFV 294
Cdd:cd01371 242 GSERQSKTGATGerlkeatkinlSLSALGNVISAL---VDGKSThiPYRDSKLTRLLQDSLGGNSKTVMCANIGPadYNY 318
|
330
....*....|....*.
gi 78706884 295 EESSSTISFGTCAKKI 310
Cdd:cd01371 319 DETLSTLRYANRAKNI 334
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
9-316 |
2.14e-60 |
|
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: 211.98 E-value: 2.14e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 9 IQVCIKVRPCEPGLTSLWQVK--EGRSIQLADSHAEP---YVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGTIFAYG 83
Cdd:cd01373 3 VKVFVRIRPPAEREGDGEYGQclKKLSSDTLVLHSKPpktFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAYG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 84 QTSSGKTYTMMG----DEQNPGVMVLAAKEIFQQISSETERD---------FLLRVGYIEIYNEKIYDLLNKKNQDLKIH 150
Cdd:cd01373 83 QTGSGKTYTMWGpsesDNESPHGLRGVIPRIFEYLFSLIQREkekagegksFLCKCSFLEIYNEQIYDLLDPASRNLKLR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 151 ES-GNGIVNVNCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIFRIIIESrKSDHSDNDTVKQSVLSLVDLA 229
Cdd:cd01373 163 EDiKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES-WEKKACFVNIRTSRLNLVDLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 230 GSEQVDPaDHAS------------SLMIFRNLVKSLSESVDSKPN--SFRDSKLPRIMLPSLGGNVLTSIICTITPSF-- 293
Cdd:cd01373 242 GSERQKD-THAEgvrlkeagninkSLSCLGHVINALVDVAHGKQRhvCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSkc 320
|
330 340
....*....|....*....|...
gi 78706884 294 VEESSSTISFGTCAKKIRCKPQV 316
Cdd:cd01373 321 FGETLSTLRFAQRAKLIKNKAVV 343
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
44-316 |
1.07e-57 |
|
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: 204.10 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 44 YVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGTIFAYGQTSSGKTYTMMGD---------EQNP--GVMVLAAKEIFQ 112
Cdd:cd01364 51 YTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwELDPlaGIIPRTLHQLFE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 113 QISSeTERDFLLRVGYIEIYNEKIYDLL---NKKNQDLKIHES---GNGIVNVNCKESIVTSEDDLLRQLYMGNKERVVG 186
Cdd:cd01364 131 KLED-NGTEYSVKVSYLEIYNEELFDLLspsSDVSERLRMFDDprnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 187 ETNMNERSSRSHAIFRIIIESRKSDHSDNDTVKQSVLSLVDLAGSEQV-------DPADHA----SSLMIFRNLVKSLSE 255
Cdd:cd01364 210 ATLMNAQSSRSHSVFSITIHIKETTIDGEELVKIGKLNLVDLAGSENIgrsgavdKRAREAgninQSLLTLGRVITALVE 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78706884 256 SVDSKPnsFRDSKLPRIMLPSLGGNVLTSIICTITPSFV--EESSSTISFGTCAKKIRCKPQV 316
Cdd:cd01364 290 RAPHVP--YRESKLTRLLQDSLGGRTKTSIIATISPASVnlEETLSTLEYAHRAKNIKNKPEV 350
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
44-294 |
2.56e-52 |
|
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: 187.89 E-value: 2.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 44 YVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGTIFAYGQTSSGKTYTMMGD----EQNPGVMVLAAKEIFQQISSETE 119
Cdd:cd01367 52 FRFDYVFDESSSNETVYRSTVKPLVPHIFEGGKATCFAYGQTGSGKTYTMGGDfsgqEESKGIYALAARDVFRLLNKLPY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 120 RDFL-LRVGYIEIYNEKIYDLLNKKnQDLKIHESGNGIVNV-NCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRS 197
Cdd:cd01367 132 KDNLgVTVSFFEIYGGKVFDLLNRK-KRVRLREDGKGEVQVvGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRS 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 198 HAIFRIIIESRKSDHSdndtvkQSVLSLVDLAGSE------------QVDPADHASSLMIFRNLVKSLSEsvDSKPNSFR 265
Cdd:cd01367 211 HAILQIILRDRGTNKL------HGKLSFVDLAGSErgadtssadrqtRMEGAEINKSLLALKECIRALGQ--NKAHIPFR 282
|
250 260 270
....*....|....*....|....*....|
gi 78706884 266 DSKLPRIMLPSL-GGNVLTSIICTITPSFV 294
Cdd:cd01367 283 GSKLTQVLKDSFiGENSKTCMIATISPGAS 312
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
9-303 |
5.38e-51 |
|
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: 183.47 E-value: 5.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 9 IQVCIKVRPCEPGL-----TSLWQVKEGRSIQLAD--SHAEP--YVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGTI 79
Cdd:cd01376 2 VRVAVRVRPFVDGTagasdPSCVSGIDSCSVELADprNHGETlkYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNATV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 80 FAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFqQISSETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNG---I 156
Cdd:cd01376 82 FAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-QMTRKEAWALSFTMSYLEIYQEKILDLLEPASKELVIREDKDGnilI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 157 VNVNCKEsiVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIFRIIIESRKSdhSDNDTVKQSVLSLVDLAGSEQ--- 233
Cdd:cd01376 161 PGLSSKP--IKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRER--LAPFRQRTGKLNLIDLAGSEDnrr 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 234 --------VDPADHASSLMIFRNLVKSLSESVDSKPnsFRDSKLPRIMLPSLGGNVLTSIICTITP--SFVEESSSTISF 303
Cdd:cd01376 237 tgnegirlKESGAINSSLFVLSKVVNALNKNLPRIP--YRDSKLTRLLQDSLGGGSRCIMVANIAPerTFYQDTLSTLNF 314
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
44-317 |
1.38e-48 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 183.79 E-value: 1.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 44 YVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQIS-SETERDF 122
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEdLSMTKDF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 123 LLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNGIVNV-NCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIF 201
Cdd:COG5059 138 AVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVaGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 202 RIIIESRKsdhSDNDTVKQSVLSLVDLAGSEQVDPADHAS-----------SLMIFRNLVKSLSESVDSKPNSFRDSKLP 270
Cdd:COG5059 218 QIELASKN---KVSGTSETSKLSLVDLAGSERAARTGNRGtrlkegasinkSLLTLGNVINALGDKKKSGHIPYRESKLT 294
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 78706884 271 RIMLPSLGGNVLTSIICTITPSF--VEESSSTISFGTCAKKIRCKPQVC 317
Cdd:COG5059 295 RLLQDSLGGNCNTRVICTISPSSnsFEETINTLKFASRAKSIKNKIQVN 343
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
44-308 |
1.88e-45 |
|
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: 168.34 E-value: 1.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 44 YVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISseterDFL 123
Cdd:cd01368 57 FSFSKVFGPNTTQKEFFQGTALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIG-----GYS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 124 LRVGYIEIYNEKIYDLL-------NKKNQDLKIHESGNGIVNV-NCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSS 195
Cdd:cd01368 132 VFVSYIEIYNEYIYDLLepspsspTKKRQSLRLREDHNGNMYVaGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESS 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 196 RSHAIFRIII-----ESRKSDHSDNDTVKQSVLSLVDLAGSEQV-------DPADHAS----SLMIFRNLVKSLSESVDS 259
Cdd:cd01368 212 RSHSVFTIKLvqapgDSDGDVDQDKDQITVSQLSLVDLAGSERTsrtqntgERLKEAGnintSLMTLGTCIEVLRENQLQ 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 78706884 260 KPNS---FRDSKLPRIMLPSLGGNVLTSIICTITPSFV--EESSSTISFGTCAK 308
Cdd:cd01368 292 GTNKmvpFRDSKLTHLFQNYFDGEGKASMIVNVNPCASdyDETLHVMKFSAIAQ 345
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
8-303 |
4.21e-45 |
|
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: 166.99 E-value: 4.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 8 SIQVCIKVRPCEPGLTSLwqVKEGRSIQLADSHAE---------------PYVFDYVFDEgASNQEVFDRMAKHIVHACM 72
Cdd:cd01375 1 KVQAFVRVRPTDDFAHEM--IKYGEDGKSISIHLKkdlrrgvvnnqqedwSFKFDGVLHN-ASQELVYETVAKDVVSSAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 73 QGSNGTIFAYGQTSSGKTYTMMGDEQN---PGVMVLAAKEIFQQISSETERDFLLRVGYIEIYNEKIYDLLNKKNQDLK- 148
Cdd:cd01375 78 AGYNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLSTLPYVGPs 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 149 ------IHESGNGIVNVNCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIFRIIIESRKSDHSDnDTVKQSV 222
Cdd:cd01375 158 vtpmtiLEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLSS-EKYITSK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 223 LSLVDLAGSEQVDPADHAS-----------SLMIFRNLVKSLSESvDSKPNSFRDSKLPRIMLPSLGGNVLTSIICTIT- 290
Cdd:cd01375 237 LNLVDLAGSERLSKTGVEGqvlkeatyinkSLSFLEQAIIALSDK-DRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIYg 315
|
330
....*....|....
gi 78706884 291 -PSFVEESSSTISF 303
Cdd:cd01375 316 eAAQLEETLSTLRF 329
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
7-316 |
8.42e-31 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 133.14 E-value: 8.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 7 SSIQVCIKVRPCEPGLTSLWQVKEGRSIQLADShAEPYVFDYVFDEGASNQEVFDRMAKHIVHACMQGSNGTIFAYGQTS 86
Cdd:PLN03188 98 SGVKVIVRMKPLNKGEEGEMIVQKMSNDSLTIN-GQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 87 SGKTYTMMG------------DEQnpGVMVLAAKEIFQQISSE----TER--DFLLRVGYIEIYNEKIYDLLNKKNQDLK 148
Cdd:PLN03188 177 SGKTYTMWGpanglleehlsgDQQ--GLTPRVFERLFARINEEqikhADRqlKYQCRCSFLEIYNEQITDLLDPSQKNLQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 149 IHESGNGIVNV-NCKESIVTSEDDLLRQLYMGNKERVVGETNMNERSSRSHAIFRIIIESRKSDHSDN-DTVKQSVLSLV 226
Cdd:PLN03188 255 IREDVKSGVYVeNLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGlSSFKTSRINLV 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 227 DLAGSEQVDPADHAS-----------SLMIFRNLVKSLSE-SVDSKPN--SFRDSKLPRIMLPSLGGNVLTSIICTITP- 291
Cdd:PLN03188 335 DLAGSERQKLTGAAGdrlkeagninrSLSQLGNLINILAEiSQTGKQRhiPYRDSRLTFLLQESLGGNAKLAMVCAISPs 414
|
330 340
....*....|....*....|....*.
gi 78706884 292 -SFVEESSSTISFGTCAKKIRCKPQV 316
Cdd:PLN03188 415 qSCKSETFSTLRFAQRAKAIKNKAVV 440
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1110-1875 |
4.94e-19 |
|
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: 94.35 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1110 TEYERRIEQLEESLQRAQEELSILEKRktdenkslqleyMAKIETSENENRSKFRAycldLKETQKRYEEQLQQTNEKLA 1189
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAE------------LQELEEKLEELRLEVSE----LEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1190 SVTTQcqvhldviKRSLQEKITQAEKERNELAVRhKAELEKIRETLKEKESSYKEKLRQAEEERDKEISRLEVMRNTIAE 1269
Cdd:TIGR02168 299 RLEQQ--------KQILRERLANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1270 LHKTNSDREVELEGVKMEKCQLKKLYDKSMLELEQLQctadqkssdllpgssnENIDDLQKKCDQYVQDLELLRGEKAEl 1349
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE----------------ARLERLEDRRERLQQEIEELLKKLEE- 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1350 lSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELERCEIAEKLETFKSKEADikeaLHCAQLRLHAYDKLVCEYE----- 1424
Cdd:TIGR02168 433 -AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE----LAQLQARLDSLERLQENLEgfseg 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1425 ------------RLKGCLSDSNKLSENLQKKVERLHAEqlALQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLENS 1492
Cdd:TIGR02168 508 vkallknqsglsGILGVLSELISVDEGYEAAIEAALGG--RLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1493 LKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQE---VRDHLESRNEELKRKL---------------------KD 1548
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGgvlVVDDLDNALELAKKLRpgyrivtldgdlvrpggvitgGS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1549 AQELQNMVDKERKLnSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDF---LKERET 1625
Cdd:TIGR02168 666 AKTNSSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarlEAEVEQ 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1626 LNLTISDLRLHNEQLLETSKNYLSDITAANNLNLEMKKNLHDLTKECKSLRSDLQSKEEYF---QTQKQLLDETISNLKE 1702
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALdelRAELTLLNEEAANLRE 824
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1703 ENRKMEEKLSsgnkALKEDCEKLRSTLESKELILQQNKQELEERLTVINEKNGKNALLDAQLKSNETAFTSLRKAWIKQS 1782
Cdd:TIGR02168 825 RLESLERRIA----ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1783 LAIEAANKRSLEMEQKVDKRTREYEELRSTLKTREINFRSEKERMDGTISSLLEDKRNLEEKlctVTELLAKLKRELPAL 1862
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENK---IEDDEEEARRRLKRL 977
|
810
....*....|...
gi 78706884 1863 HTQKVNGGDVSIE 1875
Cdd:TIGR02168 978 ENKIKELGPVNLA 990
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
929-1671 |
6.28e-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: 87.42 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 929 LVKEEDRMRDIIFQLKQEVDGKKNLIEEEKEVINNLRAQITSLNqietiKNQNAKTKILCEELQTKDTVQTANKQESQEV 1008
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELE-----EEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1009 LTLKTSLAHLKSKVCELQKKLEKQSEDEKisELQSDIGEISECCLSMELKLadivnwqaEELRPLDQLQESGVELQHHST 1088
Cdd:TIGR02168 312 ANLERQLEELEAQLEELESKLDELAEELA--ELEEKLEELKEELESLEAEL--------EELEAELEELESRLEELEEQL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1089 TAEESLNVEKPIQEQTERTLTTEYERRIEQLEESLQRAQEELSILEKRKTDENKSLQLEYMAKIETSENENRSKFRAYCL 1168
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEE 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1169 DLKETQKRYEE---QLQQTNEKLASVttqcQVHLDVIKRSLQEKITQAEKERNELAvrHKAELEKIRETLKEK---ESSY 1242
Cdd:TIGR02168 462 ALEELREELEEaeqALDAAERELAQL----QARLDSLERLQENLEGFSEGVKALLK--NQSGLSGILGVLSELisvDEGY 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1243 KEKLRQAEEER--DKEISRLEVMRNTIAELHKTNSDR----------EVELEGVKMEKCQLKKLYDKSMLELEQLQCTAD 1310
Cdd:TIGR02168 536 EAAIEAALGGRlqAVVVENLNAAKKAIAFLKQNELGRvtflpldsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLR 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1311 QKSSDLLPGS----SNENIDDLQKKCDQY----VQDLELLRGEKAELLSEIQKING--QHSNTIKKLEEIEAEMITLTTQ 1380
Cdd:TIGR02168 616 KALSYLLGGVlvvdDLDNALELAKKLRPGyrivTLDGDLVRPGGVITGGSAKTNSSilERRREIEELEEKIEELEEKIAE 695
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1381 KELERCEIAEKLETFKSKEADIKEALHCAQLRLHAYDKlvcEYERLKgclsdsnKLSENLQKKVERLHAEQLALQEGISG 1460
Cdd:TIGR02168 696 LEKALAELRKELEELEEELEQLRKELEELSRQISALRK---DLARLE-------AEVEQLEERIAQLSKELTELEAEIEE 765
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1461 RDSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSAQEGQFKqkiaDIKGSVDELQIKLKSLQEVRDHLESRNE 1540
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT----LLNEEAANLRERLESLERRIAATERRLE 841
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1541 ELKRKLKDAQELQNMVDKERklnSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLeaqtNDFL 1620
Cdd:TIGR02168 842 DLEEQIEELSEDIESLAAEI---EELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR----SELR 914
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 78706884 1621 KERETLNLTISDLRLHNEQLLETSKNYLSDITAANNLNLEMKKNLHDLTKE 1671
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1110-1614 |
8.01e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 83.57 E-value: 8.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1110 TEYERRIEQLEESLQRAQEelsiLEKRKTDENKSLqleymAKIETSENENRSKFRAYCLDLKETQKRYEEqLQQTNEKLA 1189
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTEN----IEELIKEKEKEL-----EEVLREINEISSELPELREELEKLEKEVKE-LEELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1190 SVTTQcQVHLDVIKRSLQEKITQAEKERNELAVRHKaELEKIRETLKEKE---------SSYKEKLRQAEEERDKEISRL 1260
Cdd:PRK03918 242 ELEKE-LESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELKELKekaeeyiklSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1261 EVMRNTIAELHKTNSDREVELEGVKMEKCQLKK----------LYDKSMLELEQLQcTADQKSSDLLPGSSNENIDDLQK 1330
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKELEKrleeleerheLYEEAKAKKEELE-RLKKRLTGLTPEKLEKELEELEK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1331 KCDQYVQDLELLRGEKAEL----------LSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELERceIAEKLETFKSKEA 1400
Cdd:PRK03918 399 AKEEIEEEISKITARIGELkkeikelkkaIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKR--IEKELKEIEEKER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1401 DIKEALHCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENK 1480
Cdd:PRK03918 477 KLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1481 TVREakvgLENSLKAVQENMSAQEGQ---------------------FKQKIADIKGSVDELQIKLKSLQEVRDHLESRN 1539
Cdd:PRK03918 557 KLAE----LEKKLDELEEELAELLKEleelgfesveeleerlkelepFYNEYLELKDAEKELEREEKELKKLEEELDKAF 632
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78706884 1540 EELKRKLKDAQELQNMVDKERKLNSslREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEA 1614
Cdd:PRK03918 633 EELAETEKRLEELRKELEELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
967-1743 |
1.83e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.88 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 967 QITSLNQIETIKNQNAKTKILCEELQTKDTVQTANKQESQEVLTLKTSLAHLKSKVCELQKKLEKQSEDE-KISElqsdi 1045
Cdd:PTZ00121 1225 KAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEaKKAE----- 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1046 geisecclsmELKLADIVNWQAEELRPLDQLQESGVELQHHSTTAEESLNVEKPIQEQTERtlttEYERRIEQLEESLQR 1125
Cdd:PTZ00121 1300 ----------EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA----EAEAAADEAEAAEEK 1365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1126 AQ--EELSILEKRKTDENKSLQLEYMAKIETSENENRSKFRAYCLDLKETQKRYEEQLQQTNEKlasvttqcqvhldviK 1203
Cdd:PTZ00121 1366 AEaaEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE---------------K 1430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1204 RSLQEKITQAEKERNELAVRHKAELEKIRETLKEKessyKEKLRQAEEERDK-EISRLEVMRNTIAELHKTNSDREVELE 1282
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK----AEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAA 1506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1283 GVKMEKCQLKKLYDKSmlELEQLQCTADQKSSDLLPGSSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKINGQHSN 1362
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAK--KADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE 1584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1363 TIKKLEEIEAEMITLTTQKELE-RCEIAEKLETFKSKEADIKEAlhcaqlrlhayDKLVCEYERLKGCLSDSNKLSENLQ 1441
Cdd:PTZ00121 1585 EAKKAEEARIEEVMKLYEEEKKmKAEEAKKAEEAKIKAEELKKA-----------EEEKKKVEQLKKKEAEEKKKAEELK 1653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1442 KKVE--RLHAEQLALQEgisgrdSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQEnMSAQEGQFKQKIADIKGSVD 1519
Cdd:PTZ00121 1654 KAEEenKIKAAEEAKKA------EEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKKKAEELKKAEE 1726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1520 ELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRakKVEIDRRSKelg 1599
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKR--RMEVDKKIK--- 1801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1600 EVTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHNEQLLETSKNYLSDITAANNLNLEMKKNLHDLTKECKSLRSDL 1679
Cdd:PTZ00121 1802 DIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDE 1881
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706884 1680 QSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKALKEDCEKlRSTLESKELILQQNKQEL 1743
Cdd:PTZ00121 1882 EEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIK-RDAEETREEIIKISKKDM 1944
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
45-232 |
2.02e-15 |
|
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: 75.84 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 45 VFDYVFDEGASNQEVFdRMAKHIVHACMQGSNG-TIFAYGQTSSGKTYTMMGdeqnpgvmvlaakeIFQQIsseterdfl 123
Cdd:cd01363 21 VFYRGFRRSESQPHVF-AIADPAYQSMLDGYNNqSIFAYGESGAGKTETMKG--------------VIPYL--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 124 lrvgyIEIYNEKIYDLLNKKNQdlkihesgngivnvNCKESIVTSEDDLLRQLYMGNKERvVGETNMNERSSRSHAIFRI 203
Cdd:cd01363 77 -----ASVAFNGINKGETEGWV--------------YLTEITVTLEDQILQANPILEAFG-NAKTTRNENSSRFGKFIEI 136
|
170 180
....*....|....*....|....*....
gi 78706884 204 iiesrksdhsdndtvkqsvlsLVDLAGSE 232
Cdd:cd01363 137 ---------------------LLDIAGFE 144
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
998-1706 |
2.15e-14 |
|
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: 79.34 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 998 QTANKQESQEVLTLKTS-----LAHLKSKVCELQKKLEKQSEDEKIsELQSDIGEIsecclsmELKLADIVNWQAEELRP 1072
Cdd:TIGR02169 245 QLASLEEELEKLTEEISelekrLEEIEQLLEELNKKIKDLGEEEQL-RVKEKIGEL-------EAEIASLERSIAEKERE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1073 LDQLQESGVELQ-HHSTTAEESLNVEKPIQEQTER--TLTTEYERRIEQLEESLQRAQEElSILEKRKTDENKSLQLEYM 1149
Cdd:TIGR02169 317 LEDAEERLAKLEaEIDKLLAEIEELEREIEEERKRrdKLTEEYAELKEELEDLRAELEEV-DKEFAETRDELKDYREKLE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1150 AKIETSENENRSKFRaycldLKETQKRYEEQLQQTNEKLASVTTQcQVHLDVIKRSLQEKITQAEKERNELA-------- 1221
Cdd:TIGR02169 396 KLKREINELKRELDR-----LQEELQRLSEELADLNAAIAGIEAK-INELEEEKEDKALEIKKQEWKLEQLAadlskyeq 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1222 --VRHKAELEKIRETLKEKESSY--KEKLRQAEEERDKEISRLEVMRN--------TIAELHKTNSDRE----------- 1278
Cdd:TIGR02169 470 elYDLKEEYDRVEKELSKLQRELaeAEAQARASEERVRGGRAVEEVLKasiqgvhgTVAQLGSVGERYAtaievaagnrl 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1279 ----VELEGVKMEKCQL---KKLYDKSMLELEQLQctadQKSSDLLPGSSNENID---DLQKKCDQY------------- 1335
Cdd:TIGR02169 550 nnvvVEDDAVAKEAIELlkrRKAGRATFLPLNKMR----DERRDLSILSEDGVIGfavDLVEFDPKYepafkyvfgdtlv 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1336 VQDLELLRgekaELLSEIQ--KING---QHSNTIKKLEEIEAEMITLTTQKELERCEIAEKLETFKSKEADIKEALHCAQ 1410
Cdd:TIGR02169 626 VEDIEAAR----RLMGKYRmvTLEGelfEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIE 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1411 LRLHAydklvceyerLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLE 1490
Cdd:TIGR02169 702 NRLDE----------LSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1491 NSLKAVQEnmsaQEGQFKQKIADIKgsVDELQIKLKSLQEVRDHLESRNEELKRKLKD--------AQELQNMVDKERKL 1562
Cdd:TIGR02169 772 EDLHKLEE----ALNDLEARLSHSR--IPEIQAELSKLEEEVSRIEARLREIEQKLNRltlekeylEKEIQELQEQRIDL 845
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1563 N---SSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNdflkERETLNLTISDLRLHNEQ 1639
Cdd:TIGR02169 846 KeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELER----KIEELEAQIEKKRKRLSE 921
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1640 LLETSKNYLSDITAANNLNLEMKK------NLHDLTKECKSL------------------------RSDLQSKEEYFQTQ 1689
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEipeeelSLEDVQAELQRVeeeiralepvnmlaiqeyeevlkrLDELKEKRAKLEEE 1001
|
810
....*....|....*..
gi 78706884 1690 KQLLDETISNLKEENRK 1706
Cdd:TIGR02169 1002 RKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1111-1862 |
1.43e-13 |
|
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: 76.65 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1111 EYERRIEQLEESLQRAQ---EELSILEKRKTDENKSLQLEYMAKIETSENENRSKFRAYCLDLKETQKrYEEQLQQTNEK 1187
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEeniERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEA-LERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1188 LASVttqcQVHLDVIKRSLQEK---ITQAEKERNELAVRHKAELEKIRETLKEKESSYK---EKLRQAEEERDKEISRLE 1261
Cdd:TIGR02169 246 LASL----EEELEKLTEEISELekrLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaeiASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1262 V-MRNTIAELHKTNSDREV---ELEGVKMEKCQLKKLYDKSMLELEQLQCTADQKSSDLlpGSSNENIDDLQKKCDQYVQ 1337
Cdd:TIGR02169 322 ErLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF--AETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1338 DLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELERCEIAEKLETFKSKEADikealhcaqlrLHAYD 1417
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAD-----------LSKYE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1418 KlvcEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQE-----------------GISGRDSEIKQLRSELKDAIDENK 1480
Cdd:TIGR02169 469 Q---ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEErvrggraveevlkasiqGVHGTVAQLGSVGERYATAIEVAA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1481 TVREAKVGLENSLKAVQE-----------------NMSAQEGQFKQKIADiKGSVD--------ELQIKLKSLQEVRDHL 1535
Cdd:TIGR02169 546 GNRLNNVVVEDDAVAKEAiellkrrkagratflplNKMRDERRDLSILSE-DGVIGfavdlvefDPKYEPAFKYVFGDTL 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1536 ESRNEELKRKLKDAQELQNM--------------VDKERKLNSSLREDFDKLEQTKLDLEE------QLRAKKVEIDRRS 1595
Cdd:TIGR02169 625 VVEDIEAARRLMGKYRMVTLegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGlkrelsSLQSELRRIENRL 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1596 KELGEVTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHNEQLLETSKNYLSDITAANNLNLEMKKNLHDLTKECKSL 1675
Cdd:TIGR02169 705 DELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1676 -RSDLQSKEEYFQTQKQLLDETISNLKEENRKMEEKLSS-------------GNKALKEDCEKLRSTLESKELILQQNKQ 1741
Cdd:TIGR02169 785 eARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltlekeylekeiqELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1742 ELEERLtvineKNGKNALLDaqlksnetaftsLRKAWIKQSLAIEAANKRSLEMEQKVDKRTREYEELRSTLKTREINFR 1821
Cdd:TIGR02169 865 ELEEEL-----EELEAALRD------------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 78706884 1822 SEKERMDGTISSLLEDKRNLEEKLC--TVTELLAKLKRELPAL 1862
Cdd:TIGR02169 928 ALEEELSEIEDPKGEDEEIPEEELSleDVQAELQRVEEEIRAL 970
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
913-1628 |
1.99e-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: 75.93 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 913 LKCQRFQIVKINQEQNLVKEE--DRMRDIIFQLKQEVDGKKNLIEEEKEVINNLRAQITS----LNQIETIK---NQNAK 983
Cdd:pfam15921 122 MQMERDAMADIRRRESQSQEDlrNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLShegvLQEIRSILvdfEEASG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 984 TKILCEELQTKDTVQTANKQESQEVLTLKTSLAHLKSKVCELQKKLEKQSedekiselqsdigeiSECCLSMELKLadiv 1063
Cdd:pfam15921 202 KKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALK---------------SESQNKIELLL---- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1064 nwQAEELRPLDQLQESGVELQHHSTTAEESLNVEKPIQEQTE------RTLTTEYERRIEQLEESLQRAQEELSilEKRK 1137
Cdd:pfam15921 263 --QQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEiiqeqaRNQNSMYMRQLSDLESTVSQLRSELR--EAKR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1138 TDENKSLQLEYMAKIETSE-NENRS--------------KFRAYCLDLKETQKRYEEQLQQtNEKLASVTTQCQVHLDVI 1202
Cdd:pfam15921 339 MYEDKIEELEKQLVLANSElTEARTerdqfsqesgnlddQLQKLLADLHKREKELSLEKEQ-NKRLWDRDTGNSITIDHL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1203 KRSLQEKIT----------------QAEKERNELAVRHKAE-LEKIRETLKEKESSyKEKLRQAEEERDKEISRLEVMRN 1265
Cdd:pfam15921 418 RRELDDRNMevqrleallkamksecQGQMERQMAAIQGKNEsLEKVSSLTAQLEST-KEMLRKVVEELTAKKMTLESSER 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1266 TIAELHKTNSDREVELEGVKMEKCQLKKLYDKSMLELEQLQCTADQKSsdllpgSSNENIDDLQKKCDQYVQDLELLRGE 1345
Cdd:pfam15921 497 TVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLR------NVQTECEALKLQMAEKDKVIEILRQQ 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1346 kaelLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELERCEIA-------EKLETFKSKEADIK----EALHCAQLRLH 1414
Cdd:pfam15921 571 ----IENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKilkdkkdAKIRELEARVSDLElekvKLVNAGSERLR 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1415 AYDKLVCEYERL----KGCLSDSNKLSE-------NLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVR 1483
Cdd:pfam15921 647 AVKDIKQERDQLlnevKTSRNELNSLSEdyevlkrNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAM 726
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1484 EAKVGLenslkavQENMSAQEGQfkqkiadikgsVDELQIKLKSLQEVRDHLESRNEELK-RKLKDAQELQNMVDKERKL 1562
Cdd:pfam15921 727 KVAMGM-------QKQITAKRGQ-----------IDALQSKIQFLEEAMTNANKEKHFLKeEKNKLSQELSTVATEKNKM 788
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78706884 1563 NSSLredfDKLEQTKLDLEEQLRAKKVEIDRRSKELGEvtkdCENIRSDLEaQTNDFLKERETLNL 1628
Cdd:pfam15921 789 AGEL----EVLRSQERRLKEKVANMEVALDKASLQFAE----CQDIIQRQE-QESVRLKLQHTLDV 845
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1203-1745 |
5.43e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.33 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1203 KRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKESsykeKLRQAEEERD---KEISRLEVMRNTIAELHKTNSDREV 1279
Cdd:PRK03918 177 RIERLEKFIKRTENIEELIKEKEKELEEVLREINEISS----ELPELREELEkleKEVKELEELKEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1280 ELEGVKMEKCQLKKLYDKSMLELEQLQctadqkssdllpgSSNENIDDLQKKCDQYVQdlelLRGEKAELLSEIQKINGQ 1359
Cdd:PRK03918 253 SKRKLEEKIRELEERIEELKKEIEELE-------------EKVKELKELKEKAEEYIK----LSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1360 HSNTIKKLEEIEAEMitlttqKELErcEIAEKLETFKSKEADIKEALHCAQLRLHAYDK---LVCEYERLKGCLSDSNKl 1436
Cdd:PRK03918 316 LSRLEEEINGIEERI------KELE--EKEERLEELKKKLKELEKRLEELEERHELYEEakaKKEELERLKKRLTGLTP- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1437 sENLQKKVERLHAEQLALQEGIS---GRDSEIKQLRSELKDAIDEnktVREAKVGLENSLKAVQENmsaqegqfkqkiaD 1513
Cdd:PRK03918 387 -EKLEKELEELEKAKEEIEEEISkitARIGELKKEIKELKKAIEE---LKKAKGKCPVCGRELTEE-------------H 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1514 IKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKdaqELQNMVDKERKLnSSLREDFDKLEQTKLDLE----EQLRAKKV 1589
Cdd:PRK03918 450 RKELLEEYTAELKRIEKELKEIEEKERKLRKELR---ELEKVLKKESEL-IKLKELAEQLKELEEKLKkynlEELEKKAE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1590 EIDRRSKELGEVTKDCENIRSDLEaQTNDFLKERETLNLTISDLRLHNEQLLETSKNYLSDITAANNLNLEMKKNLHDLT 1669
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEY 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1670 KECKSLRSDLQSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKALK----EDCEKLRSTLESKELILQQNKQELEE 1745
Cdd:PRK03918 605 LELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKkyseEEYEELREEYLELSRELAGLRAELEE 684
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
929-1633 |
1.09e-12 |
|
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: 73.56 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 929 LVKEEDRMRDIIFQLKQEVDGKKNLIEEEKEVINNLRAQITSLNQieTIKNQNAKTKILCEELQTkdTVQTANKQESQEV 1008
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ--LLEELNKKIKDLGEEEQL--RVKEKIGELEAEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1009 LTLKTSLAHLKSKVCELQKKLEKqsEDEKISELQSDIGEISEcclSMELKLADIVNWQAEELRPLDQLQESGVELQH--- 1085
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAK--LEAEIDKLLAEIEELER---EIEEERKRRDKLTEEYAELKEELEDLRAELEEvdk 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1086 -HSTTAEESLNVEKPIQEQTERTltTEYERRIEQLEESLQRAQEELSILE------KRKTDENKSLQLEYMAKIETSENE 1158
Cdd:TIGR02169 379 eFAETRDELKDYREKLEKLKREI--NELKRELDRLQEELQRLSEELADLNaaiagiEAKINELEEEKEDKALEIKKQEWK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1159 ------NRSKFRAYCLDLKETQKRYEEQLQQTNEKLASVTTQCQVHLD-VIKRSLQEKITQAE--------------KER 1217
Cdd:TIGR02169 457 leqlaaDLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEErVRGGRAVEEVLKASiqgvhgtvaqlgsvGER 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1218 NELA-------------VRHKAELEKIRETLKEKESSYKEKL---RQAEEERDKEISRLE-------------------- 1261
Cdd:TIGR02169 537 YATAievaagnrlnnvvVEDDAVAKEAIELLKRRKAGRATFLplnKMRDERRDLSILSEDgvigfavdlvefdpkyepaf 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1262 --------VMRNTIAELHKTNSDREVELEGVKMEKC--------QLKKLYDKSMLELEQLQCTADQKSS-DLLPGSSNEN 1324
Cdd:TIGR02169 617 kyvfgdtlVVEDIEAARRLMGKYRMVTLEGELFEKSgamtggsrAPRGGILFSRSEPAELQRLRERLEGlKRELSSLQSE 696
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1325 IDDLQKKCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELERCEIAEKLETFKSKEADI-- 1402
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLhk 776
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1403 -KEALHC--AQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISgrdsEIKQLRSELKDAIDEN 1479
Cdd:TIGR02169 777 lEEALNDleARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ----ELQEQRIDLKEQIKSI 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1480 KTVREAKVGLENSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQE-LQNMVDK 1558
Cdd:TIGR02169 853 EKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAkLEALEEE 932
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1559 ERKLNSSLREdfDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVT-------KDCENIRSDLEAQTNDFLKERETLNLTIS 1631
Cdd:TIGR02169 933 LSEIEDPKGE--DEEIPEEELSLEDVQAELQRVEEEIRALEPVNmlaiqeyEEVLKRLDELKEKRAKLEEERKAILERIE 1010
|
..
gi 78706884 1632 DL 1633
Cdd:TIGR02169 1011 EY 1012
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
622-1285 |
3.22e-12 |
|
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: 72.01 E-value: 3.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 622 QFDQLRSEIAATRMKLESMLStfshascEVSQKTTDCKRLSEQISTAHDDFGQLQEKYNNLKHKWSSQKLAIDTMQVDYN 701
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEE-------ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 702 TIQQKYLQLQDEYRHLELRSDEQCQQ---LQDENSKLQAEIGTLKERVEeihSELLEVPNPDTHPEDMELQNQELKKRLS 778
Cdd:TIGR02168 306 ILRERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEELKEELE---SLEAELEELEAELEELESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 779 KLQWEFDEIQLNYECLSNELMSTIQECDALREEH-KQRTTNSDLESMKSSGVGTECSDPENELDTDLLQQFTKLSKSIQQ 857
Cdd:TIGR02168 383 TLRSKVAQLELQIASLNNEIERLEARLERLEDRReRLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 858 IELTDYSGGRRLFIYNHAEQDQSVPSLKLCLEPAKYLEGDGKQHDASdSVFLKGFLKCQRFQIV--KINQEQN------- 928
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK-ALLKNQSGLSGILGVLseLISVDEGyeaaiea 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 929 ---------LVKEEDRMRDIIFQLKQEVDGKKNLIE-----------EEKEVINNLRAQITSLNQ--------------- 973
Cdd:TIGR02168 542 alggrlqavVVENLNAAKKAIAFLKQNELGRVTFLPldsikgteiqgNDREILKNIEGFLGVAKDlvkfdpklrkalsyl 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 974 ------IETIKNQNAKTKILCEE---------------LQTKDTVQTANK--QESQEVLTLKTSLAHLKSKVCELQKKLE 1030
Cdd:TIGR02168 622 lggvlvVDDLDNALELAKKLRPGyrivtldgdlvrpggVITGGSAKTNSSilERRREIEELEEKIEELEEKIAELEKALA 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1031 K-----QSEDEKISELQSDIGEISECCLSMELKLADIVNWQAEELRPLDQLQESGVELQHHSTTAEESLNvekpiqeqTE 1105
Cdd:TIGR02168 702 ElrkelEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE--------EA 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1106 RTLTTEYERRIEQLEESLQRAQEELSILEKRKTDENKSLQLEYMAKIETSENENRSKFRAYclDLKETQKRYEEQLQQTN 1185
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA--ATERRLEDLEEQIEELS 851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1186 EKLASVTTQcQVHLDVIKRSLQEKITQAEKER---NELAVRHKAELEKIRETLKEKESSYKEKLRQAEEERDK------E 1256
Cdd:TIGR02168 852 EDIESLAAE-IEELEELIEELESELEALLNERaslEEALALLRSELEELSEELRELESKRSELRRELEELREKlaqlelR 930
|
730 740
....*....|....*....|....*....
gi 78706884 1257 ISRLEVMRNTIAElhKTNSDREVELEGVK 1285
Cdd:TIGR02168 931 LEGLEVRIDNLQE--RLSEEYSLTLEEAE 957
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1116-1843 |
3.68e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.10 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1116 IEQLEESLQRAQEELSILEKRKTDENKSLQLEYMAKIETSENENRSKFRAYC-LDLKETQKRYEEQLQQTNEKLASVTTQ 1194
Cdd:PTZ00121 1026 IEKIEELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKdFDFDAKEDNRADEATEEAFGKAEEAKK 1105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1195 CQVHLDVIKRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKESSYKEKLRQAEEERDKEISRLEVMRNTIAELHKTN 1274
Cdd:PTZ00121 1106 TETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1275 SDREVElegvkmekcQLKKLYDKSMLElEQLQCTADQKSSDLLPGSSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQ 1354
Cdd:PTZ00121 1186 EVRKAE---------ELRKAEDARKAE-AARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIR 1255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1355 KIN-------GQHSNTIKKLEEIEAEMITLTTQK----ELERCEIAEKLETFKSKEADIKEAlhcaqlrlhayDKLVCEY 1423
Cdd:PTZ00121 1256 KFEearmahfARRQAAIKAEEARKADELKKAEEKkkadEAKKAEEKKKADEAKKKAEEAKKA-----------DEAKKKA 1324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1424 ERLKGCLSDSNKLSENLQKKVERLHAEQLALQEgiSGRDSEIKQLRSELKDAiDENKTVREAKVGLENSLKAVQENMSAQ 1503
Cdd:PTZ00121 1325 EEAKKKADAAKKKAEEAKKAAEAAKAEAEAAAD--EAEAAEEKAEAAEKKKE-EAKKKADAAKKKAEEKKKADEAKKKAE 1401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1504 EGQFK----QKIADIKGSVDELQiklKSLQEVRdhlesRNEELKRKL---KDAQELQNMVDKERKLNSSLR--EDFDKLE 1574
Cdd:PTZ00121 1402 EDKKKadelKKAAAAKKKADEAK---KKAEEKK-----KADEAKKKAeeaKKADEAKKKAEEAKKAEEAKKkaEEAKKAD 1473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1575 QTKLDLEE-----QLRAKKVEIDRRSKEL---GEVTKDCENIRSDLEAQTNDFLKEREtlnltisDLRLHNEQLLETSKN 1646
Cdd:PTZ00121 1474 EAKKKAEEakkadEAKKKAEEAKKKADEAkkaAEAKKKADEAKKAEEAKKADEAKKAE-------EAKKADEAKKAEEKK 1546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1647 YLSDITAANNL-NLEMKKNLHDLTKECKSLRSDLQSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKAlKEDCEKL 1725
Cdd:PTZ00121 1547 KADELKKAEELkKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA-KIKAEEL 1625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1726 RSTLESKELILQQNKQELEERLTV--INEKNGKNALLDAQLKSNET----AFTSLRKAWIKQSLAIEAANKRSLE----- 1794
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAeeLKKAEEENKIKAAEEAKKAEedkkKAEEAKKAEEDEKKAAEALKKEAEEakkae 1705
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 78706884 1795 -MEQKVDKRTREYEELRSTLKTREINFRSEKERMDgtissllEDKRNLEE 1843
Cdd:PTZ00121 1706 eLKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE-------EDKKKAEE 1748
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
8-140 |
4.31e-12 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 65.70 E-value: 4.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 8 SIQVCIKVRPCEPGLTSLWQVKEGRSIQLADSHAEPYVFDYVFDEGASNQEVFDRMaKHIVHACMQGSNGTIFAYGQTSS 87
Cdd:pfam16796 21 NIRVFARVRPELLSEAQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIFAYGQTGS 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 78706884 88 GKtytmmgdeqNPGVMVLAAKEIFQQISS-ETERDFLLRVGYIEIYNEKIYDLL 140
Cdd:pfam16796 100 GS---------NDGMIPRAREQIFRFISSlKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
921-1840 |
7.22e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 71.33 E-value: 7.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 921 VKINQEQNLVKEEDRMRdiiFQLKQEVDGKKNLIEEEKEVINNLRAQITS-LNQIETIKNQNAKTKILCEELQTKDTVQT 999
Cdd:PTZ00121 1018 IDFNQNFNIEKIEELTE---YGNNDDVLKEKDIIDEDIDGNHEGKAEAKAhVGQDEGLKPSYKDFDFDAKEDNRADEATE 1094
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1000 ANKQESQEVLTLKTSLAHLKSKVCELQKKLEKQSEDEKISELQsDIGEISECCLSMELKLADIVNwQAEELRPLDQlqes 1079
Cdd:PTZ00121 1095 EAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAE-DARKAEEARKAEDAKRVEIAR-KAEDARKAEE---- 1168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1080 gvelqhhSTTAEESLNVEKpiQEQTERTLTTEYERRIEQLE--ESLQRAQEELSILEKRKTDENKslQLEYMAKIETSEN 1157
Cdd:PTZ00121 1169 -------ARKAEDAKKAEA--ARKAEEVRKAEELRKAEDARkaEAARKAEEERKAEEARKAEDAK--KAEAVKKAEEAKK 1237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1158 ENRSKFRAycldlkeTQKRYEEQLQQTNEKLASVTTQCQVHLDVIKRSLQEKITQAEKERNELAVRHKAELEKIRETLKE 1237
Cdd:PTZ00121 1238 DAEEAKKA-------EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK 1310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1238 KESSYK-EKLRQAEEERDKeisRLEVMRNTIAELHKTN--SDREVELEGVKMEKCQLKKLYDKSMLELEQLQCTADQKSS 1314
Cdd:PTZ00121 1311 AEEAKKaDEAKKKAEEAKK---KADAAKKKAEEAKKAAeaAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKA 1387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1315 DllpgsSNENIDDLQKKCDQYVQDLELLRgeKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELER-CEIAEKLE 1393
Cdd:PTZ00121 1388 E-----EKKKADEAKKKAEEDKKKADELK--KAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKkAEEAKKAE 1460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1394 TFKSKEADIKEAlhcAQLRLHAYDKLVCEyerlkgclsDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELK 1473
Cdd:PTZ00121 1461 EAKKKAEEAKKA---DEAKKKAEEAKKAD---------EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK 1528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1474 DAiDENKTVREAKVGLE----NSLKAVQENMSAQEgqfKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKR----- 1544
Cdd:PTZ00121 1529 KA-EEAKKADEAKKAEEkkkaDELKKAEELKKAEE---KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKlyeee 1604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1545 KLKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDFLKERE 1624
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAE 1684
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1625 tlnltiSDLRLHNEQLLETSKNylsditaaNNLNLEMKKNLHDLTKECKSLRSDLQSKEEYFQTQKQLLDETiSNLKEEN 1704
Cdd:PTZ00121 1685 ------EDEKKAAEALKKEAEE--------AKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED-KKKAEEA 1749
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1705 RKMEEKLSSGNKALKEDCEKLRSTLESKELILQQNKQELEERLTVINEKNGKNALLDAQL-----KSNETAFTSLRKAWI 1779
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANiieggKEGNLVINDSKEMED 1829
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78706884 1780 KQSLAIEAANKRSLEMEQKVDKRTREYEELRSTLKTREINFRSEKERMDGTISSLLEDKRN 1840
Cdd:PTZ00121 1830 SAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEI 1890
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1323-1843 |
8.71e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.48 E-value: 8.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1323 ENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKEL---ERCEIAEKLETFKSKE 1399
Cdd:PRK03918 179 ERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEieeLEKELESLEGSKRKLE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1400 ADIK-------------EALHCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDS--- 1463
Cdd:PRK03918 259 EKIReleerieelkkeiEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkee 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1464 EIKQLRSELKDaIDENKTVREAKVGLENSLKAVQENMSaqegQFKQKIADIkgSVDELQIKLKSLQEVRDHLESRNEELK 1543
Cdd:PRK03918 339 RLEELKKKLKE-LEKRLEELEERHELYEEAKAKKEELE----RLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKIT 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1544 RKLKdaqELQNMVDKERKLNSSLREDFDKL-----EQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTND 1618
Cdd:PRK03918 412 ARIG---ELKKEIKELKKAIEELKKAKGKCpvcgrELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1619 FLKERETLNL-TISDLRLHNEQllETSKNYLSDITAANNLNLEMKKNLHDLTKECKSLRSDLQSKEEyFQTQKQLLDETI 1697
Cdd:PRK03918 489 LKKESELIKLkELAEQLKELEE--KLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE-LKKKLAELEKKL 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1698 SNLKEENRKMEEKLSS-GNKALKEDCEKLRStLES---KELILQQNKQELEERLTVINEKNGKNALLDAQLKSNETAFTS 1773
Cdd:PRK03918 566 DELEEELAELLKELEElGFESVEELEERLKE-LEPfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1774 LRKAwikqslaIEAANKRSLEMEQKvdKRTREYEELRSTLKTREINFRSEKERMDGTISSLLEDKRNLEE 1843
Cdd:PRK03918 645 LRKE-------LEELEKKYSEEEYE--ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
923-1768 |
9.14e-12 |
|
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: 70.77 E-value: 9.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 923 INQEQNLVKEEDRMRDIIFQLKQEVDGKKNLI-----EEEKEVINNLRAQITSLNQIETIKNQNAKTKILCEELQTKDTV 997
Cdd:pfam02463 196 KLQELKLKEQAKKALEYYQLKEKLELEEEYLLyldylKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENK 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 998 QTANKQESQEVLTLKTSLAHLKSKVCELQKKLEKQSEDEKISELQSDIGEISEcclsmelkladivnwqaeelrPLDQLQ 1077
Cdd:pfam02463 276 EEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK---------------------ELKKEK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1078 ESGVELQHHSTTAEESLNVEKPIQEQTERTLTTEYERRiEQLEESLQRAQEELSILEKRKtdENKSLQLEYMAKIETSEN 1157
Cdd:pfam02463 335 EEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLE-EELLAKKKLESERLSSAAKLK--EEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1158 ENRSKFRAYCLDLKETQKRYEEQLQQTNEKLASVTTQCQVHLDV-----IKRSLQEKITQAEKERNELAVRHKAELEKIR 1232
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKqelklLKDELELKKSEDLLKETQLVKLQEQLELLLS 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1233 ETLKEKESSYKEKLRQAEEERDKEISRLEVMRNTIAELHKTNSDREVELEGVKMEKCQLKKLYDKSMLELEQLQCTADQK 1312
Cdd:pfam02463 492 RQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALT 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1313 SSDLLPGSSNENIDDLQK-KCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQK-----ELERC 1386
Cdd:pfam02463 572 ELPLGARKLRLLIPKLKLpLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAkakesGLRKG 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1387 EIAEKLETFKSKEADIKEALHCAQLRLHAYDklvceyERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIK 1466
Cdd:pfam02463 652 VSLEEGLAEKSEVKASLSELTKELLEIQELQ------EKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1467 QLRSELKDAIDENKTVR-EAKVGLENSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRK 1545
Cdd:pfam02463 726 RVQEAQDKINEELKLLKqKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRA 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1546 LKDAQELQNMVDKER---KLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDFLKE 1622
Cdd:pfam02463 806 LEEELKEEAELLEEEqllIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLK 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1623 RETLNLTISDLRLHNEQLLETSKNYLSDItAANNLNLEMKKNLHDLTKECKSLR--SDLQSKEEYFQTQKQLLDETISNL 1700
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEE-KENEIEERIKEEAEILLKYEEEPEelLLEEADEKEKEENNKEEEEERNKR 964
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78706884 1701 KEENRKMEEKLSSGNKALKEDCEKLRSTLESKELILQQNKQELEERLTVINEKNGKNALLDAQLKSNE 1768
Cdd:pfam02463 965 LLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKG 1032
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1002-1809 |
1.12e-11 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 70.39 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1002 KQESQEVLTLKTSLAHLKSKVCELQKKLEKQSEDEKISELQSDIGEISECCLSmELKLADIVNWQAEELRPLDQLQESGV 1081
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEE-YLLYLDYLKLNEERIDLLQELLRDEQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1082 ELQhHSTTAEESLNVEKPIQEQTERTLTTE----YERRIEQLEESLQRAQEELSILEKRKTDENKSLQL-EYMAKIETSE 1156
Cdd:pfam02463 251 EEI-ESSKQEIEKEEEKLAQVLKENKEEEKekklQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKEsEKEKKKAEKE 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1157 NENRSKFRAYCLDLKETQKRYEEQLQQTNEKLASVTTQCQVHLDVIKRSLQEKI--TQAEKERNELAVRHKAELEKIRET 1234
Cdd:pfam02463 330 LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESerLSSAAKLKEEELELKSEEEKEAQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1235 LKE----KESSYKEKLRQAEEERDKEISRLEVMRNTIAEL-HKTNSDREVELEGVKMEKCQLKKLYDKSMLELEQLQCTA 1309
Cdd:pfam02463 410 LLElarqLEDLLKEEKKEELEILEEEEESIELKQGKLTEEkEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1310 DQKSSDLLPGSSNENIDDLQKKCDQYVQDLELLRGEKAELLS---EIQKINGQHSNTIKKLEEIEAEMITLTTQKELERC 1386
Cdd:pfam02463 490 LSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLgdlGVAVENYKVAISTAVIVEVSATADEVEERQKLVRA 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1387 EIAEKLETFKSKEADIKEALHCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIK 1466
Cdd:pfam02463 570 LTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLR 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1467 QLRSEL-----------KDAIDENKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHL 1535
Cdd:pfam02463 650 KGVSLEeglaeksevkaSLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQE 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1536 ESRNEELKRKLKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQ 1615
Cdd:pfam02463 730 AQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEE 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1616 TNDFLKERETLNLTISDLRLHNEQLLETSKNYLSDITAANNLNLEMKK-NLHDLTKECKSLRSDLQSKEEYFQTQKQLLD 1694
Cdd:pfam02463 810 LKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELErLEEEITKEELLQELLLKEEELEEQKLKDELE 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1695 ETISNLKEENRKMEEKLSSGNKALKEDCEKLRSTLESKELILQQNKQELEERLTVINEKNGKNALLDAQLKSN---ETAF 1771
Cdd:pfam02463 890 SKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNkrlLLAK 969
|
810 820 830
....*....|....*....|....*....|....*...
gi 78706884 1772 TSLRKAWIKQSLAIEAANKRSLEMEQKVDKRTREYEEL 1809
Cdd:pfam02463 970 EELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1011-1643 |
1.62e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1011 LKTSLAHLKSKVCELQKKLEKQSEDEKISELQSDIGEISEcclsMELKLADIvNWQAEELRplDQLQESGVELQHHSTTA 1090
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE----LEAELEEL-RLELEELE--LELEEAQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1091 EESLNVEKPIQEQTErtlttEYERRIEQLEesLQRAQEELSILEKRKTDENKSLQLEYMAKIETSENENRSKFRAYCLDL 1170
Cdd:COG1196 298 ARLEQDIARLEERRR-----ELEERLEELE--EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1171 KETQKRYEEQLQQTNEKLASVTTQCQVhldviKRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKESSyKEKLRQAE 1250
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAE-----LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE-EEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1251 EERDKEISRLEvmrNTIAELHKTNSDREVELEGVKMEKCQLKKLYDKSMLELEQLQctaDQKSSDLLPGSSNENIDDLQK 1330
Cdd:COG1196 445 EEAAEEEAELE---EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL---EAEADYEGFLEGVKAALLLAG 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1331 KCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELERceiAEKLETFKSKEADIKEALHCAQ 1410
Cdd:COG1196 519 LRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGR---ATFLPLDKIRARAALAAALARG 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1411 LRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLAlqegISGRDSEIKQLRSELKDAIDENKTVREAKVGLE 1490
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR----AVTLAGRLREVTLEGEGGSAGGSLTGGSRRELL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1491 NSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREDF 1570
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1571 DKLEQTKLDLEEQLRAKKVEIDRRSKELGEVtkdceNIRS------------DLEAQTNDFLKERETLNLTISDL-RLHN 1637
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEALGPV-----NLLAieeyeeleerydFLSEQREDLEEARETLEEAIEEIdRETR 826
|
....*.
gi 78706884 1638 EQLLET 1643
Cdd:COG1196 827 ERFLET 832
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1337-1598 |
1.99e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1337 QDLELLRGEkaELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKElercEIAEKLETFKSKEADIKEALHCAQLRLHAY 1416
Cdd:COG1196 220 EELKELEAE--LLLLKLRELEAELEELEAELEELEAELEELEAELA----ELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1417 DKlvcEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLENSLKAV 1496
Cdd:COG1196 294 LA---ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1497 QENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREDFDKLEQT 1576
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEE 450
|
250 260
....*....|....*....|..
gi 78706884 1577 KLDLEEQLRAKKVEIDRRSKEL 1598
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEA 472
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1094-1854 |
3.02e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 68.99 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1094 LNVEKPIQE-QTERTLTTEYERRIEQLEE----SLQRAQEELSILEKRKTD--ENKSLQLEYMAKIETSENENRSKFRAY 1166
Cdd:pfam15921 113 IDLQTKLQEmQMERDAMADIRRRESQSQEdlrnQLQNTVHELEAAKCLKEDmlEDSNTQIEQLRKMMLSHEGVLQEIRSI 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1167 CLDLKET--QKRYEEQLQQTN--EKLASVTTQCQVHLDVIKRSLQEKITQAEKERNELavrhKAELEKIRETLKEKessY 1242
Cdd:pfam15921 193 LVDFEEAsgKKIYEHDSMSTMhfRSLGSAISKILRELDTEISYLKGRIFPVEDQLEAL----KSESQNKIELLLQQ---H 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1243 KEKLRQAEEERDKEISRL-EVMRNTIAELHKTNSDREVELEgvkmekcQLKKLYDKSMLELEQLQCTADQKSSDLLPGSS 1321
Cdd:pfam15921 266 QDRIEQLISEHEVEITGLtEKASSARSQANSIQSQLEIIQE-------QARNQNSMYMRQLSDLESTVSQLRSELREAKR 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1322 --NENIDDLQKKcdqyvqdLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMitLTTQKELErceiAEKLETFKSKE 1399
Cdd:pfam15921 339 myEDKIEELEKQ-------LVLANSELTEARTERDQFSQESGNLDDQLQKLLADL--HKREKELS----LEKEQNKRLWD 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1400 ADIKEALHCAQLRLHAYDKLVcEYERLKGCLSdsnKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRS--ELKDAID 1477
Cdd:pfam15921 406 RDTGNSITIDHLRRELDDRNM-EVQRLEALLK---AMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLEStkEMLRKVV 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1478 ENKTVReaKVGLENSLKAVQE---NMSAQEGQFKQKIADIKGSVDELQIKLKSLQevrdHLESRNEELKRKLKDAQELQN 1554
Cdd:pfam15921 482 EELTAK--KMTLESSERTVSDltaSLQEKERAIEATNAEITKLRSRVDLKLQELQ----HLKNEGDHLRNVQTECEALKL 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1555 MVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEvtkdcenirSDLEAQTNDFLKERE-----TLNLT 1629
Cdd:pfam15921 556 QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEIND---------RRLELQEFKILKDKKdakirELEAR 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1630 ISDLRLHNEQLLETSKNYLSDITaannlnlEMKKNLHDLTKECKSLRSDLQSKEEYFQtqkqLLDETISNLKEENRKMEE 1709
Cdd:pfam15921 627 VSDLELEKVKLVNAGSERLRAVK-------DIKQERDQLLNEVKTSRNELNSLSEDYE----VLKRNFRNKSEEMETTTN 695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1710 KLSSGNKALKEDCEKLRSTLESKELILQQNKQELEERLTVINEKNGKNALLDAQLKSNETAFTSlrkawikqslaieaAN 1789
Cdd:pfam15921 696 KLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTN--------------AN 761
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78706884 1790 KRSLEMEQKVDKRTREYeelrSTLKTreinfrsEKERMDGTISSLLEDKRNLEEKLCTVTELLAK 1854
Cdd:pfam15921 762 KEKHFLKEEKNKLSQEL----STVAT-------EKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1003-1635 |
5.30e-11 |
|
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: 68.33 E-value: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1003 QESQEVLTLKTSLAHLKSKVCELQKKLEKQSED------EKISELQSDIGEISECC--LSMELKLADiVNWQA--EELRP 1072
Cdd:pfam12128 248 QEFNTLESAELRLSHLHFGYKSDETLIASRQEErqetsaELNQLLRTLDDQWKEKRdeLNGELSAAD-AAVAKdrSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1073 LD----QLQESGVELQHHSTTAEESL-----NVEKPIQEQTE--RTLTTEYERRIEQLEESLQRaqeELSILEKR--KTD 1139
Cdd:pfam12128 327 LEdqhgAFLDADIETAAADQEQLPSWqseleNLEERLKALTGkhQDVTAKYNRRRSKIKEQNNR---DIAGIKDKlaKIR 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1140 ENKSLQLEYM-AKIETSENENRSKFRAYCLDLKETQKRYEEQLQQTNEKLASVT------TQCQVHLDVIKRSlQEKITQ 1212
Cdd:pfam12128 404 EARDRQLAVAeDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATatpellLQLENFDERIERA-REEQEA 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1213 AEKERNELAvrhkAELEKIReTLKEKESsykEKLRQAEEerdkeisRLEVMRNTIAELH-----KTNSDREVELEGVKME 1287
Cdd:pfam12128 483 ANAEVERLQ----SELRQAR-KRRDQAS---EALRQASR-------RLEERQSALDELElqlfpQAGTLLHFLRKEAPDW 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1288 KCQLKKLYDKSMLELEQL--QCTADQKSSDLLPGSSNENIDDLQkkCDQYVQDLELLRGEKAELLSEIQKingQHSntik 1365
Cdd:pfam12128 548 EQSIGKVISPELLHRTDLdpEVWDGSVGGELNLYGVKLDLKRID--VPEWAASEEELRERLDKAEEALQS---ARE---- 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1366 KLEEIEAEMITLTTQkelerceiaekLETFKSKEADIKEALHCAQLRLhaydklvceyERLkgclsdsNKLSENLQKKVE 1445
Cdd:pfam12128 619 KQAAAEEQLVQANGE-----------LEKASREETFARTALKNARLDL----------RRL-------FDEKQSEKDKKN 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1446 R-LHAEQLALQEGISGRDSEIKQLRSELKDAIDENK-TVREAKVGLENSLKAVQENMSAQEGQFKQKIADIKGSVDElqi 1523
Cdd:pfam12128 671 KaLAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKeQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKA--- 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1524 KLKSLQEVRDH-LESRNEELKRKLKDAQELQNM---VDKERKLNSSLREDFDKLEQT----KLDLEEQLRAKKVEIDRRS 1595
Cdd:pfam12128 748 ELKALETWYKRdLASLGVDPDVIAKLKREIRTLerkIERIAVRRQEVLRYFDWYQETwlqrRPRLATQLSNIERAISELQ 827
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 78706884 1596 KELGEVTKDCENIRSDLEAQ--TNDFLKERETLNLTISDLRL 1635
Cdd:pfam12128 828 QQLARLIADTKLRRAKLEMErkASEKQQVRLSENLRGLRCEM 869
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
705-1598 |
6.96e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 67.77 E-value: 6.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 705 QKYLQLQDEYRHLELR-SDEQCQQLQDENSKLQAEIGTLKERVEEIHSELLEVpnpdthpedmELQNQELKKRLSKLQWE 783
Cdd:TIGR02168 213 ERYKELKAELRELELAlLVLRLEELREELEELQEELKEAEEELEELTAELQEL----------EEKLEELRLEVSELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 784 FDEIQLNYECLSNElmstIQECDALREEHKQRTTNSDLESMKssgVGTECSDPENELDtDLLQQFTKLSKSIQQIEltdy 863
Cdd:TIGR02168 283 IEELQKELYALANE----ISRLEQQKQILRERLANLERQLEE---LEAQLEELESKLD-ELAEELAELEEKLEELK---- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 864 sggrrlfiynhaeqdqsvpslklclepakylegdgkqhdasdsvflkgflkcqrfqivkiNQEQNLVKEEDRMRDIIFQL 943
Cdd:TIGR02168 351 ------------------------------------------------------------EELESLEAELEELEAELEEL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 944 KQEVDGKKNLIEEEKEVINNLRAQITSLN--------QIETIKNQNAKTKILCEELQTKdtVQTANKQESQEVL-TLKTS 1014
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNneierleaRLERLEDRRERLQQEIEELLKK--LEEAELKELQAELeELEEE 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1015 LAHLKSKVCELQKKLEKQSEDEKISELQSDIGEISECCLSMELK-LADIVNWQAEELRPLDQLQESGVELQHHSTTAEES 1093
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDsLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1094 LNVEkpiqEQTERTLTTEYERRIEQLE-ESLQRAQEELSILEKRKTDENKSLQLEYM--AKIETSENE---NRSKFRAYC 1167
Cdd:TIGR02168 529 ISVD----EGYEAAIEAALGGRLQAVVvENLNAAKKAIAFLKQNELGRVTFLPLDSIkgTEIQGNDREilkNIEGFLGVA 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1168 LDLKETQKRYE--------------------EQLQQTNEKLASVTTQCqvhlDVIKRSlqEKITQAEKERNELAVRHKAE 1227
Cdd:TIGR02168 605 KDLVKFDPKLRkalsyllggvlvvddldnalELAKKLRPGYRIVTLDG----DLVRPG--GVITGGSAKTNSSILERRRE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1228 LEKIRETLKEKEssykEKLRQAEEERDKEISRLEVMRNTIAELHKTNSDREVELEGVKMEKCQLKKlydksmlELEQLQC 1307
Cdd:TIGR02168 679 IEELEEKIEELE----EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA-------EVEQLEE 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1308 TADQKSSDLLpgssnenidDLQKKCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELERCE 1387
Cdd:TIGR02168 748 RIAQLSKELT---------ELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1388 IAEKLETFKSKEADIKEALHCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQ 1467
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1468 LRSELKDAIDENKTVREAKVGLENSLKAVQEnmsaQEGQFKQKIADIKGSVDEL-QIKLKSLQEVRDHLESRNEELKRKL 1546
Cdd:TIGR02168 899 LSEELRELESKRSELRRELEELREKLAQLEL----RLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRL 974
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78706884 1547 KdaqELQNMVDKERKLN-------SSLREDFDKLEQTKLDLEE---QLRAKKVEIDRRSKEL 1598
Cdd:TIGR02168 975 K---RLENKIKELGPVNlaaieeyEELKERYDFLTAQKEDLTEakeTLEEAIEEIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1363-1695 |
2.21e-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: 66.23 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1363 TIKKLEEIEAEMITLT-----TQKELERCEI-AEKLETFKSKEADIKEAlhcaQLRLhaydkLVCEYERLKGCLsdsnkl 1436
Cdd:TIGR02168 177 TERKLERTRENLDRLEdilneLERQLKSLERqAEKAERYKELKAELREL----ELAL-----LVLRLEELREEL------ 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1437 sENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAideNKTVREAKVGLENSLKAVQEnmsaqegqFKQKIADIKG 1516
Cdd:TIGR02168 242 -EELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL---EEEIEELQKELYALANEISR--------LEQQKQILRE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1517 SVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQ----ELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEID 1592
Cdd:TIGR02168 310 RLANLERQLEELEAQLEELESKLDELAEELAELEekleELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1593 RRSKELGEVTKDCENIRSDLE----------------------AQTNDFLKERETLNLTISDLRLHNEQLLETSKNYLSD 1650
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLErledrrerlqqeieellkkleeAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 78706884 1651 ITAANNLNLEMKKNLHDLTKECKSLRSDLQSKEEYFQTQKQLLDE 1695
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1100-1626 |
2.39e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1100 IQEQTERTLTTEYERRIEQLEESLQRAQEELSILEKRKTDENKSLQLeymakIETSENENRSKFRAYCLDLKETQKRYEE 1179
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE-----LEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1180 QLQQTNEKLASVTtqcqvHLDVIKRSLQEKITQAEKERNELAvRHKAELEKIRETLKEKESSYKEKLRQAEEERDKEISR 1259
Cdd:COG1196 293 LLAELARLEQDIA-----RLEERRRELEERLEELEEELAELE-EELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1260 LEVMRNTIAELHKTNSDREVELEGVKMEKCQLKKLYDKSMLELEQLQCTADQKSSDLLpgSSNENIDDLQKKCDQYVQDL 1339
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE--ELEEALAELEEEEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1340 ELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLT-----------TQKELERcEIAEKLETFKSKEADIKEALHC 1408
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLeelaeaaarllLLLEAEA-DYEGFLEGVKAALLLAGLRGLA 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1409 AQLRLHAYDKLVCEY----ERLKGCLSDSNKLSENLQKKVERL------------------------HAEQLALQEGISG 1460
Cdd:COG1196 524 GAVAVLIGVEAAYEAaleaALAAALQNIVVEDDEVAAAAIEYLkaakagratflpldkiraraalaaALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1461 RDSEIKQLRSELKDAIDE----------NKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQE 1530
Cdd:COG1196 604 VASDLREADARYYVLGDTllgrtlvaarLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1531 VRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRS 1610
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
570
....*....|....*.
gi 78706884 1611 DLEAQTNDFLKERETL 1626
Cdd:COG1196 764 ELERELERLEREIEAL 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1174-1549 |
2.40e-10 |
|
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: 65.86 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1174 QKRYEEQLQQTNEKLASvttqcqvhLDVIKRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKEssykeklrQAEEER 1253
Cdd:TIGR02169 669 SRSEPAELQRLRERLEG--------LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIE--------QLEQEE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1254 DKEISRLEVMRNTIAELhktnsdrEVELEGVKMEKCQLKKLYDKSMLELEQLQctadqkssdllpgssnENIDDLQKKcd 1333
Cdd:TIGR02169 733 EKLKERLEELEEDLSSL-------EQEIENVKSELKELEARIEELEEDLHKLE----------------EALNDLEAR-- 787
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1334 qyvqdleLLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELERCEIAEKLET---FKSKEADIKEALHCAQ 1410
Cdd:TIGR02169 788 -------LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQridLKEQIKSIEKEIENLN 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1411 LRLhayDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKD-------------AID 1477
Cdd:TIGR02169 861 GKK---EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSElkaklealeeelsEIE 937
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1478 ENKTVREAKVGLENSLKAVQENMSAQEGQFK----------QKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLK 1547
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEIRalepvnmlaiQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
|
..
gi 78706884 1548 DA 1549
Cdd:TIGR02169 1018 EV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
471-1270 |
3.37e-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: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 471 MMSKKYQESVPNCDAPQTEISALTASNQVAKETIEKYEEQVKRLKETIERLEMEngkavnlgeqfethKAKSKQMEEELL 550
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ--------------KQILRERLANLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 551 SSISEKDSTIVSLQQSLEELSRDVLRNSKEDQmrsmcpELESSCERICNKCLELERLLPlASASGLDSVACQFDQLRSEI 630
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLE------ELKEELESLEAELEELEAELE-ELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 631 AATRMKLESMLSTFSHASCEVSQKTTDCKRLSEQISTAHDDFGQLQEKynNLKHKWSSQKLAIDTMQVDYNTIQQKYLQL 710
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEEL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 711 QDEYRHLELRSDEQCQQLQDENSKLQAeIGTLKERVEEIHSELLEVpnpdthpedmeLQNQELKKRLSKLQWEFDEIQLN 790
Cdd:TIGR02168 467 REELEEAEQALDAAERELAQLQARLDS-LERLQENLEGFSEGVKAL-----------LKNQSGLSGILGVLSELISVDEG 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 791 YE-CLSNELMSTIQ------------ECDALREEHKQRTTNSDLESMKSSGV-GTECSDPENE-----LDTDLLQQFTKL 851
Cdd:TIGR02168 535 YEaAIEAALGGRLQavvvenlnaakkAIAFLKQNELGRVTFLPLDSIKGTEIqGNDREILKNIegflgVAKDLVKFDPKL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 852 SKSIQQIeltdySGGrrLFIynhaeqdqsVPSLKLCLEPAKYLEGDGKqhdasdSVFLKGFLKCQRFQIVKINQEQNLVk 931
Cdd:TIGR02168 615 RKALSYL-----LGG--VLV---------VDDLDNALELAKKLRPGYR------IVTLDGDLVRPGGVITGGSAKTNSS- 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 932 eedrmrdiIFQLKQEVDGKKNLIEEEKEVINNLRAQITSL-NQIETIKNQNAKTKILCEELQTKDTVQTAN-KQESQEVL 1009
Cdd:TIGR02168 672 --------ILERRREIEELEEKIEELEEKIAELEKALAELrKELEELEEELEQLRKELEELSRQISALRKDlARLEAEVE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1010 TLKTSLAHLKSKVCELQKklEKQSEDEKISELQSDIGEISECCLSMELKLADIVNWQAEELRPLDQLQESGVELQHHSTT 1089
Cdd:TIGR02168 744 QLEERIAQLSKELTELEA--EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1090 AEESLNVEKPIQEQTERTLtTEYERRIEQLEESLQRAQEELSILEKRKTDENKSLQLEYMAKIETSENENRSKFRAYCL- 1168
Cdd:TIGR02168 822 LRERLESLERRIAATERRL-EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELs 900
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1169 ----DLKETQKRYEEQLQQTNEKLASVTTQCQVhLDVIKRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKESSYKE 1244
Cdd:TIGR02168 901 eelrELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
810 820 830
....*....|....*....|....*....|...
gi 78706884 1245 KLRQ-------AEEERDKEISRLEVMRNTIAEL 1270
Cdd:TIGR02168 980 KIKElgpvnlaAIEEYEELKERYDFLTAQKEDL 1012
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
675-1751 |
3.85e-10 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 65.46 E-value: 3.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 675 LQEKYNNLKHkWSSQKLAIDTMQVDYN-----------TIQQKYLQLQDEYRH---LELRSDEQCQQLQDENSKLQAEIg 740
Cdd:TIGR01612 546 LKESYELAKN-WKKLIHEIKKELEEENedsihlekeikDLFDKYLEIDDEIIYinkLKLELKEKIKNISDKNEYIKKAI- 623
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 741 TLKERVEEIHSELLEVPNPDTHPEDMELQNQElkKRLSKLQWEFDEI-QLNYECLSNELMSTIQECDALREEHKQRTTN- 818
Cdd:TIGR01612 624 DLKKIIENNNAYIDELAKISPYQVPEHLKNKD--KIYSTIKSELSKIyEDDIDALYNELSSIVKENAIDNTEDKAKLDDl 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 819 --------SDLESMKSSGVGTECSDPEN------------------ELDTDL---LQQFTKLSKSIQQiELTDYSGGRRL 869
Cdd:TIGR01612 702 kskidkeyDKIQNMETATVELHLSNIENkknelldiiveikkhihgEINKDLnkiLEDFKNKEKELSN-KINDYAKEKDE 780
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 870 F---------IYNHAEQDQSVPSLKLclEPAKYLEGDGKQHDASDSV-------------FLKG-FL-KCQRFQIVKINQ 925
Cdd:TIGR01612 781 LnkykskiseIKNHYNDQINIDNIKD--EDAKQNYDKSKEYIKTISIkedeifkiinemkFMKDdFLnKVDKFINFENNC 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 926 EQNLVKEEDRMRDIIFQLKQEVDGKK-------------------NLIEEEKEVINNLRAQITSL----NQIETIKNQNA 982
Cdd:TIGR01612 859 KEKIDSEHEQFAELTNKIKAEISDDKlndyekkfndskslineinKSIEEEYQNINTLKKVDEYIkiceNTKESIEKFHN 938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 983 KTKILCEEL-QTKDTVQTANKQESQEVLTLKTSLAHLKSKVCELQKKLEKQSEDEKISEL-------QSDIGEISECCLS 1054
Cdd:TIGR01612 939 KQNILKEILnKNIDTIKESNLIEKSYKDKFDNTLIDKINELDKAFKDASLNDYEAKNNELikyfndlKANLGKNKENMLY 1018
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1055 MELKLADIVNWQAEELRPLDQLQESGVELQHHSTTAEESLNVEKPIQEQTErTLTTEYERRIEQLEESLQRAQEELSILE 1134
Cdd:TIGR01612 1019 HQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIE-LLNKEILEEAEINITNFNEIKEKLKHYN 1097
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1135 KrkTDENKSLQLEYMAKIETSENENRS---KFRAYCLDLKETQKR---YEEQLQQTNEKLASVTTQCQVHLDV--IKRSL 1206
Cdd:TIGR01612 1098 F--DDFGKEENIKYADEINKIKDDIKNldqKIDHHIKALEEIKKKsenYIDEIKAQINDLEDVADKAISNDDPeeIEKKI 1175
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1207 QEKITQAEKERNELAVRHK-----AELEKIRETLKEKES---SYKEKL-----RQAEEERDKEISRLEVMRNTIAELHK- 1272
Cdd:TIGR01612 1176 ENIVTKIDKKKNIYDEIKKllneiAEIEKDKTSLEEVKGinlSYGKNLgklflEKIDEEKKKSEHMIKAMEAYIEDLDEi 1255
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1273 ------------TNSDREVELEGVKMEKCQLKKLYDKSMLELEQLQcTADQKSSDLLPGSSNE-NIDDLQKKCDQYVQDL 1339
Cdd:TIGR01612 1256 kekspeienemgIEMDIKAEMETFNISHDDDKDHHIISKKHDENIS-DIREKSLKIIEDFSEEsDINDIKKELQKNLLDA 1334
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1340 ELLRGEKAELLSEIQKI-NGQHSNTIKKL-EEI-----EAEMITLTTQKELERCEIAEK-------LETFKSK---EADI 1402
Cdd:TIGR01612 1335 QKHNSDINLYLNEIANIyNILKLNKIKKIiDEVkeytkEIEENNKNIKDELDKSEKLIKkikddinLEECKSKiesTLDD 1414
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1403 KEALHCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQ---KKVERL-----HAEQLALQEGISGRDSEIkqlrSELKD 1474
Cdd:TIGR01612 1415 KDIDECIKKIKELKNHILSEESNIDTYFKNADENNENVLllfKNIEMAdnksqHILKIKKDNATNDHDFNI----NELKE 1490
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1475 AIDENKtvrEAKVGLENSLKAVQENMSAQEgQFKQKIADIKGSVDELQIKLKSLQEVRDhlesrNEELKRKLKDAQElQN 1554
Cdd:TIGR01612 1491 HIDKSK---GCKDEADKNAKAIEKNKELFE-QYKKDVTELLNKYSALAIKNKFAKTKKD-----SEIIIKEIKDAHK-KF 1560
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1555 MVDKERKlnsslREDFDKLEQTKLDLEEQLRAKkveiDRRSKELGEVTKDCENIR------SDLEAQTNDFLKERETLNL 1628
Cdd:TIGR01612 1561 ILEAEKS-----EQKIKEIKKEKFRIEDDAAKN----DKSNKAAIDIQLSLENFEnkflkiSDIKKKINDCLKETESIEK 1631
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1629 TISDLRLHNE--QLLETSKNYLSDITAANNLNlEMKKNLHDLTKECKSLRSDLQS-KEEYFQTQKQLLDETISNLKEENR 1705
Cdd:TIGR01612 1632 KISSFSIDSQdtELKENGDNLNSLQEFLESLK-DQKKNIEDKKKELDELDSEIEKiEIDVDQHKKNYEIGIIEKIKEIAI 1710
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*.
gi 78706884 1706 KMEEKLSSGNKALKEDCEKLRSTLESKELILQQNKQELEERLTVIN 1751
Cdd:TIGR01612 1711 ANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEEYNTEIG 1756
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1204-1856 |
3.90e-10 |
|
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: 65.04 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1204 RSLQEKITQAEKERNELAVRHKAELEKIR------ETLKEKESSYKEKLRQAEEERDKEISRLEVMRNTIAELHKTNSDR 1277
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINnsnnkiKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1278 EVELEGVKMEKCQLKKLYDKSMLELEQLQCTADqkssdllpgSSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKIN 1357
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELE---------KLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIK 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1358 GQHSNT-----------------IKKLEEIEAEMITLTTQKELERCEIAEKLETFKSKEADIKEALHcaqlrlhaydklv 1420
Cdd:TIGR04523 194 NKLLKLelllsnlkkkiqknkslESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD------------- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1421 cEYERLKGCLSDSNKLSENLQKKVERLhaeqlalqegisgrDSEIKQLRSELKDaidenkTVREAKVGLENSLKAVQENM 1500
Cdd:TIGR04523 261 -EQNKIKKQLSEKQKELEQNNKKIKEL--------------EKQLNQLKSEISD------LNNQKEQDWNKELKSELKNQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1501 SAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKdaqELQNMVDKERKLNSSLREDFDKLEQTKLDL 1580
Cdd:TIGR04523 320 EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE---EKQNEIEKLKKENQSYKQEIKNLESQINDL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1581 EEQLRakkvEIDRRSKELGEVTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHNEQLLETSKNYlsditaaNNLNLE 1660
Cdd:TIGR04523 397 ESKIQ----NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNL-------DNTRES 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1661 MKKNLHDLTKECKSLRSDLQSKEEYFQTQKQLLDEtisnLKEENRKMEEKLSSGNKalkedceklrstlESKELILQQNK 1740
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKK----LNEEKKELEEKVKDLTK-------------KISSLKEKIEK 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1741 QELEerltvINEKNGKNALLDAQLKSNETaftslrkawikqslaieaaNKRSLEMEQKVDKRTREYEELRSTLKTREINF 1820
Cdd:TIGR04523 529 LESE-----KKEKESKISDLEDELNKDDF-------------------ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQ 584
|
650 660 670
....*....|....*....|....*....|....*.
gi 78706884 1821 RSEKERMDGTISSLLEDKRNLEEKLCTVTELLAKLK 1856
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1422-1859 |
5.93e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1422 EYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLENSlkavqenms 1501
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL--------- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1502 aqegqfKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREDFDKL---EQTKL 1578
Cdd:PRK03918 244 ------EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELreiEKRLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1579 DLEEQLRAKKVEIDRRSK---ELGEVTKDCENIRSDLEAqtndfLKERetlnltisdlrlhnEQLLETSKNYLSDITaan 1655
Cdd:PRK03918 318 RLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEE-----LEER--------------HELYEEAKAKKEELE--- 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1656 nlnlEMKKNLHDLTKEckslrsDLQSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKALkedcEKLRS-------- 1727
Cdd:PRK03918 376 ----RLKKRLTGLTPE------KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI----EELKKakgkcpvc 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1728 ----TLESKELILQQNKQELEERLTVINEKNGKNALLDAQLKSNETAFTSLRKAWIKQSLA---IEAANKRSLEMEQKVD 1800
Cdd:PRK03918 442 grelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAeqlKELEEKLKKYNLEELE 521
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 78706884 1801 KRTREYEELRSTLKTREINFRSEKERMDgTISSLLEDKRNLEEKLCTVTELLAKLKREL 1859
Cdd:PRK03918 522 KKAEEYEKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKEL 579
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1364-1866 |
6.91e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.31 E-value: 6.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1364 IKKLEEIEAEMITLTTQKELERCEIAEKLETFKSKEADIKEalhcaqlRLHAYDKLVCEYERLKGCLSDSNKLSENLQKK 1443
Cdd:PRK03918 181 LEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELRE-------ELEKLEKEVKELEELKEEIEELEKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1444 VERLHAEQLALQEGISGRDSEIKQLRSELKD--AIDENKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADIKGSVDEL 1521
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1522 QIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSsLREDFDKLEQTKLDLE-EQLRAKKVEIDRRSKELGE 1600
Cdd:PRK03918 334 EEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELER-LKKRLTGLTPEKLEKElEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1601 VTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHNEqlLETSKNYLSDITAANNLNLEMKKNLHDLTKECKSLRSDLq 1680
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHR--KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVL- 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1681 SKEEYFQTQKQLLDETIS--------NLKEENRKMEE---------KLSSGNKALKEDCEKLRStLESKELILQQNKQEL 1743
Cdd:PRK03918 490 KKESELIKLKELAEQLKEleeklkkyNLEELEKKAEEyeklkekliKLKGEIKSLKKELEKLEE-LKKKLAELEKKLDEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1744 EERLTVINEKNGKNALLDaqLKSNETAFTSLRKAWiKQSLAIEAANKRSLEMEQKVDKRTREYEELRSTLKTREINFRSE 1823
Cdd:PRK03918 569 EEELAELLKELEELGFES--VEELEERLKELEPFY-NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 78706884 1824 KERMDGTISSLLEDK-RNLEEKLCTVTELLAKLKRELPALHTQK 1866
Cdd:PRK03918 646 RKELEELEKKYSEEEyEELREEYLELSRELAGLRAELEELEKRR 689
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
956-1599 |
1.14e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 63.83 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 956 EEKEVINNLRAQITSLNQIETIKNQNAKTKILCEELQTKDTVQtANKQESQEVLTLKTSLAHLKSK-------------- 1021
Cdd:TIGR00618 193 HGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAL-QQTQQSHAYLTQKREAQEEQLKkqqllkqlrariee 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1022 -------VCELQKKLEKQSEDEKISELQSDIGEISECCLSMELKLADIVNWQAEELRPLDQLQESGVELQHHSTTAEESL 1094
Cdd:TIGR00618 272 lraqeavLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLH 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1095 NVEKPIQEQTERTLT--TEYERRIEQLEESLQRAQEELSILEKRKTDENKSLQLEYMAKIETSENENRSKFRAYCLDLK- 1171
Cdd:TIGR00618 352 SQEIHIRDAHEVATSirEISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKk 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1172 --ETQKRYEEQLQQTNEKLASVTTQCQVHLDVIKRSLQEKITQAEKERN--ELAVRHKAELEKIRETLKEKESSYKEKLR 1247
Cdd:TIGR00618 432 qqELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQihLQETRKKAVVLARLLELQEEPCPLCGSCI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1248 QAEEER------DKEISRLEVMRNTIAELHKTNSDREVELEGvkmEKCQLKKLYDKSMLELEQLQCTA--DQKSSDLLPG 1319
Cdd:TIGR00618 512 HPNPARqdidnpGPLTRRMQRGEQTYAQLETSEEDVYHQLTS---ERKQRASLKEQMQEIQQSFSILTqcDNRSKEDIPN 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1320 SSNEnIDDLQKKCDQYVQDLELLRGEKAELLSEIQ-KINGQhsNTIKKLEEIEAEMITLTTQKELERCEIAEKLETFKSK 1398
Cdd:TIGR00618 589 LQNI-TVRLQDLTEKLSEAEDMLACEQHALLRKLQpEQDLQ--DVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1399 EADIKEALHCAQlRLHAYDKLVCEYERLKGCLSDSNKLSENLQ----------KKVERLHAEQLALQEGISGRDSEIKQL 1468
Cdd:TIGR00618 666 SIRVLPKELLAS-RQLALQKMQSEKEQLTYWKEMLAQCQTLLRelethieeydREFNEIENASSSLGSDLAAREDALNQS 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1469 RSELKDAIDENKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSL-----QEVRDHLESRNEELK 1543
Cdd:TIGR00618 745 LKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLeaeigQEIPSDEDILNLQCE 824
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 78706884 1544 RKLKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLeEQLRAKKVEIDRRSKELG 1599
Cdd:TIGR00618 825 TLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQL-AQLTQEQAKIIQLSDKLN 879
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1489-1784 |
1.35e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.42 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1489 LENSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLRE 1568
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1569 DFDKLEQTKLDLEEQLRAKKVEIDRRSKELgevtKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHNEQLLETSKNYL 1648
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEEL----EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1649 SDITAANNLNLEMKKNLHDLTKECKSLRSDLQSKEEYFQTQKQLLDETISNLKEENRKMEEklssgnkaLKEDCEKLRST 1728
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE--------LEEEEEALLEL 464
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 78706884 1729 LESKELILQQNKQELEERLTVINEKNGKNALLDAQLKSNETAFTSLRKAWIKQSLA 1784
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
923-1819 |
1.46e-09 |
|
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: 63.53 E-value: 1.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 923 INQEQNLVKEEDRMRDIIFQLKQEV---DGKKNLIEEEKEVINNLRAQITSLNQIET-----IKNQNAKTKILCEELQTK 994
Cdd:TIGR00606 178 IFSATRYIKALETLRQVRQTQGQKVqehQMELKYLKQYKEKACEIRDQITSKEAQLEssreiVKSYENELDPLKNRLKEI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 995 DTVQTANKQESQEVLTLKTSLAHLKSKVCELQKKLEK--QSEDEKISELQSDIGEISEcclSMELKLADIvnwqaeeLRP 1072
Cdd:TIGR00606 258 EHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvfQGTDEQLNDLYHNHQRTVR---EKERELVDC-------QRE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1073 LDQLQESGVELQHHSTtaeESLNVEKPIQEQTERTLTTEYERRIEQLEESLQraqEELSILEkRKTDENKSLQLEYMAKI 1152
Cdd:TIGR00606 328 LEKLNKERRLLNQEKT---ELLVEQGRLQLQADRHQEHIRARDSLIQSLATR---LELDGFE-RGPFSERQIKNFHTLVI 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1153 ETSENENRSKFRAyCLDLKETQKRYEEQLqqtneklasvtTQCQVHLDVIKRSLQEKITQAEKERNELAVRHK--AELEK 1230
Cdd:TIGR00606 401 ERQEDEAKTAAQL-CADLQSKERLKQEQA-----------DEIRDEKKGLGRTIELKKEILEKKQEELKFVIKelQQLEG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1231 IRETLKEKESSYKEKLRQAEEERDKEISRLEVMRNTIAELHKTNSDREVELEGVKMEKCQLKKLYDKSMLELEQLQCTAD 1310
Cdd:TIGR00606 469 SSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKD 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1311 QKSSDLLPGSSNE---------NIDDLQKKCDQYVQDLELLRGEKAELLSEIQKINgQHSNTIKKLEEIEAEMITLTTQK 1381
Cdd:TIGR00606 549 EQIRKIKSRHSDEltsllgyfpNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLE-QNKNHINNELESKEEQLSSYEDK 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1382 ELERCeiaeKLETFKSKEADIKEALHCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEqlaLQEgisgr 1461
Cdd:TIGR00606 628 LFDVC----GSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAE---LQE----- 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1462 dsEIKQLRSELKDAIDEnktvreakvglensLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEE 1541
Cdd:TIGR00606 696 --FISDLQSKLRLAPDK--------------LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRD 759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1542 LKR-----------------KLKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLE--------EQLRAKKVEIDRR-- 1594
Cdd:TIGR00606 760 IQRlkndieeqetllgtimpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsdldrtvQQVNQEKQEKQHEld 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1595 -----SKELGEVTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHNEQLLETSKNYLSditaannLNLEMKKNLHDLT 1669
Cdd:TIGR00606 840 tvvskIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQS-------LIREIKDAKEQDS 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1670 KECKSLRSDLQSKEEYF---QTQKQLLDETISNLKEENRKMEEKLSSGNKALKEDCEKLRSTLESKELILQQNKQELEER 1746
Cdd:TIGR00606 913 PLETFLEKDQQEKEELIsskETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKH 992
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78706884 1747 LTVINEkngknallDAQLKSNETAFTSLRKAWIKQSLAIEAANKRSLEMEQKVDKRTREYEELRSTLKTREIN 1819
Cdd:TIGR00606 993 QEKINE--------DMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQ 1057
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
644-1619 |
1.48e-09 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 63.53 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 644 FSHASCEVSQKTTDCKRLSEQISTAHDDFGQLQEKYNNLKHKWS------SQKLAIDTMQVDynTIQQKYLQLQDEYRHL 717
Cdd:TIGR01612 746 HGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELNKYKSKISeiknhyNDQINIDNIKDE--DAKQNYDKSKEYIKTI 823
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 718 ELRsdeqcqqlQDENSKLQAEIGTLKERVEEIHSELLEVPNpdTHPEDMELQNQELKKRLSKLQWEFDEIQLN-YE---- 792
Cdd:TIGR01612 824 SIK--------EDEIFKIINEMKFMKDDFLNKVDKFINFEN--NCKEKIDSEHEQFAELTNKIKAEISDDKLNdYEkkfn 893
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 793 ---CLSNELMSTIQE-----------------CDALREE----HKQRTT-----NSDLESMKSSGVGTECSdpENELDTD 843
Cdd:TIGR01612 894 dskSLINEINKSIEEeyqnintlkkvdeyikiCENTKESiekfHNKQNIlkeilNKNIDTIKESNLIEKSY--KDKFDNT 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 844 LLQQFTKLSKSIQQIELTDYSGgrrlfiyNHAEQDQSVPSLKLCLEPAK----YLEGDGKQHDASDSVFlkgflkcqrfQ 919
Cdd:TIGR01612 972 LIDKINELDKAFKDASLNDYEA-------KNNELIKYFNDLKANLGKNKenmlYHQFDEKEKATNDIEQ----------K 1034
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 920 IVKINQeqNLVKEEDRMRDIIFQLKQEVDGK--KNLIEEEKEVINNLRAQITSLNQI-ETIKNQN-------AKTKILCE 989
Cdd:TIGR01612 1035 IEDANK--NIPNIEIAIHTSIYNIIDEIEKEigKNIELLNKEILEEAEINITNFNEIkEKLKHYNfddfgkeENIKYADE 1112
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 990 ELQTKDTVQTANKQESQEVLTL-------KTSLAHLKSKVCELQKKLEKQSEDEKISELQSDIGEISECcLSMELKLADI 1062
Cdd:TIGR01612 1113 INKIKDDIKNLDQKIDHHIKALeeikkksENYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVTK-IDKKKNIYDE 1191
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1063 VNWQAEELRPLDQLQESGVELQHHSTTAEESLNveKPIQEQTErtlttEYERRIEQLEESLQRAQEELSILEKRKTDENK 1142
Cdd:TIGR01612 1192 IKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLG--KLFLEKID-----EEKKKSEHMIKAMEAYIEDLDEIKEKSPEIEN 1264
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1143 SLQLEYMAKIETSE-NENRSKFRAYCLdlkeTQKRYEEQLQQTNEKLASVTTQCQVHLDV--IKRSLQEKITQAEKERNE 1219
Cdd:TIGR01612 1265 EMGIEMDIKAEMETfNISHDDDKDHHI----ISKKHDENISDIREKSLKIIEDFSEESDIndIKKELQKNLLDAQKHNSD 1340
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1220 LAvRHKAELEKIRETLK--------EKESSYKEKLRQAEEERDKEISRLEVMRNTIAE---LHKTNSDREVELEGVKMEK 1288
Cdd:TIGR01612 1341 IN-LYLNEIANIYNILKlnkikkiiDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDdinLEECKSKIESTLDDKDIDE 1419
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1289 CqlkklydksmleleqLQCTADQKSSDLlpgSSNENIDDLQKKCDQYVQDLELL------RGEKAELLSEIQKING--QH 1360
Cdd:TIGR01612 1420 C---------------IKKIKELKNHIL---SEESNIDTYFKNADENNENVLLLfkniemADNKSQHILKIKKDNAtnDH 1481
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1361 SNTIKKLEEIEAEMITLTTQKELERCEIAEKLETFKSKEADIKEALHcaqlrlhAYDKLvceyeRLKGCLSDSNKLSENL 1440
Cdd:TIGR01612 1482 DFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLN-------KYSAL-----AIKNKFAKTKKDSEII 1549
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1441 QKKVERLHaEQLALQEGISGRD-SEIKQLRSELKDAIDENKTVREAKVGLENSLKAVqENMSAQEGQFKQKIADIKGSVD 1519
Cdd:TIGR01612 1550 IKEIKDAH-KKFILEAEKSEQKiKEIKKEKFRIEDDAAKNDKSNKAAIDIQLSLENF-ENKFLKISDIKKKINDCLKETE 1627
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1520 ELQIKLKSLQevrdhLESRNEELKRKLKDAQELQNMVdkerklnsslredfdkleqtkldleEQLRAKKVEIDRRSKELG 1599
Cdd:TIGR01612 1628 SIEKKISSFS-----IDSQDTELKENGDNLNSLQEFL-------------------------ESLKDQKKNIEDKKKELD 1677
|
1050 1060
....*....|....*....|
gi 78706884 1600 EVTKDCENIRSDLEAQTNDF 1619
Cdd:TIGR01612 1678 ELDSEIEKIEIDVDQHKKNY 1697
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1068-1768 |
1.74e-09 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 63.06 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1068 EELRPLDQLQESGVELQHHSTTAEESLNVEK----------PIQEQTERTLTTEYERRIEQLEESLQRAQEELSILEKRK 1137
Cdd:TIGR00618 170 MNLFPLDQYTQLALMEFAKKKSLHGKAELLTlrsqlltlctPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1138 TDENKSLQLEYMAKIETSENEnrsKFRAYCLDLKETQKRYEEQLQQtnEKLASVT---TQCQVHLDVIKRSLQEKITQAE 1214
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIE---ELRAQEAVLEETQERINRARKA--APLAAHIkavTQIEQQAQRIHTELQSKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1215 KERnelavRHKAELEKIRETLKEKESSYKEKLRQAEEER---DKEISRLEVMRNTIAELHktnsdREVELEGVKMEKCQL 1291
Cdd:TIGR00618 325 KLL-----MKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRdahEVATSIREISCQQHTLTQ-----HIHTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1292 KKLYDKSMLELEQLQCTADqkssdllPGSSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKingqhsnTIKKLEEIE 1371
Cdd:TIGR00618 395 LQSLCKELDILQREQATID-------TRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA-------QCEKLEKIH 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1372 AEMITlttQKELERCEIAEKLETFKSKEADIKEALHCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQ 1451
Cdd:TIGR00618 461 LQESA---QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1452 LALQEGISGRDSEIKQLRSELKdaIDENKTVREAKvglENSLKAVQENMSAQEGQFKQKIadikgsVDELQIKLKSLQEV 1531
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRA--SLKEQMQEIQQ---SFSILTQCDNRSKEDIPNLQNI------TVRLQDLTEKLSEA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1532 RDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDL-----EEQLRAKKVE----IDRRSKELGEVT 1602
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqervREHALSIRVLpkelLASRQLALQKMQ 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1603 KDCENIRSDLE--AQTNDFLKERETlnlTISDLRLHNEQLLETSKNYLSDITAANNLNLEMKKNLHDLTKE-CKSLRSDL 1679
Cdd:TIGR00618 687 SEKEQLTYWKEmlAQCQTLLRELET---HIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTvLKARTEAH 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1680 QSKEEYFQTQKQLLDE---TISNLKEENRKMEEKLSSGNKALKEDCEKLRSTLESKELILQQNKQELEERLTVINEKNGK 1756
Cdd:TIGR00618 764 FNNNEEVTAALQTGAElshLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSAT 843
|
730
....*....|..
gi 78706884 1757 NALLDAQLKSNE 1768
Cdd:TIGR00618 844 LGEITHQLLKYE 855
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1345-1866 |
4.22e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1345 EKAELLSEIQKINGQHSNTIKKLEEIEAEMItlttQKELERCEIAEKLETFKSKEADIKEALHCAQLRLhayDKLVCEYE 1424
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLN----KDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKI---NKLNSDLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1425 RLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSAQE 1504
Cdd:TIGR04523 107 KINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1505 gqfkQKIADIKGSVDELQIKLKSLQ---EVRDHLESRNEELKRKL----KDAQELQNMVDKERKLNSSLREDFDKLEQTK 1577
Cdd:TIGR04523 187 ----KNIDKIKNKLLKLELLLSNLKkkiQKNKSLESQISELKKQNnqlkDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1578 LDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDflKERETLNLTISDLRLHNEQLLETSknylSDITAANNL 1657
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQ--KEQDWNKELKSELKNQEKKLEEIQ----NQISQNNKI 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1658 NLEMKKNLHDLTKECKSLRSDLQSKEEYFQtQKQLLDETISNLKEENRKMEEKLSSGNKALK---EDCEKLRSTLESKEL 1734
Cdd:TIGR04523 337 ISQLNEQISQLKKELTNSESENSEKQRELE-EKQNEIEKLKKENQSYKQEIKNLESQINDLEskiQNQEKLNQQKDEQIK 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1735 ILQQNKQELEERLTVINEKNGKNALLDAQLKSNETAFtslrkawikqSLAIEAANKRSLEMEQKVDKRTREYEELRSTLK 1814
Cdd:TIGR04523 416 KLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK----------ELIIKNLDNTRESLETQLKVLSRSINKIKQNLE 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 78706884 1815 TREINFRSEKERmdgtISSLLEDKRNLEEKLCTVTELLAKLKRELPALHTQK 1866
Cdd:TIGR04523 486 QKQKELKSKEKE----LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEK 533
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1113-1809 |
5.48e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 5.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1113 ERRIEQLEESLQRAQEELSILEKRKtdenKSLQLEymakietsenenrskfraycldlKETQKRYeeqlqqtneklasvt 1192
Cdd:COG1196 178 ERKLEATEENLERLEDILGELERQL----EPLERQ-----------------------AEKAERY--------------- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1193 tqcqvhldvikRSLQEKITQAEKernELAVRHKAELEKIRETLKEKESSYKEKLRQAEEERDKEISRLEVMRNTIAELhk 1272
Cdd:COG1196 216 -----------RELKEELKELEA---ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-- 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1273 tnsdrevelegvkmekcqlkklydksMLELEQLQctadqkssdllpgssnENIDDLQKKCDQYVQDLELLRGEKAELLSE 1352
Cdd:COG1196 280 --------------------------ELELEEAQ----------------AEEYELLAELARLEQDIARLEERRRELEER 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1353 IQKINGQHSNTIKKLEEIEAEMITLTTQKELERCEIAEKLETFKSKEADIKEALHCAQLRLHAYDKLVCEYERLKGCLSD 1432
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1433 SNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSAQEGQFKQ--- 1509
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALlea 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1510 KIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDA------QELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQ 1583
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrglaGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1584 lRAKKVEIDRRSKELGEVTK-DCENIRSDLEAQTNDFLKERETLNLTISDLRLHNEQLLETSKNYLSDITAANNLNLEMK 1662
Cdd:COG1196 558 -VAAAAIEYLKAAKAGRATFlPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAAL 636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1663 KNLHDLTKECKSLRSDLQSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKALKEDCEKLRSTLESKELILQQNKQE 1742
Cdd:COG1196 637 RRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78706884 1743 LEERLTVINEKNGKNALLDAQLKSNETAFTSLRKAWIKQSLAIEAANkrslEMEQKVDKRTREYEEL 1809
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE----ELERELERLEREIEAL 779
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1229-1766 |
7.39e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1229 EKIRETLKEKESsYKEKLRQAEEERDKEISRLEVMRNTIAELHKTNSDREvelegvkmEKCQLKKLYDKSMLELEQlQCT 1308
Cdd:TIGR04523 159 NKYNDLKKQKEE-LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLK--------KKIQKNKSLESQISELKK-QNN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1309 ADQKSSDLLPGSSNENIDDLQKKCDQYVQDLELLRGEKAEL---LSEIQKINGQHSNTIKKLEEIEAEMITLTTQKEler 1385
Cdd:TIGR04523 229 QLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLsekQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE--- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1386 ceiAEKLETFKSKEADIKEALhcaqlrlhaydklvceyERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEI 1465
Cdd:TIGR04523 306 ---QDWNKELKSELKNQEKKL-----------------EEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQREL 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1466 KQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRK 1545
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1546 LKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDceniRSDLEAQTNDFLKERET 1625
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE----KKELEEKVKDLTKKISS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1626 LNLTISDLrlhneqlletsknylsditaaNNLNLEMKKNLHDLTKECKSLRSDLqsKEEYFQTQKQLLDETISNLKEENR 1705
Cdd:TIGR04523 522 LKEKIEKL---------------------ESEKKEKESKISDLEDELNKDDFEL--KKENLEKEIDEKNKEIEELKQTQK 578
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78706884 1706 KMEEKLSSGNKALKEDcEKLRSTLESKELILQQNKQELEERLTVINEKNGKNALLDAQLKS 1766
Cdd:TIGR04523 579 SLKKKQEEKQELIDQK-EKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1290-1814 |
1.05e-08 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 60.69 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1290 QLKKLYDKsMLELEQLQCTADQKSS---DLLPGSSNenIDDLQKKCDQYVQDLELLRGEKAE-------LLSEIQKINGQ 1359
Cdd:PRK01156 150 QRKKILDE-ILEINSLERNYDKLKDvidMLRAEISN--IDYLEEKLKSSNLELENIKKQIADdekshsiTLKEIERLSIE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1360 HSNTIKKLEEIEAEMITLTTQKElERCEIAEKLETFKSKEADIKEALHCAQLRLHAYDKL-----------VCEYERLKG 1428
Cdd:PRK01156 227 YNNAMDDYNNLKSALNELSSLED-MKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIindpvyknrnyINDYFKYKN 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1429 CLSDSNKLSENLQKKVERLHAEQLALQEGISGRDS---------EIKQLRSELKDAIDE-----------NKTVREAKVG 1488
Cdd:PRK01156 306 DIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDyikkksrydDLNNQILELEGYEMDynsylksieslKKKIEEYSKN 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1489 LENSLKAVQENMSAQE---GQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLK---------------DAQ 1550
Cdd:PRK01156 386 IERMSAFISEILKIQEidpDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEmlngqsvcpvcgttlGEE 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1551 ELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDF------LKERE 1624
Cdd:PRK01156 466 KSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIkikineLKDKH 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1625 TL---------NLTISDLRLHNEQLLET-SKNYLSDITAANNLNLEMKKNLHDLTKECKSLRSDLQSKEEYFQTQKQLLD 1694
Cdd:PRK01156 546 DKyeeiknrykSLKLEDLDSKRTSWLNAlAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIE 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1695 ETISNLKEENRKMEEKlssgnkalKEDCEKLRSTLESkeliLQQNKQELEERLTVINEKNGKNALLDAQLKSNETAFTSL 1774
Cdd:PRK01156 626 NEANNLNNKYNEIQEN--------KILIEKLRGKIDN----YKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDA 693
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 78706884 1775 RKAWIKQSLAIEAANKRSLEMEQKVDKRTREYEELRSTLK 1814
Cdd:PRK01156 694 KANRARLESTIEILRTRINELSDRINDINETLESMKKIKK 733
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1198-1866 |
1.07e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 60.76 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1198 HLDVIKRSLQEKITQAEKERNELAvRHKAELEKIRETLKEKESSYKEKLRQAEEERDKEISRLEVMRNTIAELHKTNSDR 1277
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELI-IDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1278 EVELEGVKMEKCQLKKLYDKSMLELEQL---QCTADQKSSDLLPGSSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQ 1354
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKenkEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1355 KINGQHSNTIKKLEEIEAEMITLTTQKELERCEIAEkletfkskeadikealhCAQLRLHAydklvceyERLKGCLSDSN 1434
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE-----------------LEKLQEKL--------EQLEEELLAKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1435 KLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADI 1514
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1515 KGSvDELQIKLKS--LQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEID 1592
Cdd:pfam02463 460 LLK-DELELKKSEdlLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1593 RRSKELGEVTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHNEQLLETSKNYLSDITAANNLNLEMKKNLHDLTKEC 1672
Cdd:pfam02463 539 ENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADED 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1673 KSLRSDLQSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKALKEDCEKLRSTLESKELILQQNKQELEERLTVINE 1752
Cdd:pfam02463 619 DKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1753 KNGKNALLDAQLKSNETAFTSLRKAWIKQSLAIEAANKRSLEMEQKVDKRTREYEELRSTLKTREINFRSEKERMDGTIS 1832
Cdd:pfam02463 699 LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAE 778
|
650 660 670
....*....|....*....|....*....|....
gi 78706884 1833 SLLEDKRNLEEKlcTVTELLAKLKRELPALHTQK 1866
Cdd:pfam02463 779 EREKTEKLKVEE--EKEEKLKAQEEELRALEEEL 810
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1382-1859 |
1.69e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1382 ELERCEIAEKLETFKSKEADIKEALHCAQLRLHAYDKLVCEYERLKGCLSDsnklsenLQKKVERLHAEQLALQEGISGR 1461
Cdd:PRK02224 212 ESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED-------LRETIAETEREREELAEEVRDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1462 DSEIKQLRSELKDAIDEnktvreakVGLEN----SLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLES 1537
Cdd:PRK02224 285 RERLEELEEERDDLLAE--------AGLDDadaeAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1538 RNEELKRKLKDAQ-ELQNMvdkerklnsslREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQT 1616
Cdd:PRK02224 357 RAEELREEAAELEsELEEA-----------REAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1617 NDfLKERETLNLTISDLRLHNEQLLETSKnylsditaannlnlemkknlhdltkeCKSLRSDLQSKE-----EYFQTQKQ 1691
Cdd:PRK02224 426 ER-EAELEATLRTARERVEEAEALLEAGK--------------------------CPECGQPVEGSPhvetiEEDRERVE 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1692 LLDETISNLKEENRKMEEKLSSGnKALKEDCEKLRSTLESKELIlqqnKQELEERLTVINEKNGKNALLDAQLKSNETAF 1771
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDL----EELIAERRETIEEKRERAEELRERAAELEAEA 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1772 TSLRKAWIKQSLAIEAANKRSLEMEQK---VDKRTREYEELRSTLKTREiNFRSEKERMDGTISSLLEDKRNLEEKLCTV 1848
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKlaeLKERIESLERIRTLLAAIA-DAEDEIERLREKREALAELNDERRERLAEK 632
|
490
....*....|.
gi 78706884 1849 TELLAKLKREL 1859
Cdd:PRK02224 633 RERKRELEAEF 643
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1108-1447 |
2.02e-08 |
|
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: 59.85 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1108 LTTEYERRIEQLEESLQRAQEELSILEKRKTDENKSLqleymakietsENENRSKFRAycldlKETQKRYEEQLQQTNEK 1187
Cdd:pfam12128 598 SEEELRERLDKAEEALQSAREKQAAAEEQLVQANGEL-----------EKASREETFA-----RTALKNARLDLRRLFDE 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1188 LASVTTQCQVHLDVIKRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKESSYKEKLRQAEEERDKEISRLEvmrnti 1267
Cdd:pfam12128 662 KQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLK------ 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1268 AELHKTNSDREVELEgvkmekcQLKKLYDKSMLELeqlqctadqkssdllpGSSNENIDDLQKKCDQYVQDLELLRGEKA 1347
Cdd:pfam12128 736 AAIAARRSGAKAELK-------ALETWYKRDLASL----------------GVDPDVIAKLKREIRTLERKIERIAVRRQ 792
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1348 ELLS-----------EIQKINGQHSNTIKKLEEIEAEMITLTTQKELERCEIA-----------------EKLETFKSKE 1399
Cdd:pfam12128 793 EVLRyfdwyqetwlqRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEmerkasekqqvrlsenlRGLRCEMSKL 872
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 78706884 1400 ADIKEALHCAQLRLHAYDKLVCeyerLKGCLSDSNKLSENLQKKVERL 1447
Cdd:pfam12128 873 ATLKEDANSEQAQGSIGERLAQ----LEDLKLKRDYLSESVKKYVEHF 916
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1335-1865 |
2.94e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.30 E-value: 2.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1335 YVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMitltTQKELERCEIAEKLETFKSKEADIKEALHCAQLRLH 1414
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL----EELRLEVSELEEEIEELQKELYALANEISRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1415 AYDKlvcEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEgisgrdsEIKQLRSELKDAIDENKTVREAKVGLENSLK 1494
Cdd:TIGR02168 306 ILRE---RLANLERQLEELEAQLEELESKLDELAEELAELEE-------KLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1495 AVQENMSAQEG---QFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQ--ELQNMVDKERKLNSSLRED 1569
Cdd:TIGR02168 376 ELEEQLETLRSkvaQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElkELQAELEELEEELEELQEE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1570 FDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDF------LKERETLNLTISDLrlhnEQLLET 1643
Cdd:TIGR02168 456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSegvkalLKNQSGLSGILGVL----SELISV 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1644 SKNYLSDITAANNLNLEMkknlhdltkeckSLRSDLQSKEEYFQTQKQ---------LLDETISNLKEENRKMEEKLSSG 1714
Cdd:TIGR02168 532 DEGYEAAIEAALGGRLQA------------VVVENLNAAKKAIAFLKQnelgrvtflPLDSIKGTEIQGNDREILKNIEG 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1715 NKALKEDCEKLRSTLE---------------------------------------------------SKELILQQNKQEL 1743
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRkalsyllggvlvvddldnalelakklrpgyrivtldgdlvrpggvitggsaKTNSSILERRREI 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1744 EERLTVINEKNGKNALLDAQLKSNETAFT-------SLRKAWIKQSLAIEAANKRSLEMEQKVDKRTREYEELRSTLKTR 1816
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEeleeeleQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 78706884 1817 EINFRSEKERMDGTISSLLEDKRN---LEEKLCTVTELLAKLKRELPALHTQ 1865
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEieeLEAQIEQLKEELKALREALDELRAE 811
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1213-1710 |
3.46e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.90 E-value: 3.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1213 AEKERNELAVRhKAELEKIRETLKEKESSYKEKLRQAEEERDKEISRLEVMRNTIAELhktnSDREVELEGVKMEKCQLK 1292
Cdd:PRK02224 197 EEKEEKDLHER-LNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREEL----ETLEAEIEDLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1293 KLYDKSMLELEQLQCTADQKSSDLLPGSSNENIDDL-QKKCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIE 1371
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDAdAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1372 AEMITLTTQKELERCEIAEKLETFKSKEADIKEALhcaqlrlhayDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQ 1451
Cdd:PRK02224 352 DDLEERAEELREEAAELESELEEAREAVEDRREEI----------EELEEEIEELRERFGDAPVDLGNAEDFLEELREER 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1452 lalqEGISGRDSEIKQLRSELKDAIDENKTVREA----KVG--LENSLKA-VQENMSAQEGQFKQKIADIKGSVDELQIK 1524
Cdd:PRK02224 422 ----DELREREAELEATLRTARERVEEAEALLEAgkcpECGqpVEGSPHVeTIEEDRERVEELEAELEDLEEEVEEVEER 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1525 LKSLQEVRDhLESRNEELKRKLKDAQEL----QNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGE 1600
Cdd:PRK02224 498 LERAEDLVE-AEDRIERLEERREDLEELiaerRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1601 VTKDCENIRSDLEAQTN--DFLKERETLNLTISDLRLHNEQLLEtsknylsditaannLNLEMKKNLHDLTKECKSLRSD 1678
Cdd:PRK02224 577 LNSKLAELKERIESLERirTLLAAIADAEDEIERLREKREALAE--------------LNDERRERLAEKRERKRELEAE 642
|
490 500 510
....*....|....*....|....*....|...
gi 78706884 1679 LQ-SKEEYFQTQKQLLDETISNLKEENRKMEEK 1710
Cdd:PRK02224 643 FDeARIEEAREDKERAEEYLEQVEEKLDELREE 675
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
904-1618 |
6.34e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 57.72 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 904 SDSVFLKGFLKCQRFQIVKINQEQNLVKEEDRMRD-IIFQLKQEVDGKKNLIEEEKEVINNLRAQITSLnqietiknQNA 982
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKkNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEEL--------ENE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 983 KTKILCEELQTKDTVQTANKQESQevltLKTSLAHLKSKVcELQKKLEKQSEDEK---------ISELQSDIGEISECCL 1053
Cdd:TIGR04523 175 LNLLEKEKLNIQKNIDKIKNKLLK----LELLLSNLKKKI-QKNKSLESQISELKkqnnqlkdnIEKKQQEINEKTTEIS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1054 SMELKLADIVNWQAEELrplDQLQESGVELQHHSTTAEESLNVEKPIQ-------EQTERTLTTEYERRIEQLEESLQRA 1126
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIK---KQLSEKQKELEQNNKKIKELEKQLNQLKseisdlnNQKEQDWNKELKSELKNQEKKLEEI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1127 QEELSILEKRKTDENKSL-QLEymAKIETSENENRSKfraycldlketqkryEEQLQQTNEKLASVTTQcqvhldviKRS 1205
Cdd:TIGR04523 327 QNQISQNNKIISQLNEQIsQLK--KELTNSESENSEK---------------QRELEEKQNEIEKLKKE--------NQS 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1206 LQEKITQAEKERNELavrhKAELEKIRETLKEKESSYKeKLRQAEEERDKEISRLEVMR----NTIAELHKTNSDREVEL 1281
Cdd:TIGR04523 382 YKQEIKNLESQINDL----ESKIQNQEKLNQQKDEQIK-KLQQEKELLEKEIERLKETIiknnSEIKDLTNQDSVKELII 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1282 EGVKMEKCQLKKLYDKSMLELEqlqctadqkssdllpgSSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKINGQHS 1361
Cdd:TIGR04523 457 KNLDNTRESLETQLKVLSRSIN----------------KIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKIS 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1362 NTIKKLEEIEAEMitltTQKELERCEIAEKLETFKS--KEADIKEALhcaqlrlhayDKLVCEYERLKGCLSDSNKLSEN 1439
Cdd:TIGR04523 521 SLKEKIEKLESEK----KEKESKISDLEDELNKDDFelKKENLEKEI----------DEKNKEIEELKQTQKSLKKKQEE 586
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1440 LQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADikgsvd 1519
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK------ 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1520 elqiklkslqevRDHLESRNEELKRKLKDAQELQNMVDKErklnSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELG 1599
Cdd:TIGR04523 661 ------------WPEIIKKIKESKTKIDDIIELMKDWLKE----LSLHYKKYITRMIRIKDLPKLEEKYKEIEKELKKLD 724
|
730
....*....|....*....
gi 78706884 1600 EVTKDCENIRSDLEAQTND 1618
Cdd:TIGR04523 725 EFSKELENIIKNFNKKFDD 743
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
499-1357 |
1.06e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 499 VAKETIEKYEEQVKRLKETIERLEMENGKAvnlgeqfETHKAKSKQMEE----ELLSSISEKDSTIVSLQQSLEELSRdv 574
Cdd:TIGR02169 181 EVEENIERLDLIIDEKRQQLERLRREREKA-------ERYQALLKEKREyegyELLKEKEALERQKEAIERQLASLEE-- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 575 lrnskedqmrsmcpELESSCERICNKCLELERLLPLasasgLDSVACQFDQLRS-EIAATRMKLESMLSTFSHASCEVSQ 653
Cdd:TIGR02169 252 --------------ELEKLTEEISELEKRLEEIEQL-----LEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 654 KTTDCKRLSEQISTAHDDFGQLQEKYNNLKHKWSSQKLAIDTMQVDYNTIQQKYLQLQDEYRHLELRSDEqcqqLQDENS 733
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE----TRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 734 KLQAEIGTLKERVEEIHSELL----EVPNPDTHPEDMELQNQELKKRLSKLQWEFDEIQLNYECLSNELMSTIQECDALR 809
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDrlqeELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 810 EEHKQ-RTTNSDLESmkssgvgtECSDPENELDTDLLQQFTKLSKSIQQIELTDYSGGRRLFIYNHAEQDQSV-PSLKLC 887
Cdd:TIGR02169 469 QELYDlKEEYDRVEK--------ELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVgERYATA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 888 LEPAK-------YLEGDGkqhDASDSVFLKGFLKCQRFQIVKINQeqnlVKEEDRMRDIIfQLKQEVDGKKNLIEEEKEV 960
Cdd:TIGR02169 541 IEVAAgnrlnnvVVEDDA---VAKEAIELLKRRKAGRATFLPLNK----MRDERRDLSIL-SEDGVIGFAVDLVEFDPKY 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 961 INNLRAQITS---LNQIETIKNQNAKTKI--LCEELQTKDTVQTAN-----------KQESQEVLTLKTSLAHLKSKVCE 1024
Cdd:TIGR02169 613 EPAFKYVFGDtlvVEDIEAARRLMGKYRMvtLEGELFEKSGAMTGGsraprggilfsRSEPAELQRLRERLEGLKRELSS 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1025 LQKKLEKQseDEKISELQSdigEISECCLSMELKLADIVNWQAEELRPLDQLQESGVELQhhsTTAEESLNVEKPIQEqt 1104
Cdd:TIGR02169 693 LQSELRRI--ENRLDELSQ---ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS---SLEQEIENVKSELKE-- 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1105 ertltteYERRIEQLEESLQRAQEELSILEKR-------KTDENKSLQLEYMAKIETSENENRSKFRAYCLDLKETQKRY 1177
Cdd:TIGR02169 763 -------LEARIEELEEDLHKLEEALNDLEARlshsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1178 EEQLQQTNE-KLASVTTQCQVHLDVI-KRSLQEKITQAEKERNELAVRHKaELEKIRETLKEKESSYKEKLRQAEEERDK 1255
Cdd:TIGR02169 836 QELQEQRIDlKEQIKSIEKEIENLNGkKEELEEELEELEAALRDLESRLG-DLKKERDELEAQLRELERKIEELEAQIEK 914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1256 EISRLEVMRNTIAELhktnSDREVELEGVKMEkcqlKKLYDKSMLELEQLQCTADQKSSDLLP-GSSN----ENIDDLQK 1330
Cdd:TIGR02169 915 KRKRLSELKAKLEAL----EEELSEIEDPKGE----DEEIPEEELSLEDVQAELQRVEEEIRAlEPVNmlaiQEYEEVLK 986
|
890 900
....*....|....*....|....*..
gi 78706884 1331 KCDQYVQDLELLRGEKAELLSEIQKIN 1357
Cdd:TIGR02169 987 RLDELKEKRAKLEEERKAILERIEEYE 1013
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
930-1498 |
1.41e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 930 VKEEDRMRDIIFQLKQEVDGKKNLIEEEKEVINNLRAQItslnqietiknqnAKTKILCEELQTKDTVQTANKQESQEVL 1009
Cdd:PRK03918 230 VKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERI-------------EELKKEIEELEEKVKELKELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1010 TLKTSLAHLKSKVCELQKKLEKQSedEKISELQSDIGEISEcclsMELKLADIVNWQAEELRPLDQLQESgvelqhhstt 1089
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLE--EEINGIEERIKELEE----KEERLEELKKKLKELEKRLEELEER---------- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1090 aEESLNVEKPIQEQTERTLTTEYERRIEQLEeslqraqEELSILEKRKTDENKSLQleymaKIETSENENRSKfraycld 1169
Cdd:PRK03918 361 -HELYEEAKAKKEELERLKKRLTGLTPEKLE-------KELEELEKAKEEIEEEIS-----KITARIGELKKE------- 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1170 lketqkryEEQLQQTNEKLASVTTQCQvhldVIKRSLQekitqaEKERNELAVRHKAELEKIRETLKE---KESSYKEKL 1246
Cdd:PRK03918 421 --------IKELKKAIEELKKAKGKCP----VCGRELT------EEHRKELLEEYTAELKRIEKELKEieeKERKLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1247 RQAEEERDKEiSRLEVMRNTIAELHKTnsdrEVELEGVKMEKCQLK-KLYDKSMLELEQLQCTADQKSSDLlpgssnENI 1325
Cdd:PRK03918 483 RELEKVLKKE-SELIKLKELAEQLKEL----EEKLKKYNLEELEKKaEEYEKLKEKLIKLKGEIKSLKKEL------EKL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1326 DDLQKKCDQYVQDLELLRGEKAELLSEIQKINGQH----SNTIKKLEEIEAEMITLTTQKElercEIAEKLETFKSKEAD 1401
Cdd:PRK03918 552 EELKKKLAELEKKLDELEEELAELLKELEELGFESveelEERLKELEPFYNEYLELKDAEK----ELEREEKELKKLEEE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1402 IKEALHCAQLRLHAYDKLVCEYERLKGCLSDsnKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKT 1481
Cdd:PRK03918 628 LDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
570
....*....|....*..
gi 78706884 1482 VREAKVGLENSLKAVQE 1498
Cdd:PRK03918 706 REKAKKELEKLEKALER 722
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1320-1551 |
1.55e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1320 SSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQ-KELERcEIAEKLETFKSK 1398
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAElAELEK-EIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1399 EADIKEALHCAQlRLHAYDklvceyeRLKGCLSdsnklSENLQKKVERLHAEQlALQEGISGRDSEIKQLRSELKDAIDE 1478
Cdd:COG4942 103 KEELAELLRALY-RLGRQP-------PLALLLS-----PEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78706884 1479 NKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQE 1551
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1364-1591 |
2.18e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1364 IKKLEEIEAEMITLTTQKE-LER-CEIAEKLETFKSKEADIKEALHCAQL--RLHAYDKLVCEYERLKGCLSDSNKLSEN 1439
Cdd:COG4913 234 FDDLERAHEALEDAREQIElLEPiRELAERYAAARERLAELEYLRAALRLwfAQRRLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1440 LQKKVERLHAEQLALQEGISGRD-SEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADIKGSV 1518
Cdd:COG4913 314 LEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706884 1519 DELQIKLKSLQEVRDHLESRNEELKRKLKDAQ-ELQNMvdKERKLNSSLRedfdkLEQTKLDLEEQLRAKKVEI 1591
Cdd:COG4913 394 EALEEELEALEEALAEAEAALRDLRRELRELEaEIASL--ERRKSNIPAR-----LLALRDALAEALGLDEAEL 460
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1029-1272 |
2.69e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.08 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1029 LEKQSEDEKISELQSDIGEISEcclsMELKLADIvnwqAEELRPLDQLQESGVELQHHSTTAEESLNVEKPIQEQTERTL 1108
Cdd:COG4913 218 LEEPDTFEAADALVEHFDDLER----AHEALEDA----REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1109 TTEYERRIEQLEESLQRAQEELSILEKRKTDENKSLQlEYMAKIETSENENRSkfrayclDLKETQKRYEEQLQQTNEKL 1188
Cdd:COG4913 290 LELLEAELEELRAELARLEAELERLEARLDALREELD-ELEAQIRGNGGDRLE-------QLEREIERLERELEERERRR 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1189 ASVTTQCqvhldvikRSLQEKITQAEKERNEL---AVRHKAELEKIRETLKEKESSYKEKLRQAEEERD---KEISRLEV 1262
Cdd:COG4913 362 ARLEALL--------AALGLPLPASAEEFAALraeAAALLEALEEELEALEEALAEAEAALRDLRRELReleAEIASLER 433
|
250
....*....|.
gi 78706884 1263 MRNTI-AELHK 1272
Cdd:COG4913 434 RKSNIpARLLA 444
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1227-1780 |
3.88e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 55.83 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1227 ELEKIRETLKEKESSYKEKLRQAEEERDKeisrLEVMRNTIAELhKTNSDREVELEGVKMEKCqlKKLYDKSMLELEQLQ 1306
Cdd:TIGR01612 752 DLNKILEDFKNKEKELSNKINDYAKEKDE----LNKYKSKISEI-KNHYNDQINIDNIKDEDA--KQNYDKSKEYIKTIS 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1307 CTADQKSSDLlpGSSNENIDDLQKKCDQYV---------------QDLELLRGEKAELLSEIQKINGQHSNTIKKL---- 1367
Cdd:TIGR01612 825 IKEDEIFKII--NEMKFMKDDFLNKVDKFInfennckekidseheQFAELTNKIKAEISDDKLNDYEKKFNDSKSLinei 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1368 -EEIEAEMITLTTQKE----LERCE-IAEKLETFKSKEADIKEalhcaqlRLHAYDKLVCEYERLKGclSDSNKLSENLQ 1441
Cdd:TIGR01612 903 nKSIEEEYQNINTLKKvdeyIKICEnTKESIEKFHNKQNILKE-------ILNKNIDTIKESNLIEK--SYKDKFDNTLI 973
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1442 KKVERLHA--EQLALQEgISGRDSEIKQLRSELKDAIDENKtvreakvglENSLKAVQENMSAQEGQFKQKIADIKGSVD 1519
Cdd:TIGR01612 974 DKINELDKafKDASLND-YEAKNNELIKYFNDLKANLGKNK---------ENMLYHQFDEKEKATNDIEQKIEDANKNIP 1043
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1520 ELQIKL-KSLQEVRDHLES---RNEEL--KRKLKDAQ-ELQNMVDKERKLNSSLREDFDKLEQTKL-----DLEEQLRAK 1587
Cdd:TIGR01612 1044 NIEIAIhTSIYNIIDEIEKeigKNIELlnKEILEEAEiNITNFNEIKEKLKHYNFDDFGKEENIKYadeinKIKDDIKNL 1123
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1588 KVEIDRRSKELGEVTKDCENIRSDLEAQTNDFLKeretlnltISDLRLHNEQLLETSK---NYLSDITAANNLNLEMKKN 1664
Cdd:TIGR01612 1124 DQKIDHHIKALEEIKKKSENYIDEIKAQINDLED--------VADKAISNDDPEEIEKkieNIVTKIDKKKNIYDEIKKL 1195
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1665 LHDLTKECKSLRSDLQSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKALKE-DCEKLRSTLESKELILQQNKQEL 1743
Cdd:TIGR01612 1196 LNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEHMIKAMEAYIEDlDEIKEKSPEIENEMGIEMDIKAE 1275
|
570 580 590
....*....|....*....|....*....|....*..
gi 78706884 1744 EERLTVINEKNGKNALLDaqlKSNETAFTSLRKAWIK 1780
Cdd:TIGR01612 1276 METFNISHDDDKDHHIIS---KKHDENISDIREKSLK 1309
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1169-1730 |
8.67e-07 |
|
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: 53.98 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1169 DLKETQKRYEEQLQQTNEKLASVTTQCQVHLDViKRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKES-SYKEKLR 1247
Cdd:pfam05557 17 EKKQMELEHKRARIELEKKASALKRQLDRESDR-NQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEAlNKKLNEK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1248 QAEEERDKEISRleVMRNTIAELHKTNSDREVELEGVKMEKCQLK---KLYDKSMLELEQLQCTADQKSSDLLpgSSNEN 1324
Cdd:pfam05557 96 ESQLADAREVIS--CLKNELSELRRQIQRAELELQSTNSELEELQerlDLLKAKASEAEQLRQNLEKQQSSLA--EAEQR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1325 IDDLQKKCDQYVQDLELLRGEKAELLS--EIQKINGQHSNTIKKLEEIEAEMITLTTQKElerceiaeKLETFKSKEADI 1402
Cdd:pfam05557 172 IKELEFEIQSQEQDSEIVKNSKSELARipELEKELERLREHNKHLNENIENKLLLKEEVE--------DLKRKLEREEKY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1403 KEALHCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTV 1482
Cdd:pfam05557 244 REEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1483 REAKVGLENSLKavqeNMSAQEGQFKQKIADIKGSVDELQIKLKSLqevrDHLESRNEELKRKLKDAQELQNMVDKERKL 1562
Cdd:pfam05557 324 LKKIEDLNKKLK----RHKALVRRLQRRVLLLTKERDGYRAILESY----DKELTMSNYSPQLLERIEEAEDMTQKMQAH 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1563 NSSLREDFDKLEQTKLDLEEQLRAKKVEID-RRSKELgevtkdcenirsdleaqtndfLKERETLNLTISDLRLHNEQLL 1641
Cdd:pfam05557 396 NEEMEAQLSVAEEELGGYKQQAQTLERELQaLRQQES---------------------LADPSYSKEEVDSLRRKLETLE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1642 etsknylsditaANNLNLEMKKNLHDLTKECKSLRSDLQSKEEYFQtqkQLLDETISNLKEENRKMEEKLSSGNKALKED 1721
Cdd:pfam05557 455 ------------LERQRLREQKNELEMELERRCLQGDYDPKKTKVL---HLSMNPAAEAYQQRKNQLEKLQAEIERLKRL 519
|
....*....
gi 78706884 1722 CEKLRSTLE 1730
Cdd:pfam05557 520 LKKLEDDLE 528
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1529-1779 |
1.20e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1529 QEVRDHLESRNEELKRKLKDAQELQNMVDKERKlnsSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENI 1608
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEK---ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1609 RSDLEAQTNDFlkeRETLNLTISDLRLHNEQLLETSKNYLSDITAANNLNlEMKKNLHDLTKECKSLRSDLQSKEEYFQT 1688
Cdd:COG4942 96 RAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLK-YLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1689 QKQLLDETISNLKEENRKMEEKLSSGNKALKEDcEKLRSTLESKELILQQNKQELEERLTVINEkngknALLDAQLKSNE 1768
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARL-EKELAELAAELAELQQEAEELEALIARLEA-----EAAAAAERTPA 245
|
250
....*....|.
gi 78706884 1769 TAFTSLRKAWI 1779
Cdd:COG4942 246 AGFAALKGKLP 256
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
924-1647 |
1.40e-06 |
|
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: 53.49 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 924 NQEQNLVKEEDRMRDIIFQLKQEVDGKKNLIEEEKEVINNLRAQITSLNQ-IETIKNQNAKTKILCEELqTKDTVQTAN- 1001
Cdd:TIGR04523 33 TEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQqIKDLNDKLKKNKDKINKL-NSDLSKINSe 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1002 -KQESQEVLTLKTSLAHLKSKVCELQKKLEKQSEDekISELQSDIGEISEcclsmelKLADIVNWQAEELRPLDQLQESG 1080
Cdd:TIGR04523 112 iKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTE--IKKKEKELEKLNN-------KYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1081 VELQHHSTTAEESLNvekpiQEQTERTLTTEYERRIEQLEESLQRAQEELSILEKRKTDENKSLQlEYMAKIETSENEnr 1160
Cdd:TIGR04523 183 LNIQKNIDKIKNKLL-----KLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN-EKTTEISNTQTQ-- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1161 skfrayCLDLKETQKRYEEQLQQTneklasvttqcQVHLDVIKRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKES 1240
Cdd:TIGR04523 255 ------LNQLKDEQNKIKKQLSEK-----------QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1241 SYKEKLRQAEEERDKEISRLEVMRNTIAELHKT-------NSDREVELEGVKMEKCQLKKLYDKSMLELEQLQctadQKS 1313
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKIISQLNEQISQLKKEltnseseNSEKQRELEEKQNEIEKLKKENQSYKQEIKNLE----SQI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1314 SDLlpgssNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKI---NGQHSNTIKKLEEIEAEMITLTTQKELERCEIAE 1390
Cdd:TIGR04523 394 NDL-----ESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLketIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1391 KLETFKSKEADIKEALHCAQLRLhayDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRS 1470
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKEL---KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1471 ELKDAIDENKtvreaKVGLENSLKAVQENMSaqegQFKQKIADIKGSVDELQIKLKSLQEVRDHLesrNEELKRKLKDAQ 1550
Cdd:TIGR04523 546 ELNKDDFELK-----KENLEKEIDEKNKEIE----ELKQTQKSLKKKQEEKQELIDQKEKEKKDL---IKEIEEKEKKIS 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1551 ELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQL----------RAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDFL 1620
Cdd:TIGR04523 614 SLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVkqiketikeiRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHY 693
|
730 740
....*....|....*....|....*..
gi 78706884 1621 KERETLNLTISDLRLHNEQLLETSKNY 1647
Cdd:TIGR04523 694 KKYITRMIRIKDLPKLEEKYKEIEKEL 720
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1113-1588 |
1.54e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 53.37 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1113 ERRIEQLEESLQRAQEELSILEKrKTDENKSLQLEYMAKIETSENENRSKFRAYCldlketqkRYEEQLQQTNEKLASVT 1192
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELE-KNNYYKELEERHMKIINDPVYKNRNYINDYF--------KYKNDIENKKQILSNID 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1193 TQCQVHLDVIKrslqeKITQAEKERNELAV--RHKAELEKIRETLKEKESSYKEKLRQAEEERDKEISRLEVMRNTIAEL 1270
Cdd:PRK01156 319 AEINKYHAIIK-----KLSVLQKDYNDYIKkkSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1271 HKTNSDREVELEGVKMEKCQLKKLYDKSMLELEQLQCTADQKSSDLLPGSSNENIDDLQKKC----------------DQ 1334
Cdd:PRK01156 394 SEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCpvcgttlgeeksnhiiNH 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1335 YVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELERCEIAEKLETFKSKEADIKEALHCAQLRLH 1414
Cdd:PRK01156 474 YNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKN 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1415 AYDKLVCE------YERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAI---DENKTVREA 1485
Cdd:PRK01156 554 RYKSLKLEdldskrTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIreiENEANNLNN 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1486 KVGLENSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDkerklnsS 1565
Cdd:PRK01156 634 KYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIE-------I 706
|
490 500
....*....|....*....|...
gi 78706884 1566 LREDFDKLEQTKLDLEEQLRAKK 1588
Cdd:PRK01156 707 LRTRINELSDRINDINETLESMK 729
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1333-1777 |
2.31e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 52.65 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1333 DQYVQDLELLRGEKAELLSE--IQKINGQHSNTIKKLEEIEAEMITLT----TQKELERCEIAEKLETFKSKEADIkEAL 1406
Cdd:COG5185 117 DILISLLYLYKSEIVALKDEliKVEKLDEIADIEASYGEVETGIIKDIfgklTQELNQNLKKLEIFGLTLGLLKGI-SEL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1407 HCAQLRLHAYDKLVCEYERLKGclsdSNKLSENLQKKVERLHAEQLAlqEGISGRDSEIKQLRSELKDAIDENKTVREAK 1486
Cdd:COG5185 196 KKAEPSGTVNSIKESETGNLGS----ESTLLEKAKEIINIEEALKGF--QDPESELEDLAQTSDKLEKLVEQNTDLRLEK 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1487 VGLEN-SLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLkslqevrdHLESRNEELKRklkdAQELQNMVDKERKLNSS 1565
Cdd:COG5185 270 LGENAeSSKRLNENANNLIKQFENTKEKIAEYTKSIDIKK--------ATESLEEQLAA----AEAEQELEESKRETETG 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1566 LREDFDKLEQTKLDLEEQLRAKKVEID---------RRSKELGEVTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLH 1636
Cdd:COG5185 338 IQNLTAEIEQGQESLTENLEAIKEEIEnivgevelsKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKA 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1637 NEQLLEtskNYLSDITAANNLNLEMKKNLHDLTKECKSLRSDLQSKEEYFQTQKQllDETISNLKEENRKMEEKLSSGNK 1716
Cdd:COG5185 418 ADRQIE---ELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAY--DEINRSVRSKKEDLNEELTQIES 492
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78706884 1717 ALKEDCEKLRSTLESKELILQQNKQELEERLTVINEKNGKNALLDAQLKSNETAFTSLRKA 1777
Cdd:COG5185 493 RVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQA 553
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
943-1394 |
2.39e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 943 LKQEVDGKKNLIEEEKEVINNLRAQI--------TSLNQIETIKNQNAKTKilcEELQTKDT-VQTANKQ---ESQEVLT 1010
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAglddadaeAVEARREELEDRDEELR---DRLEECRVaAQAHNEEaesLREDADD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1011 LKTSLAHLKSKVCELQKKLEKQSED-----EKISELQSDIGEISECCLSMELKLADIVNWQAEELRPLDQLQESGVELQH 1085
Cdd:PRK02224 354 LEERAEELREEAAELESELEEAREAvedrrEEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEA 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1086 HSTTAEESLN-------------VEKPIQEQTERTLTTEYERRIEQLEESLQRAQEELSILEKRkTDENKSLQlEYMAKI 1152
Cdd:PRK02224 434 TLRTARERVEeaealleagkcpeCGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEER-LERAEDLV-EAEDRI 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1153 ETSEnENRSKFRAYCLDLKETQKRYEEQLQQTNEKLASVTTQCQVHLDvikrSLQEKITQAEKERNELavrhkAELEKIR 1232
Cdd:PRK02224 512 ERLE-ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKRE----AAAEAEEEAEEAREEV-----AELNSKL 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1233 ETLKEKESSYkEKLRQAEEERDKEISRLEVMRNTIAELHKTNSDREVELEGVKMEKCQLKKLYDKSMLEleqlqcTADQK 1312
Cdd:PRK02224 582 AELKERIESL-ERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIE------EARED 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1313 ssdllpgssNENIDDLQKKCDQYvqdLELLRGEKAELLSEIqkinGQHSNTIKKLEEIEAEMITLTTQKE-LERC-EIAE 1390
Cdd:PRK02224 655 ---------KERAEEYLEQVEEK---LDELREERDDLQAEI----GAVENELEELEELRERREALENRVEaLEALyDEAE 718
|
....
gi 78706884 1391 KLET 1394
Cdd:PRK02224 719 ELES 722
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
925-1316 |
3.37e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.42 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 925 QEQNLVKEEDRMRDIIFQLKQevdgKKNLIEEEKEVINNLRAQITSLNQI----ETIKNQNAKTKILCEELQTKDT---- 996
Cdd:pfam05483 368 EQQRLEKNEDQLKIITMELQK----KSSELEEMTKFKNNKEVELEELKKIlaedEKLLDEKKQFEKIAEELKGKEQelif 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 997 -VQTANKQESQ---EVLTLKTSLAHLKSKVCELQKKLEKQ---------SEDEKISELQSDIGEISECCLSMELKLADIV 1063
Cdd:pfam05483 444 lLQAREKEIHDleiQLTAIKTSEEHYLKEVEDLKTELEKEklknieltaHCDKLLLENKELTQEASDMTLELKKHQEDII 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1064 NWQAEELRPLDQ---LQESGVELQHHSTTAEESLNVEK-PIQEQTERTLTTEYERRIEQLEESLQRAQEELSILEKRKTD 1139
Cdd:pfam05483 524 NCKKQEERMLKQienLEEKEMNLRDELESVREEFIQKGdEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1140 ENKSLQLEYMAKiETSENENRSKFRAYCLDLKETQ-KRYEEQLQQTNEKLASVTTQCQVHLDVIKRSLQEKITQAEKERN 1218
Cdd:pfam05483 604 ENKNKNIEELHQ-ENKALKKKGSAENKQLNAYEIKvNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKA 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1219 --ELAVRHKAELE-----KIRETLKEKESsYKEKLRQAEEERDKEisrLEVMRNTIAELHKTNSDREVELEGVKMEKCQL 1291
Cdd:pfam05483 683 iaDEAVKLQKEIDkrcqhKIAEMVALMEK-HKHQYDKIIEERDSE---LGLYKNKEQEQSSAKAALEIELSNIKAELLSL 758
|
410 420
....*....|....*....|....*
gi 78706884 1292 KKLYDKSMLELEQLQCTADQKSSDL 1316
Cdd:pfam05483 759 KKQLEIEKEEKEKLKMEAKENTAIL 783
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1462-1626 |
3.79e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1462 DSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSAQEgqfkQKIADIKGSVDELQIKLKSLQEvrdHLESRNEE 1541
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ----AELEALQAEIDKLQAEIAEAEA---EIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1542 LKRKLKDAQE--------------------------LQNMVDKERKLNSSLREDFDKLEQTKLDLEEQ---LRAKKVEID 1592
Cdd:COG3883 88 LGERARALYRsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKlaeLEALKAELE 167
|
170 180 190
....*....|....*....|....*....|....
gi 78706884 1593 RRSKELGEVTKDCENIRSDLEAQTNDFLKERETL 1626
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAEL 201
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1029-1298 |
6.24e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 51.08 E-value: 6.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1029 LEKQSEDEKISELQSDIGEISECcLSmelKLADIVNWQAEELRPLDQLQESGVE-LQHHSttAEESLNVEKPIQEQTERT 1107
Cdd:PRK05771 36 LKEELSNERLRKLRSLLTKLSEA-LD---KLRSYLPKLNPLREEKKKVSVKSLEeLIKDV--EEELEKIEKEIKELEEEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1108 ltTEYERRIEQLEESLQRAQ------EELSILEKRKT--------DENKSLQLEYMAKIETSENENRSKFRAYCL--DLK 1171
Cdd:PRK05771 110 --SELENEIKELEQEIERLEpwgnfdLDLSLLLGFKYvsvfvgtvPEDKLEELKLESDVENVEYISTDKGYVYVVvvVLK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1172 ETQKRYEEQLQQTNEKLASVTTqcqvhldviKRSLQEKITQAEKERNELavrhKAELEKIRETLKEKESSYKEKLRQAEE 1251
Cdd:PRK05771 188 ELSDEVEEELKKLGFERLELEE---------EGTPSELIREIKEELEEI----EKERESLLEELKELAKKYLEELLALYE 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 78706884 1252 ERDKEISRLEVMRNTiaelhkTNSDREVELEG---VKMEKcQLKKLYDKS 1298
Cdd:PRK05771 255 YLEIELERAEALSKF------LKTDKTFAIEGwvpEDRVK-KLKELIDKA 297
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1172-1553 |
8.27e-06 |
|
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: 50.89 E-value: 8.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1172 ETQKRYEEQLQQTNEKLASVTTQCQVHLDVIKRSLQEKITQAEKERnelaVRHKAElEKIRETLKEKESSYKEKLRQAEE 1251
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQER----LRQEKE-EKAREVERRRKLEEAEKARQAEM 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1252 ERDKEI----SRLEVMRNTiaELHKTN-SDREVELEGVKMEKCQLKKlydKSMLELEQLQCTADQKSSDL---LPGSSNE 1323
Cdd:pfam17380 330 DRQAAIyaeqERMAMERER--ELERIRqEERKRELERIRQEEIAMEI---SRMRELERLQMERQQKNERVrqeLEAARKV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1324 NI--DDLQKKCDQYVQDLELLRGEKAELLSEiqkingqhsnTIKKLEEIEAEMITLTTQKELERceiAEKLETFKSKEAD 1401
Cdd:pfam17380 405 KIleEERQRKIQQQKVEMEQIRAEQEEARQR----------EVRRLEEERAREMERVRLEEQER---QQQVERLRQQEEE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1402 IKEalhcaqlrlhayDKLVCEYERLKgclsdsNKLSENLQKKVerLHAEQLALQEGISGRDSEIKQLRSELKD---AIDE 1478
Cdd:pfam17380 472 RKR------------KKLELEKEKRD------RKRAEEQRRKI--LEKELEERKQAMIEEERKRKLLEKEMEErqkAIYE 531
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78706884 1479 NKTVREAKvglenslkavQENMSAQEGQFKQKIadikgsvdelQIKLKSLQEVRDHLES--RNEELKRKLKDAQELQ 1553
Cdd:pfam17380 532 EERRREAE----------EERRKQQEMEERRRI----------QEQMRKATEERSRLEAmeREREMMRQIVESEKAR 588
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1491-1627 |
1.18e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.77 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1491 NSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNS------ 1564
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEAlqkeie 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78706884 1565 SLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDFLKERETLN 1627
Cdd:COG1579 100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1101-1315 |
1.23e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1101 QEQTERTLTTEYERRIEQLEESLQRAQEELSILEKRKTD---ENKSLQLEYMAKIETSE-NENRSKFRAYCLDLKETQKR 1176
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqKNGLVDLSEEAKLLLQQlSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1177 Y---EEQLQQTNEKLASVTTqcqvhlDVIKRSLQEKITQAEKERNELAVRHKAE-------LEKIRETLKEKESSYKEKL 1246
Cdd:COG3206 242 LaalRAQLGSGPDALPELLQ------SPVIQQLRAQLAELEAELAELSARYTPNhpdvialRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78706884 1247 RQAEEERDKEISRLEVMRNTIAELH---KTNSDREVELEGVKMEKCQLKKLYDKSMLELEQLQCTADQKSSD 1315
Cdd:COG3206 316 ASLEAELEALQAREASLQAQLAQLEarlAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1235-1834 |
1.60e-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: 50.12 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1235 LKEKESSYkekLRQAEEERDKEISRLEVMRNTIAELHKTNSDREVELegvkmeKCQLKKlydkSMLELEQLQCTADQKSS 1314
Cdd:pfam15921 100 LHEKQKFY---LRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDL------RNQLQN----TVHELEAAKCLKEDMLE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1315 DllpgsSNENIDDLQK----------KCDQYVQDLELLRGEKAELLSEIQKINGQHSNTI--KKLEEIEAEMITLTTQKe 1382
Cdd:pfam15921 167 D-----SNTQIEQLRKmmlshegvlqEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAisKILRELDTEISYLKGRI- 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1383 lerCEIAEKLETFKSKEADIKEALhcAQLRLHAYDKLVCEYE--------RLKGCLSDSNKLSENLQKKVERLHAEQLAL 1454
Cdd:pfam15921 241 ---FPVEDQLEALKSESQNKIELL--LQQHQDRIEQLISEHEveitglteKASSARSQANSIQSQLEIIQEQARNQNSMY 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1455 QEGISGRDSEIKQLRSELKDA--IDENKTVR-EAKVGLENS----LKAVQENMSAQEG----QFKQKIADIKGSVDELQI 1523
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAkrMYEDKIEElEKQLVLANSelteARTERDQFSQESGnlddQLQKLLADLHKREKELSL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1524 KLK--------------SLQEVRDHLESRNEELKRK---LKDAQ-ELQNMVDKERKLNSSLREDFDKLEQTKLDLE---- 1581
Cdd:pfam15921 396 EKEqnkrlwdrdtgnsiTIDHLRRELDDRNMEVQRLealLKAMKsECQGQMERQMAAIQGKNESLEKVSSLTAQLEstke 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1582 ------EQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDFLKERETLnltisDLRLHNEQLLETSKNYLSDITAan 1655
Cdd:pfam15921 476 mlrkvvEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRV-----DLKLQELQHLKNEGDHLRNVQT-- 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1656 nlnlemkknlhdltkECKSLRSDLQSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKALKEdceklrstleskeli 1735
Cdd:pfam15921 549 ---------------ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKE--------------- 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1736 LQQNKQELEERLTVINEKNGKNALLDAQLKSNETAFTSLRKAWIKQSLAIEAANKRSLEMEQKVDKRTREYEELRSTLKT 1815
Cdd:pfam15921 599 INDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEV 678
|
650
....*....|....*....
gi 78706884 1816 REINFRSEKERMDGTISSL 1834
Cdd:pfam15921 679 LKRNFRNKSEEMETTTNKL 697
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1489-1850 |
1.62e-05 |
|
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: 49.51 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1489 LENSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLRE 1568
Cdd:pfam07888 46 LLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1569 D----FDKLEQTKLDLEEQLRAKKVEIDR---RSKELGEVTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHNEQ-- 1639
Cdd:pfam07888 126 AhearIRELEEDIKTLTQRVLERETELERmkeRAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQrd 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1640 -----LLETSKNYLSDITAANNLNLEMKKnlhdLTKECKSLRSDLQSKEEYFQTQKQLL-------DETISNLKE---EN 1704
Cdd:pfam07888 206 tqvlqLQDTITTLTQKLTTAHRKEAENEA----LLEELRSLQERLNASERKVEGLGEELssmaaqrDRTQAELHQarlQA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1705 RKMEEKLSSGNKALKEDceklRSTLESKELILQQNKQELEERLtvinekngknALLDAQLKSNETAFTSLRKAwiKQSLA 1784
Cdd:pfam07888 282 AQLTLQLADASLALREG----RARWAQERETLQQSAEADKDRI----------EKLSAELQRLEERLQEERME--REKLE 345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78706884 1785 IEAANKRSLEMEQKVDKRtREYEELRSTLKTreinFRSEKERMDGTISSLLEDKRNLEEKLCTVTE 1850
Cdd:pfam07888 346 VELGREKDCNRVQLSESR-RELQELKASLRV----AQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1438-1858 |
1.65e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1438 ENLQKKVERLHAEQLALQEGISgrdsEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQenMSAQEGQFKQKIADIKGS 1517
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQE----ELEELEEELEELEAELEELREELEKLEKLLQLLP--LYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1518 VDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLN-SSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSK 1596
Cdd:COG4717 148 LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1597 ELGEVTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHNEQLLETSKNYLSDITAANNLNLEMkknlhdLTKECKSLR 1676
Cdd:COG4717 228 ELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL------LAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1677 SDLQSKEEyFQTQKQLLDETISNLKEENRKMEEKLSSGNKALKEDCEKLRStleskeliLQQNKQELEERLTVINEKNGK 1756
Cdd:COG4717 302 KEAEELQA-LPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE--------LLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1757 NALLDAQLKSNETAFTslrkAWIKQSLAIEAANKRSLEMEQKVDKRTREYEELRSTLKTREInfRSEKERMDGTISSLLE 1836
Cdd:COG4717 373 AALLAEAGVEDEEELR----AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL--EEELEELEEELEELEE 446
|
410 420
....*....|....*....|..
gi 78706884 1837 DKRNLEEKLCTVTELLAKLKRE 1858
Cdd:COG4717 447 ELEELREELAELEAELEQLEED 468
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1061-1602 |
1.79e-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: 49.72 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1061 DIVNWQAEELRPLDQLQESGVELQHHSTTAEESLNVekpiqeQTERTLTTEyerriEQLEESLQRAQEELSILEkrktdE 1140
Cdd:pfam05483 268 DKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKM------SLQRSMSTQ-----KALEEDLQIATKTICQLT-----E 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1141 NKSLQLEYMAKIETSENENRSKFRAYCLDLKETQKRYEEQLQQTNEKLASVTTQCQ---VHLDVIKRSLQEKITQAEKER 1217
Cdd:pfam05483 332 EKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQkksSELEEMTKFKNNKEVELEELK 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1218 NELA-----VRHKAELEKIRETLKEKEssykEKLRQAEEERDKEISRLEVMRNTI--AELH--KTNSDREVELEGVKMEK 1288
Cdd:pfam05483 412 KILAedeklLDEKKQFEKIAEELKGKE----QELIFLLQAREKEIHDLEIQLTAIktSEEHylKEVEDLKTELEKEKLKN 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1289 CQLKKLYDKSMLELEQLQctadQKSSDLLpgssneniddLQKKCDQyvQDLELLRGEKAELLSEIQKINGQHSNTIKKLE 1368
Cdd:pfam05483 488 IELTAHCDKLLLENKELT----QEASDMT----------LELKKHQ--EDIINCKKQEERMLKQIENLEEKEMNLRDELE 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1369 EIEAEMItltTQKELERCEIAEKLETFKSKEADIKEALHCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLH 1448
Cdd:pfam05483 552 SVREEFI---QKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1449 AEQLALQEGISGRDSEIKQLRSELKDAIDE-NKTVREAKVGLENSLKAVQE-NMSAQEGQFKQKIADIKGS---VDELQI 1523
Cdd:pfam05483 629 KQLNAYEIKVNKLELELASAKQKFEEIIDNyQKEIEDKKISEEKLLEEVEKaKAIADEAVKLQKEIDKRCQhkiAEMVAL 708
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78706884 1524 KLKSLQEVRDHLESRNEELKRKLKDAQElqnmvdkERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVT 1602
Cdd:pfam05483 709 MEKHKHQYDKIIEERDSELGLYKNKEQE-------QSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
987-1263 |
2.03e-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: 49.74 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 987 LCEELQTKDTVQTANKQESQEVLTLKTSLAHLKSKVCELQKKLEKQSEDEKISELQsdigEISECCLSMELkladivnwq 1066
Cdd:pfam17380 308 KAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELE----RIRQEEIAMEI--------- 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1067 aEELRPLDQLQesgVELQHHSTTAEESLNVEKP--IQEQTERTLTTEYERRIEQLEESLQRA-QEELSILEKRKTDENKS 1143
Cdd:pfam17380 375 -SRMRELERLQ---MERQQKNERVRQELEAARKvkILEEERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAREMER 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1144 LQLEYMAKIETSE-----NENRSKFRAYCLDLKETQKRYEEQLQQTNEKLASVTTQCQVHLDVIKRSLQEKITQAEKERN 1218
Cdd:pfam17380 451 VRLEEQERQQQVErlrqqEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIY 530
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 78706884 1219 ELAVRHKAELEKIRETLKEKESSYKEKLRQAEEERdkeiSRLEVM 1263
Cdd:pfam17380 531 EEERRREAEEERRKQQEMEERRRIQEQMRKATEER----SRLEAM 571
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1199-1705 |
2.44e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1199 LDVIKRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKESSYKEkLRQAEEERDKEISRLEVMRNTIAEL--HKTNSD 1276
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELreELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1277 REVELEGVKMEKCQLKKLYDKSMLELEQLQctadqkssdllpgssneniddlqkkcdQYVQDLELLRGEKAELLSEIQKI 1356
Cdd:COG4717 123 KLLQLLPLYQELEALEAELAELPERLEELE---------------------------ERLEELRELEEELEELEAELAEL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1357 NgqhsntikklEEIEAEMITLTTQKELERCEIAEKLETFKSKEADIKEALHCAQLRLHAYDKLVCEYERLKGCLSDSNKL 1436
Cdd:COG4717 176 Q----------EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1437 SEnlqkkvERLHAEQLALQEGISGRDSEIKQLRSELKDAIdenkTVREAKVGLENSLKAVQENMSAQEGQFKQKIADIKG 1516
Cdd:COG4717 246 KE------ARLLLLIAAALLALLGLGGSLLSLILTIAGVL----FLVLGLLALLFLLLAREKASLGKEAEELQALPALEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1517 SVDELQIKLKSLQEVRDHLE-SRNEELKRKLKDAQELQNMVD---KERKLNSSLREDFDKLEQTKLDLEEQLRAkKVEID 1592
Cdd:COG4717 316 LEEEELEELLAALGLPPDLSpEELLELLDRIEELQELLREAEeleEELQLEELEQEIAALLAEAGVEDEEELRA-ALEQA 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1593 RRSKELgevTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHN--EQLLETSKNYLSDITAANNLNLEMKK-----NL 1665
Cdd:COG4717 395 EEYQEL---KEELEELEEQLEELLGELEELLEALDEEELEEELEEleEELEELEEELEELREELAELEAELEQleedgEL 471
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 78706884 1666 HDLTKECKSLRSDLQSKEEYFQTQK---QLLDETISNLKEENR 1705
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAALKlalELLEEAREEYREERL 514
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
958-1485 |
2.70e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 958 KEVINNLRAQITSLNQIEtiknqnaktkilcEELQTK-DTVQTANKQESQEVLTLKTSLAHLKSKVCELQKKL-EKQSED 1035
Cdd:PRK01156 172 KDVIDMLRAEISNIDYLE-------------EKLKSSnLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMdDYNNLK 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1036 EKISELQSDIGEISEccLSMELKLADI-VNWQAEELRPLDQLQESGVELQHHSTTAE-----ESLNVEKPIQEQTE---- 1105
Cdd:PRK01156 239 SALNELSSLEDMKNR--YESEIKTAESdLSMELEKNNYYKELEERHMKIINDPVYKNrnyinDYFKYKNDIENKKQilsn 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1106 -RTLTTEYERRIEQLEEsLQRAQEELSILEKRKTDENKSLQ-----------------------LEYMAKIETSENENRS 1161
Cdd:PRK01156 317 iDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDDLNNQILelegyemdynsylksieslkkkiEEYSKNIERMSAFISE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1162 KFRAYCLDLKETQKRYEE---QLQQTNEKLASvttqcqvhLDVIKRSLQEKITQAEKERNELAVRHKA----------EL 1228
Cdd:PRK01156 396 ILKIQEIDPDAIKKELNEinvKLQDISSKVSS--------LNQRIRALRENLDELSRNMEMLNGQSVCpvcgttlgeeKS 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1229 EKIRETLKEKESSYKEKLRQAE-------EERDKEISRLEVM-----RNTIAELHKTnSDREVELEGVKMEKCQLKKLYD 1296
Cdd:PRK01156 468 NHIINHYNEKKSRLEEKIREIEievkdidEKIVDLKKRKEYLeseeiNKSINEYNKI-ESARADLEDIKIKINELKDKHD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1297 KSMLELEQLQCTA----DQKSSD---LLPGSSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEE 1369
Cdd:PRK01156 547 KYEEIKNRYKSLKledlDSKRTSwlnALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIEN 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1370 iEAEM----ITLTTQKELERCEIAEKLETFKSKEADIKEALHCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVE 1445
Cdd:PRK01156 627 -EANNlnnkYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIE 705
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 78706884 1446 RLHAEQLALQEGISGRDSEIKQLRSeLKDAIDENKTVREA 1485
Cdd:PRK01156 706 ILRTRINELSDRINDINETLESMKK-IKKAIGDLKRLREA 744
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1653-1865 |
3.75e-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: 48.22 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1653 AANNLNLEMKKNLHDLTKECKSLRSDL---QSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKALKEdcekLRSTL 1729
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELaalKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE----LEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1730 ESKELILQQNKQELEERLTVInEKNGKNALLDAQLKSNETAFTSLRKAWIKQslaieaankrsleMEQKVDKRTREYEEL 1809
Cdd:COG4942 93 AELRAELEAQKEELAELLRAL-YRLGRQPPLALLLSPEDFLDAVRRLQYLKY-------------LAPARREQAEELRAD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 78706884 1810 RSTLKTREINFRSEKERMDGTISSLLEDKRNLEEKLCTVTELLAKLKRELPALHTQ 1865
Cdd:COG4942 159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1126-1880 |
4.98e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.89 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1126 AQEELSILEKRKTDE-------NKSLQLEYM-----------AKIETSENENRSKFRAYCLDLKETQKRYEEQLQQTNEK 1187
Cdd:TIGR01612 881 SDDKLNDYEKKFNDSkslineiNKSIEEEYQnintlkkvdeyIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLI 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1188 LASVTTQCQVHLDVIKRSLQEKITQA-----EKERNELAVRH---KAELEKIRETLKEKESSYKEK----LRQAEEERDK 1255
Cdd:TIGR01612 961 EKSYKDKFDNTLIDKINELDKAFKDAslndyEAKNNELIKYFndlKANLGKNKENMLYHQFDEKEKatndIEQKIEDANK 1040
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1256 EISRLEV-----MRNTIAELHK----------TNSDREVELEGVKMEKCQLK-KLYDKSMLELEQLQCTADQKSSdllpg 1319
Cdd:TIGR01612 1041 NIPNIEIaihtsIYNIIDEIEKeigkniellnKEILEEAEINITNFNEIKEKlKHYNFDDFGKEENIKYADEINK----- 1115
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1320 sSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKingqhsnTIKKLEEIEAEMITLTTQKELERCE--IAEKLETFKS 1397
Cdd:TIGR01612 1116 -IKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKA-------QINDLEDVADKAISNDDPEEIEKKIenIVTKIDKKKN 1187
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1398 KEADIKEALHcaqlrlhaydkLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISgrDSEIKQLRSELKD--A 1475
Cdd:TIGR01612 1188 IYDEIKKLLN-----------EIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKS--EHMIKAMEAYIEDldE 1254
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1476 IDENKTVREAKVGLENSLKAVQENMSAQEGQFKQK-IADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKlkdaqELQN 1554
Cdd:TIGR01612 1255 IKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHhIISKKHDENISDIREKSLKIIEDFSEESDINDIKK-----ELQK 1329
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1555 MVDKERKLNSSLREDFDKLEqtklDLEEQLRAKKVE--IDRRSKELGEVTKDCENIRSDLEAQTNDFLKERETLNLTISD 1632
Cdd:TIGR01612 1330 NLLDAQKHNSDINLYLNEIA----NIYNILKLNKIKkiIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECK 1405
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1633 LRLHNE----------QLLETSKNY-LSDITAANNLNLEMKKNLHDLTKECKSLRSDLQSKEEYFQTQKQL----LDETI 1697
Cdd:TIGR01612 1406 SKIESTlddkdideciKKIKELKNHiLSEESNIDTYFKNADENNENVLLLFKNIEMADNKSQHILKIKKDNatndHDFNI 1485
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1698 SNLKEENRKmeeklssgNKALKEDCEKLRSTLESKELILQQNKQELEERLTVINEKNGKNALLDAQLKSNE--TAFTSLR 1775
Cdd:TIGR01612 1486 NELKEHIDK--------SKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEIiiKEIKDAH 1557
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1776 KAWI--------------KQSLAIE-------AANKRSLEMEQKVDKRTREYEELrSTLKTREINFRSEKERMDGTISSL 1834
Cdd:TIGR01612 1558 KKFIleaekseqkikeikKEKFRIEddaakndKSNKAAIDIQLSLENFENKFLKI-SDIKKKINDCLKETESIEKKISSF 1636
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 78706884 1835 LEDKRnlEEKLCTVTELLAKLKRELPALHTQKVNGGDVSIELNSSN 1880
Cdd:TIGR01612 1637 SIDSQ--DTELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDELD 1680
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1526-1867 |
5.00e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.54 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1526 KSLQEVRDHLESRnEELKRKLKDAQELQNMVDKERKLNSSLREDFD-KLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKd 1604
Cdd:COG5022 797 IKLQPLLSLLGSR-KEYRSYLACIIKLQKTIKREKKLRETEEVEFSlKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSA- 874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1605 ceNIRSDLEAQTNDFLKERETLN-LTISDLRLHNEqLLETSKNYLSDITAANNLNLEMKKNLHDL-----TKECKSLRSD 1678
Cdd:COG5022 875 --QRVELAERQLQELKIDVKSISsLKLVNLELESE-IIELKKSLSSDLIENLEFKTELIARLKKLlnnidLEEGPSIEYV 951
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1679 LQSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKAlkedCEKLRSTleskelilQQNKQELEERLTVINEKNgkna 1758
Cdd:COG5022 952 KLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKA----NSELKNF--------KKELAELSKQYGALQEST---- 1015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1759 lldAQLKSNETAFTSLRKAwIKQSLAIEAANKRSLEMEQKVDKRTREYEELRSTLKtrEINFRSEKERMDGTISSLLEDK 1838
Cdd:COG5022 1016 ---KQLKELPVEVAELQSA-SKIISSESTELSILKPLQKLKGLLLLENNQLQARYK--ALKLRRENSLLDDKQLYQLEST 1089
|
330 340
....*....|....*....|....*....
gi 78706884 1839 RNLEEKLCTVTELLAKLKRELPALHTQKV 1867
Cdd:COG5022 1090 ENLLKTINVKDLEVTNRNLVKPANVLQFI 1118
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1352-1859 |
5.85e-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: 48.25 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1352 EIQKINGQHSNTIKKLEEIEAEMITLTTQK---------ELERCEIAEKLET-FKSKEADIKEALHCAQLRLHAydklvc 1421
Cdd:pfam01576 13 ELQKVKERQQKAESELKELEKKHQQLCEEKnalqeqlqaETELCAEAEEMRArLAARKQELEEILHELESRLEE------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1422 EYERLKGCLSDSNKLSENLQKKVERLHAEQLA---LQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQE 1498
Cdd:pfam01576 87 EEERSQQLQNEKKKMQQHIQDLEEQLDEEEAArqkLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1499 NMSAQEGQFK--QKIADIKGSV-DELQIKLKSLQEVRDHLEsrneELKRKLK-DAQELQNMVDKERKLNSSLREDFDKLE 1574
Cdd:pfam01576 167 NLAEEEEKAKslSKLKNKHEAMiSDLEERLKKEEKGRQELE----KAKRKLEgESTDLQEQIAELQAQIAELRAQLAKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1575 ---QTKLDLEEQLRAKKVEIDRRSKEL----GEVTKDCEN---IRSDLEAQTNDFLKERETLNLTISD----------LR 1634
Cdd:pfam01576 243 eelQAALARLEEETAQKNNALKKIRELeaqiSELQEDLESeraARNKAEKQRRDLGEELEALKTELEDtldttaaqqeLR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1635 LHNEQLLETSKNYLSDITAANNLNLEMKKNLHDLTKEckslrsDLQSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSG 1714
Cdd:pfam01576 323 SKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALE------ELTEQLEQAKRNKANLEKAKQALESENAELQAELRTL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1715 NKAlKEDCEKLRSTLESKELILQQNKQELEERLTVINEKNGKnalLDAQLKSNETAFTSLRKAWIKQSLAIEAANKRSLE 1794
Cdd:pfam01576 397 QQA-KQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSK---LQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQD 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78706884 1795 MEQKVDKRTREYEELRSTLKTREINFRSEKERMDGTIssllEDKRNLEEKLCTVTELLAKLKREL 1859
Cdd:pfam01576 473 TQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEE----EAKRNVERQLSTLQAQLSDMKKKL 533
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
703-1370 |
6.72e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 703 IQQKYLQLQDEYRHLELRSDEQCQQLQDENSKLQAEIGTLKERVEEIH-----SELLEVPNPDTHPE-DMELQNQELKKR 776
Cdd:TIGR00618 240 QSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINrarkaAPLAAHIKAVTQIEqQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 777 LSKLQWEFDEI------QLNYECLSNELMSTIQECDALREEHKQRTTNSDLESMKssgvgTECSDPENELDTDLLQQFTK 850
Cdd:TIGR00618 320 MRSRAKLLMKRaahvkqQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ-----HTLTQHIHTLQQQKTTLTQK 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 851 LSKSIQQIELTDYSGGRRLFiynhaeQDQSVPSLKLCLEPAKYLEGDGKQHDASDSVFLKGFLKCQRFQIVKINQEQNLV 930
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDT------RTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 931 KEEdrmrdiIFQLKQevdgKKNLIEEEKEvINNLRAQITSLNQIEtiknqnakTKILCEELqtkdtvqtankQESQEVLT 1010
Cdd:TIGR00618 469 KER------EQQLQT----KEQIHLQETR-KKAVVLARLLELQEE--------PCPLCGSC-----------IHPNPARQ 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1011 LKTSLAHLKSKVCELQKKLEKQSEDEKISELQsdigeiseccLSMELKLADIVNWQAEELRplDQLQESGVELQHHSTTA 1090
Cdd:TIGR00618 519 DIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQ----------LTSERKQRASLKEQMQEIQ--QSFSILTQCDNRSKEDI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1091 EESLNVEKPIQEQTERTLTTEYERRIEQLEESLQRaQEELSILEKRKTDEN--KSLQLEYMAKIETSENENRSKFRAYCL 1168
Cdd:TIGR00618 587 PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKL-QPEQDLQDVRLHLQQcsQELALKLTALHALQLTLTQERVREHAL 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1169 DLKETQKRYEEQLQQTNEKLASVTTQCQV------HLDVIKRSLQEKITQAEKERNELAVRHKA-------ELEKIRETL 1235
Cdd:TIGR00618 666 SIRVLPKELLASRQLALQKMQSEKEQLTYwkemlaQCQTLLRELETHIEEYDREFNEIENASSSlgsdlaaREDALNQSL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1236 KEKESSYKEKLRQAEEERDKEISRLEVMRNTIAELHKTNSDREVELEGVKMEKCQLKKL---------YDKSMLELEQLQ 1306
Cdd:TIGR00618 746 KELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLeaeigqeipSDEDILNLQCET 825
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78706884 1307 CTADQKSSDLL---PGSSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEI 1370
Cdd:TIGR00618 826 LVQEEEQFLSRleeKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDA 892
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1200-1858 |
6.90e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.21 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1200 DVIKRSLQEKITQAEKERNELAvrHKAELEKIRETLKEKESSYK-EKLRQAEEERDKEISRlevmrnTIAELHKTNSDRE 1278
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEA--KKTETGKAEEARKAEEAKKKaEDARKAEEARKAEDAR------KAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1279 VELEgvkmekcqlKKLYDKSMLELEQlqctadqKSSDllpgssneniddlQKKCDQYVQDLELLRGEKAELLSEIQKIN- 1357
Cdd:PTZ00121 1154 VEIA---------RKAEDARKAEEAR-------KAED-------------AKKAEAARKAEEVRKAEELRKAEDARKAEa 1204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1358 GQHSNTIKKLEEIEaemitltTQKELERCEIAEKLETFKSKEADIKEA---LHCAQLRLHAYDKLVCEYERLKGCLSDSN 1434
Cdd:PTZ00121 1205 ARKAEEERKAEEAR-------KAEDAKKAEAVKKAEEAKKDAEEAKKAeeeRNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1435 KLSENLQKKVERLHAEQLalqegisgRDSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQE-NMSAQEGQFKQKIAd 1513
Cdd:PTZ00121 1278 RKADELKKAEEKKKADEA--------KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAaKKKAEEAKKAAEAA- 1348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1514 iKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAkkveiDR 1593
Cdd:PTZ00121 1349 -KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA-----DE 1422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1594 RSKELGEVTKDCENIRSDLEAQTNDFLKEREtlnltisdlrlhneqlletsknylsditaannlnlEMKKNLHDLTKECK 1673
Cdd:PTZ00121 1423 AKKKAEEKKKADEAKKKAEEAKKADEAKKKA-----------------------------------EEAKKAEEAKKKAE 1467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1674 SLRSDLQSKEEyfqtqkqlldetisnlKEENRKMEEKLSSGNKAlKEDCEKLRSTLESKELILQQNKQELEERLTVINEK 1753
Cdd:PTZ00121 1468 EAKKADEAKKK----------------AEEAKKADEAKKKAEEA-KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1754 NGKNALLDAQLKSNETAFTSLRKAwikqslaieaANKRSLEMEQKVDKRTREYEELRSTLKTREINFRSEKERMDGTISS 1833
Cdd:PTZ00121 1531 EEAKKADEAKKAEEKKKADELKKA----------EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600
|
650 660
....*....|....*....|....*
gi 78706884 1834 LLEDKRNLEEKLCTVTEllAKLKRE 1858
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEE--AKIKAE 1623
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1318-1551 |
7.16e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1318 PGSSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMitlttqKELERcEIAEKLETFKS 1397
Cdd:COG3883 11 PAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEI------DKLQA-EIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1398 KEADIKEALHCAQLRLHAYDKLvceyERLKGclsdsnklSENLQKKVERLHAeqlalqegisgrdseIKQLRSELKDAID 1477
Cdd:COG3883 84 RREELGERARALYRSGGSVSYL----DVLLG--------SESFSDFLDRLSA---------------LSKIADADADLLE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706884 1478 ENKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQE 1551
Cdd:COG3883 137 ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1490-1814 |
7.40e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1490 ENSLKAVQENMsaqegqfkQKIADIkgsVDELQIKLKSLQEVRDHLEsRNEELKRKLKDAQ------ELQNMVDKERKLN 1563
Cdd:TIGR02168 178 ERKLERTRENL--------DRLEDI---LNELERQLKSLERQAEKAE-RYKELKAELRELElallvlRLEELREELEELQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1564 SSLREDFDKLEQTKLDLE------EQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHN 1637
Cdd:TIGR02168 246 EELKEAEEELEELTAELQeleeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1638 EQLLETSKNYLSDITaannlnlEMKKNLHDLTKECKSLRSDLQSKEEYFQ---TQKQLLDETISNLKEENRKMEEKLSSG 1714
Cdd:TIGR02168 326 EELESKLDELAEELA-------ELEEKLEELKEELESLEAELEELEAELEeleSRLEELEEQLETLRSKVAQLELQIASL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1715 NKALKEdcekLRSTLESKELILQQNKQELEERLTVINEKNGKnaLLDAQLKSNETAFTSLRKAWIKQSLAIEAANKRSLE 1794
Cdd:TIGR02168 399 NNEIER----LEARLERLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELREELEE 472
|
330 340
....*....|....*....|
gi 78706884 1795 MEQKVDKRTREYEELRSTLK 1814
Cdd:TIGR02168 473 AEQALDAAERELAQLQARLD 492
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1207-1845 |
7.50e-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: 47.79 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1207 QEKITQAEKERNELAVRHKAELEKIRETLKEKESSYKEKLRQAEEERDKEISRLEVMRNTIAELHKTNSDREVELEGVKM 1286
Cdd:pfam05483 62 QEGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1287 EKCQLKKLYD--KSMLELEQLQCTADQKSSDLLPGSSNENID---DLQKKCDQYVQDLELLRGEKAELLSEIQ-KINGQH 1360
Cdd:pfam05483 142 ENKDLIKENNatRHLCNLLKETCARSAEKTKKYEYEREETRQvymDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDH 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1361 SNTIKKLEEIEAEMITLTTQKELERCEIAEKLETFKSKEADIKEALHCAQlrlHAYDKLVCEYERLKGCLSDSNKLS--- 1437
Cdd:pfam05483 222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKAN---QLEEKTKLQDENLKELIEKKDHLTkel 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1438 ENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVREAK----VGLENSLKAVQENMSAQEGQFKQKIAD 1513
Cdd:pfam05483 299 EDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHsfvvTEFEATTCSLEELLRTEQQRLEKNEDQ 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1514 IKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREdfdkLEQTKLDLEEQLRAKKVEIDR 1593
Cdd:pfam05483 379 LKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEE----LKGKEQELIFLLQAREKEIHD 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1594 RSKELGEVTKDCENirsdleaqtndFLKERETLNLTISDLRLHNEQLLETSknylsditaaNNLNLEMKKnlhdLTKECK 1673
Cdd:pfam05483 455 LEIQLTAIKTSEEH-----------YLKEVEDLKTELEKEKLKNIELTAHC----------DKLLLENKE----LTQEAS 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1674 SLRSDLQSKEEyfqtqkqlldeTISNlkeeNRKMEEKLSSGNKALKEDCEKLRSTLESKELILQQNKQELEERLTVINEK 1753
Cdd:pfam05483 510 DMTLELKKHQE-----------DIIN----CKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1754 ----NGKNALLDAQLKSNETAFTSLRKAWIKQSLAIEAANKRSLEMEQKVDKRTREYEELRSTLKTREINFRSEKER--- 1826
Cdd:pfam05483 575 arsiEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKfee 654
|
650
....*....|....*....
gi 78706884 1827 MDGTISSLLEDKRNLEEKL 1845
Cdd:pfam05483 655 IIDNYQKEIEDKKISEEKL 673
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1116-1640 |
7.70e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1116 IEQLEESLQRAQEELSILEKRKTDENKSLQLeYMAKIETSENENRSKFRAY---------CLDLKETQKRYEEQLQQTNE 1186
Cdd:PRK01156 185 IDYLEEKLKSSNLELENIKKQIADDEKSHSI-TLKEIERLSIEYNNAMDDYnnlksalneLSSLEDMKNRYESEIKTAES 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1187 KLASVTTQCQVHLDVIKRSLQEKITQAEKERNELA--VRHKAELE---KIRETLKEKESSYKEKLRQAEEeRDKEISRLE 1261
Cdd:PRK01156 264 DLSMELEKNNYYKELEERHMKIINDPVYKNRNYINdyFKYKNDIEnkkQILSNIDAEINKYHAIIKKLSV-LQKDYNDYI 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1262 VMRNTIAELHKTNSDreveLEGVKMEkcqlkklYDKSMLELEQLQCTADQKSSDLLPGSsneniDDLQKKCDQYVQDLEL 1341
Cdd:PRK01156 343 KKKSRYDDLNNQILE----LEGYEMD-------YNSYLKSIESLKKKIEEYSKNIERMS-----AFISEILKIQEIDPDA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1342 LRGEKAELLSEIQKINGQHSN-------TIKKLEEIEAEMITLTTQKELERCeiAEKLETFKSKeaDIKEALHCAQLRLH 1414
Cdd:PRK01156 407 IKKELNEINVKLQDISSKVSSlnqriraLRENLDELSRNMEMLNGQSVCPVC--GTTLGEEKSN--HIINHYNEKKSRLE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1415 AydklvcEYERLKGCLSDSNKLSENLQKKVERLHAEQLalqEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLEnslK 1494
Cdd:PRK01156 483 E------KIREIEIEVKDIDEKIVDLKKRKEYLESEEI---NKSINEYNKIESARADLEDIKIKINELKDKHDKYE---E 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1495 AVQENMSAQEGQFKQK---------------IADIKGSVDELQIKLKS----LQEVRDHLESRNEELKRKLKDAQELQNM 1555
Cdd:PRK01156 551 IKNRYKSLKLEDLDSKrtswlnalavislidIETNRSRSNEIKKQLNDlesrLQEIEIGFPDDKSYIDKSIREIENEANN 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1556 VDKERKLNSSLREDFDKLEQTKLDLEEQLrAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDFLKERETLNLTISDLRL 1635
Cdd:PRK01156 631 LNNKYNEIQENKILIEKLRGKIDNYKKQI-AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLESTIEILRT 709
|
....*
gi 78706884 1636 HNEQL 1640
Cdd:PRK01156 710 RINEL 714
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1350-1753 |
8.74e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1350 LSEIQKINGQ-HSNTIKKLEEIEAEMITLTTQKElERCEIAEKLETFKSKEADIKEALHCAQLRLHAYDKLVCEYERLKG 1428
Cdd:COG4717 55 ADELFKPQGRkPELNLKELKELEEELKEAEEKEE-EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1429 CLSDSNKLSEnLQKKVERLHAEQLALQEgisgRDSEIKQLRSELkdaidenktvREAKVGLENSLKAVQENMSAQEGQFK 1508
Cdd:COG4717 134 LEALEAELAE-LPERLEELEERLEELRE----LEEELEELEAEL----------AELQEELEELLEQLSLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1509 QKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNS-SLREDFDKLEQTKLDLEEQ---- 1583
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIaAALLALLGLGGSLLSLILTiagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1584 ------LRAKKVEIDRRSKELGEVTKD---CENIRSDLEAQTNDFLKERETLNLTISDLRLhnEQLLETSKNYLSDITAA 1654
Cdd:COG4717 279 lflvlgLLALLFLLLAREKASLGKEAEelqALPALEELEEEELEELLAALGLPPDLSPEEL--LELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1655 NNLNLEMKknLHDLTKECKSL--RSDLQSKEEYFQTQKQLldETISNLKEENRKMEEKLSSGNKALKEDCEKL-RSTLES 1731
Cdd:COG4717 357 EELEEELQ--LEELEQEIAALlaEAGVEDEEELRAALEQA--EEYQELKEELEELEEQLEELLGELEELLEALdEEELEE 432
|
410 420
....*....|....*....|..
gi 78706884 1732 KELILQQNKQELEERLTVINEK 1753
Cdd:COG4717 433 ELEELEEELEELEEELEELREE 454
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1452-1684 |
8.78e-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: 8.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1452 LALQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSAQEgqfkQKIADIKGSVDELQIKLKSLQ-- 1529
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA----RRIRALEQELAALEAELAELEke 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1530 --EVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCEN 1607
Cdd:COG4942 92 iaELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 78706884 1608 IRSDLEAQTNDFLKERETLNLTISDlrlhNEQLLETSKnylSDITAANNLNLEMKKNLHDLTKECKSLRSDLQSKEE 1684
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAE----RQKLLARLE---KELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
954-1406 |
8.89e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 954 IEEEKEVINNLRAQITSLNqIETIKNQNAKTKILCEELQTKDTVQTANKQESQEVLTLKTSLAHLKSKVCELQKKLEKQS 1033
Cdd:COG4717 51 LEKEADELFKPQGRKPELN-LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1034 EDEKISELQSDIGEISECCLSMELKLADIVNWQAEelrpLDQLQEsgvELQHHSTTAEESLNVEKPIQEQTERTLTTEYE 1113
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEE----LEELEA---ELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1114 R---RIEQLEESLQRAQEELSILEKRKTDENKSLQLEYMAKiETSENEN-------RSKFRAYCLDLKETQKRYEEQLQ- 1182
Cdd:COG4717 203 ElqqRLAELEEELEEAQEELEELEEELEQLENELEAAALEE-RLKEARLllliaaaLLALLGLGGSLLSLILTIAGVLFl 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1183 -----------QTNEKLASVTTQCQVHLDVIKRSLQEKITQAEKERneLAVRHKAELEKIREtLKEKESSYKEKLRQAEE 1251
Cdd:COG4717 282 vlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAA--LGLPPDLSPEELLE-LLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1252 ERdKEISRLEVMRNTIAELHKTNSDREVELEgvkmEKCQLKKLYDKSMLELEQLQCTADQKSSDLLPGSSNENIDDLQKK 1331
Cdd:COG4717 359 LE-EELQLEELEQEIAALLAEAGVEDEEELR----AALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEE 433
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78706884 1332 CDQYVQDLELLRGEKAELLSEIQkingqhsntikkleEIEAEMITLTTQKELerceiAEKLETFKSKEADIKEAL 1406
Cdd:COG4717 434 LEELEEELEELEEELEELREELA--------------ELEAELEQLEEDGEL-----AELLQELEELKAELRELA 489
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1169-1682 |
1.26e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1169 DLKETQKRYE--EQLQQTNEKLASVTTQCQvHLDVIKRSLQekiTQAEKERNELAVRHKAELEKIRETLKEKESSYKEKL 1246
Cdd:COG4913 243 ALEDAREQIEllEPIRELAERYAAARERLA-ELEYLRAALR---LWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1247 RQAEEERDK-EISRLEVMRNTIAELHKTNSDREVELEGVKMEKCQLKKL-------YDKSMLELEQLQCTADQKSSDLlp 1318
Cdd:COG4913 319 DALREELDElEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalglpLPASAEEFAALRAEAAALLEAL-- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1319 gssNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELERCEIAEKLETfKSK 1398
Cdd:COG4913 397 ---EEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGELIEV-RPE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1399 EAD----IKEALHCAQLRL---HAYDKLVCEY---ERLKGCLsDSNKLSENLQK-KVERLHAEQLA-------------L 1454
Cdd:COG4913 473 EERwrgaIERVLGGFALTLlvpPEHYAAALRWvnrLHLRGRL-VYERVRTGLPDpERPRLDPDSLAgkldfkphpfrawL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1455 QEGISGR------DSEiKQLRSE---------LKD-----AIDENKTVREAKV-GLENS--LKAVQenmsAQEGQFKQKI 1511
Cdd:COG4913 552 EAELGRRfdyvcvDSP-EELRRHpraitragqVKGngtrhEKDDRRRIRSRYVlGFDNRakLAALE----AELAELEEEL 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1512 ADIKGSVDELQIKLKSLQEVRDHLEsRNEELKRKLKDAQELQNMV-DKERKLnSSLREDFDKLEQtkldLEEQLRAKKVE 1590
Cdd:COG4913 627 AEAEERLEALEAELDALQERREALQ-RLAEYSWDEIDVASAEREIaELEAEL-ERLDASSDDLAA----LEEQLEELEAE 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1591 IDRRSKELGEVTKDCENIRSDLEAQTNDFLKERETLNLTISDLRLHNEQLLEtskNYLSDITAANNLNlEMKKNLHDLTK 1670
Cdd:COG4913 701 LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLE---ERFAAALGDAVER-ELRENLEERID 776
|
570
....*....|..
gi 78706884 1671 ECKSLRSDLQSK 1682
Cdd:COG4913 777 ALRARLNRAEEE 788
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1111-1297 |
1.56e-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: 46.30 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1111 EYERRIEQLEESLQRAQEELSILEKRKTDENKSLQL--EYMAKIETSENENRSKFRAYCLDLKETQKRYEEQLQQ----- 1183
Cdd:COG4942 38 ELEKELAALKKEEKALLKQLAALERRIAALARRIRAleQELAALEAELAELEKEIAELRAELEAQKEELAELLRAlyrlg 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1184 TNEKLASVTTQCQVHLDVIKRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKESSYKEKLRQAEEERDKEISRLEVM 1263
Cdd:COG4942 118 RQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
170 180 190
....*....|....*....|....*....|....
gi 78706884 1264 RNTIAELHKTNSDREVELEGVKMEKCQLKKLYDK 1297
Cdd:COG4942 198 QKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
924-1238 |
1.59e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.85 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 924 NQEQNLVKEEDRMRDIIFQLKQEVDGKKNLIEEEKEVINNLRAQITSLNQ---IETIKNQNAKTKILcEELQTKDTVQTA 1000
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiaRLEERRRELEERLE-ELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1001 NKQESQEVLTLKTSLAHLKSKVCELQKKLE--KQSEDEKISELQSDIGEISECCLSMELKLADIVNWQAEELRPLDQLQE 1078
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAeaEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1079 SGVELQHHSTTAEESLNVEKPIQEQTERTLTTEYERRIEQLEESLQRAQEELSILEKRKTDEnksLQLEYMAKIETSENE 1158
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA---LLEAALAELLEELAE 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1159 NRSKFRAycldLKETQKRYEEQLQ-----QTNEKLASVTTQCQVHLDVIKRSLQEKITQAEKERNELAVRHKAELEKIRE 1233
Cdd:COG1196 489 AAARLLL----LLEAEADYEGFLEgvkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE 564
|
....*
gi 78706884 1234 TLKEK 1238
Cdd:COG1196 565 YLKAA 569
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
971-1711 |
1.93e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.61 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 971 LNQIETIKNQNAKTKILCEELQTKDT-VQTANKQESQEVLTLKTSLAHLKSKVCELQKKLEKQSEDEKISELQSDIGEIS 1049
Cdd:COG5022 816 LACIIKLQKTIKREKKLRETEEVEFSlKAEVLIQKFGRSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSIS 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1050 ecclsmelKLADIVNwqaeelrpldQLQESGVELqhhSTTAEESLNVEKPIQEQtertLTTEYERRIE--QLEESLQRAQ 1127
Cdd:COG5022 896 --------SLKLVNL----------ELESEIIEL---KKSLSSDLIENLEFKTE----LIARLKKLLNniDLEEGPSIEY 950
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1128 EELSILEKRKTDEN--KSLQLEYMAKIETSENenrskfraycldLKETQKRYEEQLQQTNEKLASVTTQcqvhldviKRS 1205
Cdd:COG5022 951 VKLPELNKLHEVESklKETSEEYEDLLKKSTI------------LVREGNKANSELKNFKKELAELSKQ--------YGA 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1206 LQEKITQAEKERNELAVRHKAElekiretlKEKESSYKEKLRQAEEERDKEISRLEVMRNTiAELHKTNSDREVELEGVK 1285
Cdd:COG5022 1011 LQESTKQLKELPVEVAELQSAS--------KIISSESTELSILKPLQKLKGLLLLENNQLQ-ARYKALKLRRENSLLDDK 1081
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1286 MEKCQLKKLYDKSMLELEQLQCTADQKssdLLPGSSNENIDDLQKKCDQYVQDLELLRgekaELLSEIQKINGQHSNTIK 1365
Cdd:COG5022 1082 QLYQLESTENLLKTINVKDLEVTNRNL---VKPANVLQFIVAQMIKLNLLQEISKFLS----QLVNTLEPVFQKLSVLQL 1154
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1366 KLEEIEAEMITLTTQKELERCEIAEKlETFKSKEADIKEALHCAQLRLhAYDKLVCEYERLKGCLSDSNKLsENLQKKVE 1445
Cdd:COG5022 1155 ELDGLFWEANLEALPSPPPFAALSEK-RLYQSALYDEKSKLSSSEVND-LKNELIALFSKIFSGWPRGDKL-KKLISEGW 1231
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1446 RLHAEQLALQEGISGRDSEIKQlrselkdAIDENKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADIK-GSVDELQIK 1524
Cdd:COG5022 1232 VPTEYSTSLKGFNNLNKKFDTP-------ASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINvGLFNALRTK 1304
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1525 LKSLqevrdhlesrneELKRklkdaqelqnmvDKERKLNSSLREDFDK---LEQTKLDLEEQLRAKKVEIDRRS--KELG 1599
Cdd:COG5022 1305 ASSL------------RWKS------------ATEVNYNSEELDDWCRefeISDVDEELEELIQAVKVLQLLKDdlNKLD 1360
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1600 EVTKDCENIrSDLEAQTndfLKERETLnltiSDLRLHNEQllETSKNYLSDIT-AANNLNLEMKKNLHDLTKECKSLRSD 1678
Cdd:COG5022 1361 ELLDACYSL-NPAEIQN---LKSRYDP----ADKENNLPK--EILKKIEALLIkQELQLSLEGKDETEVHLSEIFSEEKS 1430
|
730 740 750
....*....|....*....|....*....|...
gi 78706884 1679 LQSKEEYFQTQKQLLDETISNLKEENRKMEEKL 1711
Cdd:COG5022 1431 LISLDRNSIYKEEVLSSLSALLTKEKIALLDRK 1463
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1111-1572 |
2.12e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1111 EYERRIEQLEESLQRAQEELSILEKRKTD-ENKSLQLEYMAKIETSENENRSkfraycldLKETQKRYEEQLQQTNEKLA 1189
Cdd:COG4717 85 EKEEEYAELQEELEELEEELEELEAELEElREELEKLEKLLQLLPLYQELEA--------LEAELAELPERLEELEERLE 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1190 SVttqcqvhldvikRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKESSYKEKLRQAEEERDKEISRLEVMRNTIAE 1269
Cdd:COG4717 157 EL------------RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1270 LHKTNSDREVELEGVKMEKcQLKKLydKSMLELEQLQCTADQKSSDLLpgssneniddlqkkcDQYVQDLELLRGEKAEL 1349
Cdd:COG4717 225 LEEELEQLENELEAAALEE-RLKEA--RLLLLIAAALLALLGLGGSLL---------------SLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1350 LSEIQKINGQHSNTIKKLEEIEAemitLTTQKELERCEIAEKLETFKSKEAdikealhcaqLRLHAYDKLVCEYERLKGC 1429
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQA----LPALEELEEEELEELLAALGLPPD----------LSPEELLELLDRIEELQEL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1430 LSDSNKLSENLQKKVERLHAEQLALQEGISGRDsEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSA-QEGQFK 1508
Cdd:COG4717 353 LREAEELEEELQLEELEQEIAALLAEAGVEDEE-ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAlDEEELE 431
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78706884 1509 QKIADIKGSVDELQIKLKSLQEVRDHLESRNEElkrkLKDAQELQNMVDKERKLNSSLREDFDK 1572
Cdd:COG4717 432 EELEELEEELEELEEELEELREELAELEAELEQ----LEEDGELAELLQELEELKAELRELAEE 491
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1393-1603 |
2.26e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.91 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1393 ETFKSKEADIKEALHCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSEL 1472
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1473 KDAIDE-NKTVREA-KVGLENSLKAVQENMSAQEGQ-----FKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRK 1545
Cdd:COG4942 100 EAQKEElAELLRALyRLGRQPPLALLLSPEDFLDAVrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78706884 1546 LKDAQE----LQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTK 1603
Cdd:COG4942 180 LAELEEeraaLEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1025-1859 |
2.38e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 46.32 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1025 LQKKLEKQSED--EKISELQSDIGEISECCLSMELKLADIVNWQAEELRPLDQLQESGVELQHHSTTAEESLNVEKPIQE 1102
Cdd:pfam01576 209 AKRKLEGESTDlqEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARN 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1103 QTE---RTLTTEYERRIEQLEESLQR--AQEELSILEKRKTDENKSLqleymakietsenenrskfraycldLKETQKRY 1177
Cdd:pfam01576 289 KAEkqrRDLGEELEALKTELEDTLDTtaAQQELRSKREQEVTELKKA-------------------------LEEETRSH 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1178 EEQLQQTNEKLASVTTQCQVHLDVIKRSLQ--EKITQA-EKERNELAV------RHKAELEKIRETLKEKESSYKEKLRQ 1248
Cdd:pfam01576 344 EAQLQEMRQKHTQALEELTEQLEQAKRNKAnlEKAKQAlESENAELQAelrtlqQAKQDSEHKRKKLEGQLQELQARLSE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1249 AEEERDKEISRLEVMRNTIAELhkTNSDREVELEGVKMEKcQLKKLYDKSMLELEQLQCTADQKSSdllpgsSNENIDDL 1328
Cdd:pfam01576 424 SERQRAELAEKLSKLQSELESV--SSLLNEAEGKNIKLSK-DVSSLESQLQDTQELLQEETRQKLN------LSTRLRQL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1329 QKKCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITL-------------TTQKELERCEIAEKLETF 1395
Cdd:pfam01576 495 EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALeegkkrlqreleaLTQQLEEKAAAYDKLEKT 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1396 KSKeadIKEALHCAQLRLHAYDKLVCEYER----LKGCLSDSNKLSENLQKKVERLHAE-----------QLALQEGISG 1460
Cdd:pfam01576 575 KNR---LQQELDDLLVDLDHQRQLVSNLEKkqkkFDQMLAEEKAISARYAEERDRAEAEareketralslARALEEALEA 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1461 RDS---EIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADIKGSVD---ELQIKLKSL--QEVR 1532
Cdd:pfam01576 652 KEElerTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDaklRLEVNMQALkaQFER 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1533 D--HLESRNEELKRKL-KDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEvtkdcenir 1609
Cdd:pfam01576 732 DlqARDEQGEEKRRQLvKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKK--------- 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1610 sdLEAQTNDFLKEREtlnltisDLRLHNEQLLETSKNYLSDITAANNLNLEMKKNL---HDLTKECKSLRSDLQ------ 1680
Cdd:pfam01576 803 --LQAQMKDLQRELE-------EARASRDEILAQSKESEKKLKNLEAELLQLQEDLaasERARRQAQQERDELAdeiasg 873
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1681 -SKEEYFQTQKQLLDETISNLKEENRKME---EKLSSGNKALKEDCEKLRSTLESKELILQQN---KQELEErltvinek 1753
Cdd:pfam01576 874 aSGKSALQDEKRRLEARIAQLEEELEEEQsntELLNDRLRKSTLQVEQLTTELAAERSTSQKSesaRQQLER-------- 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1754 ngKNALLDAQLKSNETAFTSlrkawiKQSLAIEAANKRSLEMEQKVDKRTREYEEL-----RSTLKTREINFRSEKER-- 1826
Cdd:pfam01576 946 --QNKELKAKLQEMEGTVKS------KFKSSIAALEAKIAQLEEQLEQESRERQAAnklvrRTEKKLKEVLLQVEDERrh 1017
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 78706884 1827 -------MDGTISSLLEDKRNLEEKLCTVTELLA---KLKREL 1859
Cdd:pfam01576 1018 adqykdqAEKGNSRMKQLKRQLEEAEEEASRANAarrKLQREL 1060
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1440-1608 |
2.55e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.78 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1440 LQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSA-QEG--------QFKQ- 1509
Cdd:PHA02562 218 KQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMyEKGgvcptctqQISEg 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1510 --KIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAK 1587
Cdd:PHA02562 298 pdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDN 377
|
170 180
....*....|....*....|.
gi 78706884 1588 KVEIDRRSKELGEVTKDCENI 1608
Cdd:PHA02562 378 AEELAKLQDELDKIVKTKSEL 398
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1438-1617 |
2.72e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1438 ENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSAQEGQFKQKIADI--- 1514
Cdd:COG3883 19 QAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1515 ---------------------------------KGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQ----ELQNMVD 1557
Cdd:COG3883 99 ggsvsyldvllgsesfsdfldrlsalskiadadADLLEELKADKAELEAKKAELEAKLAELEALKAELEaakaELEAQQA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1558 KERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTN 1617
Cdd:COG3883 179 EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1179-1618 |
3.77e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 45.23 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1179 EQLQQTNEKLASVTTQcqvhLDVIKRSLQEKITQAEKERNELAvrhkaELEKIRETLKEKESSYKEKLRQAEEERDKEIS 1258
Cdd:pfam06160 86 KALDEIEELLDDIEED----IKQILEELDELLESEEKNREEVE-----ELKDKYRELRKTLLANRFSYGPAIDELEKQLA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1259 RLEVMRNTIAELhKTNSD----REVeLEGVKMEKCQLKKLYDKSMLELEQLQctadqkssDLLPgssnENIDDLQKKCDQ 1334
Cdd:pfam06160 157 EIEEEFSQFEEL-TESGDyleaREV-LEKLEEETDALEELMEDIPPLYEELK--------TELP----DQLEELKEGYRE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1335 YVQDLELLrgEKAELLSEIQKINGQHSNTIKKLEEIEAEmitlTTQKELErcEIAEKLETFkskeADIKEAlhcaqlRLH 1414
Cdd:pfam06160 223 MEEEGYAL--EHLNVDKEIQQLEEQLEENLALLENLELD----EAEEALE--EIEERIDQL----YDLLEK------EVD 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1415 AYDKLVCEYERLKGCLSDSNKLSENLQKKVER------LHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVReakvg 1488
Cdd:pfam06160 285 AKKYVEKNLPEIEDYLEHAEEQNKELKEELERvqqsytLNENELERVRGLEKQLEELEKRYDEIVERLEEKEVAY----- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1489 leNSLKAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLkdaqELQNMvdkeRKLNSSLRE 1568
Cdd:pfam06160 360 --SELQEELEEILEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLV----EKSNL----PGLPESYLD 429
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 78706884 1569 DFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENirsdLEAQTND 1618
Cdd:pfam06160 430 YFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDT----LYEKTEE 475
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
1342-1619 |
3.93e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1342 LRGEKAELLSEIQKINGQHSNTIKklEEIEAEMITLTTqKELERC-EIAEKLETFKSKEADIKEAlhcaqlrlhaydKLV 1420
Cdd:PRK05771 14 LKSYKDEVLEALHELGVVHIEDLK--EELSNERLRKLR-SLLTKLsEALDKLRSYLPKLNPLREE------------KKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1421 CEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLR------SELKDAID-ENKTVREAKVGLENSL 1493
Cdd:PRK05771 79 VSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLEpwgnfdLDLSLLLGfKYVSVFVGTVPEDKLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1494 KAVQEN-----------------MSAQEGQFKQKIADI--KGSVDELQIK-LKSLQEVRDHLESRNEELKRKLKDaqelq 1553
Cdd:PRK05771 159 ELKLESdvenveyistdkgyvyvVVVVLKELSDEVEEElkKLGFERLELEeEGTPSELIREIKEELEEIEKERES----- 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78706884 1554 nmvdkerkLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKEL---------GEV-TKDCENIRSDLEAQTNDF 1619
Cdd:PRK05771 234 --------LLEELKELAKKYLEELLALYEYLEIELERAEALSKFLktdktfaieGWVpEDRVKKLKELIDKATGGS 301
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1110-1764 |
4.67e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1110 TEYERRIEQLEESLQRAQEELSILEKRKTD-ENKSLQL--EYMAKIETSENENRskfraYCLDLKETQKRYEEQLQQTNE 1186
Cdd:pfam01576 1 TRQEEEMQAKEEELQKVKERQQKAESELKElEKKHQQLceEKNALQEQLQAETE-----LCAEAEEMRARLAARKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1187 KLASVTT------QCQVHLDVIKRSLQEKITQAEKE-RNELAVRHKAELEKIreTLKEKESSYKEKLRQAEEERDKEISR 1259
Cdd:pfam01576 76 ILHELESrleeeeERSQQLQNEKKKMQQHIQDLEEQlDEEEAARQKLQLEKV--TTEAKIKKLEEDILLLEDQNSKLSKE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1260 LEVMRNTIAELHKTNSDREvelEGVKM-EKCQLK------------KLYDKSMLELEQLQCTADQKSSDLlpgssNENID 1326
Cdd:pfam01576 154 RKLLEERISEFTSNLAEEE---EKAKSlSKLKNKheamisdleerlKKEEKGRQELEKAKRKLEGESTDL-----QEQIA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1327 DLQKKCDQYVQDLELLRGEKAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTQKELERC----------EIAEKLETFK 1396
Cdd:pfam01576 226 ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAarnkaekqrrDLGEELEALK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1397 SKEADIKEALhCAQLRLHAydKLVCEYERLKGCLSDSNKLSE---------------NLQKKVERLHAEQLALQEGISGR 1461
Cdd:pfam01576 306 TELEDTLDTT-AAQQELRS--KREQEVTELKKALEEETRSHEaqlqemrqkhtqaleELTEQLEQAKRNKANLEKAKQAL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1462 DSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQENMSAQEGQfKQKIADikgSVDELQIKLKSLQEVRDHLESRNEE 1541
Cdd:pfam01576 383 ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQ-RAELAE---KLSKLQSELESVSSLLNEAEGKNIK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1542 LKR-------KLKDAQEL-QNMVDKERKLNSSLREdfdkLEQTKLDLEEQLrakkveidrrsKELGEVTKDCENIRSDLE 1613
Cdd:pfam01576 459 LSKdvsslesQLQDTQELlQEETRQKLNLSTRLRQ----LEDERNSLQEQL-----------EEEEEAKRNVERQLSTLQ 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1614 AQTNDFLKERETLNLTIsdlrlhnEQLLETSKNYLSDITAANNLNLEMKKNLHDLTKECKSLRSDLQSKEEYFQTQKQLl 1693
Cdd:pfam01576 524 AQLSDMKKKLEEDAGTL-------EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQL- 595
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78706884 1694 detISNLKEENRKM-----EEKLSSGNKAlkEDCEKLRSTLESKELILQQNKQELEERLTVINEKNGKNALLDAQL 1764
Cdd:pfam01576 596 ---VSNLEKKQKKFdqmlaEEKAISARYA--EERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEM 666
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1328-1700 |
5.87e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.94 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1328 LQKKCDQYVQDLELLRgEKAELLSEIqkingqhsntikkLEEIEAEMITLttQKELERCEiaEKLETFKSKEADIKEALH 1407
Cdd:COG3096 345 QQEKIERYQEDLEELT-ERLEEQEEV-------------VEEAAEQLAEA--EARLEAAE--EEVDSLKSQLADYQQALD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1408 CAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQLALqegisgrDSEIKQLRSELKDAidenktvREAKV 1487
Cdd:COG3096 407 VQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQA-------TEEVLELEQKLSVA-------DAARR 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1488 GLENSLKAVqenmsaqegqfkQKIAdikGSVDELQIKLKSLQEVRD-----HLESRNEELKRKLKDA-QELQNMVDKERk 1561
Cdd:COG3096 473 QFEKAYELV------------CKIA---GEVERSQAWQTARELLRRyrsqqALAQRLQQLRAQLAELeQRLRQQQNAER- 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1562 lnssLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDF------LKERETLNLTISD--- 1632
Cdd:COG3096 537 ----LLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLrarikeLAARAPAWLAAQDale 612
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78706884 1633 -LRLHNEQLLETSknylSDITAANNLNLEmkkNLHDLTKEckslrsdlqskEEYFQTQKQLLDETISNL 1700
Cdd:COG3096 613 rLREQSGEALADS----QEVTAAMQQLLE---REREATVE-----------RDELAARKQALESQIERL 663
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1517-1754 |
8.89e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.52 E-value: 8.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1517 SVDELQIKLKSLQEvRDHLESRNEELKRKLKDAQELQNMVDKERKlnsslreDFDKLEQTKLDLEEQLRAKKVEIDRRSK 1596
Cdd:PRK11281 37 TEADVQAQLDALNK-QKLLEAEDKLVQQDLEQTLALLDKIDRQKE-------ETEQLKQQLAQAPAKLRQAQAELEALKD 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1597 ELGEVTKDCENIRS--DLEAQTNDFLKERETLNLTISDLrlhNEQL--LET-SKNYLSDITAANNLNLEMKKNLHDLTKE 1671
Cdd:PRK11281 109 DNDEETRETLSTLSlrQLESRLAQTLDQLQNAQNDLAEY---NSQLvsLQTqPERAQAALYANSQRLQQIRNLLKGGKVG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1672 CKSLRSDLQSKeeyFQTQKQLLdetisNLKEENRKmeeKLSSGNKALKEDCEKLRSTLESKELILQQNKQELEErltVIN 1751
Cdd:PRK11281 186 GKALRPSQRVL---LQAEQALL-----NAQNDLQR---KSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQLLQE---AIN 251
|
...
gi 78706884 1752 EKN 1754
Cdd:PRK11281 252 SKR 254
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1222-1585 |
9.48e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.56 E-value: 9.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1222 VRHKAELekiRETLKEKESSYKEKLRqAEEERDKEISRLEVMRNTIAELHKTNSDREVELEGV---------------KM 1286
Cdd:PRK04863 275 MRHANER---RVHLEEALELRRELYT-SRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAsdhlnlvqtalrqqeKI 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1287 EKCQ--LKKLYDKsmLElEQLQCTADQK----SSDLLPGSSNENIDDLQKKCDQYVQDLELLrgekaellseiQKINGQH 1360
Cdd:PRK04863 351 ERYQadLEELEER--LE-EQNEVVEEADeqqeENEARAEAAEEEVDELKSQLADYQQALDVQ-----------QTRAIQY 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1361 SNTIKKLEEIEaemiTLTTQKELERCEIAEKLETFKSKEADIKEALHCAQLRLHAYDKLVCEYE-------RLKGCLSDS 1433
Cdd:PRK04863 417 QQAVQALERAK----QLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEqayqlvrKIAGEVSRS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1434 NklSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVREAK----VGLEN----------------SL 1493
Cdd:PRK04863 493 E--AWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCkrlgKNLDDedeleqlqeelearleSL 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1494 KAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRNEELKRKLKDAQEL----QNMVDKERklnsSLRED 1569
Cdd:PRK04863 571 SESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVteymQQLLERER----ELTVE 646
|
410
....*....|....*.
gi 78706884 1570 FDKLEQTKLDLEEQLR 1585
Cdd:PRK04863 647 RDELAARKQALDEEIE 662
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1423-1790 |
1.13e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.27 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1423 YERLKGCLSDSNKLSENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQEnmsa 1502
Cdd:TIGR01612 539 YKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISD---- 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1503 qEGQFKQKIADIK-------GSVDEL--------------------QIKLKSLQEVRDHLESRNEELKRKLKDaQELQNM 1555
Cdd:TIGR01612 615 -KNEYIKKAIDLKkiiennnAYIDELakispyqvpehlknkdkiysTIKSELSKIYEDDIDALYNELSSIVKE-NAIDNT 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1556 VDKER--KLNSSLREDFDKL-----EQTKLDL------EEQLRAKKVEIDRR-----SKELGEVTKDCENIRSDLEAQTN 1617
Cdd:TIGR01612 693 EDKAKldDLKSKIDKEYDKIqnmetATVELHLsnienkKNELLDIIVEIKKHihgeiNKDLNKILEDFKNKEKELSNKIN 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1618 DFLKERETLNLTISDlrlhneqlLETSKNYLSDITAANNLNLEMKKNLHDLTKE---CKSLRSDLQSKeeYFQTQKQLLD 1694
Cdd:TIGR01612 773 DYAKEKDELNKYKSK--------ISEIKNHYNDQINIDNIKDEDAKQNYDKSKEyikTISIKEDEIFK--IINEMKFMKD 842
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1695 ETISNLK-----EENRKmeEKLSSGNKALKEDCEKLRSTLESKELILQQNKqeLEERLTVINEKNGK--------NAL-- 1759
Cdd:TIGR01612 843 DFLNKVDkfinfENNCK--EKIDSEHEQFAELTNKIKAEISDDKLNDYEKK--FNDSKSLINEINKSieeeyqniNTLkk 918
|
410 420 430
....*....|....*....|....*....|.
gi 78706884 1760 LDAQLKSNETAFTSLRKAWIKQSLAIEAANK 1790
Cdd:TIGR01612 919 VDEYIKICENTKESIEKFHNKQNILKEILNK 949
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1329-1700 |
1.23e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1329 QKKCDQYVQDLELL--RGEKAELLSEIQKingqhsntiKKLEEIEAEmitlTTQKELERCEIAEKLetfkskeADIKEAL 1406
Cdd:PRK04863 347 QEKIERYQADLEELeeRLEEQNEVVEEAD---------EQQEENEAR----AEAAEEEVDELKSQL-------ADYQQAL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1407 HCAQLRLHAYDKLVCEYERLKGCLSDSNKLSENLQKKVERLHAEQlalqegisgrdseikqlrselkdaidenKTVREAK 1486
Cdd:PRK04863 407 DVQQTRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKE----------------------------QEATEEL 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1487 VGLENSLkAVQENMSAQEGQFKQKIADIKGSVDELQIKLKSLQEVRDHLESRN-----EELKRKLKDA-QELQNMVDKER 1560
Cdd:PRK04863 459 LSLEQKL-SVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLREQRHlaeqlQQLRMRLSELeQRLRQQQRAER 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1561 klnssLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQtndflkeRETLNLTISDLRLHNEQL 1640
Cdd:PRK04863 538 -----LLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ-------LEQLQARIQRLAARAPAW 605
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78706884 1641 LET--SKNYLSDITAANNLNLEMKKNLHDLTKEckSLRSDLQSKEEYfQTQKQLLDETISNL 1700
Cdd:PRK04863 606 LAAqdALARLREQSGEEFEDSQDVTEYMQQLLE--RERELTVERDEL-AARKQALDEEIERL 664
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
931-1261 |
1.65e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 931 KEEDRMRDIIFQLKQEVDGKKNLIEEEKEVINNLRAQITSLNQIEtiknqnaktKILCEELQTKD----TVQTANKQESQ 1006
Cdd:PRK04863 279 NERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAE---------SDLEQDYQAASdhlnLVQTALRQQEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1007 evltlktsLAHLKSKVCELQKKLEKQSE-----DEKISELQSDIGEISECCLSMELKLADIVnwQAeelrpLDQLQESGV 1081
Cdd:PRK04863 350 --------IERYQADLEELEERLEEQNEvveeaDEQQEENEARAEAAEEEVDELKSQLADYQ--QA-----LDVQQTRAI 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1082 ELQHHSTTAEE--SLNVEKPIQEQTERTLTTEYERRIEQLEESLQRAQEELSILEKRKTDENKSLQLEYMAKIETSENEN 1159
Cdd:PRK04863 415 QYQQAVQALERakQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEA 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1160 RSKFRAYCLDLkETQKRYEEQLQQTNEKLASVTTQCQVHLDViKRSLQE--KITQAEKERNELAVRHKAELEKIRETLKE 1237
Cdd:PRK04863 495 WDVARELLRRL-REQRHLAEQLQQLRMRLSELEQRLRQQQRA-ERLLAEfcKRLGKNLDDEDELEQLQEELEARLESLSE 572
|
330 340
....*....|....*....|....*..
gi 78706884 1238 KESSYKEK---LRQAEEERDKEISRLE 1261
Cdd:PRK04863 573 SVSEARERrmaLRQQLEQLQARIQRLA 599
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1438-1547 |
1.87e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1438 ENLQKKVERLHAEQLALQEGISGRDSEIKQLRSELKDAidenKTVREAKVGLENslkavqenmsaqegqfkqKIADIKGS 1517
Cdd:COG2433 416 RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEA----RSEERREIRKDR------------------EISRLDRE 473
|
90 100 110
....*....|....*....|....*....|
gi 78706884 1518 VDELQIKLKSLQEVRDHLESRNEELKRKLK 1547
Cdd:COG2433 474 IERLERELEEERERIEELKRKLERLKELWK 503
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1199-1406 |
2.20e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.69 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1199 LDVIKRSLQEKITQAEK---ERNELAVRHKAELEKIRETLKEKESSYKEKLRQAEEErdkeisrlevmrntIAELHKTNS 1275
Cdd:PHA02562 186 LDMKIDHIQQQIKTYNKnieEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDE--------------LLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1276 DREVELEGVKMEKCQLK---KLYDKSMLELEQLQ----CTADQKSSDLLPGSSNENIDDLQKKCDQY---VQDLELLRGE 1345
Cdd:PHA02562 252 DPSAALNKLNTAAAKIKskiEQFQKVIKMYEKGGvcptCTQQISEGPDRITKIKDKLKELQHSLEKLdtaIDELEEIMDE 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78706884 1346 -------KAELLSEIQKINGQHSNTIKKLEEIEAEMITLTTqkelERCEIAEKLETFKSKEADIKEAL 1406
Cdd:PHA02562 332 fneqskkLLELKNKISTNKQSLITLVDKAKKVKAAIEELQA----EFVDNAEELAKLQDELDKIVKTK 395
|
|
| CENP-H |
pfam05837 |
Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H ... |
1204-1266 |
2.50e-03 |
|
Centromere protein H (CENP-H); This family consists of several eukaryotic centromere protein H (CENP-H) sequences. Macromolecular centromere-kinetochore complex plays a critical role in sister chromatid separation, but its complete protein composition as well as its precise dynamic function during mitosis has not yet been clearly determined. CENP-H contains a coiled-coil structure and a nuclear localization signal. CENP-H is specifically and constitutively localized in kinetochores throughout the cell cycle. CENP-H may play a role in kinetochore organization and function throughout the cell cycle. This the C-terminus of the region, which is conserved from fungi to humans.
Pssm-ID: 461756 [Multi-domain] Cd Length: 114 Bit Score: 39.49 E-value: 2.50e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 78706884 1204 RSLQEKITQAEKERNELAVRHKAELEKIRETLKEKES-----SYKEKLRQAEEERDKEISRLEVMRNT 1266
Cdd:pfam05837 23 RELQEELTEVEKENLRLKRKNRELAAELLELAKEKESrredpKLRAQLEKLEAELKKSRRRWRVMKNV 90
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
939-1394 |
2.59e-03 |
|
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: 42.81 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 939 IIFQLKQEVdgKKNLIEEEKEVINNLRAQITSLNQIETIKNQNaktkilcEELQTKDTVQTANKQESQEVLTLKTSLAHL 1018
Cdd:pfam05557 10 RLSQLQNEK--KQMELEHKRARIELEKKASALKRQLDRESDRN-------QELQKRIRLLEKREAEAEEALREQAELNRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1019 KSKVCELQKKL--EKQSEDEKISELQSDI-GEISECCLSMELKLADI--VNWQAEELRPLDQLQE---SGVEL------- 1083
Cdd:pfam05557 81 KKKYLEALNKKlnEKESQLADAREVISCLkNELSELRRQIQRAELELqsTNSELEELQERLDLLKakaSEAEQlrqnlek 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1084 -QHHSTTAEESL-NVEKPIQEQTERTLTT-----------EYERRIEQLEES---LQRAQEELSILEKRKTD-------- 1139
Cdd:pfam05557 161 qQSSLAEAEQRIkELEFEIQSQEQDSEIVknskselaripELEKELERLREHnkhLNENIENKLLLKEEVEDlkrklere 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1140 -----ENKSLQLEyMAKIETSENENRSKFRAYCLDLK--ETQKRYEEQLQQTN----EKLASVTTQCQvHLDVIKRSLQE 1208
Cdd:pfam05557 241 ekyreEAATLELE-KEKLEQELQSWVKLAQDTGLNLRspEDLSRRIEQLQQREivlkEENSSLTSSAR-QLEKARRELEQ 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1209 KITQAEKERNELAVRHKAELEKIRETLKEKESSYKEK--LRQAEEERDKEIS----------RLEVMRNTIAELHKTNSD 1276
Cdd:pfam05557 319 ELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgYRAILESYDKELTmsnyspqlleRIEEAEDMTQKMQAHNEE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1277 REVELEGVKMEKCQLKKLYDKSMLELEQLQCTADQKSsdllPGSSNENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKI 1356
Cdd:pfam05557 399 MEAQLSVAEEELGGYKQQAQTLERELQALRQQESLAD----PSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERR 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 78706884 1357 NGQ-------------HSNTIKKLEEIEAEMITLtTQKELERC-EIAEKLET 1394
Cdd:pfam05557 475 CLQgdydpkktkvlhlSMNPAAEAYQQRKNQLEK-LQAEIERLkRLLKKLED 525
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
505-729 |
2.93e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 505 EKYEEQVKRLKETIERLEMENGKAVNLGEQFETHKAKSKQMEEELLSSISEKDSTIVSLQQSLEELSRDvLRNSKED--- 581
Cdd:pfam15921 614 DKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN-FRNKSEEmet 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 582 -------QMRSMCPELESSceRICNKCLELERLLPLASASGLDSvacQFDQLRSEIAATRMKLESMLSTFSHASCEVSQK 654
Cdd:pfam15921 693 ttnklkmQLKSAQSELEQT--RNTLKSMEGSDGHAMKVAMGMQK---QITAKRGQIDALQSKIQFLEEAMTNANKEKHFL 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 655 TTDCKRLSEQISTAHDDFGQ-------LQEKYNNLKHKWSSQKLAIDTMQVDYNTIQQKYLQLQDEYRHLELRSDEQCQQ 727
Cdd:pfam15921 768 KEEKNKLSQELSTVATEKNKmagelevLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQHTLDVKE 847
|
..
gi 78706884 728 LQ 729
Cdd:pfam15921 848 LQ 849
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
502-1582 |
3.51e-03 |
|
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: 42.47 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 502 ETIEKYEEQVKRLKETIERLEMENGKAVNLGEQFETHK---AKSKQMEEELLSSISEKDSTIVSLQQSLEELSRDVLRNS 578
Cdd:pfam01576 5 EEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKnalQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 579 KEDQMRSMcpELESSCERICNKCLELErllplasaSGLDSVACQFDQLRSEIAATRMKLESMLSTFSHASCEVSQKTTDC 658
Cdd:pfam01576 85 EEEEERSQ--QLQNEKKKMQQHIQDLE--------EQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 659 KRLSEQISTAHDDFGQLQEKYNNLKHKWSSQKLAIDTMQVDYNTIQQKYLQLQDEYRHLELRSDEqcqqLQDENSKLQAE 738
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTD----LQEQIAELQAQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 739 IGTLKERVEEIHSELLEVPNpdtHPEDMELQNQELKKRLSKLQWEFDEIQLNYEclsnelmstiQECDALREEHKQ-RTT 817
Cdd:pfam01576 231 IAELRAQLAKKEEELQAALA---RLEEETAQKNNALKKIRELEAQISELQEDLE----------SERAARNKAEKQrRDL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 818 NSDLESMKSSGVGT-ECSDPENELDTDLLQQFTKLSKSIQQiELTDYSGGRRLFIYNHAeqdQSVPSLKLCLEPAKYLEG 896
Cdd:pfam01576 298 GEELEALKTELEDTlDTTAAQQELRSKREQEVTELKKALEE-ETRSHEAQLQEMRQKHT---QALEELTEQLEQAKRNKA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 897 D---GKQHDASDSVFLKGFLKCqrFQIVKINQEQNLVKEEDRMRDIIFQLKQEVDGKKNLIEEEKEVINNLRAQITSLNQ 973
Cdd:pfam01576 374 NlekAKQALESENAELQAELRT--LQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNE 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 974 IETiKNQNAKTKILCEELQTKDTvQTANKQESQEVLTLKTSLAHLKSKVCELQKKLEKQSEDEKISELQsdigeisecCL 1053
Cdd:pfam01576 452 AEG-KNIKLSKDVSSLESQLQDT-QELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQ---------LS 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1054 SMELKLADIVNWQAEELRPLDQLQESGVELQHHSTTAEESLNVEKPIQEQTERTlTTEYERRIEQLEESLQRAQEELSIL 1133
Cdd:pfam01576 521 TLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKT-KNRLQQELDDLLVDLDHQRQLVSNL 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1134 EK--RKTD----ENKSLQLEYMAKIETSENENRSK-FRAYCL--------DLKETQKRYEEQLQQTNEKLASVTTQC--Q 1196
Cdd:pfam01576 600 EKkqKKFDqmlaEEKAISARYAEERDRAEAEAREKeTRALSLaraleealEAKEELERTNKQLRAEMEDLVSSKDDVgkN 679
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1197 VH-LDVIKRSL----QEKITQAEKERNELAVRHKAELeKIRETLKEKESSYKEKLrQAEEERDKEISRLevmrntiaeLH 1271
Cdd:pfam01576 680 VHeLERSKRALeqqvEEMKTQLEELEDELQATEDAKL-RLEVNMQALKAQFERDL-QARDEQGEEKRRQ---------LV 748
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1272 KTNSDREVELEGVKMEKCQLKKLYDKSMLELEQL--QCTADQKSSDllpgSSNENIDDLQKKCDQYVQDLELLRGEKAEL 1349
Cdd:pfam01576 749 KQVRELEAELEDERKQRAQAVAAKKKLELDLKELeaQIDAANKGRE----EAVKQLKKLQAQMKDLQRELEEARASRDEI 824
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1350 LSeiqkingQHSNTIKKLEEIEAEMITLTT----------QKELERCEIAEKLETFKSKEADIKEalhcaqlrlhaydkl 1419
Cdd:pfam01576 825 LA-------QSKESEKKLKNLEAELLQLQEdlaaserarrQAQQERDELADEIASGASGKSALQD--------------- 882
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1420 vcEYERLKGCLSDSNKLSENLQKKVERLHAEQLALQegisgrdSEIKQLRSELKDAIDENKTVREAKVGLENSLKAVQEN 1499
Cdd:pfam01576 883 --EKRRLEARIAQLEEELEEEQSNTELLNDRLRKST-------LQVEQLTTELAAERSTSQKSESARQQLERQNKELKAK 953
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1500 MSAQEGQFKQKIadiKGSVDELQIKLKSLQEVRDHlESR-----NEELKRKLKDAQELQNMVDKERKLNSSLREDFDK-- 1572
Cdd:pfam01576 954 LQEMEGTVKSKF---KSSIAALEAKIAQLEEQLEQ-ESRerqaaNKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKgn 1029
|
1130
....*....|..
gi 78706884 1573 --LEQTKLDLEE 1582
Cdd:pfam01576 1030 srMKQLKRQLEE 1041
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1111-1297 |
4.18e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1111 EYERRIEQLEESLQRAQEELSILEKRKTDENKSLQlEYMAKIETSENEnRSKFRAYCLDLKETQKRYEEQLQQ--TNEKL 1188
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLE-AAKTELEDLEKE-IKRLELEIEEVEARIKKYEEQLGNvrNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1189 ASVTTQCQvhldvikrSLQEKITQAEKERNELAVRhKAELEKIRETLKEKESSYKEKLRQAEEERDKEISRLEvmrntiA 1268
Cdd:COG1579 92 EALQKEIE--------SLKRRISDLEDEILELMER-IEELEEELAELEAELAELEAELEEKKAELDEELAELE------A 156
|
170 180
....*....|....*....|....*....
gi 78706884 1269 ELHKTNSDREVELEGVKMEkcqLKKLYDK 1297
Cdd:COG1579 157 ELEELEAEREELAAKIPPE---LLALYER 182
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1006-1306 |
4.24e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1006 QEVLTLKTSLAHLKSKVCELQKKLEKQSEDEkiSELQSDIGEISecclsmelklaDIVNWQAEELRPLDQLQESGVELQH 1085
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAE--SDLEQDYQAAS-----------DHLNLVQTALRQQEKIERYQADLEE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1086 HSTTAEESLNVEKPIQEQTErtlttEYERRIEQLEESLQRA-------QEELSILEKRKTDENKSLQLeyMAKIE----- 1153
Cdd:PRK04863 360 LEERLEEQNEVVEEADEQQE-----ENEARAEAAEEEVDELksqladyQQALDVQQTRAIQYQQAVQA--LERAKqlcgl 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1154 ---TSENenrskfraycldLKETQKRYEEQLQQTNEKLASVTTQCQVHLD----------------------VIKRSLQE 1208
Cdd:PRK04863 433 pdlTADN------------AEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsqfeqayqlvrkiagevsrsEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1209 KITQAEKERNeLAVRhkaeLEKIRETLKEKESSYKEKlRQAEEERDKEISRLEVMRNTIAELHKTNSDREVELEGVKMEK 1288
Cdd:PRK04863 501 LLRRLREQRH-LAEQ----LQQLRMRLSELEQRLRQQ-QRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESV 574
|
330
....*....|....*...
gi 78706884 1289 CQLKKLYDKSMLELEQLQ 1306
Cdd:PRK04863 575 SEARERRMALRQQLEQLQ 592
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
938-1145 |
4.80e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 938 DIIFQLKQEVDGKKNLIEEEKEVINNLRAQITSL-NQIETIKNQNAKTKILCEELQTKDTVQTANKQESQ-EVLTLKTSL 1015
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALlKQLAALERRIAALARRIRALEQELAALEAELAELEkEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1016 AHLKSKVCELQKKLEKQSEDEKISEL--QSDIGEIseccLSMELKLADIVNWQAEELRPLDQLQESGVELQHHSTTAEES 1093
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLlsPEDFLDA----VRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 78706884 1094 LNVEKPIQEQTERTLTTEYERR---IEQLEESLQRAQEELSILEKRKTDENKSLQ 1145
Cdd:COG4942 176 LEALLAELEEERAALEALKAERqklLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
490-1193 |
4.92e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.13 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 490 ISALTASNQVAKETIEKYEEQVKRLKETIE---RLEMENGKAVNLGEQFEThkAKSKQMEEELLS-SISEKDSTIVSLQQ 565
Cdd:pfam12128 202 IVAILEDDGVVPPKSRLNRQQVEHWIRDIQaiaGIMKIRPEFTKLQQEFNT--LESAELRLSHLHfGYKSDETLIASRQE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 566 SLEELSRDV--LRNSKEDQMRSMCPE----LESSCERICNKCLELERLlplasasglDSVACQFDQLRSEIAATRMkleS 639
Cdd:pfam12128 280 ERQETSAELnqLLRTLDDQWKEKRDElngeLSAADAAVAKDRSELEAL---------EDQHGAFLDADIETAAADQ---E 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 640 MLSTFShascevsqktTDCKRLSEQISTAHDDFGQLQEKYNNLKHKWSSQkLAIDTMQVDYNTIQQK---YLQLQDEYRH 716
Cdd:pfam12128 348 QLPSWQ----------SELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ-NNRDIAGIKDKLAKIRearDRQLAVAEDD 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 717 LElrsdEQCQQLQDENSKLQAEIGTLKERVEEIHSELLEVPNPDTHPEDMELQNQELKKRLSKLQWEFDEIQLNYECLSN 796
Cdd:pfam12128 417 LQ----ALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQS 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 797 ELMS----TIQECDALREEH----KQRTTNSDLESMKSSGVGT-----------------ECSDPENELDTDLLQQFTKL 851
Cdd:pfam12128 493 ELRQarkrRDQASEALRQASrrleERQSALDELELQLFPQAGTllhflrkeapdweqsigKVISPELLHRTDLDPEVWDG 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 852 SKSiqqIELTDYSGGRRLFIYNHAEQDQSVPSLKLCLEPAKY-LEGDGKQHDASDSVFLKGFLKCQRFQIVKINQEQNLV 930
Cdd:pfam12128 573 SVG---GELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEaLQSAREKQAAAEEQLVQANGELEKASREETFARTALK 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 931 KEEDRMRDIIFQLKQEVDGKKNLIEEEKEVINnlraqiTSLNQIETIKNQNAKT-KILCEELQ-TKDTVQTANKQESQEV 1008
Cdd:pfam12128 650 NARLDLRRLFDEKQSEKDKKNKALAERKDSAN------ERLNSLEAQLKQLDKKhQAWLEEQKeQKREARTEKQAYWQVV 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1009 L-TLKTSLAHLKSKVCELQKKLE---KQSEDEKISELQS-DIGEISECCLSMEL-----KLADIVNWQAEELRPLDQLQE 1078
Cdd:pfam12128 724 EgALDAQLALLKAAIAARRSGAKaelKALETWYKRDLASlGVDPDVIAKLKREIrtlerKIERIAVRRQEVLRYFDWYQE 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1079 SgvELQHHSTTAEESLNVEKPIQE--QTERTLTTEYERRIEQLEESLQ--RAQEELSILEKRKTDenksLQLEYMAKIET 1154
Cdd:pfam12128 804 T--WLQRRPRLATQLSNIERAISElqQQLARLIADTKLRRAKLEMERKasEKQQVRLSENLRGLR----CEMSKLATLKE 877
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 78706884 1155 SENENRSK----FRAYCL-DLKETQKRYEEQLQQTNEKLASVTT 1193
Cdd:pfam12128 878 DANSEQAQgsigERLAQLeDLKLKRDYLSESVKKYVEHFKNVIA 921
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
953-1130 |
4.94e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 953 LIEEEKEVINNLRAQITSLNQIETIKNQNAKTKILCEELQTKDTVQTANKQESQEVLTLKTSLAHLKSKVCELqKKLEKQ 1032
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDL-AALEEQ 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1033 SED--EKISELQSDIGEISECCLSMELKLADIVNWQAEELRPLDQLQESGVELQHhsTTAEESLnvEKPIQEQTERTLTT 1110
Cdd:COG4913 694 LEEleAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR--ALLEERF--AAALGDAVERELRE 769
|
170 180
....*....|....*....|
gi 78706884 1111 EYERRIEQLEESLQRAQEEL 1130
Cdd:COG4913 770 NLEERIDALRARLNRAEEEL 789
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
920-1305 |
5.18e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 920 IVKINQEQNLVKEEDRMRDIIFQLKQEVDGKKNLIEEEKEVINNLRAQITSLNQIETIKNQNAKTKILCEELQTKDTVQT 999
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1000 ANKQESQEVLTLKTSLAHLKSKVCELQKKLEKQSED------EKISELQSDIGEISECCLSMELKLADIVNWQAEELRPL 1073
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQlslateEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1074 DQLQESGVELQHHSTTAEE-----------SLNVEKPIQEQTERT----------LTTEYERRIEQLEESLQRAQEELSI 1132
Cdd:COG4717 230 EQLENELEAAALEERLKEArlllliaaallALLGLGGSLLSLILTiagvlflvlgLLALLFLLLAREKASLGKEAEELQA 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1133 LEKRKTDENKSLQlEYMAKIETSENENRSKFRAYCLDLKETQKRyEEQLQQTNEKLasvttQCQVHLDVIKRSLQEKITQ 1212
Cdd:COG4717 310 LPALEELEEEELE-ELLAALGLPPDLSPEELLELLDRIEELQEL-LREAEELEEEL-----QLEELEQEIAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1213 AEKERNELAVRH------KAELEKIRETLKEKESSYKEKLRQAEEER-DKEISRLEVMRNTIAELHKTNSDREVELEGvK 1285
Cdd:COG4717 383 DEEELRAALEQAeeyqelKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREELAELEA-E 461
|
410 420
....*....|....*....|
gi 78706884 1286 MEKCQLKKLYDKSMLELEQL 1305
Cdd:COG4717 462 LEQLEEDGELAELLQELEEL 481
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1201-1404 |
5.74e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1201 VIKRSLQEKITQAEKERNELavrhkaelekIRETLKEKESSYKEKLRQAEEERDKEISrlevmrntiaELHKTNSDREVE 1280
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRI----------LEEAKKEAEAIKKEALLEAKEEIHKLRN----------EFEKELRERRNE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1281 LEgvKMEKcqlkKLYDKSmlelEQLqctaDQKSsdllpgssnENIDDLQKKCDQYVQDLELLRGEKAELLSEIQKIngqH 1360
Cdd:PRK12704 84 LQ--KLEK----RLLQKE----ENL----DRKL---------ELLEKREEELEKKEKELEQKQQELEKKEEELEEL---I 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 78706884 1361 SNTIKKLEEI------EA-EMITLTTQKELErceiAEKLETFKSKEADIKE 1404
Cdd:PRK12704 138 EEQLQELERIsgltaeEAkEILLEKVEEEAR----HEAAVLIKEIEEEAKE 184
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1204-1889 |
5.79e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 41.66 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1204 RSLQEKITQAEKERNELAVRHKAELEKIRETLKE-KESSYKEKLR-QAEEERDKEISRLEVMRNTIAELHKTnsdrevEL 1281
Cdd:pfam07111 51 RSLELEGSQALSQQAELISRQLQELRRLEEEVRLlRETSLQQKMRlEAQAMELDALAVAEKAGQAEAEGLRA------AL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1282 EGVKMEKcqlKKLYDKSMLELEQLQcTADQKSSDLLPGSSNENIDDLQKKCD---QYVQDLELLRGEKAELLSEIQK--- 1355
Cdd:pfam07111 125 AGAEMVR---KNLEEGSQRELEEIQ-RLHQEQLSSLTQAHEEALSSLTSKAEgleKSLNSLETKRAGEAKQLAEAQKeae 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1356 -INGQHSNTikkLEEIEAEMITLTTQK----------------ELERCEIAEKLETFKSKEADIKEALHCAQLRLHAYDK 1418
Cdd:pfam07111 201 lLRKQLSKT---QEELEAQVTLVESLRkyvgeqvppevhsqtwELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1419 LVCEYErlkgclsdsnklsENLQKKVERLHAEQLALQegisgrdseiKQLRSELKDAidenktvREAKVGLENSLKAvqe 1498
Cdd:pfam07111 278 MLALQE-------------EELTRKIQPSDSLEPEFP----------KKCRSLLNRW-------REKVFALMVQLKA--- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1499 nmsaQEGQFKQKIADIKGSVDELQIKLKSLQE----VRDHLESRNEELKRKLKDAQELQNMVDKERKLNSSLREDFDKLE 1574
Cdd:pfam07111 325 ----QDLEHRDSVKQLRGQVAELQEQVTSQSQeqaiLQRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1575 QTKLDLEEQLRAKKVEIDRRSKELGEVTKDCENIRSDLEAQTNDF--LKERETLNLTISDLRLHNEQLLETSKNYLSDIT 1652
Cdd:pfam07111 401 EQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVhtIKGLMARKVALAQLRQESCPPPPPAPPVDADLS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1653 AA--------NNLNLEMKKNLHDLTKECKSLRsdlqskeEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKALKEDCEK 1724
Cdd:pfam07111 481 LEleqlreerNRLDAELQLSAHLIQQEVGRAR-------EQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQG 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1725 LRSTLESKELILQQNKQELEERLTVINEKNGK-NALLDAQLKSNETAFTSLRKAWIKQSLAIEAANKRSLEMEQKVDKRT 1803
Cdd:pfam07111 554 QQESTEEAASLRQELTQQQEIYGQALQEKVAEvETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQELR 633
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1804 REYEELRstlktreinfRSEKERMDGTISSLLEDKrNLEEKLCTVTELLAKLKRE-----LPALHTQKVNGGDVSIELNS 1878
Cdd:pfam07111 634 RLQDEAR----------KEEGQRLARRVQELERDK-NLMLATLQQEGLLSRYKQQrllavLPSGLDKKSVVSSPRPECSA 702
|
730
....*....|.
gi 78706884 1879 SngSPTPAAVP 1889
Cdd:pfam07111 703 S--APIPAAVP 711
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1171-1264 |
5.95e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 41.74 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1171 KETQKRYEEQLQQTNEKLASVTTQcqvhldviKRSLQEKITQAEKERNELAVRH------KAELEKIRETLKEK-ESSYK 1243
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEEL--------ERELEQKAEEAEALLKEAEKLKeeleekKEKLQEEEDKLLEEaEKEAQ 576
|
90 100
....*....|....*....|.
gi 78706884 1244 EKLRQAEEERDKEISRLEVMR 1264
Cdd:PRK00409 577 QAIKEAKKEADEIIKELRQLQ 597
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1660-1866 |
6.30e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.59 E-value: 6.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1660 EMKKNLHDLTKECKSLRSDLQSKEEYFQTQKQLLDETISN-------LKEENRKMEEKLSSGNKALKEDCEKL---RSTL 1729
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRleeieqlLEELNKKIKDLGEEEQLRVKEKIGELeaeIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1730 ESKELILQQNKQELEERLTVINEKNGKnalLDAQLKSNETAFTSLRKAWIKQSLAIEAANKRSLEMEQK---VDKRTREY 1806
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDK---LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAEleeVDKEFAET 383
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1807 EELRSTLKTREINFRSEKERMDGTISSLLEDKRNLEEKLCTVTELLAKLKRELPALHTQK 1866
Cdd:TIGR02169 384 RDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
705-1283 |
6.42e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 705 QKYLQLQDEYRHLE--LRSDEQcQQLQDENSKLQAEIGTLKERVEEIHSELlevpnpdthpEDMELQNQELKKRLSKLQW 782
Cdd:COG1196 213 ERYRELKEELKELEaeLLLLKL-RELEAELEELEAELEELEAELEELEAEL----------AELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 783 EFDEIQLNYECLSNELMSTIQECDALREEHKQRTTNsdlesmkssgvgtecsdpENELDTDLLQQFTKLSKSIQQIELTD 862
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEER------------------LEELEEELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 863 YSGGRRLFIYNHAEQDQSVPSLKLCLEPAKYLEGDGKQHDASDSVF--LKGFLKCQRFQIVKINQEQNLVKEEDRMRDII 940
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLeaLRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 941 FQLKQEVDGKKNLIEEEKEVINNLRAQitslnQIETIKNQNAKTKILCEELQTKDTVQTANKQESQEVLTLKTSLAHLKs 1020
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEE-----EAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL- 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1021 kvcELQKKLEKQSEDEKISELQSDIGEISECCLsmELKLADIVNWQAEELRPLDQLQESGVELQHHSTTAEESLnVEKPI 1100
Cdd:COG1196 498 ---EAEADYEGFLEGVKAALLLAGLRGLAGAVA--VLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYL-KAAKA 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1101 QEQTERTLTTEYERRIEQLEESLQRAQEELSILEKRKTDENKSLQLEYMAKIETSENENRSKFRAYCLDLKETQKRYEEQ 1180
Cdd:COG1196 572 GRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1181 LQQTNEKLASVTTQcqvhldvIKRSLQEKITQAEKERNELAVRHKAELEKIRETLKEKESSyKEKLRQAEEERDKEISRL 1260
Cdd:COG1196 652 EGEGGSAGGSLTGG-------SRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE-ERELAEAEEERLEEELEE 723
|
570 580
....*....|....*....|...
gi 78706884 1261 EVMRNTIAELHKTNSDREVELEG 1283
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEE 746
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1113-1261 |
6.98e-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: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1113 ERRIEQLEESLQRAQEELSILEKRKTDENKslQLEYMAKIEtSENENRSKFRAYCLDLKETQKRYEE------QLQQTNE 1186
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEA--ELDALQERR-EALQRLAEYSWDEIDVASAEREIAEleaeleRLDASSD 685
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78706884 1187 KLasvttqcqvhldvikRSLQEKITQAEKERNelavrhkaELEKIRETLKEKESSYKEKLRQAEEERDKEISRLE 1261
Cdd:COG4913 686 DL---------------AALEEQLEELEAELE--------ELEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1659-1745 |
7.61e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1659 LEMKKNLHDLT----KECKSLRSDLQSKEEYFQTQKQLLDETISNLKEENRKMEEKLSSGNKaLKEDCEKLRSTLEskEL 1734
Cdd:PRK12704 60 LEAKEEIHKLRnefeKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQ-KQQELEKKEEELE--EL 136
|
90
....*....|.
gi 78706884 1735 ILQQNkQELEE 1745
Cdd:PRK12704 137 IEEQL-QELER 146
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1519-1645 |
8.79e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1519 DELQIKLKSLQEVRDHLESRNEELKRKLKdaqELQNMVDKERKLNSSLREDFDKLEQTKLDLEEQLRAKKVEIDRRSKEL 1598
Cdd:COG2433 388 KELPEEEPEAEREKEHEERELTEEEEEIR---RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKD 464
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 78706884 1599 GEVTKdcenirsdLEAQTNDFLKERETLNLTISDLRLHNEQLLETSK 1645
Cdd:COG2433 465 REISR--------LDREIERLERELEEERERIEELKRKLERLKELWK 503
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1660-1859 |
9.16e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1660 EMKKNLHDLTKECKSLRSDLQSKE---EYFQTQKQLLDETISNLKEENRKMEEKLSSGNKALKEDCEKLRSTLESkeliL 1736
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER----L 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78706884 1737 QQNKQELEERLTVINEKNGKNALLDAQLKSNETAFTSLRKAWIKQSLAIEAANKRSLEMEQKVDKRTREYEELRST---L 1813
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAaaeL 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 78706884 1814 KTREINFRSEKERMDGTISSLLEDKRNLEEKLCTVTELLAKLKREL 1859
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
|
| |
