|
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 ... |
8-321 |
2.59e-128 |
|
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: 405.95 E-value: 2.59e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 8 SIQVCIKVRPCEPGLT-----SLWQVKERrSIHLADSHAEPYVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIFAY 82
Cdd:cd01374 1 KITVTVRVRPLNSREIgineqVAWEIDND-TIYLVEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 83 GQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISSETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHE-SGNGIVNVNC 161
Cdd:cd01374 80 GQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDdVEKGVYVAGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 162 EECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSDDDAVIQSVLNLVDLAGSERADQTGARG 241
Cdd:cd01374 160 TEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTVRVSTLNLIDLAGSERAAQTGAAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 242 ARLKEGGHINKSLLFLSNVIKSLSENADNRFTNYRDSKLTRILQASLGGNAFTSIICTIKP--SIMEESQSTLSFATRAK 319
Cdd:cd01374 240 VRRKEGSHINKSLLTLGTVISKLSEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPaeSHVEETLNTLKFASRAK 319
|
..
gi 442627454 320 KI 321
Cdd:cd01374 320 KI 321
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
8-328 |
1.12e-120 |
|
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: 385.00 E-value: 1.12e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 8 SIQVCIKVRP-----CEPGLTSLWQV--KERRSIHLADSHAEP----YVFDYVFDEGASNQEVFDRMAKHIVHACMQGFN 76
Cdd:smart00129 1 NIRVVVRVRPlnkreKSRKSPSVVPFpdKVGKTLTVRSPKNRQgekkFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 77 GTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISS-ETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNG 155
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKrEEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIREDEKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 156 IVNV-NCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDhSDDDAVIQSVLNLVDLAGSERA 234
Cdd:smart00129 161 GVYVkGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN-SSSGSGKASKLNLVDLAGSERA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 235 DQTGARGARLKEGGHINKSLLFLSNVIKSLSENADNRFTNYRDSKLTRILQASLGGNAFTSIICTIKPSI--MEESQSTL 312
Cdd:smart00129 240 KKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSsnLEETLSTL 319
|
330
....*....|....*.
gi 442627454 313 SFATRAKKIRIKPQVN 328
Cdd:smart00129 320 RFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
2-321 |
7.06e-118 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 376.53 E-value: 7.06e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 2 SAKNASSIQVCIKVRPCEPGLTSLWQVKERRSihladshaepYVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIFA 81
Cdd:pfam00225 10 KERGSSVIVSVESVDSETVESSHLTNKNRTKT----------FTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 82 YGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISSETERD-FLLRVGYIEIYNEKIYDLLNKKNQD---LKIHESGNGIV 157
Cdd:pfam00225 80 YGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSeFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKKGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 158 NV-NCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSDDDAVIQSVLNLVDLAGSERADQ 236
Cdd:pfam00225 160 YVkGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSERASK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 237 TG-ARGARLKEGGHINKSLLFLSNVIKSLSENADNrFTNYRDSKLTRILQASLGGNAFTSIICTIKPSI--MEESQSTLS 313
Cdd:pfam00225 240 TGaAGGQRLKEAANINKSLSALGNVISALADKKSK-HIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSsnYEETLSTLR 318
|
....*...
gi 442627454 314 FATRAKKI 321
Cdd:pfam00225 319 FASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
8-319 |
1.49e-109 |
|
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: 352.71 E-value: 1.49e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 8 SIQVCIKVRP----CEPGLTSLWQVKERRSIHL---ADSHAEP--YVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGT 78
Cdd:cd00106 1 NVRVAVRVRPlngrEARSAKSVISVDGGKSVVLdppKNRVAPPktFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 79 IFAYGQTSSGKTYTMMGDEQN-PGVMVLAAKEIFQQISS--ETERDFLLRVGYIEIYNEKIYDLLNKKNQ-DLKIHESGN 154
Cdd:cd00106 81 IFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERIDKrkETKSSFSVSASYLEIYNEKIYDLLSPVPKkPLSLREDPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 155 -GIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDhSDDDAVIQSVLNLVDLAGSER 233
Cdd:cd00106 161 rGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNRE-KSGESVTSSKLNLVDLAGSER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 234 ADQTGARGARLKEGGHINKSLLFLSNVIKSLSENaDNRFTNYRDSKLTRILQASLGGNAFTSIICTIKPSIM--EESQST 311
Cdd:cd00106 240 AKKTGAEGDRLKEGGNINKSLSALGKVISALADG-QNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSEnfEETLST 318
|
....*...
gi 442627454 312 LSFATRAK 319
Cdd:cd00106 319 LRFASRAK 326
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
44-321 |
3.21e-92 |
|
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast kinesin KIP3 plays a role in positioning the mitotic spindle. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276821 [Multi-domain] Cd Length: 345 Bit Score: 303.50 E-value: 3.21e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 44 YVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISS-ETERDF 122
Cdd:cd01370 63 YVFDRVFDETSTQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESlKDEKEF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 123 LLRVGYIEIYNEKIYDLLNKKNQDLKIHE-SGNGIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIF 201
Cdd:cd01370 143 EVSMSYLEIYNETIRDLLNPSSGPLELREdAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 202 KIIIESRKSDHSDDDAVIQSVLNLVDLAGSERADQTGARGARLKEGGHINKSLLFLSNVIKSLSENA-DNRFTNYRDSKL 280
Cdd:cd01370 223 QITVRQQDKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGkKNKHIPYRDSKL 302
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 442627454 281 TRILQASLGGNAFTSIICTIKPSIM--EESQSTLSFATRAKKI 321
Cdd:cd01370 303 TRLLKDSLGGNCRTVMIANISPSSSsyEETHNTLKYANRAKNI 345
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
7-321 |
1.27e-91 |
|
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: 301.17 E-value: 1.27e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 7 SSIQVCIKVRPcEPGLT------SLWQVKERRSIHLADSHAE-PYVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTI 79
Cdd:cd01369 2 CNIKVVCRFRP-LNELEvlqgskSIVKFDPEDTVVIATSETGkTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 80 FAYGQTSSGKTYTMMG---DEQNPGVMVLAAKEIFQQISSETERD-FLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNG 155
Cdd:cd01369 81 FAYGQTSSGKTYTMEGklgDPESMGIIPRIVQDIFETIYSMDENLeFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 156 IVNV-NCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRksdHSDDDAVIQSVLNLVDLAGSERA 234
Cdd:cd01369 161 GPYVkGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE---NVETEKKKSGKLYLVDLAGSEKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 235 DQTGARGARLKEGGHINKSLLFLSNVIKSLSENADNrFTNYRDSKLTRILQASLGGNAFTSIICTIKPSIMEESQ--STL 312
Cdd:cd01369 238 SKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKT-HIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESEtlSTL 316
|
....*....
gi 442627454 313 SFATRAKKI 321
Cdd:cd01369 317 RFGQRAKTI 325
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
7-322 |
2.93e-89 |
|
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: 295.01 E-value: 2.93e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 7 SSIQVCIKVRP------CEPGLTSLWQVKERRSIHLADSHAepYVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIF 80
Cdd:cd01372 1 SSVRVAVRVRPllpkeiIEGCRICVSFVPGEPQVTVGTDKS--FTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 81 AYGQTSSGKTYTMMG------DEQNPGVMVLAAKEIFQQIS-SETERDFLLRVGYIEIYNEKIYDLLN---KKNQDLKIH 150
Cdd:cd01372 79 AYGQTGSGKTYTMGTaytaeeDEEQVGIIPRAIQHIFKKIEkKKDTFEFQLKVSFLEIYNEEIRDLLDpetDKKPTISIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 151 ESGNG-IVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRK-------SDHSDDDAVIQSV 222
Cdd:cd01372 159 EDSKGgITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKkngpiapMSADDKNSTFTSK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 223 LNLVDLAGSERADQTGARGARLKEGGHINKSLLFLSNVIKSL-SENADNRFTNYRDSKLTRILQASLGGNAFTSIICTIK 301
Cdd:cd01372 239 FHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALgDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVS 318
|
330 340
....*....|....*....|...
gi 442627454 302 PSI--MEESQSTLSFATRAKKIR 322
Cdd:cd01372 319 PADsnFEETLNTLKYANRARNIK 341
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
7-328 |
5.55e-88 |
|
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: 291.95 E-value: 5.55e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 7 SSIQVCIKVRP-----CEPGLTSLWQVKERRSIHLADSHAE-----------PYVFDYVFDE-------GASNQEVFDRM 63
Cdd:cd01365 1 ANVKVAVRVRPfnsreKERNSKCIVQMSGKETTLKNPKQADknnkatrevpkSFSFDYSYWShdsedpnYASQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 64 AKHIVHACMQGFNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQI--SSETERDFLLRVGYIEIYNEKIYDLLN 141
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIadTTNQNMSYSVEVSYMEIYNEKVRDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 142 KKN----QDLKIHES-GNGIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSD-HSDD 215
Cdd:cd01365 161 PKPkknkGNLKVREHpVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDaETNL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 216 DAVIQSVLNLVDLAGSERADQTGARGARLKEGGHINKSLLFLSNVIKSLSENAD------NRFTNYRDSKLTRILQASLG 289
Cdd:cd01365 241 TTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkkSSFIPYRDSVLTWLLKENLG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 442627454 290 GNAFTSIICTIKPSIM--EESQSTLSFATRAKKIRIKPQVN 328
Cdd:cd01365 321 GNSKTAMIAAISPADInyEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
9-323 |
6.96e-85 |
|
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: 281.79 E-value: 6.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 9 IQVCIKVRPCEPGLT----SLWQVKE--RRSIHLADSHAEPYVF--DYVFDEGASNQEVFdRMAKHIVHACMQGFNGTIF 80
Cdd:cd01366 4 IRVFCRVRPLLPSEEnedtSHITFPDedGQTIELTSIGAKQKEFsfDKVFDPEASQEDVF-EEVSPLVQSALDGYNVCIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 81 AYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISSETERD--FLLRVGYIEIYNEKIYDLLNK---KNQDLKI-HESGN 154
Cdd:cd01366 83 AYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGwsYTIKASMLEIYNETIRDLLAPgnaPQKKLEIrHDSEK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 155 GIVNV-NCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRksdHSDDDAVIQSVLNLVDLAGSER 233
Cdd:cd01366 163 GDTTVtNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGR---NLQTGEISVGKLNLVDLAGSER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 234 ADQTGARGARLKEGGHINKSLLFLSNVIKSLSENadNRFTNYRDSKLTRILQASLGGNAFTSIICTIKP--SIMEESQST 311
Cdd:cd01366 240 LNKSGATGDRLKETQAINKSLSALGDVISALRQK--QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPaeSNLNETLNS 317
|
330
....*....|..
gi 442627454 312 LSFATRAKKIRI 323
Cdd:cd01366 318 LRFASKVNSCEL 329
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
8-321 |
5.15e-83 |
|
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: 276.65 E-value: 5.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 8 SIQVCIKVRPC-----EPGLTSLWQVKE-RRSIHL----ADSHAEP--YVFDYVFDEGASNQEVFDRMAKHIVHACMQGF 75
Cdd:cd01371 2 NVKVVVRCRPLngkekAAGALQIVDVDEkRGQVSVrnpkATANEPPktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 76 NGTIFAYGQTSSGKTYTMMG---DEQNPGVMVLAAKEIFQQISSETE-RDFLLRVGYIEIYNEKIYDLLNK-KNQDLKIH 150
Cdd:cd01371 82 NGTIFAYGQTGTGKTYTMEGkreDPELRGIIPNSFAHIFGHIARSQNnQQFLVRVSYLEIYNEEIRDLLGKdQTKRLELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 151 ES-GNGIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSDDDAVIQSVLNLVDLA 229
Cdd:cd01371 162 ERpDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 230 GSERADQTGARGARLKEGGHINKSLLFLSNVIKSLsenADNRFTN--YRDSKLTRILQASLGGNAFTSIICTIKP--SIM 305
Cdd:cd01371 242 GSERQSKTGATGERLKEATKINLSLSALGNVISAL---VDGKSTHipYRDSKLTRLLQDSLGGNSKTVMCANIGPadYNY 318
|
330
....*....|....*.
gi 442627454 306 EESQSTLSFATRAKKI 321
Cdd:cd01371 319 DETLSTLRYANRAKNI 334
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
7-329 |
1.16e-79 |
|
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: 267.65 E-value: 1.16e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 7 SSIQVCIKVRP---------------CEPgltSLWQVKERRSIHLADSHAEPYVFDYVFDEGASNQEVFDRMAKHIVHAC 71
Cdd:cd01364 2 KNIQVVVRCRPfnlrerkasshsvveVDP---VRKEVSVRTGGLADKSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 72 MQGFNGTIFAYGQTSSGKTYTMMGD---------EQNP--GVMVLAAKEIFQQISSeTERDFLLRVGYIEIYNEKIYDLL 140
Cdd:cd01364 79 LMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwELDPlaGIIPRTLHQLFEKLED-NGTEYSVKVSYLEIYNEELFDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 141 ---NKKNQDLKIHES---GNGIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSD 214
Cdd:cd01364 158 spsSDVSERLRMFDDprnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 215 DDAVIQSVLNLVDLAGSERADQTGARGARLKEGGHINKSLLFLSNVIKSLSENADNrfTNYRDSKLTRILQASLGGNAFT 294
Cdd:cd01364 238 EELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPH--VPYRESKLTRLLQDSLGGRTKT 315
|
330 340 350
....*....|....*....|....*....|....*..
gi 442627454 295 SIICTIKPSI--MEESQSTLSFATRAKKIRIKPQVNE 329
Cdd:cd01364 316 SIIATISPASvnLEETLSTLEYAHRAKNIKNKPEVNQ 352
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
9-329 |
1.10e-78 |
|
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: 264.76 E-value: 1.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 9 IQVCIKVRPCEPGLTSL---WQVKERRSIHLAdSHAEP---YVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIFAY 82
Cdd:cd01373 3 VKVFVRIRPPAEREGDGeygQCLKKLSSDTLV-LHSKPpktFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 83 GQTSSGKTYTMMG----DEQNPGVMVLAAKEIFQQISSETERD---------FLLRVGYIEIYNEKIYDLLNKKNQDLKI 149
Cdd:cd01373 82 GQTGSGKTYTMWGpsesDNESPHGLRGVIPRIFEYLFSLIQREkekagegksFLCKCSFLEIYNEQIYDLLDPASRNLKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 150 HES-GNGIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESrKSDHSDDDAVIQSVLNLVDL 228
Cdd:cd01373 162 REDiKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES-WEKKACFVNIRTSRLNLVDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 229 AGSERADQTGARGARLKEGGHINKSLLFLSNVIKSLSENAD--NRFTNYRDSKLTRILQASLGGNAFTSIICTIKPSI-- 304
Cdd:cd01373 241 AGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgkQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSkc 320
|
330 340
....*....|....*....|....*
gi 442627454 305 MEESQSTLSFATRAKKIRIKPQVNE 329
Cdd:cd01373 321 FGETLSTLRFAQRAKLIKNKAVVNE 345
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
2-359 |
1.10e-71 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 252.35 E-value: 1.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 2 SAKNASSIQVCIKVRPCEPGLTsLWQVKERRSIHLADSHAEPYVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIFA 81
Cdd:COG5059 17 NEKSVSDIKSTIRIIPGELGER-LINTSKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 82 YGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQIS-SETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNGIVNV- 159
Cdd:COG5059 96 YGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEdLSMTKDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVa 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 160 NCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSDDdavIQSVLNLVDLAGSERADQTGA 239
Cdd:COG5059 176 GLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTS---ETSKLSLVDLAGSERAARTGN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 240 RGARLKEGGHINKSLLFLSNVIKSLSENADNRFTNYRDSKLTRILQASLGGNAFTSIICTIKPS--IMEESQSTLSFATR 317
Cdd:COG5059 253 RGTRLKEGASINKSLLTLGNVINALGDKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSsnSFEETINTLKFASR 332
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 442627454 318 AKKIRIKPQVNEMVSdatmmkrLEREIKVLKDKLAEEERKNE 359
Cdd:COG5059 333 AKSIKNKIQVNSSSD-------SSREIEEIKFDLSEDRSEIE 367
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
9-319 |
2.23e-68 |
|
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: 233.93 E-value: 2.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 9 IQVCIKVRPCEPGL-----TSLWQVKERRSIHLAD--SHAEP--YVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTI 79
Cdd:cd01376 2 VRVAVRVRPFVDGTagasdPSCVSGIDSCSVELADprNHGETlkYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNATV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 80 FAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFqQISSETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNG---I 156
Cdd:cd01376 82 FAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-QMTRKEAWALSFTMSYLEIYQEKILDLLEPASKELVIREDKDGnilI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 157 VNVNCEEciITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSdhSDDDAVIQSVLNLVDLAGSERADQ 236
Cdd:cd01376 161 PGLSSKP--IKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRER--LAPFRQRTGKLNLIDLAGSEDNRR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 237 TGARGARLKEGGHINKSLLFLSNVIKSLSENAdnRFTNYRDSKLTRILQASLGGNAFTSIICTIKPSI--MEESQSTLSF 314
Cdd:cd01376 237 TGNEGIRLKESGAINSSLFVLSKVVNALNKNL--PRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERtfYQDTLSTLNF 314
|
....*
gi 442627454 315 ATRAK 319
Cdd:cd01376 315 AARSR 319
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
9-319 |
8.82e-66 |
|
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: 226.79 E-value: 8.82e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 9 IQVCIKVRPCE--------------PGLTSLWQVKERRSIHLADSH-AEPYVFDYVFDEGASNQEVFDRMAKHIVHACMQ 73
Cdd:cd01367 2 IKVCVRKRPLNkkevakkeidvvsvPSKLTLIVHEPKLKVDLTKYIeNHTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 74 GFNGTIFAYGQTSSGKTYTMMGD----EQNPGVMVLAAKEIFQQISSETERDFL-LRVGYIEIYNEKIYDLLNKKnQDLK 148
Cdd:cd01367 82 GGKATCFAYGQTGSGKTYTMGGDfsgqEESKGIYALAARDVFRLLNKLPYKDNLgVTVSFFEIYGGKVFDLLNRK-KRVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 149 IHESGNGIVNV-NCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSdddaviQSVLNLVD 227
Cdd:cd01367 161 LREDGKGEVQVvGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTNKL------HGKLSFVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 228 LAGSER-ADQTGARGARLKEGGHINKSLLFLSNVIKSLSENadNRFTNYRDSKLTRILQASL-GGNAFTSIICTIKPSI- 304
Cdd:cd01367 235 LAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQN--KAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGAs 312
|
330
....*....|....*.
gi 442627454 305 -MEESQSTLSFATRAK 319
Cdd:cd01367 313 sCEHTLNTLRYADRVK 328
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
8-319 |
2.08e-62 |
|
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: 217.45 E-value: 2.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 8 SIQVCIKVRPCEP---GLTSLWQVKERRSIHLADSHAEPYV----------FDYVFDEgASNQEVFDRMAKHIVHACMQG 74
Cdd:cd01375 1 KVQAFVRVRPTDDfahEMIKYGEDGKSISIHLKKDLRRGVVnnqqedwsfkFDGVLHN-ASQELVYETVAKDVVSSALAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 75 FNGTIFAYGQTSSGKTYTMMGDEQN---PGVMVLAAKEIFQQISSETERDFLLRVGYIEIYNEKIYDLLNKKNQDLK--- 148
Cdd:cd01375 80 YNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLSTLPYVGPsvt 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 149 ----IHESGNGIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSdDDAVIQSVLN 224
Cdd:cd01375 160 pmtiLEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLS-SEKYITSKLN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 225 LVDLAGSERADQTGARGARLKEGGHINKSLLFLSNVIKSLSENaDNRFTNYRDSKLTRILQASLGGNAFTSIICTI--KP 302
Cdd:cd01375 239 LVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDK-DRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIygEA 317
|
330
....*....|....*..
gi 442627454 303 SIMEESQSTLSFATRAK 319
Cdd:cd01375 318 AQLEETLSTLRFASRVK 334
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
27-319 |
2.19e-61 |
|
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: 214.57 E-value: 2.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 27 QVKERRSIHLADSHAEPYVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLA 106
Cdd:cd01368 40 GSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 107 AKEIFQQISseterDFLLRVGYIEIYNEKIYDLL-------NKKNQDLKIHESGNGIVNV-NCEECIITSEVDLLRLLCL 178
Cdd:cd01368 120 LDVIFNSIG-----GYSVFVSYIEIYNEYIYDLLepspsspTKKRQSLRLREDHNGNMYVaGLTEIEVKSTEEARKVLKR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 179 GNKERTVGETNMNERSSRSHAIFKIII-----ESRKSDHSDDDAVIQSVLNLVDLAGSERADQTGARGARLKEGGHINKS 253
Cdd:cd01368 195 GQKNRSVAGTKLNRESSRSHSVFTIKLvqapgDSDGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTS 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627454 254 LLFLSNVIKSLSENADNRFTN---YRDSKLTRILQASLGGNAFTSIICTIKPSI--MEESQSTLSFATRAK 319
Cdd:cd01368 275 LMTLGTCIEVLRENQLQGTNKmvpFRDSKLTHLFQNYFDGEGKASMIVNVNPCAsdYDETLHVMKFSAIAQ 345
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
7-351 |
1.02e-50 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 198.24 E-value: 1.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 7 SSIQVCIKVRPCEPGLTSLWQVKERRSIHLADShAEPYVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIFAYGQTS 86
Cdd:PLN03188 98 SGVKVIVRMKPLNKGEEGEMIVQKMSNDSLTIN-GQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 87 SGKTYTMMG------------DEQnpGVMVLAAKEIFQQISSE----TER--DFLLRVGYIEIYNEKIYDLLNKKNQDLK 148
Cdd:PLN03188 177 SGKTYTMWGpanglleehlsgDQQ--GLTPRVFERLFARINEEqikhADRqlKYQCRCSFLEIYNEQITDLLDPSQKNLQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 149 IHE---SGNGIVNVNcEECIITSEvDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSDDDAVIQ-SVLN 224
Cdd:PLN03188 255 IREdvkSGVYVENLT-EEYVKTMK-DVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSFKtSRIN 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 225 LVDLAGSERADQTGARGARLKEGGHINKSLLFLSNVIKSLSE---NADNRFTNYRDSKLTRILQASLGGNAFTSIICTIK 301
Cdd:PLN03188 333 LVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEisqTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAIS 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 442627454 302 P--SIMEESQSTLSFATRAKKIRIKPQVNEMVSDAtmMKRLEREIKVLKDKL 351
Cdd:PLN03188 413 PsqSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDD--VNFLREVIRQLRDEL 462
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
539-1431 |
2.96e-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: 95.51 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 539 LAEVTAQRDNLEQEslAEK-ERYDALEKEVTSLRADNEAAnsKISELEEKLSTLKQTMRIMEVEnqvavglEFEFEAHKK 617
Cdd:TIGR02168 195 LNELERQLKSLERQ--AEKaERYKELKAELRELELALLVL--RLEELREELEELQEELKEAEEE-------LEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 618 SSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVlrnSKEGHMLSIAPEQEDIAGDSIcnkcEELEKLIADLESKKnsce 697
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALANEI---SRLEQQKQILRERLANLERQL----EELEAQLEELESKL---- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 698 cDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEH 777
Cdd:TIGR02168 333 -DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 778 VQEKYQKLQEEYEQLEsraRSASSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNS----ESTVEKLRIQNHELT 853
Cdd:TIGR02168 412 LEDRRERLQQEIEELL---KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEleeaEQALDAAERELAQLQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 854 AKIKELETNFEEMQREYDCLSNQLMESVQEND---ALREEIKQRP--TSHVEESMRSSG---ISSDFDEQKQDINLLHQ- 924
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSGLSGilgVLSELISVDEgyEAAIEAALGGRLqavVVENLNAAKKAIAFLKQn 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 925 ---------FVQLSESVQQIELQHHSGISRLFRANQMKLDQSEPGLKLCLES-------AEYIEEDNRQSDATEP----I 984
Cdd:TIGR02168 569 elgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPgyriV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 985 CLKGFLKRHRFQIKRlsqehvdmGEEKRLLDIISQlEQEIEEKSALMEATEATINEMREQMTNLESALLEksvIINKVED 1064
Cdd:TIGR02168 649 TLDGDLVRPGGVITG--------GSAKTNSSILER-RREIEELEEKIEELEEKIAELEKALAELRKELEE---LEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1065 YQRQIESLEKQNAEMTMVYEELQDRVTRESSMSESLlrvppdedtlpgcptspsrrEQEVATLKTSITELQSQVSDLKAE 1144
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQL--------------------SKELTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1145 LENHLRQIQlkdgniaRLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHK 1224
Cdd:TIGR02168 777 LAEAEAEIE-------ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1225 ATESLSLADAkpdqillssqydsQIEKLNQLLNAAKDELhdvrrikdDEISALRMEFLLQIETNEKEnqakfYAELQETK 1304
Cdd:TIGR02168 850 LSEDIESLAA-------------EIEELEELIEELESEL--------EALLNERASLEEALALLRSE-----LEELSEEL 903
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1305 DRYESNVAELKEKLLQVEETLSSVTVRCQaELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQqs 1384
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLE-GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK-- 980
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 442627454 1385 kmedafRAEINEVRATLMEQLNQTKEDRD---KGASKLEEVKKTLEQMIN 1431
Cdd:TIGR02168 981 ------IKELGPVNLAAIEEYEELKERYDfltAQKEDLTEAKETLEEAIE 1024
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1009-1773 |
1.25e-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: 90.12 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1009 EEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEdyqRQIESLEKQNAEMTMVYEELQD 1088
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE---QQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1089 RVTRESSMSESLLrvppdedtlpgcpTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEE 1168
Cdd:TIGR02168 324 QLEELESKLDELA-------------EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1169 MSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLvEQYHKATESLSLADAKPDQILLSSQYDSQ 1248
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1249 IEKLNQLLNAAKDELHDVRRikddeisalRMEFLLQIETNekenqakfyaelQETKDRYESNVAELKEKLLQVEETLSSV 1328
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQA---------RLDSLERLQEN------------LEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1329 tVRCQAELEALKSAHKENISQAVEERNN----LIVQHQAEMETIRETL-------KNKLAEASTQQSKMEDAFRAEINEV 1397
Cdd:TIGR02168 529 -ISVDEGYEAAIEAALGGRLQAVVVENLnaakKAIAFLKQNELGRVTFlpldsikGTEIQGNDREILKNIEGFLGVAKDL 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1398 RaTLMEQLNQTKEDR-------DKGASKLEEVKKTLEQ---------------MINGGRVMSDT--------IAELEKTK 1447
Cdd:TIGR02168 608 V-KFDPKLRKALSYLlggvlvvDDLDNALELAKKLRPGyrivtldgdlvrpggVITGGSAKTNSsilerrreIEELEEKI 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1448 AEQDLAVNKLTKDNIELEKQcsktQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLE 1527
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1528 KLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKekcdFETKLETFTFKITDLEEvlkEAQHKVILYDDLVSQHER 1607
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA----LREALDELRAELTLLNE---EAANLRERLESLERRIAA 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1608 LKICLAEANELSSNLQKKVMSLHTELIDSQkgissrdVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAE 1687
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELE-------ELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1688 KFTReaanLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLrnMLDEeskmcisLKEKLVKLEDAKTSLEQQLR 1767
Cdd:TIGR02168 909 KRSE----LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL--TLEE-------AEALENKIEDDEEEARRRLK 975
|
....*.
gi 442627454 1768 DNKSEI 1773
Cdd:TIGR02168 976 RLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
703-1451 |
1.79e-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: 89.73 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 703 LEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKY 782
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 783 QKLQEEYEQLEsrarsassAEFQRLQNDNTKFQADIASLNERLEEAQNmltEVQNSESTVEKLRIQNHELTAKIKELETN 862
Cdd:TIGR02168 312 ANLERQLEELE--------AQLEELESKLDELAEELAELEEKLEELKE---ELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 863 FEEMQREYDCLSNQ---LMESVQENDALREEIKQRPTSHVEE--SMRSSGISSDFDEQKQDINLLHQ-FVQLSESVQQIE 936
Cdd:TIGR02168 381 LETLRSKVAQLELQiasLNNEIERLEARLERLEDRRERLQQEieELLKKLEEAELKELQAELEELEEeLEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 937 LQHHSgISRLFRANQMKLDQSEPGLKLcLESAEYIEEDNRQSDATEPICLKgFLKRHRFQIK----RLSQE-HVDMGEEK 1011
Cdd:TIGR02168 461 EALEE-LREELEEAEQALDAAERELAQ-LQARLDSLERLQENLEGFSEGVK-ALLKNQSGLSgilgVLSELiSVDEGYEA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1012 RL-------------------LDIISQLEQEIEEKSALMEATEATINEM----REQMTNLESALLEKSVIINKVEDYQRQ 1068
Cdd:TIGR02168 538 AIeaalggrlqavvvenlnaaKKAIAFLKQNELGRVTFLPLDSIKGTEIqgndREILKNIEGFLGVAKDLVKFDPKLRKA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1069 IESLEKQnaemTMVYEELQDRVTRESSMSESLLRVPPDEDTLPGC--------PTSPSR--REQEVATLKTSITELQSQV 1138
Cdd:TIGR02168 618 LSYLLGG----VLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGgvitggsaKTNSSIleRRREIEELEEKIEELEEKI 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1139 SDLKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDdlclidqLQKKNAQL 1218
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE-------LEAEIEEL 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1219 VEQYHKATESLSLADAKpdqillssqydsqIEKLNQLLNAAKDELHDVRRIKD---DEISALRMEFLLQieTNEKENQAK 1295
Cdd:TIGR02168 767 EERLEEAEEELAEAEAE-------------IEELEAQIEQLKEELKALREALDelrAELTLLNEEAANL--RERLESLER 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1296 FYAELQETKDRYESNVAELKEKLLQVEETLSSVTVRC---QAELEAL---KSAHKENISQAVEERNNLIVQhQAEMETIR 1369
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeelESELEALlneRASLEEALALLRSELEELSEE-LRELESKR 910
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1370 ETLKNKLAEASTQQSKME---DAFRAEINEVRATLMEQLNQTKED-------RDKGASKLEEVKKTLEQMING-GRVMSD 1438
Cdd:TIGR02168 911 SELRRELEELREKLAQLElrlEGLEVRIDNLQERLSEEYSLTLEEaealenkIEDDEEEARRRLKRLENKIKElGPVNLA 990
|
810
....*....|...
gi 442627454 1439 TIAELEKTKAEQD 1451
Cdd:TIGR02168 991 AIEEYEELKERYD 1003
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
45-263 |
2.50e-17 |
|
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: 81.62 E-value: 2.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 45 VFDYVFDEGASNQEVFdRMAKHIVHACMQGFNG-TIFAYGQTSSGKTYTMMGdeqnpgvmvlaakeIFQQIsseterdfl 123
Cdd:cd01363 21 VFYRGFRRSESQPHVF-AIADPAYQSMLDGYNNqSIFAYGESGAGKTETMKG--------------VIPYL--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 124 lrvgyIEIYNEKIYDLLNKKNQdlkihesgngivnvNCEECIITSEVDLLRLLCLGNKERTvGETNMNERSSRSHAIFKI 203
Cdd:cd01363 77 -----ASVAFNGINKGETEGWV--------------YLTEITVTLEDQILQANPILEAFGN-AKTTRNENSSRFGKFIEI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 204 iiesrksdhsdddaviqsvlnLVDLAGSERadqtgargarlkegghINKSLLFLSNVIKS 263
Cdd:cd01363 137 ---------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1011-1828 |
1.23e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.03 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1011 KRLLDIISQLEQEIEEKSALMEATEATInEMREQMTNLEsalleKSVIINKVEDYQRQIESLEKQNAEMtmvyEELQDRV 1090
Cdd:TIGR02168 189 DRLEDILNELERQLKSLERQAEKAERYK-ELKAELRELE-----LALLVLRLEELREELEELQEELKEA----EEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1091 TRESSMSESLLrvppdedtlpgcptspSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMS 1170
Cdd:TIGR02168 259 TAELQELEEKL----------------EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1171 ErclsmevRLAELDEDTKQKQELLDRQAQKlsddlclIDQLQKKNAQLVEqyhkateslsladakpdqillssqydsQIE 1250
Cdd:TIGR02168 323 A-------QLEELESKLDELAEELAELEEK-------LEELKEELESLEA---------------------------ELE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1251 KLNQLLNAAKDELHDVRRikddeisalrmefllqietnEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVTV 1330
Cdd:TIGR02168 362 ELEAELEELESRLEELEE--------------------QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1331 RCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKnKLAEASTQQSKMEDAFRAEINEV--RATLMEQLNQT 1408
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE-ELREELEEAEQALDAAERELAQLqaRLDSLERLQEN 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1409 KEDRDKGASKLEEVKKTLEQMINggrVMSDTI-------AELEKTKAE--QDLAVNKLT--KDNIELEKQCSKTQEQLQM 1477
Cdd:TIGR02168 501 LEGFSEGVKALLKNQSGLSGILG---VLSELIsvdegyeAAIEAALGGrlQAVVVENLNaaKKAIAFLKQNELGRVTFLP 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1478 ESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCdQQVLE--LDKCRLEKlSLESEIQKANSEHSCTM------EKL 1549
Cdd:TIGR02168 578 LDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL-RKALSylLGGVLVVD-DLDNALELAKKLRPGYRivtldgDLV 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1550 --------QELQAEMKVLSNRNEKEKCdfETKLETFTFKITDLEEVLKEAQHKVILY----DDLVSQHERLKICLAEANE 1617
Cdd:TIGR02168 656 rpggvitgGSAKTNSSILERRREIEEL--EEKIEELEEKIAELEKALAELRKELEELeeelEQLRKELEELSRQISALRK 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1618 LSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFT---REAA 1694
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelrAELT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1695 NLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQ----NLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNK 1770
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSedieSLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627454 1771 SEIYqrhtELTKEVELGRNRIGELTKKCEELCSDLEnsdQIRLDLQETKEQLKKTLEN 1828
Cdd:TIGR02168 894 SELE----ELSEELRELESKRSELRRELEELREKLA---QLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1137-1926 |
4.04e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.11 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1137 QVSDLKAELENHLRQIQLKdgniARLQTDFEEMSErclsmEVRLAELDEDTKQKQELLDRqaqklsddlclIDQLQKKNA 1216
Cdd:TIGR02168 190 RLEDILNELERQLKSLERQ----AEKAERYKELKA-----ELRELELALLVLRLEELREE-----------LEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1217 QLVEQYHKATESLSLADAKPDQIllssqyDSQIEKLNQLLNAAKDELHDVRRikddEISALRMEflLQIETNEKENQAKF 1296
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEEL------RLEVSELEEEIEELQKELYALAN----EISRLEQQ--KQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1297 YAELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELEALKSAHKEniSQAVEERNnlivqhqAEMETIRETLKNKL 1376
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE--LEELESRL-------EELEEQLETLRSKV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1377 AEASTQQSKMedafRAEINEVRATLmEQLNQTKEDRDKGASKLEEVKKTLEqminggrvMSDTIAELEKTKAEQDlavnK 1456
Cdd:TIGR02168 389 AQLELQIASL----NNEIERLEARL-ERLEDRRERLQQEIEELLKKLEEAE--------LKELQAELEELEEELE----E 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1457 LTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIvasskKRIIELEEKCDQQVLELDKCRLEK---LSLES 1533
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL-----ERLQENLEGFSEGVKALLKNQSGLsgiLGVLS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1534 EIQKANSEHSCTMEK-LQE-LQAemkVLSNRNEKEKCDFETKLETFTFKITDLE--------------EVLKEAQHKVIL 1597
Cdd:TIGR02168 527 ELISVDEGYEAAIEAaLGGrLQA---VVVENLNAAKKAIAFLKQNELGRVTFLPldsikgteiqgndrEILKNIEGFLGV 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1598 YDDLVSQHERLKIC-------------LAEANELSSNLQKKVM--SLHTELI-----------DSQKGISSRDVEINELR 1651
Cdd:TIGR02168 604 AKDLVKFDPKLRKAlsyllggvlvvddLDNALELAKKLRPGYRivTLDGDLVrpggvitggsaKTNSSILERRREIEELE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1652 EELKAAMDAKATASAEQMTLVTQLKDVEER-----------------MANQAEKFTREAANLKGSINELLLKL----NSM 1710
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEEleqlrkeleelsrqisaLRKDLARLEAEVEQLEERIAQLSKELteleAEI 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1711 QETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNKSeiyqRHTELTKEVELGRNR 1790
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----RLESLERRIAATERR 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1791 IGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLEnnlGWQQKVDEVTRECEKLRFDMQSKEVQN---ESKVQELISE 1867
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELE---ALLNERASLEEALALLRSELEELSEELrelESKRSELRRE 916
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1868 CEELRSTLKSKEASFQSEKESMDRTISSLLED-----------KRNLEEKLCSANDIVAKLETEIAALRP 1926
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEysltleeaealENKIEDDEEEARRRLKRLENKIKELGP 986
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1166-1931 |
6.52e-15 |
|
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: 81.32 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1166 FEEMSERCLSMEVRLAELDE-DTKQK----QELLDRQA--QKLSDDLCLIDQLQKKNAQ----LVEQYHKATESLSLADA 1234
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNElHEKQKfylrQSVIDLQTklQEMQMERDAMADIRRRESQsqedLRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1235 KPDQILLSSqyDSQIEKLNQLLNAAKDELHDVRRIKDD--EISALRMEFLLQIETNEKENQAKFYAELQETKDryeSNVA 1312
Cdd:pfam15921 160 LKEDMLEDS--NTQIEQLRKMMLSHEGVLQEIRSILVDfeEASGKKIYEHDSMSTMHFRSLGSAISKILRELD---TEIS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1313 ELKEKLLQVEETLSSVTVRCQAELEALKSAHKENISQaveernnLIVQHQAEMETIRETLKNKLAEASTQQSKMEdAFRA 1392
Cdd:pfam15921 235 YLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQ-------LISEHEVEITGLTEKASSARSQANSIQSQLE-IIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1393 EINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEqminggrvmsDTIAELEKTKAeqdLAVNKLTKDNIElekqcsktQ 1472
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE----------DKIEELEKQLV---LANSELTEARTE--------R 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1473 EQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEK-------CDQQVLELDKCRLEKLSLESEIQKANSEHSCT 1545
Cdd:pfam15921 366 DQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1546 MEKlqelqaEMKVLSNRNEKEKcdfetKLETFTFKITDLEEVLKeaqhKVIlyDDLVSQHERLKICLAEANELSSNLQKK 1625
Cdd:pfam15921 446 MER------QMAAIQGKNESLE-----KVSSLTAQLESTKEMLR----KVV--EELTAKKMTLESSERTVSDLTASLQEK 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1626 VMSLHTELIDSQKGISSRDVEINELrEELKAAMDAKATASAEQMTLVTQLKD---VEERMANQAEKFTR----------- 1691
Cdd:pfam15921 509 ERAIEATNAEITKLRSRVDLKLQEL-QHLKNEGDHLRNVQTECEALKLQMAEkdkVIEILRQQIENMTQlvgqhgrtaga 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1692 ---EAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNsqnlrnmldeeskmcisLKEKLVKLEDAKTSLEQQLRD 1768
Cdd:pfam15921 588 mqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD-----------------LELEKVKLVNAGSERLRAVKD 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1769 nkseIYQRHTELTKEVELGRNRIGELTKKCEELCSDLEN--------SDQIRLDLQETKEQLKKT--------------L 1826
Cdd:pfam15921 651 ----IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNkseemettTNKLKMQLKSAQSELEQTrntlksmegsdghaM 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1827 ENNLGWQQKVDEVTRECEKLRFDMQSKE--VQNESKVQELIsecEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLE 1904
Cdd:pfam15921 727 KVAMGMQKQITAKRGQIDALQSKIQFLEeaMTNANKEKHFL---KEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLK 803
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 442627454 1905 EKLCS--------------ANDIVAKLETEIAALRPRKSLD 1931
Cdd:pfam15921 804 EKVANmevaldkaslqfaeCQDIIQRQEQESVRLKLQHTLD 844
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
617-1422 |
1.49e-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: 80.11 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 617 KSSKLRVDDLLSALLEKESTI-----ESLQKSLDNLTRDVlrNSKEGHMLSIAPEQEDIAgdsicNKCEELEKLIADLES 691
Cdd:TIGR02169 207 REKAERYQALLKEKREYEGYEllkekEALERQKEAIERQL--ASLEEELEKLTEEISELE-----KRLEEIEQLLEELNK 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 692 KKNSCECDqlrlEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAgittl 771
Cdd:TIGR02169 280 KIKDLGEE----EQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK----- 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 772 heKHEHVQEKYQKLQEEYEQLESRARSASsAEFQRLQNDNTKFQADIASLNERLEEAQN----MLTEVQNSESTVEKLRI 847
Cdd:TIGR02169 351 --RRDKLTEEYAELKEELEDLRAELEEVD-KEFAETRDELKDYREKLEKLKREINELKReldrLQEELQRLSEELADLNA 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 848 QNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQRPTSHVEESMRSSGISSDFDEQKQDINLLHQFVQ 927
Cdd:TIGR02169 428 AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVR 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 928 LSESVQQIELQHHSGISRLFRanqmKLDQSEPGLKLCLESAEYIEEDN--RQSDATEPICLKgFLKRHR------FQIKR 999
Cdd:TIGR02169 508 GGRAVEEVLKASIQGVHGTVA----QLGSVGERYATAIEVAAGNRLNNvvVEDDAVAKEAIE-LLKRRKagratfLPLNK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1000 LSQEHVDMGEEKR------LLDIIsQLEQEIEE-------KSALMEATEATINEM-REQMTNLESALLEKSviinkvedy 1065
Cdd:TIGR02169 583 MRDERRDLSILSEdgvigfAVDLV-EFDPKYEPafkyvfgDTLVVEDIEAARRLMgKYRMVTLEGELFEKS--------- 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1066 qrqieslekqnAEMTMVYEELQDRVTRESSMSESLLRVPPDEDTLpgcptspsrrEQEVATLKTSITELQSQVSDLKAEL 1145
Cdd:TIGR02169 653 -----------GAMTGGSRAPRGGILFSRSEPAELQRLRERLEGL----------KRELSSLQSELRRIENRLDELSQEL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1146 ENHLRQIQLKDGNIARLQTDFEEMSErclsmevRLAELDEDTKQKQelldrqaQKLSDDLCLIDQLQKKNAQLVEQYHKA 1225
Cdd:TIGR02169 712 SDASRKIGEIEKEIEQLEQEEEKLKE-------RLEELEEDLSSLE-------QEIENVKSELKELEARIEELEEDLHKL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1226 TESLSLADAKPDQillssqydSQIEKLNQLLNAAKDELHDVR-RIKDDEISALRMEFLLQIETNEKENQAKFYAELQETK 1304
Cdd:TIGR02169 778 EEALNDLEARLSH--------SRIPEIQAELSKLEEEVSRIEaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1305 DRYESNVAEL---KEKLLQVEETLSSVTVRCQAELEALKSAHKENISQ--AVEERNNLIVQHQAEMETIRETLKNKLAEA 1379
Cdd:TIGR02169 850 KSIEKEIENLngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQlrELERKIEELEAQIEKKRKRLSELKAKLEAL 929
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 442627454 1380 STQQSKMEDAFRAEINEVRATL-MEQLNQTKEDRDKGASKLEEV 1422
Cdd:TIGR02169 930 EEELSEIEDPKGEDEEIPEEELsLEDVQAELQRVEEEIRALEPV 973
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1061-1902 |
8.30e-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: 77.42 E-value: 8.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1061 KVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSMSESLLRVppDEDTLPGCPTSPSRREQEVATLKTSITELQSQVSD 1140
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERY--QALLKEKREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1141 LKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSM----EVRLAELDEDTKQKQELLDRQAQKLSDDLcliDQLQKKNA 1216
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeQLRVKEKIGELEAEIASLERSIAEKEREL---EDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1217 QLVEQYHKATESL-----SLADAKPDQILLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDdEISALRMEflLQIETNEKE 1291
Cdd:TIGR02169 326 KLEAEIDKLLAEIeelerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-ELKDYREK--LEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1292 NQAKFYAELQETKDRYESNVAELKEKLLQVEETLssvtvrcqAELEALKSAHKENISQAVEERNNLivqhQAEMETIRET 1371
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKI--------NELEEEKEDKALEIKKQEWKLEQL----AADLSKYEQE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1372 LKNKLAEASTQQSKMEDAfRAEINEVRATLmeqlnQTKEDRDKGASKLEEVKKTLEQMINGgrvmsdTIAELEKTKAEQD 1451
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKL-QRELAEAEAQA-----RASEERVRGGRAVEEVLKASIQGVHG------TVAQLGSVGERYA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1452 LAV-----NKLTKDNIELEKQCSKTQEQLQMESLTRdqISFEIEAHIKKLELIVASSKKR--------IIELEEKC---- 1514
Cdd:TIGR02169 539 TAIevaagNRLNNVVVEDDAVAKEAIELLKRRKAGR--ATFLPLNKMRDERRDLSILSEDgvigfavdLVEFDPKYepaf 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1515 -----DQQVLE--------LDKCRLekLSLESEIQK--------ANSEHSCTM------EKLQELQAE---MKVLSNRNE 1564
Cdd:TIGR02169 617 kyvfgDTLVVEdieaarrlMGKYRM--VTLEGELFEksgamtggSRAPRGGILfsrsepAELQRLRERlegLKRELSSLQ 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1565 KEKCDFETKLETFTFKITDLEEVLKEAQHKVILYDDlvsQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRD 1644
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ---EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1645 VEINELREELkaamdakatASAEQMTLVTQLKDVEermaNQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGNEEL 1724
Cdd:TIGR02169 772 EDLHKLEEAL---------NDLEARLSHSRIPEIQ----AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1725 KEQLRNSQNLRNMLDEESKmciSLKEKLVKLEDAKTSLEQQLRDNKSeiyqRHTELTKEVELGRNRIGELTKKCEELCSD 1804
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIE---NLNGKKEELEEELEELEAALRDLES----RLGDLKKERDELEAQLRELERKIEELEAQ 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1805 LENSDQIRLDLQETKEQLK---KTLENNLGWQQKV-------DEVTRECEKLRFDMQSKEVQNESKVQELiSECEELRST 1874
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEeelSEIEDPKGEDEEIpeeelslEDVQAELQRVEEEIRALEPVNMLAIQEY-EEVLKRLDE 990
|
890 900
....*....|....*....|....*...
gi 442627454 1875 LKSKEASFQSEKESMDRTISSLLEDKRN 1902
Cdd:TIGR02169 991 LKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
766-1609 |
1.20e-13 |
|
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: 77.02 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 766 AGITTLHEKHEHVQEKYQKLQEEYE-----------QLESRARSASSAE-FQRLQNDntKFQADIASLNERLEEAQNmlt 833
Cdd:TIGR02168 165 AGISKYKERRKETERKLERTRENLDrledilnelerQLKSLERQAEKAErYKELKAE--LRELELALLVLRLEELRE--- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 834 EVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIkqrptshveesmrssgisSDFD 913
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI------------------SRLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 914 EQKQdinllHQFVQLSESVQQIElqhhsgisrlfranqmkldqsepglklclESAEYIEEDNRQSDatepiCLKGFLKRH 993
Cdd:TIGR02168 302 QQKQ-----ILRERLANLERQLE-----------------------------ELEAQLEELESKLD-----ELAEELAEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 994 RFQIKRLSQEHVDmgeekrlldiisqLEQEIEEKSALMEATEATINEMREQMTNLESALLEKsviinkvedyQRQIESLE 1073
Cdd:TIGR02168 343 EEKLEELKEELES-------------LEAELEELEAELEELESRLEELEEQLETLRSKVAQL----------ELQIASLN 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1074 KQNAEMTMVYEELQDRVTRESSMSESLLRVPPDEDTlpgcptspSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQ 1153
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--------KELQAELEELEEELEELQEELERLEEALEELREELE 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1154 LKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQ--------------------- 1212
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISvdegyeaaieaalggrlqavv 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1213 -------KKNAQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKLNQLLNAAKDELHDVR------------RIKDDE 1273
Cdd:TIGR02168 552 venlnaaKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvLVVDDL 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1274 ISALRMEFLLQIETN-------------------EKENQAKFY-----AELQETKDRYESNVAELKEKLLQVEETLSSVt 1329
Cdd:TIGR02168 632 DNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILErrreiEELEEKIEELEEKIAELEKALAELRKELEEL- 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1330 vrcQAELEALKSAhKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEastqqskmedafRAEINEVRATLMEQLNQTK 1409
Cdd:TIGR02168 711 ---EEELEQLRKE-LEELSRQISALRKDLARLEAEVEQLEERIAQLSKE------------LTELEAEIEELEERLEEAE 774
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1410 EDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEI 1489
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1490 E---AHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKE 1566
Cdd:TIGR02168 855 EslaAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 442627454 1567 KCDFETKLETFTFKITDLEEVLKEaqHKVILYDDLVSQHERLK 1609
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAEA--LENKIEDDEEEARRRLK 975
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1012-1801 |
2.06e-13 |
|
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: 76.25 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1012 RLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKS----VIINKVEDYQRQIESLEKQNAEMTMVYEELQ 1087
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelyALANEISRLEQQKQILRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1088 DRVTRESSMSESLLrvppdedtlpgcpTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFE 1167
Cdd:TIGR02168 323 AQLEELESKLDELA-------------EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1168 EMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLvEQYHKATESLSLADAKPDQILLSSQYDS 1247
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEEALEELRE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1248 QIEKLNQLLNAAKDELHDVRRikddeisalRMEFLLQIETNekenqakfyaelQETKDRYESNVAELKEKLLQVEETLSS 1327
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQA---------RLDSLERLQEN------------LEGFSEGVKALLKNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1328 VtVRCQAELEALKSAHKENISQAVEERNN----LIVQHQAEMETIRETL-------KNKLAEASTQQSKMEDAFRAEINE 1396
Cdd:TIGR02168 528 L-ISVDEGYEAAIEAALGGRLQAVVVENLnaakKAIAFLKQNELGRVTFlpldsikGTEIQGNDREILKNIEGFLGVAKD 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1397 VRaTLMEQLNQTKEDR-------DKGASKLEEVKKTLEQ---------------MINGGRVMSDT--------IAELEKT 1446
Cdd:TIGR02168 607 LV-KFDPKLRKALSYLlggvlvvDDLDNALELAKKLRPGyrivtldgdlvrpggVITGGSAKTNSsilerrreIEELEEK 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1447 KAEQDLAVNKLTKDNIELEKQcsktQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRL 1526
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1527 EKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKekcdfetkletftfkitdLEEVLKEAQhkvilyddlvSQHE 1606
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA------------------LREALDELR----------AELT 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1607 RLKICLAEANELSSNLQKKVMSLHTELIDSQKgissrdvEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQA 1686
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEE-------QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1687 EkftreaanlkgSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEEskmcisLKEKLVKLEDAKTSLEQQL 1766
Cdd:TIGR02168 887 E-----------ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR------LEGLEVRIDNLQERLSEEY 949
|
810 820 830
....*....|....*....|....*....|....*
gi 442627454 1767 RDNKSEIYQRHTELTKEVELGRNRIGELTKKCEEL 1801
Cdd:TIGR02168 950 SLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
531-1323 |
7.78e-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: 74.33 E-value: 7.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 531 EVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISEL-EEKLSTLKQTMRimEVENQVAvgle 609
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIG--ELEAEIA---- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 610 fEFEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSKEGHMLSiapeqediagDSICNKCEELEKLIADL 689
Cdd:TIGR02169 305 -SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT----------EEYAELKEELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 690 ESKknSCECDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGIT 769
Cdd:TIGR02169 374 EEV--DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 770 TLHEKHEHVQEKYQKLQEEYEQLEsrarsassAEFQRLQNDNTKFQADIASLNERLEEAQnmlTEVQNSESTVEKLRIQN 849
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLK--------EEYDRVEKELSKLQRELAEAEAQARASE---ERVRGGRAVEEVLKASI 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 850 HELTAKIKELETNFEEMQREYD-CLSNQLMESVQENDALREE----IKQR--------PTSHVEESMRSSGISS------ 910
Cdd:TIGR02169 521 QGVHGTVAQLGSVGERYATAIEvAAGNRLNNVVVEDDAVAKEaielLKRRkagratflPLNKMRDERRDLSILSedgvig 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 911 ------DFDEQKQdiNLLHQFVQLSESVQQIE-------------------------------LQHHSGISRLFRANQMK 953
Cdd:TIGR02169 601 favdlvEFDPKYE--PAFKYVFGDTLVVEDIEaarrlmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQR 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 954 LDQSEPGLKLCLES--AEYIEEDNRQSDATEPIC-LKGFLKRHRFQIKRLSQEHVDMGEE-KRLLDIISQLEQEIEEKSA 1029
Cdd:TIGR02169 679 LRERLEGLKRELSSlqSELRRIENRLDELSQELSdASRKIGEIEKEIEQLEQEEEKLKERlEELEEDLSSLEQEIENVKS 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1030 LMEATEATINEMREQMTNLESAL--LEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSMSESLlrvppde 1107
Cdd:TIGR02169 759 ELKELEARIEELEEDLHKLEEALndLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL------- 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1108 dtlpgcptspsrrEQEVATLKTSITELQSQVSDLKAELENhlrqiqlKDGNIARLQTDFEEMSERCLSMEVRLAELDEDT 1187
Cdd:TIGR02169 832 -------------EKEIQELQEQRIDLKEQIKSIEKEIEN-------LNGKKEELEEELEELEAALRDLESRLGDLKKER 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1188 KQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKLNQllnaakdelhdVR 1267
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQA-----------EL 960
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627454 1268 RIKDDEISALRMEFLLQIEtnEKENQAKFYAELQETKDRYESNVAELKEKLLQVEE 1323
Cdd:TIGR02169 961 QRVEEEIRALEPVNMLAIQ--EYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1288-1867 |
9.07e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.94 E-value: 9.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1288 NEKENQAKFYAELQETKDRYESNVAELKEKLLQVEEtLSSVTVRCQAELEALKS------AHKENISQAvEERNNLIVQH 1361
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREINE-ISSELPELREELEKLEKevkeleELKEEIEEL-EKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1362 QAEMETIRETLKNKLAEASTQQSKMEDAfRAEINEVR--ATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGgrvMSDT 1439
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING---IEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1440 IAELEKTKAEqdlaVNKLTKDNIELEKQCSKTQEQL-----------QMESLTRDQISFEIEAHIKKLELiVASSKKRII 1508
Cdd:PRK03918 330 IKELEEKEER----LEELKKKLKELEKRLEELEERHelyeeakakkeELERLKKRLTGLTPEKLEKELEE-LEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1509 ELEEKCDQQVLELDKCRLEKLSLESEIQKANSE-----HSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITD 1583
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1584 LEEVLKEaQHKVI----LYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMD 1659
Cdd:PRK03918 485 LEKVLKK-ESELIklkeLAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1660 AKATASAEQMTLVTQL--------KDVEERMaNQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNS 1731
Cdd:PRK03918 564 KLDELEEELAELLKELeelgfesvEELEERL-KELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1732 QNLRNMLDEeskmcislKEKLVKLEDAKtsleqqlrdnksEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLEnsdqi 1811
Cdd:PRK03918 643 EELRKELEE--------LEKKYSEEEYE------------ELREEYLELSRELAGLRAELEELEKRREEIKKTLE----- 697
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627454 1812 rlDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISE 1867
Cdd:PRK03918 698 --KLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASE 751
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
537-1258 |
1.79e-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: 73.17 E-value: 1.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 537 EKLAEVTAQRDNLEQESLA-----EKERYDALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRIMEVENQVAVGLEFE 611
Cdd:TIGR02168 213 ERYKELKAELRELELALLVlrleeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 612 -------FEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSKEghmlsIAPEQEDIagDSICNKCEELEK 684
Cdd:TIGR02168 293 laneisrLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK-----LEELKEEL--ESLEAELEELEA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 685 LIADLESKKNSCEcdqlrleivsvrDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQ 764
Cdd:TIGR02168 366 ELEELESRLEELE------------EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 765 QagITTLHEKHEHVQEKYQKLQEEYEQLESRARSASsAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVEK 844
Cdd:TIGR02168 434 E--LKELQAELEELEEELEELQEELERLEEALEELR-EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 845 LRIQNHELTAKI----------KELETNFEEMQREYdcLSNQLMESVQEN----DALREEIKQRPTSHVEESMRSSGISS 910
Cdd:TIGR02168 511 LLKNQSGLSGILgvlselisvdEGYEAAIEAALGGR--LQAVVVENLNAAkkaiAFLKQNELGRVTFLPLDSIKGTEIQG 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 911 DFDEQKQDIN----LLHQFVQLSESV----------------------QQIELQHHSGI--------------------- 943
Cdd:TIGR02168 589 NDREILKNIEgflgVAKDLVKFDPKLrkalsyllggvlvvddldnaleLAKKLRPGYRIvtldgdlvrpggvitggsakt 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 944 --SRLFRANqmKLDQSEPGLKLcLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIKRLSQEHVDMGEE-KRLLDIISQL 1020
Cdd:TIGR02168 669 nsSILERRR--EIEELEEKIEE-LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDlARLEAEVEQL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1021 EQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVE----DYQRQIESLEKQNAEMTMVYEELQDRVTRESSM 1096
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEaqieQLKEELKALREALDELRAELTLLNEEAANLRER 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1097 SESLLRVPPD-EDTLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSERCLS 1175
Cdd:TIGR02168 826 LESLERRIAAtERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRE 905
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1176 MEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQkknAQLVEQYhkaTESLSLADAKPDQILLSSQY-DSQIEKLNQ 1254
Cdd:TIGR02168 906 LESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ---ERLSEEY---SLTLEEAEALENKIEDDEEEaRRRLKRLEN 979
|
....
gi 442627454 1255 LLNA 1258
Cdd:TIGR02168 980 KIKE 983
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1246-1887 |
1.26e-11 |
|
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: 70.38 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1246 DSQIEKLNQLLNAAKDELHDVRRIKDDEISALRMEfllQIETNEKENQAKFYAELQETKDRYE-------SNVAELKEKL 1318
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA---LQQTQQSHAYLTQKREAQEEQLKKQqllkqlrARIEELRAQE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1319 LQVEETLSSVTVRCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEAST---QQSKMEDAFRAEI- 1394
Cdd:TIGR00618 277 AVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSieeQRRLLQTLHSQEIh 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1395 ----NEVRATLMEQLNQTKEDRDKgASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCsk 1470
Cdd:TIGR00618 357 irdaHEVATSIREISCQQHTLTQH-IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ-- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1471 tqeQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEK-L 1549
Cdd:TIGR00618 434 ---ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGsC 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1550 QELQAEMKVLSN---------RNEKEKCDFETKLETFTFKITDLEEVLKEAQHKVILYDDLVSqheRLKICLAEANELSS 1620
Cdd:TIGR00618 511 IHPNPARQDIDNpgpltrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFS---ILTQCDNRSKEDIP 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1621 NLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATA------SAEQMTLVTQLKDVEERMANQAEK----FT 1690
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRlhlqqcSQELALKLTALHALQLTLTQERVRehalSI 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1691 REAANLKGSINELLL-----KLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQ 1765
Cdd:TIGR00618 668 RVLPKELLASRQLALqkmqsEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1766 LRDNKSEIYQrHTELTKEVELGRNRIGELTKKCEElcsDLENSDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTR--EC 1843
Cdd:TIGR00618 748 LMHQARTVLK-ARTEAHFNNNEEVTAALQTGAELS---HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILnlQC 823
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 442627454 1844 EKLRFDMQSKEVQNESKVQELIS---ECEELRSTLKSKEASFQSEKE 1887
Cdd:TIGR00618 824 ETLVQEEEQFLSRLEEKSATLGEithQLLKYEECSKQLAQLTQEQAK 870
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
8-140 |
2.07e-11 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 63.78 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 8 SIQVCIKVRPCEPGLTSLWQVKERRSIHLADSHAEPYVFDYVFDEGASNQEVFDRMaKHIVHACMQGFNGTIFAYGQTSS 87
Cdd:pfam16796 21 NIRVFARVRPELLSEAQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIFAYGQTGS 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 442627454 88 GKtytmmgdeqNPGVMVLAAKEIFQQISS-ETERDFLLRVGYIEIYNEKIYDLL 140
Cdd:pfam16796 100 GS---------NDGMIPRAREQIFRFISSlKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1259-1932 |
4.49e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 68.63 E-value: 4.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1259 AKDELHDVRRIKDdeisALRMEFLLQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELEA 1338
Cdd:PTZ00121 1120 AKKKAEDARKAEE----ARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRK 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1339 LKSAHKENISQAVEERNNLIVQHQAEMETIRETLKnklaEASTQQSKMEDAFRAEI--NEVRATLMEQLNQTKEDRDKGA 1416
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK----KAEEAKKDAEEAKKAEEerNNEEIRKFEEARMAHFARRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1417 SKLEEVKKTLEQMINGGRVMSDTIAELE--------KTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQmESLTRDQISfE 1488
Cdd:PTZ00121 1272 IKAEEARKADELKKAEEKKKADEAKKAEekkkadeaKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE-EAKKAAEAA-K 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1489 IEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMK----VLSNRNE 1564
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKkadeAKKKAEE 1429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1565 KEKCDFETKLETFTFKITDL----------EEVLKEAQHKVILyDDLVSQHERLKIClAEANELSSNLQKKVMSLHTELI 1634
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAkkkaeeakkaEEAKKKAEEAKKA-DEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAE 1507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1635 DSQKGISSRDVEINELREELKAAMDAKAT---------ASAEQMTLVTQLKDVEERMANQAEKFTREAANLKGSINELLL 1705
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKAdeakkaeekKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1706 KLnsmqETKDMLESGNEELKEQLRNSQNLRNMLDEESKmcislKEKLVKLEDAKTSLEQqLRDNKSEIYQRHTELTKEVE 1785
Cdd:PTZ00121 1588 KA----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-----AEELKKAEEEKKKVEQ-LKKKEAEEKKKAEELKKAEE 1657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1786 LGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQ---KVDEVTRECEKLRfdmqSKEVQNESKVQ 1862
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkKEAEEKKKAEELK----KAEEENKIKAE 1733
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1863 ELISECEElrstlKSKEASFQSEKESMDRTISSLLEDKRNLEEKLCSANDIVAKLETEIAALRPRKSLDR 1932
Cdd:PTZ00121 1734 EAKKEAEE-----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
680-1177 |
6.55e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 67.76 E-value: 6.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 680 EELEKLIADLESKKNSCEC--DQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDAL 757
Cdd:PRK02224 254 ETLEAEIEDLRETIAETERerEELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEC 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 758 DQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASSAEFQRlQNDNTKFQADIASLNERLEEAQnmlTEVQN 837
Cdd:PRK02224 334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR-REEIEELEEEIEELRERFGDAP---VDLGN 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 838 SESTVEKLRIQNHELTAKIKELETNFEEMQreydclsnqlmESVQENDALREEIKQrPT--SHVEESMRSSGISSDfDEQ 915
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTAR-----------ERVEEAEALLEAGKC-PEcgQPVEGSPHVETIEED-RER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 916 KQDinllhqfvqLSESVQQIELQHHSGISRLFRANQMKldQSEPGLKLCLESAEYIEEDNRQSDATepiclkgfLKRHRF 995
Cdd:PRK02224 477 VEE---------LEAELEDLEEEVEEVEERLERAEDLV--EAEDRIERLEERREDLEELIAERRET--------IEEKRE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 996 QIKRL---SQEHVDMGEEKRllDIISQLEQEIE---EKSALMEATEATINEMREQMTNLESALLEksviinkVEDYQRQI 1069
Cdd:PRK02224 538 RAEELrerAAELEAEAEEKR--EAAAEAEEEAEearEEVAELNSKLAELKERIESLERIRTLLAA-------IADAEDEI 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1070 ESLEKQNAEMTMVYEE----LQDRVTRESSMSESLlrvppDEDTLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAE- 1144
Cdd:PRK02224 609 ERLREKREALAELNDErrerLAEKRERKRELEAEF-----DEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEi 683
|
490 500 510
....*....|....*....|....*....|....*
gi 442627454 1145 --LENHLRQiqlkdgnIARLQTDFEEMSERCLSME 1177
Cdd:PRK02224 684 gaVENELEE-------LEELRERREALENRVEALE 711
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1284-2124 |
1.16e-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: 67.39 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1284 QIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSsvtvRCQAELEALKSAH--KENISQAVEERNNLIVQH 1361
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQ----ELEEKLEELRLEVseLEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1362 QAEMETIRETLKNKLAEASTQQskmedafrAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIA 1441
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQL--------EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1442 ELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQL-----QMESLT--RDQISFEIEAHIKKL-ELIVASSKKRIIELEEK 1513
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIerleaRLERLEdrRERLQQEIEELLKKLeEAELKELQAELEELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1514 CDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRnekekcdfETKLETFTFKITDLEEVLKEAQH 1593
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL--------QENLEGFSEGVKALLKNQSGLSG 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1594 KVILYDDLVSQHERLKICLAEAneLSSNLQKKVMslhtelidsqKGISSRDVEINELREELKAamdaKATASAEQMTLVT 1673
Cdd:TIGR02168 521 ILGVLSELISVDEGYEAAIEAA--LGGRLQAVVV----------ENLNAAKKAIAFLKQNELG----RVTFLPLDSIKGT 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1674 QLKDVEERMANQAEKFTREAANLKGSINELLLKLNSMqetkdmleSGNEELKEQLRNSQNLRNMLDEESkMCISLKEKLV 1753
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYL--------LGGVLVVDDLDNALELAKKLRPGY-RIVTLDGDLV 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1754 kledaktsleqqlrdNKSEIYQRHTELTKEVELGRNR-IGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLEnnlGW 1832
Cdd:TIGR02168 656 ---------------RPGGVITGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELE---QL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1833 QQKVDEVTRECEKLRFDMQSKEvQNESKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEKLCSAND 1912
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLE-AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1913 IVAKLETEIAALRPRKSLDRNPVPRKSITFESEIRKNRRISVHDERRQSYWNDVREfgimtdpvdnncNCAELNSKLQDC 1992
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE------------DIESLAAEIEEL 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1993 QRELfiresqvTALKMELDHHplkdenaqltkrvIEEQDKAKVEQKRLKMKLQDLNARINDLTTASAKEPESNQMAQAAK 2072
Cdd:TIGR02168 865 EELI-------EELESELEAL-------------LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627454 2073 PATVAAQTQTESDLETILEKTNVKYQ----EAVRMLRYRYHLIQELKEKLRQNENS 2124
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSltleEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1392-1905 |
1.37e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1392 AEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMinggrvmSDTIAELEKTKAEqdlaVNKLTKDNIELEKQCSKT 1471
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKL-------EKEVKELEELKEE----IEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1472 QEQLQMeslTRDQISfEIEAHIKKLELIVasskKRIIELEEKCDQqVLELDKCRLEKLSLESEIQKANSEHSctmEKLQE 1551
Cdd:PRK03918 258 EEKIRE---LEERIE-ELKKEIEELEEKV----KELKELKEKAEE-YIKLSEFYEEYLDELREIEKRLSRLE---EEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1552 LQAEMKVLSNRNEKekcdfetkLETFTFKITDLEEVLKEAQHKVILYDD---LVSQHERLKICLA-----EANELSSNLQ 1623
Cdd:PRK03918 326 IEERIKELEEKEER--------LEELKKKLKELEKRLEELEERHELYEEakaKKEELERLKKRLTgltpeKLEKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1624 KKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATA-----------SAEQMTLVT-QLKDVEERMA---NQAEK 1688
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelteehRKELLEEYTaELKRIEKELKeieEKERK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1689 FTREAANLKGSINEL--LLKLNSMQETKDMLES-----GNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLED---A 1758
Cdd:PRK03918 478 LRKELRELEKVLKKEseLIKLKELAEQLKELEEklkkyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkK 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1759 KTSLEQQLRDNKSEIYQRHTELTkevELGRNRIGELTKKCEELCS------DLENSDQirlDLQETKEQLKKTLENNLGW 1832
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELE---ELGFESVEELEERLKELEPfyneylELKDAEK---ELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627454 1833 QQKVDEVTRECEKLRFDMQSKEVQ-NESKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEE 1905
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1067-1401 |
1.44e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.88 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1067 RQIESLEKQnAEMTMVYEELQDRVtRESSMSESLLRVppdedtlpgcptspSRREQEVATLKTSITELQSQVSDLKAELE 1146
Cdd:COG1196 200 RQLEPLERQ-AEKAERYRELKEEL-KELEAELLLLKL--------------RELEAELEELEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1147 NHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQyhKAT 1226
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE--LEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1227 ESLSLADAKPDQILLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDDEISALRMEFLLQIETNEKENQAkfyAELQETKDR 1306
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE---EALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1307 YESNVAELKEKLLQVEETLSSV--TVRCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQS 1384
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEeeALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
330
....*....|....*..
gi 442627454 1385 kMEDAFRAEINEVRATL 1401
Cdd:COG1196 499 -AEADYEGFLEGVKAAL 514
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
680-1044 |
2.07e-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: 66.62 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 680 EELEKLIADLESKknsceCDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQ 759
Cdd:TIGR02168 680 EELEEKIEELEEK-----IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 760 QWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLE------SRARSASSAEFQRLQNDNTKFQADIASLNERLEEAQNML- 832
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEaqieqlKEELKALREALDELRAELTLLNEEAANLRERLESLERRIa 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 833 ---TEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQrptshVEESMRSsgIS 909
Cdd:TIGR02168 835 ateRRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE-----LSEELRE--LE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 910 SDFDEQKQDINLL-HQFVQLSESVQQIELQHHSGISRLFRANQMKLDQSEPGLKLCLESAEYIEEDnrqsdatepiclkg 988
Cdd:TIGR02168 908 SKRSELRRELEELrEKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRR-------------- 973
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627454 989 fLKRHRFQIKRLSQehVDMG-------EEKRLLDIISQLEQEIEEKSALMEATEATINEMREQ 1044
Cdd:TIGR02168 974 -LKRLENKIKELGP--VNLAaieeyeeLKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1520-1822 |
3.63e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1520 ELDKcRLEKLSLESEiqKAnsehsctmEKLQELQAEMKVLSNR---NEKEkcDFETKLETFTFKITDLEEVLKEAQHKVi 1596
Cdd:COG1196 197 ELER-QLEPLERQAE--KA--------ERYRELKEELKELEAElllLKLR--ELEAELEELEAELEELEAELEELEAEL- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1597 lyDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLK 1676
Cdd:COG1196 263 --AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1677 DVEERMANQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLE 1756
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627454 1757 DAKTSLEQQLRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQL 1822
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1316-2120 |
5.36e-10 |
|
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: 65.07 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1316 EKLLQVEETLSSVTVRCQAELEALKsahkENISQAVEERNNlIVQHQAEMETIRETLKNKLAEASTQQSKMEdafraEIN 1395
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLK----QYKEKACEIRDQ-ITSKEAQLESSREIVKSYENELDPLKNRLK-----EIE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1396 EVRATLME------QLNQTKEDRDKGASKLEEVKK-----TLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIEL 1464
Cdd:TIGR00606 259 HNLSKIMKldneikALKSRKKQMEKDNSELELKMEkvfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1465 EKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKAN----- 1539
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLcadlq 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1540 SEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVlkEAQHKVILYDDLVSQHERLKICLAEANELS 1619
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQL--EGSSDRILELDQELRKAERELSKAEKNSLT 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1620 SNLQKKVMSLHTELIDSQKGISSRDVEINELREElKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLKGS 1699
Cdd:TIGR00606 497 ETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1700 INELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKL---EDAKTSLEQqLRDNKSEIYQR 1776
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLER-LKEEIEKSSKQ 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1777 HTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQ 1856
Cdd:TIGR00606 655 RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPG 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1857 NESKVQELISECEELRSTLKSKEASFQSEKESMDR------TISSLLEDKRNLE------EKLCSANDIVAKLETEIAAL 1924
Cdd:TIGR00606 735 RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEqetllgTIMPEEESAKVCLtdvtimERFQMELKDVERKIAQQAAK 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1925 RPRKSLDRNPVP---------RKSITFESEIRKNRRISV-HDERRQSYWNDVREFGIMTDPVDNNCNCA--------ELN 1986
Cdd:TIGR00606 815 LQGSDLDRTVQQvnqekqekqHELDTVVSKIELNRKLIQdQQEQIQHLKSKTNELKSEKLQIGTNLQRRqqfeeqlvELS 894
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1987 SKLQDCQRELFIRESQVTALKMELDHhpLKDENAQLTKRVIEEQDKAKVEQKRLKMKLQDLNARINDLTTASAKEPESNQ 2066
Cdd:TIGR00606 895 TEVQSLIREIKDAKEQDSPLETFLEK--DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYL 972
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627454 2067 MAQAAKPATVAAQ--------TQTESDLETILEKTNVKYQEAVRM-----LRYRYHLIQELKEKLRQ 2120
Cdd:TIGR00606 973 KQKETELNTVNAQleecekhqEKINEDMRLMRQDIDTQKIQERWLqdnltLRKRENELKEVEEELKQ 1039
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
990-1735 |
9.19e-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: 64.32 E-value: 9.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 990 LKRHRFQIKRLSQEHVDMGEEKRLLDI-ISQLEQEIEEKSALMEATEATI-----NEMREQMTNLESALLEKSVIINKVE 1063
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEeISELEKRLEEIEQLLEELNKKIkdlgeEEQLRVKEKIGELEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1064 DYQRQIESLEKQNAEMTMVY-------EELQDRVTRESSMSESLL-RVPPDEDTLPGCPTSPSRREQEVATLKTSITELQ 1135
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIdkllaeiEELEREIEEERKRRDKLTeEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1136 SQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLS---DDLCLIDQ-- 1210
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEqlaADLSKYEQel 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1211 --LQKKNAQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKL------------NQLLN-----------AAKDELHD 1265
Cdd:TIGR02169 472 ydLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVlkasiqgvhgtvAQLGSvgeryataievAAGNRLNN 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1266 VrRIKDDEISALRMEFLLQ--------IETNE-----------KENQAKFYA-ELQETKDRYESNVAELKEKLLQVEETL 1325
Cdd:TIGR02169 552 V-VVEDDAVAKEAIELLKRrkagratfLPLNKmrderrdlsilSEDGVIGFAvDLVEFDPKYEPAFKYVFGDTLVVEDIE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1326 SSVTVRCQAELEAL------KS--------AHKENISQAVEERNNLI-VQHQAE-METIRETLKNKLAEASTQQSKMEDA 1389
Cdd:TIGR02169 631 AARRLMGKYRMVTLegelfeKSgamtggsrAPRGGILFSRSEPAELQrLRERLEgLKRELSSLQSELRRIENRLDELSQE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1390 FRAEINEVRaTLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCS 1469
Cdd:TIGR02169 711 LSDASRKIG-EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1470 ktQEQLQmesltrdqisfEIEAHIKKLELIVASSKKRIIELEEKcdqqvleLDKCRLEKLSLESEIqkansehsctmekl 1549
Cdd:TIGR02169 790 --HSRIP-----------EIQAELSKLEEEVSRIEARLREIEQK-------LNRLTLEKEYLEKEI-------------- 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1550 QELQAEMKVLSNRnekeKCDFETKLETFTFKITDLEEVLKEAQHKVilyDDLVSQHERLKICLAEANELSSNLQKKVMSL 1629
Cdd:TIGR02169 836 QELQEQRIDLKEQ----IKSIEKEIENLNGKKEELEEELEELEAAL---RDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1630 HTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLKG--SINELLLKL 1707
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAiqEYEEVLKRL 988
|
810 820
....*....|....*....|....*...
gi 442627454 1708 NSMQETKDMLESGNEELKEQLRNSQNLR 1735
Cdd:TIGR02169 989 DELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
680-894 |
1.04e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.19 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 680 EELEKLIADLESKKNscECDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQ 759
Cdd:COG1196 253 AELEELEAELAELEA--ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 760 QWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASSAEFQRLQNDNTKFQADIASLNERLEEAQ---NMLTEVQ 836
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleELEEAEE 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627454 837 NSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQR 894
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1237-1924 |
1.28e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1237 DQILLSSQYDSQIEKlnqllnaAKDELHDVRRiKDDEISALRMEFLLQIETNEKE-NQAKFYAELQETKDRYE-----SN 1310
Cdd:TIGR02169 160 DEIAGVAEFDRKKEK-------ALEELEEVEE-NIERLDLIIDEKRQQLERLRRErEKAERYQALLKEKREYEgyellKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1311 VAELKEKLLQVEETLSSVTvRCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQSKMEDAF 1390
Cdd:TIGR02169 232 KEALERQKEAIERQLASLE-EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1391 RAEINEVRaTLMEQLNQTKEDRDKGASKLEEVKKTLEQ-----------MINGGRVMSDTIAELEKTKAEQDLAVNKLTK 1459
Cdd:TIGR02169 311 AEKERELE-DAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklteeYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1460 DNIELEK----------QCSKTQEQLQMESLTRDQISFEI---EAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRL 1526
Cdd:TIGR02169 390 YREKLEKlkreinelkrELDRLQEELQRLSEELADLNAAIagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1527 EKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKcdfetkletftfkitDLEEVLKEAQHKVI-LYDDLVSQH 1605
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR---------------AVEEVLKASIQGVHgTVAQLGSVG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1606 ERLKICL----------------AEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMD--------AK 1661
Cdd:TIGR02169 535 ERYATAIevaagnrlnnvvveddAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDlvefdpkyEP 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1662 ATASAEQMTLVTQLKDVEERMANQAEKFTREAanlkgsinELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEE 1741
Cdd:TIGR02169 615 AFKYVFGDTLVVEDIEAARRLMGKYRMVTLEG--------ELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1742 SKMCISLKEKLVKLEDAKTSLEQQLRDNK---SEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQET 1818
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASrkiGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1819 KEQLKKTLENnlgWQQKVDEVTRECEKLRFDmqskEVQNE-SKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLL 1897
Cdd:TIGR02169 767 IEELEEDLHK---LEEALNDLEARLSHSRIP----EIQAElSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
730 740
....*....|....*....|....*..
gi 442627454 1898 EDKRNLEEKLCSANDIVAKLETEIAAL 1924
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
824-1502 |
8.60e-09 |
|
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: 61.01 E-value: 8.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 824 RLEEAQNMLTEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVqenDALREEIKQRptshveesm 903
Cdd:pfam12128 235 GIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLL---RTLDDQWKEK--------- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 904 rssgissdFDEQKQDINLLHQFVQLSES-VQQIELQHhsGISRLFRANQMKLDQS------------EPGLKLCLESAEY 970
Cdd:pfam12128 303 --------RDELNGELSAADAAVAKDRSeLEALEDQH--GAFLDADIETAAADQEqlpswqselenlEERLKALTGKHQD 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 971 IEE--DNRQSDATEpiclkgflkRHRFQIKRLSQEHVDMGEEK-RLLDIISQLEQEIEekSALMEATEATINEMREQMTN 1047
Cdd:pfam12128 373 VTAkyNRRRSKIKE---------QNNRDIAGIKDKLAKIREARdRQLAVAEDDLQALE--SELREQLEAGKLEFNEEEYR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1048 LESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSMSESLLRVPPDEDTLPGCPTSPSRREQEVatl 1127
Cdd:pfam12128 442 LKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEER--- 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1128 KTSITELQSQVSDLKAELENHLR-QIQLKDGNIARL-------QTDFE-EMSERCLSMEVRLAELDEDTKQKQ------- 1191
Cdd:pfam12128 519 QSALDELELQLFPQAGTLLHFLRkEAPDWEQSIGKVispellhRTDLDpEVWDGSVGGELNLYGVKLDLKRIDvpewaas 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1192 -ELLDRQAQKLSDDL----CLIDQLQKKNAQLVEQYHKATESLSLA-----DAKPDQILLSSQYDSQIEKLNQLLNAAKD 1261
Cdd:pfam12128 599 eEELRERLDKAEEALqsarEKQAAAEEQLVQANGELEKASREETFArtalkNARLDLRRLFDEKQSEKDKKNKALAERKD 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1262 ELHDVRRikddeisalrmefllQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELEALKS 1341
Cdd:pfam12128 679 SANERLN---------------SLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRS 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1342 AHKENISQAVEERNNLIV------QHQAEMETIRETLKNKLAEASTQQSKMEDAFR------AEINEVRATLMEQLNQTK 1409
Cdd:pfam12128 744 GAKAELKALETWYKRDLAslgvdpDVIAKLKREIRTLERKIERIAVRRQEVLRYFDwyqetwLQRRPRLATQLSNIERAI 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1410 EDRDKGASKLEEVKKTLEQMINGGRVMSDTIA-----ELEKTKAEQD-LAVNKLTKDNIELEKQCSKTQEQLQMESLTRD 1483
Cdd:pfam12128 824 SELQQQLARLIADTKLRRAKLEMERKASEKQQvrlseNLRGLRCEMSkLATLKEDANSEQAQGSIGERLAQLEDLKLKRD 903
|
730
....*....|....*....
gi 442627454 1484 QISFEIEAHIKKLELIVAS 1502
Cdd:pfam12128 904 YLSESVKKYVEHFKNVIAD 922
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1360-2081 |
1.30e-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: 60.46 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1360 QHQAEMETIRETLKNKLAEASTQQSKME-DAFRAEINEVRatlmEQLNQTKEDRDKGASKLEEVKKTLEQMInggrvmsD 1438
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVLRlEELREELEELQ----EELKEAEEELEELTAELQELEEKLEELR-------L 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1439 TIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLEL---IVASSKKRIIELEEKCD 1515
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDElaeELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1516 QQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSN---RNEKEKCDFETKLETFTFKITDLEEVLKEAQ 1592
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeieRLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1593 HKVI---------LYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQ-------------------------- 1637
Cdd:TIGR02168 435 LKELqaeleeleeELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslerlqenlegfsegvkallkn 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1638 ----KGISSRDVEINELREELKAAMDAkATASAEQMTLVTQLKDVEERMANQAEKFTREAANL----------KGSINEL 1703
Cdd:TIGR02168 515 qsglSGILGVLSELISVDEGYEAAIEA-ALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLpldsikgteiQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1704 LLKLNSMQETKDMLESGNEELK-------------EQLRNSQNLRNMLDEESkMCISLKEKLVKLE------DAKTSLEQ 1764
Cdd:TIGR02168 594 LKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvDDLDNALELAKKLRPGY-RIVTLDGDLVRPGgvitggSAKTNSSI 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1765 QLRDNKSEiyqrhtELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNlgwQQKVDEVTRECE 1844
Cdd:TIGR02168 673 LERRREIE------ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL---RKDLARLEAEVE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1845 KLRFDMQSKEVQNES---KVQELISECEELRSTLKSKEAsfqsEKESMDRTISSLLEDKRNLEEKLCSANDIVAKLETEI 1921
Cdd:TIGR02168 744 QLEERIAQLSKELTEleaEIEELEERLEEAEEELAEAEA----EIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1922 AALRPRKSLDRNPVPRKSITFESEIRKNRRISVHDERRQSYWNDVREFgimtdpvdnncnCAELNSKLQDCQRELFIRES 2001
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL------------IEELESELEALLNERASLEE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 2002 QVTALKMELDHhpLKDENAQLTKRVIEEQDKAKVEQKRL---KMKLQDLNARINDLTTASAKEPESNQMAQAAKPATVAA 2078
Cdd:TIGR02168 888 ALALLRSELEE--LSEELRELESKRSELRRELEELREKLaqlELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965
|
...
gi 442627454 2079 QTQ 2081
Cdd:TIGR02168 966 DEE 968
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
531-1092 |
1.71e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.95 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 531 EVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISELEEKLSTLKQtmRIMEVENQVAVGLEf 610
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA--ELARLEQDIARLEE- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 611 efeahkkssklRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSKeghmlsiapEQEDIAgdsicnkcEELEKLIADLE 690
Cdd:COG1196 310 -----------RRRELEERLEELEEELAELEEELEELEEELEELEE---------ELEEAE--------EELEEAEAELA 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 691 SKKnscecdQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITT 770
Cdd:COG1196 362 EAE------EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 771 LHEKHEHVQEKYQKLQEEYEQLESRARSASSA---EFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVEKLRI 847
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAElleEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 848 QN---------HELTAKIKELETNFEEmqREYDCLSNQLMESVQENDALREEIKQRPTSHVEESMRSSGISSDFDEQKQD 918
Cdd:COG1196 516 LAglrglagavAVLIGVEAAYEAALEA--ALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 919 INLLHQFVQLSESvqqiELQHHSGISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIK 998
Cdd:COG1196 594 RGAIGAAVDLVAS----DLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRE 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 999 RLSQEHVDMGEEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQ--- 1075
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEElle 749
|
570 580
....*....|....*....|..
gi 442627454 1076 -----NAEMTMVYEELQDRVTR 1092
Cdd:COG1196 750 eealeELPEPPDLEELERELER 771
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
680-1043 |
3.03e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 680 EELEKLIADLESKKNscECDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQ 759
Cdd:TIGR02169 674 AELQRLRERLEGLKR--ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 760 QWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASSAEFQRLQNDNTKFQADI--------ASLNERLEEAQNM 831
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIearlreieQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 832 LTEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQRptshvEESMRSsgISSD 911
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL-----EAQLRE--LERK 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 912 FDEQKQDINLLHQFVQLSESVQQIELQHHSGISRLFRAnqmklDQSEPGLKLCLES-AEYIEEDNRQSDATEPICLKGFl 990
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-----DEEIPEEELSLEDvQAELQRVEEEIRALEPVNMLAI- 978
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 442627454 991 krhrfqikrlsQEHVDmgEEKRLLDIISQLEQEIEEKSALMEATEATINEMRE 1043
Cdd:TIGR02169 979 -----------QEYEE--VLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1013-1907 |
3.64e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.03 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1013 LLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTR 1092
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1093 ESSMSEsllrvppdeDTLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSER 1172
Cdd:pfam01576 153 ERKLLE---------ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1173 CLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKpdqillSSQYDSQIEKL 1252
Cdd:pfam01576 224 IAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAA------RNKAEKQRRDL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1253 NQLLNAAKDELHDV--RRIKDDEISALRMEFLLQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEetlssvtv 1330
Cdd:pfam01576 298 GEELEALKTELEDTldTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAK-------- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1331 RCQAELEALKSA-HKENISQAVEERnnLIVQHQAEMETIRETLKNKLAEAstqQSKMEDAFRAeinevRATLMEQLNqtk 1409
Cdd:pfam01576 370 RNKANLEKAKQAlESENAELQAELR--TLQQAKQDSEHKRKKLEGQLQEL---QARLSESERQ-----RAELAEKLS--- 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1410 edrdKGASKLEEVKKTLEqminggrvmsdtiaelektkaEQDLAVNKLTKDNIELEKQCSKTQEQLQMEslTRDQISfeI 1489
Cdd:pfam01576 437 ----KLQSELESVSSLLN---------------------EAEGKNIKLSKDVSSLESQLQDTQELLQEE--TRQKLN--L 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1490 EAHIKKLELIVASSKKRIIELEEKcdqqvleldkcrleKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCD 1569
Cdd:pfam01576 488 STRLRQLEDERNSLQEQLEEEEEA--------------KRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1570 FETKLETFTFKITDLEEVLKEAQHKVILYDDLVSQHERLKiclaeanELSSNLQKKVMSLHTELIDsQKGISSRDVEINE 1649
Cdd:pfam01576 554 LEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQR-------QLVSNLEKKQKKFDQMLAE-EKAISARYAEERD 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1650 LREELKAAMDAKATASAEQMTLVTQLKDVEERmANQAEKftREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLr 1729
Cdd:pfam01576 626 RAEAEAREKETRALSLARALEEALEAKEELER-TNKQLR--AEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQL- 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1730 nsqnlrnmldEEskmcisLKEKLVKLEDAKTSLEQQLRDNKSeiyQRHTELTKEVELGRNRIGELTKKCEELCSDLENSD 1809
Cdd:pfam01576 702 ----------EE------LEDELQATEDAKLRLEVNMQALKA---QFERDLQARDEQGEEKRRQLVKQVRELEAELEDER 762
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1810 QIR-----------LDLQETKEQLKKT-------LENNLGWQQKVDEVTRECEKLRFD-----MQSKEVQNESK------ 1860
Cdd:pfam01576 763 KQRaqavaakkkleLDLKELEAQIDAAnkgreeaVKQLKKLQAQMKDLQRELEEARASrdeilAQSKESEKKLKnleael 842
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 442627454 1861 --VQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEKL 1907
Cdd:pfam01576 843 lqLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARI 891
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1392-2183 |
6.25e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.16 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1392 AEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMinggrvmsdtiaELEKTKAE---------QDLAVNKLTKDNI 1462
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERL------------RREREKAEryqallkekREYEGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1463 ELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELdKCRLEKLSLE-SEIQKANSE 1541
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIGELEAEiASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1542 HSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKvilYDDLVSQHERLKICLAEANELSSN 1621
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE---LEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1622 LQKKVMSLHTElidsqkgissrdveINELREELKAAMDAKATASAEQMTLVTQLKDVEERMAnqaekftreaanlkgsin 1701
Cdd:TIGR02169 390 YREKLEKLKRE--------------INELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN------------------ 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1702 elllklnsmqETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLrdnkseiyqrhTELT 1781
Cdd:TIGR02169 438 ----------ELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL-----------AEAE 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1782 KEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQKV-----DEVTRECEKLRFDMQS---- 1852
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvvedDAVAKEAIELLKRRKAgrat 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1853 ----KEVQNESKVQELIS------------ECEE---------LRSTLKSKeaSFQSEKESMD----------------- 1890
Cdd:TIGR02169 577 flplNKMRDERRDLSILSedgvigfavdlvEFDPkyepafkyvFGDTLVVE--DIEAARRLMGkyrmvtlegelfeksga 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1891 -----RTISSLLEDKRNLEEKLCSANDIVAKLETEIAALRPRKSLDRNPVPRKSITFESEIRKNRRISVHDERRQSYWND 1965
Cdd:TIGR02169 655 mtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1966 VREfgimtdpvdnncNCAELNSKLQDCQRELFIRESQVTAL-----KMELDHHPLKDENAQLTKRVIEEQ--------DK 2032
Cdd:TIGR02169 735 LKE------------RLEELEEDLSSLEQEIENVKSELKELearieELEEDLHKLEEALNDLEARLSHSRipeiqaelSK 802
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 2033 AKVEQKRLKMKLQDLNARINDLTTASAKEPESNQMAQAAKPAT---VAAQTQTESDLETILEKTNVKYQEAVRMLRyryH 2109
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEELEAALR---D 879
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627454 2110 LIQELKEKLRQNENsdtsnitslsagqtsaLKAQCESQKKEILAIKYKYEAAKRILAIRNDDLDALREKLAKYE 2183
Cdd:TIGR02169 880 LESRLGDLKKERDE----------------LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1352-1880 |
8.26e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.74 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1352 EERNNLIVQHQAEMETIRET-LKNKLAEASTQQSKMEDAFRaEINEVRATLMEQLNQTKEDRDKGASKLEEVKkTLEQMI 1430
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKdLHERLNGLESELAELDEEIE-RYEEQREQARETRDEADEVLEEHEERREELE-TLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1431 NGGRvmsDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEahikklelivasskkriiEL 1510
Cdd:PRK02224 261 EDLR---ETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE------------------EL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1511 EEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLsnrnEKEKCDFETKLETFTFKITDLEEVLKE 1590
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEL----ESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1591 AQHKVilyDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQK----------------------------GISS 1642
Cdd:PRK02224 396 LRERF---GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARErveeaealleagkcpecgqpvegsphveTIEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1643 RDVEINELREELkAAMDAKATASAEQMTLVTQLKDVE---ERMANQAEKFTREAANLKGSINELLLKLNSMQETKDMLES 1719
Cdd:PRK02224 473 DRERVEELEAEL-EDLEEEVEEVEERLERAEDLVEAEdriERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1720 GNEELKEQLR----NSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLE--QQLRDNKSEIYQRHTELTKEVELGRNRIGE 1793
Cdd:PRK02224 552 EAEEKREAAAeaeeEAEEAREEVAELNSKLAELKERIESLERIRTLLAaiADAEDEIERLREKREALAELNDERRERLAE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1794 LTKKCEELCSDLENSdqiRLD-LQETKEQLKKTLENnlgwqqkVDEVTRECEKLRFDMQSKEVQNESKVQELisecEELR 1872
Cdd:PRK02224 632 KRERKRELEAEFDEA---RIEeAREDKERAEEYLEQ-------VEEKLDELREERDDLQAEIGAVENELEEL----EELR 697
|
....*...
gi 442627454 1873 STLKSKEA 1880
Cdd:PRK02224 698 ERREALEN 705
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1478-1797 |
8.69e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 8.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1478 ESLTR-DQISFEIEAHIKKLEL--IVASSKKRIIELEEKCDQQ--VLELDKCRLEKLSLESEIQKANsehsctmEKLQEL 1552
Cdd:COG1196 186 ENLERlEDILGELERQLEPLERqaEKAERYRELKEELKELEAEllLLKLRELEAELEELEAELEELE-------AELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1553 QAEMKVLsnrnekekcdfETKLETFTFKITDLEEVLKEAQHKvilYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTE 1632
Cdd:COG1196 259 EAELAEL-----------EAELEELRLELEELELELEEAQAE---EYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1633 LIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLKGSINELLLKLNSMQE 1712
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1713 TKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNKSEIYQRHTELTKEVELGRNRIG 1792
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
....*
gi 442627454 1793 ELTKK 1797
Cdd:COG1196 485 ELAEA 489
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
749-1322 |
1.13e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 749 QLQERYDALDQQWQAQQAGITTLHekHEHVQEKYQKLQEEYEQLEsrarsassAEFQRLQNDNTKFQADIASLNERLEEA 828
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELR--------AELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 829 QNMLTEVQNSEstVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQRPTSHVEESMRssgI 908
Cdd:COG4913 329 EAQIRGNGGDR--LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA---L 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 909 SSDFDEQKQDI-NLLHQFVQLSESVQQIElQHHSGISR---LFR---ANQMKLDQSEP---------------------- 959
Cdd:COG4913 404 EEALAEAEAALrDLRRELRELEAEIASLE-RRKSNIPArllALRdalAEALGLDEAELpfvgelievrpeeerwrgaier 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 960 ---GLKLCLesaeyIEEDNRQSDATEpiclkgFLKRHRFQiKRLSQEHVDMGEEKRLLDIISQ----------------- 1019
Cdd:COG4913 483 vlgGFALTL-----LVPPEHYAAALR------WVNRLHLR-GRLVYERVRTGLPDPERPRLDPdslagkldfkphpfraw 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1020 LEQEIEEKSALM--EATEATINE----MREQMT---------NLESALLEKSVI----INKVEDYQRQIESLEKQNAEMT 1080
Cdd:COG4913 551 LEAELGRRFDYVcvDSPEELRRHpraiTRAGQVkgngtrhekDDRRRIRSRYVLgfdnRAKLAALEAELAELEEELAEAE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1081 MVYEELQ---DRVTRESSMSESLLRVPPDEDTLPGCPTSPSRREQEVATLKTS---ITELQSQVSDLKAELENHLRQIQL 1154
Cdd:COG4913 631 ERLEALEaelDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASsddLAALEEQLEELEAELEELEEELDE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1155 KDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQ-ELLDRQAQKLSDDLC---LIDQLQKKNAQLVEQYHKATESL- 1229
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDAVereLRENLEERIDALRARLNRAEEELe 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1230 -SLADAKPDQILLSSQYDSQIEKLNQLLnaakdELHDvrRIKDDEISALRMEFLLQIETNEKENQAKFYAELQETKDRYE 1308
Cdd:COG4913 791 rAMRAFNREWPAETADLDADLESLPEYL-----ALLD--RLEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIK 863
|
650
....*....|....
gi 442627454 1309 SNVAELKEKLLQVE 1322
Cdd:COG4913 864 ERIDPLNDSLKRIP 877
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
530-1089 |
1.20e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 530 EEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRIMEVENQVAVGLE 609
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 610 FEFEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSKEghmlsIAPEQEDIagdsicnkcEELEKLIADL 689
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE-----LAEAEEEL---------EELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 690 ESKKNscecdQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGIT 769
Cdd:COG1196 392 LRAAA-----ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 770 TLHEKHEHVQEKYQKLQEEYEQLESRARSASSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQN 849
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 850 HELTAKIKELETnfEEMQREYdcLSNQLMESVQENDALREEIKQRPTSHVEESMRSSGISSDFDEQKQDINLLHQFVQLS 929
Cdd:COG1196 547 ALQNIVVEDDEV--AAAAIEY--LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 930 ESVQQIELQHHSGISRLFRANQMKLDQSE--PGLKLCLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIKRLSQEHVDM 1007
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLegEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1008 GEEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDY-----QRQIESLEKQNAEMTMV 1082
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPdleelERELERLEREIEALGPV 782
|
570
....*....|....
gi 442627454 1083 -------YEELQDR 1089
Cdd:COG1196 783 nllaieeYEELEER 796
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
991-1428 |
3.62e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 991 KRHRFQIKRLSQEHVDMGEEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLEsALLEKSVIINKVEDYQRQIE 1070
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1071 SLEKQNAEMTMVYEELQDRVTRESSMSESLLRVPPDEDTLpgCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLR 1150
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEEL--LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1151 QIQLKDGNIARLQTDFEEMSERC---------------LSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKN 1215
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEErlkearlllliaaalLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1216 AQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKlnqllNAAKDELHDVRRIKDDEISALRMEFLLQIETNEKENQAK 1295
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSP-----EELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1296 FYAELQETKDRYESNvAELKEKLLQVEETLSSVTVRCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNK 1375
Cdd:COG4717 376 LAEAGVEDEEELRAA-LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREE 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 442627454 1376 LAEASTQQSKMEDAFR-AEINEVRATLMEQLNQTKEDRDK---GASKLEEVKKTLEQ 1428
Cdd:COG4717 455 LAELEAELEQLEEDGElAELLQELEELKAELRELAEEWAAlklALELLEEAREEYRE 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1583-1880 |
4.12e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1583 DLEEVLKEAQHKVILYDDLVSQHErlkicLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKA 1662
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAE-----LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1663 TASAEQMTLVTQLKDVEERMANQAEkftrEAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEEs 1742
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEE----RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1743 kmcislKEKLVKLEDAKTSLEQQLRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQL 1822
Cdd:COG1196 367 ------LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627454 1823 KKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISECEELRSTLKSKEA 1880
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1433-1907 |
5.74e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.05 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1433 GRVMSDTIAELEKTKA------EQDL--AVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLElivassk 1504
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAqieekeEKDLheRLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1505 kRIIELEEKCDQQVLELDKCRLEKLSLESEIQkansEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDL 1584
Cdd:PRK02224 252 -ELETLEAEIEDLRETIAETEREREELAEEVR----DLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1585 EEVLKEAQHKVilyDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATA 1664
Cdd:PRK02224 327 RDRLEECRVAA---QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1665 SaeqmtlvTQLKDVEERMANQAEkftrEAANLKGSINELLLKL----NSMQETKDMLESGN--------------EELKE 1726
Cdd:PRK02224 404 P-------VDLGNAEDFLEELRE----ERDELREREAELEATLrtarERVEEAEALLEAGKcpecgqpvegsphvETIEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1727 QLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQ--QLRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELCSD 1804
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRieRLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1805 LEnsdQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRfdmqskevqNESKVQELISECEELRSTLKSKEASFQS 1884
Cdd:PRK02224 553 AE---EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE---------RIRTLLAAIADAEDEIERLREKREALAE 620
|
490 500
....*....|....*....|...
gi 442627454 1885 EKESMDRTISSLLEDKRNLEEKL 1907
Cdd:PRK02224 621 LNDERRERLAEKRERKRELEAEF 643
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1392-1735 |
7.56e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1392 AEINEVRATLMEQLNQTKEDRDKgASKLEEVKKTLEQMinGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKT 1471
Cdd:COG1196 189 ERLEDILGELERQLEPLERQAEK-AERYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1472 QEQLQMESLTRDQISFEIEAHIKKLELIVAsskkRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQE 1551
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLA----ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1552 LQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKVILYDDLVSQHERLKICLAEANELSSNLQKKVMSLHT 1631
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1632 ELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEkftrEAANLKGSINELLLKLNSMQ 1711
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA----ALAELLEELAEAAARLLLLL 497
|
330 340
....*....|....*....|....
gi 442627454 1712 ETKDMLESGNEELKEQLRNSQNLR 1735
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRG 521
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1021-1870 |
1.07e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.21 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1021 EQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTM----VYEELQDRVTRESSM 1096
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLdylkLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1097 SESLLRVPPDEDTLpgcPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKdgniARLQTDFEEMSERCLSM 1176
Cdd:pfam02463 249 EQEEIESSKQEIEK---EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK----LERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1177 EVRLAElDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKLNQLL 1256
Cdd:pfam02463 322 EKKKAE-KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1257 NAAKDELHDVRRIKDDEISALRMEFLLQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSvtVRCQAEL 1336
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE--DLLKETQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1337 EALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRDKGA 1416
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1417 SKLEEVKKTLEqmINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTqEQLQMESLTRDQISFEIEAHIKKL 1496
Cdd:pfam02463 559 EVEERQKLVRA--LTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA-TLEADEDDKRAKVVEGILKDTELT 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1497 ELIVaSSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLET 1576
Cdd:pfam02463 636 KLKE-SAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1577 FTFKITDLEEVLKEAQHKVILYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKA 1656
Cdd:pfam02463 715 LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1657 AMDAKATASAEqmtLVTQLKDVEERMANQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRN 1736
Cdd:pfam02463 795 KLKAQEEELRA---LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1737 MLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQ 1816
Cdd:pfam02463 872 LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKE 951
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 442627454 1817 ETKeqLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISECEE 1870
Cdd:pfam02463 952 ENN--KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
990-1557 |
1.17e-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: 53.96 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 990 LKRHRFQIKRLSQEHVDMGEEKR-----LLDIISQLEQEIEEKSALMEATEATINEMRE----QMTNLESALLEKSVIIN 1060
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDKEkqvslLLIQITEKENKMKDLTFLLEESRDKANQLEEktklQDENLKELIEKKDHLTK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1061 KVEDYQRqieSLEKQNAEMTMVYEELQDRVTRESSMSESllrvppDEDTLPGCPTSPSRREQEVATLKTSITELQSQVSD 1140
Cdd:pfam05483 297 ELEDIKM---SLQRSMSTQKALEEDLQIATKTICQLTEE------KEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1141 LKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLD--RQAQKLSDDLC-----LIDQLQK 1213
Cdd:pfam05483 368 EQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDekKQFEKIAEELKgkeqeLIFLLQA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1214 KNAQL-------------VEQYHKATESL--SLADAKPDQILLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDDEISALR 1278
Cdd:pfam05483 448 REKEIhdleiqltaiktsEEHYLKEVEDLktELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKK 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1279 ME--FLLQIETNEkENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELEALKSAHKE--NISQAVEER 1354
Cdd:pfam05483 528 QEerMLKQIENLE-EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnNLKKQIENK 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1355 NNLIVQHQAEmetiretlKNKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMinggr 1434
Cdd:pfam05483 607 NKNIEELHQE--------NKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKL----- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1435 vmsdtIAELEKTKAEQDLAVnKLTKdniELEKQCS-KTQEQLQMESLTRDQISFEIEAHIKKLELIvassKKRIIELEEK 1513
Cdd:pfam05483 674 -----LEEVEKAKAIADEAV-KLQK---EIDKRCQhKIAEMVALMEKHKHQYDKIIEERDSELGLY----KNKEQEQSSA 740
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 442627454 1514 CDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMK 1557
Cdd:pfam05483 741 KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
749-1339 |
1.37e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 749 QLQERYDALDQQ-----WQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASsAEFQRLQNDNTKFQADIASLNE 823
Cdd:COG1196 217 ELKEELKELEAEllllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELR-LELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 824 RLEEAQNMLT----EVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQrptshv 899
Cdd:COG1196 296 ELARLEQDIArleeRRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 900 EESMRSSGISSDFDEQKQDINLLHQFVQLSESVQQIELQHHSGISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSD 979
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 980 AtepiclkgfLKRHRFQIKRLSQEHVDMGEEKRLLDiisQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVII 1059
Cdd:COG1196 450 E---------EAELEEEEEALLELLAELLEEAALLE---AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1060 NkvedyQRQIESLEKQNAEMTMVYEelqdRVTRESSMSESLLRVPPDEDTLPGCptspsrREQEVATLKTSITELQSQVS 1139
Cdd:COG1196 518 G-----LRGLAGAVAVLIGVEAAYE----AALEAALAAALQNIVVEDDEVAAAA------IEYLKAAKAGRATFLPLDKI 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1140 DLKAELENHLRQIQLKDGnIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLV 1219
Cdd:COG1196 583 RARAALAAALARGAIGAA-VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1220 EQYHKATESLSLADAKpdQILLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDDEISALRMEFLLQIETNEKENQAKFYAE 1299
Cdd:COG1196 662 LTGGSRRELLAALLEA--EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 442627454 1300 LQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELEAL 1339
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1670-1925 |
1.41e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1670 TLVTQLKDVE-ERMANQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKmciSL 1748
Cdd:COG1196 217 ELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY---EL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1749 KEKLVKLEDAKTSLEQQLRDNKSEIyqrhTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLEN 1828
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERL----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1829 NLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELisecEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEKLC 1908
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250
....*....|....*..
gi 442627454 1909 SANDIVAKLETEIAALR 1925
Cdd:COG1196 446 EAAEEEAELEEEEEALL 462
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1291-1906 |
1.67e-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: 53.57 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1291 ENQAKFYAELQETKDRYESNVAELKEKLLQVEEtlssvtVRCQAELEALKSAHKenISQAVEERNNLIVQHQAEMETIRE 1370
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEE------LRVQAENARLEMHFK--LKEDHEKIQHLEEEYKKEINDKEK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1371 TLKNKLAEASTQQSKMED-AFRAEINEVRATLMEQ--------LNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIA 1441
Cdd:pfam05483 241 QVSLLLIQITEKENKMKDlTFLLEESRDKANQLEEktklqdenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQ 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1442 ------------------ELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIVASS 1503
Cdd:pfam05483 321 iatkticqlteekeaqmeELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1504 KKRIIELEEkcdqqvleLDKCRLEKLSLESEiqkaNSEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTfkiTD 1583
Cdd:pfam05483 401 NNKEVELEE--------LKKILAEDEKLLDE----KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIK---TS 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1584 LEEVLKEAQhkvilydDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKAT 1663
Cdd:pfam05483 466 EEHYLKEVE-------DLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1664 ASAEQMTLVTQLKDVEERMANQAE----KFTREAANLKGSINELLLKLNSMQET-------KDMLESGNEELKEQLRNSQ 1732
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDevkcKLDKSEENARSIEYEVLKKEKQMKILenkcnnlKKQIENKNKNIEELHQENK 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1733 NLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDnKSEIYQRHTELTKEVElgRNRIGELTKKCEELCSDLENSDQIR 1812
Cdd:pfam05483 619 ALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE-IIDNYQKEIEDKKISE--EKLLEEVEKAKAIADEAVKLQKEID 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1813 LDLQETKEQLKKTLENNlgwQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISECEELRSTLKSKEASFQSEKESMDRT 1892
Cdd:pfam05483 696 KRCQHKIAEMVALMEKH---KHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKL 772
|
650
....*....|....
gi 442627454 1893 ISSLLEDKRNLEEK 1906
Cdd:pfam05483 773 KMEAKENTAILKDK 786
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1118-1345 |
2.06e-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: 52.46 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1118 SRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQ 1197
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1198 AQKLSDdlcLIDQLQKKNAQlveqyhkATESLSLADAKPDQILLSSQYdsqiekLNQLLNAAKDELHDVRRIKdDEISAL 1277
Cdd:COG4942 103 KEELAE---LLRALYRLGRQ-------PPLALLLSPEDFLDAVRRLQY------LKYLAPARREQAEELRADL-AELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627454 1278 RMEFllqieTNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVtvrcQAELEALKSAHKE 1345
Cdd:COG4942 166 RAEL-----EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL----AAELAELQQEAEE 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1017-1236 |
2.19e-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: 52.46 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1017 ISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVED----YQRQIESLEKQNAEMTMVYEELQDRVTR 1092
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaaLEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1093 ESSMSESLLRVPPDEDTLPgcPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSER 1172
Cdd:COG4942 109 LLRALYRLGRQPPLALLLS--PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627454 1173 clsmevrLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKP 1236
Cdd:COG4942 187 -------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1284-1924 |
2.47e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1284 QIETNEKE-NQAKFYAELQETKDRYESNVAELKEKLLQveetlssvtvrcqAELEALKSAHKENisqavEERNNLIVQHQ 1362
Cdd:COG1196 201 QLEPLERQaEKAERYRELKEELKELEAELLLLKLRELE-------------AELEELEAELEEL-----EAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1363 AEMETIRETLKNKLAEASTQQSKMEDAFRAEINEVrATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAE 1442
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1443 LEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLelivASSKKRIIELEEKCDQQVLELD 1522
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA----AELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1523 KCRLEKLSLESEIQKANSEhsctmeKLQELQAEMKVLSNRNEKEkcdfeTKLETFTFKITDLEEVLKEAQHKVILYDDLV 1602
Cdd:COG1196 418 RLEEELEELEEALAELEEE------EEEEEEALEEAAEEEAELE-----EEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1603 SQHERLKICLAEANELSSNLQKKVMSLHteLIDSQKGISSRDVEINELREELKAAMDAKATASAEQmtlvtqlkDVEERM 1682
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAAL--LLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN--------IVVEDD 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1683 ANQAEKFTREAANLKGSINELLLklnsmqetkDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSL 1762
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPL---------DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1763 EQQLRDNKSEIYQRHTELTKEVELGRnrigeltkkceelcsdlensDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRE 1842
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEG--------------------EGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1843 CEKLRFDMQSKEVQNESKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEKLCSANDI--------- 1913
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEppdleeler 767
|
650
....*....|..
gi 442627454 1914 -VAKLETEIAAL 1924
Cdd:COG1196 768 eLERLEREIEAL 779
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
625-887 |
3.26e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.61 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 625 DLLSALLEKESTIESLQKSLDNLTRDVLRNSKEGHMLSiAPEQEDIAgdsicnkcEELEKL-IADLESKKNScecdqlrl 703
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALK-DDNDEETR--------ETLSTLsLRQLESRLAQ-------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 704 eivsVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQ------------NAFGQLQERYDALDqQWQAQQAGITTL 771
Cdd:PRK11281 133 ----TLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSqrlqqirnllkgGKVGGKALRPSQRV-LLQAEQALLNAQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 772 HEKHEHVQEKYQKLQEeyeqLESRARSASSAEFQRLQNDNTKFQADIASlnERLEEAQNMLTEVQNSESTVeklRIQNHE 851
Cdd:PRK11281 208 NDLQRKSLEGNTQLQD----LLQKQRDYLTARIQRLEHQLQLLQEAINS--KRLTLSEKTVQEAQSQDEAA---RIQANP 278
|
250 260 270
....*....|....*....|....*....|....*.
gi 442627454 852 LTAkiKELETNFEemqreydcLSNQLMESVQENDAL 887
Cdd:PRK11281 279 LVA--QELEINLQ--------LSQRLLKATEKLNTL 304
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
596-1333 |
3.90e-06 |
|
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: 52.53 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 596 RIMEVENQVAvGLEFEFEAhKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVlrnskeghmlsiaPEQEDIAGDSI 675
Cdd:pfam12128 235 GIMKIRPEFT-KLQQEFNT-LESAELRLSHLHFGYKSDETLIASRQEERQETSAEL-------------NQLLRTLDDQW 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 676 CNKCEELEKLIADLESKKNSCECDQLRLEIVSVRDKLESVESAfNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYD 755
Cdd:pfam12128 300 KEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETA-AADQEQLPSWQSELENLEERLKALTGKHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 756 ALDQQWQAQ-QAGITTLHEKHEHVQEKYQKLQEE----YEQLESRARSassaefqRLQNDNTKFQADIASLNERLEEAQN 830
Cdd:pfam12128 379 RRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVaeddLQALESELRE-------QLEAGKLEFNEEEYRLKSRLGELKL 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 831 MLTEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALReeikqrptshvEESMRSSGISS 910
Cdd:pfam12128 452 RLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALR-----------QASRRLEERQS 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 911 DFDEQKQDI----NLLHQFVQ-----LSESVQQI---ELQHHSGISRLFRANQMKLDQSEPGLKLCLEsaeyieednrQS 978
Cdd:pfam12128 521 ALDELELQLfpqaGTLLHFLRkeapdWEQSIGKVispELLHRTDLDPEVWDGSVGGELNLYGVKLDLK----------RI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 979 DATEPICLKGFLKRHRFQIKRLSQEHVDMgeEKRLLDIISQLEQEIEEKSALMEATEATI-----------NEMREQMTN 1047
Cdd:pfam12128 591 DVPEWAASEEELRERLDKAEEALQSAREK--QAAAEEQLVQANGELEKASREETFARTALknarldlrrlfDEKQSEKDK 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1048 LESALLEKsviINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSMS--ESLLRVPPDEDTLPGC--PTSPSRREQE 1123
Cdd:pfam12128 669 KNKALAER---KDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEkqAYWQVVEGALDAQLALlkAAIAARRSGA 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1124 VATLKTSITELQSQ----------VSDLKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQEL 1193
Cdd:pfam12128 746 KAELKALETWYKRDlaslgvdpdvIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISE 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1194 LDRQAQKLSDDLCL-IDQLQKKNAQLVEQYHKATESLSLADAKPDQiLLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDD 1272
Cdd:pfam12128 826 LQQQLARLIADTKLrRAKLEMERKASEKQQVRLSENLRGLRCEMSK-LATLKEDANSEQAQGSIGERLAQLEDLKLKRDY 904
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627454 1273 EISALRMEfllqIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQ 1333
Cdd:pfam12128 905 LSESVKKY----VEHFKNVIADHSGSGLAETWESLREEDHYQNDKGIRLLDYRKLVPYLEQ 961
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
506-807 |
5.42e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 506 DKIKKEIQDLQM-FTSLEKHFEVECEEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISEL 584
Cdd:COG1196 242 EELEAELEELEAeLEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 585 EEKLSTLKQTMRIMEVENQVAVGLEFEFEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSKEghmlsIA 664
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-----AA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 665 PEQEDIagdsicnkcEELEKLIADLESKKnscecDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQ 744
Cdd:COG1196 397 ELAAQL---------EELEEAEEALLERL-----ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627454 745 NAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEkyqkLQEEYEQLESRARSASSAEFQRL 807
Cdd:COG1196 463 ELLAELLEEAALLEAALAELLEELAEAAARLLLLLE----AEADYEGFLEGVKAALLLAGLRG 521
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
519-1089 |
6.06e-06 |
|
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: 51.60 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 519 TSLEKHFEVECEEVQGLKEKL-----AEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISELEEKLSTLKQ 593
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLeeaelKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 594 TMRIMEVENQVAVGLeFEFEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTR----DVLRNSKEGHMLSIA-PEQE 668
Cdd:TIGR02168 490 RLDSLERLQENLEGF-SEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGgrlqAVVVENLNAAKKAIAfLKQN 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 669 DIAGDSIC--NKCEELEKLIADLESKKNSCECDQLRLEIVSVRDKLESVESAFnLASSEIIQKATDCERLSKEL------ 740
Cdd:TIGR02168 569 ELGRVTFLplDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYL-LGGVLVVDDLDNALELAKKLrpgyri 647
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 741 -------------------STSQNAFGQLQERyDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASs 801
Cdd:TIGR02168 648 vtldgdlvrpggvitggsaKTNSSILERRREI-EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS- 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 802 AEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSEstvEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESV 881
Cdd:TIGR02168 726 RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI---EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 882 QENDALREEIKQRPTSHVEESMRSSGISSDFDEQKQDINLLH-QFVQLSESVQQIELQHHSGisrlfranQMKLDQSEPG 960
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEeQIEELSEDIESLAAEIEEL--------EELIEELESE 874
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 961 LKLCLESAEYIEEDnrqsdatepiclkgfLKRHRFQIKRLSQEHVDMGEE-KRLLDIISQLEQEIEEKSALMEATEATIN 1039
Cdd:TIGR02168 875 LEALLNERASLEEA---------------LALLRSELEELSEELRELESKrSELRRELEELREKLAQLELRLEGLEVRID 939
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627454 1040 EMREQMTNLESALLE-----KSVIINKVEDYQRQIESLEKQNAEMTMV-------YEELQDR 1089
Cdd:TIGR02168 940 NLQERLSEEYSLTLEeaealENKIEDDEEEARRRLKRLENKIKELGPVnlaaieeYEELKER 1001
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1197-1824 |
7.42e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1197 QAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKPDQIllsSQYDSQIEKLNQLLnaakDELHDVRRIKDDEISA 1276
Cdd:PRK01156 150 QRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKL---KSSNLELENIKKQI----ADDEKSHSITLKEIER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1277 LRMEFllQIETNEKEN---QAKFYAELQETKDRYESNVAELKEKLLQVEETLSsvtvrcqaELEALKSAHKENISQAVEE 1353
Cdd:PRK01156 223 LSIEY--NNAMDDYNNlksALNELSSLEDMKNRYESEIKTAESDLSMELEKNN--------YYKELEERHMKIINDPVYK 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1354 RNNLIVQH---QAEMETIRETLKNKLAEASTQQSKMEdafRAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMI 1430
Cdd:PRK01156 293 NRNYINDYfkyKNDIENKKQILSNIDAEINKYHAIIK---KLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1431 NGGRVMSDTIAELEKTKAEQDLAVNKLTK----DNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIvaSSKKR 1506
Cdd:PRK01156 370 KSIESLKKKIEEYSKNIERMSAFISEILKiqeiDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDEL--SRNME 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1507 IIELEEKC--------DQQVLELDKCRLEKLS-LESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETF 1577
Cdd:PRK01156 448 MLNGQSVCpvcgttlgEEKSNHIINHYNEKKSrLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1578 TFKITDLEEVLKEAQHKVILYDDLVSQHERLKICLAEANelssnlqkkvmslHTELIDSQKGISSRDVEINELREELKAa 1657
Cdd:PRK01156 528 RADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSK-------------RTSWLNALAVISLIDIETNRSRSNEIK- 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1658 mdakatasaeqmtlvTQLKDVEERMANQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGN---EELKEQLRNSQNL 1734
Cdd:PRK01156 594 ---------------KQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKiliEKLRGKIDNYKKQ 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1735 RNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNKSEIYqrhtELTKEVELGRNRIGELTKKCEELCSDLENSDQIRL- 1813
Cdd:PRK01156 659 IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA----RLESTIEILRTRINELSDRINDINETLESMKKIKKa 734
|
650
....*....|...
gi 442627454 1814 --DLQETKEQLKK 1824
Cdd:PRK01156 735 igDLKRLREAFDK 747
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
722-893 |
9.28e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 722 ASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEE----YEQLESRAR 797
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieerREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 798 SA-----------------SSAEF-------QRLQNDNTKFQADIASLNERLEEAQNMLtevqnsESTVEKLRIQNHELT 853
Cdd:COG3883 94 ALyrsggsvsyldvllgseSFSDFldrlsalSKIADADADLLEELKADKAELEAKKAEL------EAKLAELEALKAELE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442627454 854 AKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQ 893
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1289-1846 |
9.97e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.94 E-value: 9.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1289 EKENQAKfYAELQETKDRY---ESNVAELKEKLLQVEETLSSVTVRCQAELEALksahkeniSQAVEERNNLIVQHQaEM 1365
Cdd:pfam01576 4 EEEMQAK-EEELQKVKERQqkaESELKELEKKHQQLCEEKNALQEQLQAETELC--------AEAEEMRARLAARKQ-EL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1366 ETIRETLKNKLAEASTQQSKMEDAfRAEINEVRATLMEQLNQTKEDRDK----------GASKLEEVKKTLE----QMIN 1431
Cdd:pfam01576 74 EEILHELESRLEEEEERSQQLQNE-KKKMQQHIQDLEEQLDEEEAARQKlqlekvtteaKIKKLEEDILLLEdqnsKLSK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1432 GGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDqisfEIEAHIKKLELIVASSKKRIIELE 1511
Cdd:pfam01576 153 ERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQ----ELEKAKRKLEGESTDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1512 EKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEM----------KVLSNRNEKEKCDFETKLETFTfki 1581
Cdd:pfam01576 229 AQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQIselqedleseRAARNKAEKQRRDLGEELEALK--- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1582 TDLEEVLKEAQHKVILYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDS---------------QKGISSRDVE 1646
Cdd:pfam01576 306 TELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEElteqleqakrnkanlEKAKQALESE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1647 INELREELKAAMDAKATASAEQMTLVTQLKDVEER----------MANQAEKFTREAANLKGSINELLLKLNSMQETKDM 1716
Cdd:pfam01576 386 NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARlseserqraeLAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSS 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1717 LESgneelkeQLRNSQNLrnmLDEESKMCISLKEKLVKLEDAKTSLEQQLrdnkSEIYQRHTELTKEVELGRNRIGELTK 1796
Cdd:pfam01576 466 LES-------QLQDTQEL---LQEETRQKLNLSTRLRQLEDERNSLQEQL----EEEEEAKRNVERQLSTLQAQLSDMKK 531
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 442627454 1797 KCEELCSDLENsdqirldLQETKEQLKKTLENNlgwQQKVDEVTRECEKL 1846
Cdd:pfam01576 532 KLEEDAGTLEA-------LEEGKKRLQRELEAL---TQQLEEKAAAYDKL 571
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
506-798 |
1.16e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 506 DKIKKEIQDLQMFTS-LEKHFEVECEEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISEL 584
Cdd:TIGR02169 705 DELSQELSDASRKIGeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 585 EEKLStlkqTMRIMEVENQVAvglefEFEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDvlRNSKEGHMLSIA 664
Cdd:TIGR02169 785 EARLS----HSRIPEIQAELS-----KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ--RIDLKEQIKSIE 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 665 PEQEDIAGD--SICNKCEELEKLIADLESKKNSCECDQLRLE--IVSVRDKLESVESAFNLASSEIIQKATDCERLSKEL 740
Cdd:TIGR02169 854 KEIENLNGKkeELEEELEELEAALRDLESRLGDLKKERDELEaqLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627454 741 STSQNAFGQLQE------RYDALDQQWQAQQAGITTLH-------EKHEHVQEKYQKLQEEYEQLESRARS 798
Cdd:TIGR02169 934 SEIEDPKGEDEEipeeelSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1393-1906 |
1.21e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.40 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1393 EINEVRATLMEQLNQTKEDRDKGASKLEEVKK----------TLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNI 1462
Cdd:TIGR04523 163 DLKKQKEELENELNLLEKEKLNIQKNIDKIKNkllklelllsNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1463 ELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLElivaSSKKRIIELEEKCDQQVLELDKCRLEKL------------S 1530
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE----QNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkelkselkN 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1531 LESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKVILYDDLVSQHERLKI 1610
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLES 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1611 CLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKAtasaEQMTLVTQLKDVEERMANQAEKFT 1690
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS----VKELIIKNLDNTRESLETQLKVLS 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1691 REAANLKgsinelllklNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNK 1770
Cdd:TIGR04523 475 RSINKIK----------QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1771 SEIYQRHTELTKevELGRNRIGELTKKCEELCSDLENSdqirLDLQETKEQLKKTLEnnlgwqQKVDEVTRECEKLRFDM 1850
Cdd:TIGR04523 545 DELNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSL----KKKQEEKQELIDQKE------KEKKDLIKEIEEKEKKI 612
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627454 1851 QSKEvQNESKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEK 1906
Cdd:TIGR04523 613 SSLE-KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK 667
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
530-894 |
1.23e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 530 EEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLR-------ADNEAANSKISELEEKLSTLKQTMRimevEN 602
Cdd:PRK02224 258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLaeaglddADAEAVEARREELEDRDEELRDRLE----EC 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 603 QVAVGlefEFEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNlTRDVLRNSKEghMLSIAPEQEDIAGDSICNKCEEL 682
Cdd:PRK02224 334 RVAAQ---AHNEEAESLREDADDLEERAEELREEAAELESELEE-AREAVEDRRE--EIEELEEEIEELRERFGDAPVDL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 683 EKLIADLESKKNscECDQLRLEIVSVRDKLESVESAfnLASSEIIQKATDCERLSKELSTSQNA--FGQLQERYDALDQQ 760
Cdd:PRK02224 408 GNAEDFLEELRE--ERDELREREAELEATLRTARER--VEEAEALLEAGKCPECGQPVEGSPHVetIEEDRERVEELEAE 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 761 WQAQQAGITTLHEKHEHVqEKYQKLQEEYEQLESRARSASsaefQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSES 840
Cdd:PRK02224 484 LEDLEEEVEEVEERLERA-EDLVEAEDRIERLEERREDLE----ELIAERRETIEEKRERAEELRERAAELEAEAEEKRE 558
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 442627454 841 TVEKLRIQNHELTAKIKELETNFEEMQREYDCLsNQLMESVQENDALREEIKQR 894
Cdd:PRK02224 559 AAAEAEEEAEEAREEVAELNSKLAELKERIESL-ERIRTLLAAIADAEDEIERL 611
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
785-1108 |
1.52e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 50.31 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 785 LQEEYEQLESRARSASSAEFQRL-QNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQNHELTAK--IKELET 861
Cdd:PRK05771 14 LKSYKDEVLEALHELGVVHIEDLkEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEelIKDVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 862 NFEEMQREYDCLSNQLMEsvqendaLREEIKqrptshveesmrssgissdfdEQKQDINLLHQFVQLSESVqqIELQHHS 941
Cdd:PRK05771 94 ELEKIEKEIKELEEEISE-------LENEIK---------------------ELEQEIERLEPWGNFDLDL--SLLLGFK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 942 GISRlfRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIKRLSQEHVDMGEEKRLLDIISQLE 1021
Cdd:PRK05771 144 YVSV--FVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLGFERLELEEEGTPSELIREIK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1022 QEIEEKSALMEATEATINEMREQMTNLESALLEK-SVIINKVEDYQRQIESlekqnaEMTMV---------YEELQDRVT 1091
Cdd:PRK05771 222 EELEEIEKERESLLEELKELAKKYLEELLALYEYlEIELERAEALSKFLKT------DKTFAiegwvpedrVKKLKELID 295
|
330
....*....|....*..
gi 442627454 1092 RESSMSESLLRVPPDED 1108
Cdd:PRK05771 296 KATGGSAYVEFVEPDEE 312
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1501-1703 |
1.93e-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: 49.38 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1501 ASSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLS---NRNEKEKCDFETKLETf 1577
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEaelAELEKEIAELRAELEA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1578 tfKITDLEEVLKEAQH-------KVILYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINEL 1650
Cdd:COG4942 102 --QKEELAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442627454 1651 REELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLKGSINEL 1703
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1403-2122 |
2.20e-05 |
|
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: 49.97 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1403 EQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQD----LAVNKLTKDNIELEKQCSKTQEQLQME 1478
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyllyLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1479 SLTRDQISFEIEAHIKKL----ELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEhsctMEKLQELQA 1554
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKEnkeeEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE----KKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1555 EMKVLSNRNEKEKCDFETKLETFTFKITDLEEV-LKEAQHKVILYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTEL 1633
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLqEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1634 IDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLKgsinELLLKLNSMQET 1713
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK----ETQLVKLQEQLE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1714 KDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLV--KLEDAKTSLEQQLRDNKSEIYQRHTELTKEVELGRNRI 1791
Cdd:pfam02463 488 LLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAhgRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLV 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1792 GELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISECEEL 1871
Cdd:pfam02463 568 RALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESG 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1872 RSTLKSKEASFQSEKEsmDRTISSLLEDKRNLEEKLCSANDIVAKLETEIAALRPRKSLDRNPVPRKSITFESEIRKNRR 1951
Cdd:pfam02463 648 LRKGVSLEEGLAEKSE--VKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1952 ISVHDERRQSYWNDVREFGIMtdpvDNNCNCAELNSKLQDCQRELFIRESQVTALKMELDHHPLKDENAQLTKRVIEEQD 2031
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKID----EEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 2032 KAKVEQKRLKMKLQDLNARINDLTTASAKEPESNQMAQAAKPATVAAQTQTESDLETILEKTNVKYQEAVRMLRYRYHLI 2111
Cdd:pfam02463 802 ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEE 881
|
730
....*....|.
gi 442627454 2112 QELKEKLRQNE 2122
Cdd:pfam02463 882 QKLKDELESKE 892
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1300-1923 |
2.40e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1300 LQETKDRYESNVAELKEKLLQVEETLSsvtvRCQAELEALKSAHKENISQAVEER------NNLIVQHQAEMETIRETLK 1373
Cdd:pfam01576 122 LQLEKVTTEAKIKKLEEDILLLEDQNS----KLSKERKLLEERISEFTSNLAEEEekakslSKLKNKHEAMISDLEERLK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1374 nKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLeqminggrvmsdtiAELEKTKAEQDLA 1453
Cdd:pfam01576 198 -KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL--------------ARLEEETAQKNNA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1454 VNKLTkdniELEKQCSKTQEQLQMESLTRDQ-------ISFEIEAHIKKLELIVASSKKRIiELEEKCDQQVLELDKC-R 1525
Cdd:pfam01576 263 LKKIR----ELEAQISELQEDLESERAARNKaekqrrdLGEELEALKTELEDTLDTTAAQQ-ELRSKREQEVTELKKAlE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1526 LEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKvilYDDLVSQH 1605
Cdd:pfam01576 338 EETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHK---RKKLEGQL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1606 ERLKICLAEANELSSNLQKKVMSLHTELiDSQKGIssrdveINELreELKAAMDAKATASAEqmtlvTQLKDVEERMANQ 1685
Cdd:pfam01576 415 QELQARLSESERQRAELAEKLSKLQSEL-ESVSSL------LNEA--EGKNIKLSKDVSSLE-----SQLQDTQELLQEE 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1686 aekfTREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLrnsQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQ 1765
Cdd:pfam01576 481 ----TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQL---STLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1766 LrDNKSEIYQRHTELTKEVELGRNRigeLTKKCEELCSDLENSDQIRLDLQETKEQLKKTLEnnlgwQQKVDEVTRECEK 1845
Cdd:pfam01576 554 L-EALTQQLEEKAAAYDKLEKTKNR---LQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLA-----EEKAISARYAEER 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1846 LRFDMQSKEvqNESKVQELISECEELRSTLKSKEASFQSEKESMDRTISS----------LLEDKRNLEEKLCSANDIVA 1915
Cdd:pfam01576 625 DRAEAEARE--KETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSkddvgknvheLERSKRALEQQVEEMKTQLE 702
|
....*...
gi 442627454 1916 KLETEIAA 1923
Cdd:pfam01576 703 ELEDELQA 710
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
530-1376 |
3.03e-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: 49.35 E-value: 3.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 530 EEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSkiseleeklstLKQTMRimevenqvavgle 609
Cdd:pfam15921 110 QSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC-----------LKEDML------------- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 610 fefeahkKSSKLRVDDLLSALLEKESTIESLqksldnltRDVLRNSKEGHMLSIApEQEDIAGDSICNKCEELEKLIADL 689
Cdd:pfam15921 166 -------EDSNTQIEQLRKMMLSHEGVLQEI--------RSILVDFEEASGKKIY-EHDSMSTMHFRSLGSAISKILREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 690 ESkknscECDQLRLEIVSVRDKLESVEsafnlasseiiqkatdcerlskelSTSQNAFG-QLQERYDALDQQWQAQQAGI 768
Cdd:pfam15921 230 DT-----EISYLKGRIFPVEDQLEALK------------------------SESQNKIElLLQQHQDRIEQLISEHEVEI 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 769 TTLHEKHEHVQEKYQKLQEEYEQLESRARSASSAEFQRLqndnTKFQADIASLNERLEEAQNMLTEvqNSESTVEKLRIQ 848
Cdd:pfam15921 281 TGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQL----SDLESTVSQLRSELREAKRMYED--KIEELEKQLVLA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 849 NHELTakikELETNFEEMQREYDCLSNQLMESVQENDALREEIKQRPTSHVEESMRSSGISSDFDEQKQDINLLHQFVQL 928
Cdd:pfam15921 355 NSELT----EARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQR 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 929 SESVqqielqhhsgISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKgflkrhrfQIKRLSQEHVDMG 1008
Cdd:pfam15921 431 LEAL----------LKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRK--------VVEELTAKKMTLE 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1009 EEKRlldIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQD 1088
Cdd:pfam15921 493 SSER---TVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQ 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1089 RVTRESSMSESLLR----VPPDEDTLPGCPTSPSRREQEVATLK----TSITELQSQVSDLKaelenhLRQIQLKDGNIA 1160
Cdd:pfam15921 570 QIENMTQLVGQHGRtagaMQVEKAQLEKEINDRRLELQEFKILKdkkdAKIRELEARVSDLE------LEKVKLVNAGSE 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1161 RLQT--DFEEMSERCLSmEVRLAELDEDT-KQKQELLDRQAQKLSDDLCLID---QLQKKNAQL-VEQYHKATESLSLAD 1233
Cdd:pfam15921 644 RLRAvkDIKQERDQLLN-EVKTSRNELNSlSEDYEVLKRNFRNKSEEMETTTnklKMQLKSAQSeLEQTRNTLKSMEGSD 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1234 AKPDQILLSSQydSQIEKlnqllnaakdelhdvrriKDDEISAL--RMEFLLQIETNekENQAKFYAELQETKDRYE-SN 1310
Cdd:pfam15921 723 GHAMKVAMGMQ--KQITA------------------KRGQIDALqsKIQFLEEAMTN--ANKEKHFLKEEKNKLSQElST 780
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627454 1311 VAELKEKLLQVEETLSSVTVRCQAELEALKSAHKENISQAVEERNnlIVQHQaEMETIRETLKNKL 1376
Cdd:pfam15921 781 VATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQD--IIQRQ-EQESVRLKLQHTL 843
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
823-1336 |
3.36e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 823 ERLEEAQNMLTEVQNSESTVEklriqnhELTAKIKELETNFEEMQREYDCLSnqlmESVQENDALREEIKQRPTSHVEES 902
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELE-------TLEAEIEDLRETIAETEREREELA----EEVRDLRERLEELEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 903 MRSSGISSDFDEQKQDinLLHQFVQLSESVQQ--IELQHHSGISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDA 980
Cdd:PRK02224 303 GLDDADAEAVEARREE--LEDRDEELRDRLEEcrVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 981 TEPICLKGFLKRHRFQIKRLSQEHVDMGEEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESA--------L 1052
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqP 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1053 LEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSMSESLLRVPPDEDTLpgcptspSRREQEVATLKTSIT 1132
Cdd:PRK02224 461 VEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERR-------EDLEELIAERRETIE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1133 ELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAqKLSDDLCLIDQLQ 1212
Cdd:PRK02224 534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERLR 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1213 KKNAQLVEQYHKATESLSLADAKPDQiLLSSQYDSQIEKLNQLLNAAKDELHDVrrikDDEISALRMEF-LLQIETNEKE 1291
Cdd:PRK02224 613 EKREALAELNDERRERLAEKRERKRE-LEAEFDEARIEEAREDKERAEEYLEQV----EEKLDELREERdDLQAEIGAVE 687
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 442627454 1292 NQAKFYAELQETKDRYESNVAELkEKLLQVEETLSSVTVRCQAEL 1336
Cdd:PRK02224 688 NELEELEELRERREALENRVEAL-EALYDEAEELESMYGDLRAEL 731
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
780-1415 |
4.17e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.92 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 780 EKYQKLQEEYEQLESRARSASSAEFQRLQNDNTKF-----QADIASLNERLEEAQNMLTEVQNSESTVEKLRIQNHELTA 854
Cdd:COG5022 827 KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFsllkkETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELES 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 855 KIKELetnfeemqreydclSNQLMESVQENDALREEIKQRPTSHVEESMRSSGISSDFDEQKQDINLLHQFVQLSESVQQ 934
Cdd:COG5022 907 EIIEL--------------KKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 935 IEL---QHHSGISRLFRAN-QMKLDQSEPGLKLCLESAeyIEEDNRQSDATEPIclkgfLKRHRFQIKRLSQEHVDMGEE 1010
Cdd:COG5022 973 YEDllkKSTILVREGNKANsELKNFKKELAELSKQYGA--LQESTKQLKELPVE-----VAELQSASKIISSESTELSIL 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1011 KRLLDIISQLEQEIEEKSALMEA-----------------------TEATINEMREQMTNLESALLEKSVIINKVE---- 1063
Cdd:COG5022 1046 KPLQKLKGLLLLENNQLQARYKAlklrrensllddkqlyqlestenLLKTINVKDLEVTNRNLVKPANVLQFIVAQmikl 1125
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1064 DYQRQIESLEKQNAE----MTMVYEELQDRVtressmsESLLRVPPDEDTLPGCP---TSPSRrEQEVATLKTSITELQS 1136
Cdd:COG5022 1126 NLLQEISKFLSQLVNtlepVFQKLSVLQLEL-------DGLFWEANLEALPSPPPfaaLSEKR-LYQSALYDEKSKLSSS 1197
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1137 QVSDLKAELENHLRQIQlKDGNIARLQTDF--EEMSERCLSMEVRLAELDEDTKQKQEllDRQAQKLSDDLCLIDQLQKK 1214
Cdd:COG5022 1198 EVNDLKNELIALFSKIF-SGWPRGDKLKKLisEGWVPTEYSTSLKGFNNLNKKFDTPA--SMSNEKLLSLLNSIDNLLSS 1274
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1215 NAQLVEQYHKateslsladakpdqillssqydsqieKLNQLLNAAKDELHDVRRIKDdeiSALRMEFLLQIETNEKENQA 1294
Cdd:COG5022 1275 YKLEEEVLPA--------------------------TINSLLQYINVGLFNALRTKA---SSLRWKSATEVNYNSEELDD 1325
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1295 KF--------YAELQETKDRyeSNVAELKEK-LLQVEETLSSVTVRCQAELEALKSAHkenisQAVEERNNLIVQHQAEM 1365
Cdd:COG5022 1326 WCrefeisdvDEELEELIQA--VKVLQLLKDdLNKLDELLDACYSLNPAEIQNLKSRY-----DPADKENNLPKEILKKI 1398
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 442627454 1366 ETirETLKNKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRDKG 1415
Cdd:COG5022 1399 EA--LLIKQELQLSLEGKDETEVHLSEIFSEEKSLISLDRNSIYKEEVLS 1446
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
540-1230 |
4.93e-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: 48.81 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 540 AEVTAQRDNLEQESLAEKERY----DALEKEVTSLRADNEAANSKISELEEKLSTLKQTmrimevENQVAVGLEfefeah 615
Cdd:TIGR00618 183 LMEFAKKKSLHGKAELLTLRSqlltLCTPCMPDTYHERKQVLEKELKHLREALQQTQQS------HAYLTQKRE------ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 616 KKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSkegHMLSIAPEQEDIAGdsiCNKceELEKLIADLESKKNS 695
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRAR---KAAPLAAHIKAVTQ---IEQ--QAQRIHTELQSKMRS 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 696 cecdqlRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKElSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKH 775
Cdd:TIGR00618 323 ------RAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA-HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 776 EHVQEKYQKLQEEYEQLESRArSASSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQNHELTAK 855
Cdd:TIGR00618 396 QSLCKELDILQREQATIDTRT-SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 856 IKELEtNFEEMQREYDCLSNQLMESVQENDALREEikqrPTSHVEESMRSSGISSDfdEQKQDINLLHQFVQLSESVQQI 935
Cdd:TIGR00618 475 LQTKE-QIHLQETRKKAVVLARLLELQEEPCPLCG----SCIHPNPARQDIDNPGP--LTRRMQRGEQTYAQLETSEEDV 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 936 ELQHHSGISRLFR-ANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIKRLSQEHVDMGEEKRLL 1014
Cdd:TIGR00618 548 YHQLTSERKQRASlKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1015 DIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRES 1094
Cdd:TIGR00618 628 QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLR 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1095 SMSESLLRVPPD-EDTLPGCPTSPSRREQEVATLKTSITELQSQV-SDLKAELENHLRQIQLKdgnIARLQTDfEEMSER 1172
Cdd:TIGR00618 708 ELETHIEEYDREfNEIENASSSLGSDLAAREDALNQSLKELMHQArTVLKARTEAHFNNNEEV---TAALQTG-AELSHL 783
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627454 1173 CLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLS 1230
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKS 841
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1109-1385 |
6.61e-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: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1109 TLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTK 1188
Cdd:COG3883 3 ALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1189 QKQELLD---RQAQKLSDDLCLIDQLqkknaqlveqyhkaTESLSLADakpdqillssqYDSQIEKLNQLLNAAKDELHD 1265
Cdd:COG3883 83 ERREELGeraRALYRSGGSVSYLDVL--------------LGSESFSD-----------FLDRLSALSKIADADADLLEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1266 VRRIKDdeisalrmefllQIETNEKENQAKFyAELQETKDRYESNVAELKEKllqveetlssvtvrcQAELEALKSAHKE 1345
Cdd:COG3883 138 LKADKA------------ELEAKKAELEAKL-AELEALKAELEAAKAELEAQ---------------QAEQEALLAQLSA 189
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 442627454 1346 NISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQSK 1385
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
704-893 |
8.31e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 704 EIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQ 783
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 784 KLQEEY-EQLESRARSA---------SSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVE----KLRIQN 849
Cdd:COG4942 101 AQKEELaELLRALYRLGrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEaeraELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442627454 850 HELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQ 893
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
507-860 |
1.07e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 507 KIKKEIQDLQMFTSLEKHFEVECEEVQGLKEKLAEVTAQRDNLEQESLAEKerYDALEKEVTSLRADNEAANSKISELEE 586
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKE--LEELEKAKEEIEEEISKITARIGELKK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 587 KLSTLKQTM-RIMEVENQVAVGLEFEFEAHKK----SSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSKEGHML 661
Cdd:PRK03918 420 EIKELKKAIeELKKAKGKCPVCGRELTEEHRKelleEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLK 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 662 SIAPEQEDIAGDSICNKCEELEKLIADLESKKNscECDQLRLEIVSVRDKLESVEsAFNLASSEIIQKATDCERLSKELS 741
Cdd:PRK03918 500 ELAEQLKELEEKLKKYNLEELEKKAEEYEKLKE--KLIKLKGEIKSLKKELEKLE-ELKKKLAELEKKLDELEEELAELL 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 742 TSQNAFG------------QLQERYDA----------LDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSA 799
Cdd:PRK03918 577 KELEELGfesveeleerlkELEPFYNEylelkdaekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627454 800 SSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVqnsESTVEKLRIQNHELTAKIKELE 860
Cdd:PRK03918 657 SEEEYEELREEYLELSRELAGLRAELEELEKRREEI---KKTLEKLKEELEEREKAKKELE 714
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1010-1586 |
1.15e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1010 EKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDR 1089
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1090 VTRESSmsesllrvppdedtlpgcptspsrREQEVATLKTSITELQSQVSDLKAELEN------HLRQIQLKDGNIARLQ 1163
Cdd:PRK03918 244 EKELES------------------------LEGSKRKLEEKIRELEERIEELKKEIEEleekvkELKELKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1164 TDFEEMSERCLSMEVRLAELDEDTKQKQELLdrqaQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSL---ADAKPDQI- 1239
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHELyeeAKAKKEELe 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1240 -LLSSQYDSQIEKLNQLLNA---AKDELHDVRRIKDDEISALRmefllqietNEKENQAKFYAELQETKDR--------Y 1307
Cdd:PRK03918 376 rLKKRLTGLTPEKLEKELEElekAKEEIEEEISKITARIGELK---------KEIKELKKAIEELKKAKGKcpvcgrelT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1308 ESNVAELKEKLLQVEETLSSVTVRCQAELEALKsAHKENISQAVEERNNLIVQHQA--EMETIRETLKNKLAEASTQQSK 1385
Cdd:PRK03918 447 EEHRKELLEEYTAELKRIEKELKEIEEKERKLR-KELRELEKVLKKESELIKLKELaeQLKELEEKLKKYNLEELEKKAE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1386 MEDAFRAEINEVRATL------MEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMS-DTIAELEKTKAEQDLAVNK-L 1457
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIkslkkeLEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEyL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1458 TKDNIELEKQcsKTQEQLQMESLTRDQISFEIEAHIKKLELIvassKKRIIELEEKCDQQvlELDKCRLEKLSLESEIQK 1537
Cdd:PRK03918 606 ELKDAEKELE--REEKELKKLEEELDKAFEELAETEKRLEEL----RKELEELEKKYSEE--EYEELREEYLELSRELAG 677
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 442627454 1538 ANSEHSCTMEKLQELQAEMKVLSNRNEKEKcDFETKLETFTFKITDLEE 1586
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEELEERE-KAKKELEKLEKALERVEE 725
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
530-892 |
1.15e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 47.32 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 530 EEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISELEEKLSTLKQ-TMRIMEVENQVAvgl 608
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKkIQKNKSLESQIS--- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 609 efEFEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSKEGHMLSIAPEQEDIAGDSICNKCEELEKLIAD 688
Cdd:TIGR04523 222 --ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISD 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 689 LESKKNSCECDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTS--------------QNAFGQLQERY 754
Cdd:TIGR04523 300 LNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSesensekqreleekQNEIEKLKKEN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 755 DALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASSaEFQRLQNDNTKFQADIASLNERLEEAQnmlTE 834
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK-EIERLKETIIKNNSEIKDLTNQDSVKE---LI 455
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627454 835 VQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIK 892
Cdd:TIGR04523 456 IKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVK 513
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
710-1172 |
1.19e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 710 DKLESVESAFNLASS---EIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQ--AGITTLHEKHEHVQEKYQK 784
Cdd:COG4717 71 KELKELEEELKEAEEkeeEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 785 LQEEYEQLESRarsassaefqrlqndntkfQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQnheltakikELETNFE 864
Cdd:COG4717 151 LEERLEELREL-------------------EEELEELEAELAELQEELEELLEQLSLATEEELQ---------DLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 865 EMQREYDCLSNQLMESVQENDALREEIKQRPTSHVEEsmrssgissdfdEQKQDINLLHQFVQLSESVQQIELQHHSGIS 944
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAA------------ALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 945 RLFRAnqMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIKRLSQEHvdMGEEKRLLDIISQLEQEI 1024
Cdd:COG4717 271 LILTI--AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL--GLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1025 EEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNaEMTMVYEELQDRVTRESSMSESLLRVP 1104
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627454 1105 PDEDTlpgcptspsrrEQEVATLKTSITELQSQVSDL---KAELENHLRQIQlKDGNIARLQTDFEEMSER 1172
Cdd:COG4717 426 DEEEL-----------EEELEELEEELEELEEELEELreeLAELEAELEQLE-EDGELAELLQELEELKAE 484
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1282-1506 |
1.47e-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: 46.68 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1282 LLQIETNEKENQAKFyAELQETKDRYESNVAELKEKLLQVEETLSSVtvrcQAELEALKSAHKENISQAVEERNNLIVQH 1361
Cdd:COG4942 29 LEQLQQEIAELEKEL-AALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1362 QAEMETIRETLKNKLAEAST---QQSKMEDAFRA-----EINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGg 1433
Cdd:COG4942 104 EELAELLRALYRLGRQPPLAlllSPEDFLDAVRRlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE- 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627454 1434 rvMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQmesltrdqisfEIEAHIKKLELIVASSKKR 1506
Cdd:COG4942 183 --LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE-----------ELEALIARLEAEAAAAAER 242
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
530-864 |
2.22e-04 |
|
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: 46.04 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 530 EEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRIMEVEnqvavgLE 609
Cdd:pfam07888 80 SRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE------LE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 610 fefeahkkSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSKEGHMLSIAPEQEDIAGDSICNKCEELEKLIAdl 689
Cdd:pfam07888 154 --------RMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLT-- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 690 ESKKNSCECDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGI- 768
Cdd:pfam07888 224 TAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWa 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 769 ---TTLHEKHEHVQEKYQKLQEEYEQLESRarsassaeFQRLQNDNTKFQADIA--------SLNERLEEAQNMLTEVQN 837
Cdd:pfam07888 304 qerETLQQSAEADKDRIEKLSAELQRLEER--------LQEERMEREKLEVELGrekdcnrvQLSESRRELQELKASLRV 375
|
330 340
....*....|....*....|....*..
gi 442627454 838 SESTVEKLRIQNHELTAKIKELETNFE 864
Cdd:pfam07888 376 AQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
545-809 |
2.28e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 545 QRDNLEQESLAEKERYDALEKEVTSLRAdneaansKISELEEKLSTLKQTMRIMEVENQVAVGLEfefeahkkssklRVD 624
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRK-------ELEEAEAALEEFRQKNGLVDLSEEAKLLLQ------------QLS 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 625 DLLSALLEKESTIESLQKSLDNLTRDVLRNSKEGHMLSIAPEQediagdsicnkcEELEKLIADLESKKnscecDQLRL- 703
Cdd:COG3206 223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVI------------QQLRAQLAELEAEL-----AELSAr 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 704 ------EIVSVRDKLESVESAFNLASSEIIQKA-TDCERLSKELSTSQNAFGQLQERYDALDQQwQAQQAGIttlhekhe 776
Cdd:COG3206 286 ytpnhpDVIALRAQIAALRAQLQQEAQRILASLeAELEALQAREASLQAQLAQLEARLAELPEL-EAELRRL-------- 356
|
250 260 270
....*....|....*....|....*....|...
gi 442627454 777 hvQEKYQKLQEEYEQLESRARSASSAEFQRLQN 809
Cdd:COG3206 357 --EREVEVARELYESLLQRLEEARLAEALTVGN 387
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
521-803 |
2.71e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 521 LEKHFEVECEEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRimev 600
Cdd:COG1196 300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA---- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 601 enqvavglefEFEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSKEGHMLSIAPEQEDIAGDSICNKCE 680
Cdd:COG1196 376 ----------EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 681 ELEKLIADLESKKNscecdQLRLEIVSVRDKLESVESAFNLASSEIIQKAtdcerlSKELSTSQNAFGQLQERYDALDQQ 760
Cdd:COG1196 446 EAAEEEAELEEEEE-----ALLELLAELLEEAALLEAALAELLEELAEAA------ARLLLLLEAEADYEGFLEGVKAAL 514
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 442627454 761 WQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASSAE 803
Cdd:COG1196 515 LLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
515-1212 |
2.76e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.12 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 515 LQMFTSLEKHFEvecEEVQGLKEKLAEVTAQRDNLEQESLAEKERYDAL--EKEVTSLRADNEAANSKISELEEKLSTLK 592
Cdd:TIGR00618 221 KQVLEKELKHLR---EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRarIEELRAQEAVLEETQERINRARKAAPLAA 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 593 QTMRIMEVENQVAVGLEFEFEAHKKSSKLRVDdlLSALLEKESTIESLQKSLDNLTRDVLRNSkeghmlsIAPEQEDIAG 672
Cdd:TIGR00618 298 HIKAVTQIEQQAQRIHTELQSKMRSRAKLLMK--RAAHVKQQSSIEEQRRLLQTLHSQEIHIR-------DAHEVATSIR 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 673 DSICNKCEELEKLIADLESKKNSCECDQLRLEIVSVRDKLESVESAFNLASSEIIQKATdceRLSKELstsqnafgQLQE 752
Cdd:TIGR00618 369 EISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA---HAKKQQ--------ELQQ 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 753 RYDALDQQWQAQQAGITTLHEKHehVQEKYQKLQEEYEQLesrarsassaefQRLQNDNTKFQADIASLNERLEEAQNML 832
Cdd:TIGR00618 438 RYAELCAAAITCTAQCEKLEKIH--LQESAQSLKEREQQL------------QTKEQIHLQETRKKAVVLARLLELQEEP 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 833 TEVQNSESTVEKLRIQNHELTAKIKELEtnfeEMQREYDCLSNQLMESVQENDALREEIKQRPTSHVEESMRSSGISSDF 912
Cdd:TIGR00618 504 CPLCGSCIHPNPARQDIDNPGPLTRRMQ----RGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 913 DEQKQDINLLHQFVQLSESVQQIELQHHSGISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFLKR 992
Cdd:TIGR00618 580 NRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQER 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 993 HRFQIKRLSQEHVDMGEEKRLLdiISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESL 1072
Cdd:TIGR00618 660 VREHALSIRVLPKELLASRQLA--LQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1073 EKQNAEMTMVYEELQDRVTRESSMSE--SLLRVPPDEDTLpgcpTSPSRREQEVATLKTSITELQSQVSDLKAELENHLR 1150
Cdd:TIGR00618 738 EDALNQSLKELMHQARTVLKARTEAHfnNNEEVTAALQTG----AELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP 813
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627454 1151 --------QIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQ--KLSDDLCLIDQLQ 1212
Cdd:TIGR00618 814 sdedilnlQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKiiQLSDKLNGINQIK 885
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
500-888 |
2.76e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 500 KGPLTTDKIKKEIQDLQMFTSLEKHFEVECEEVQGLKEKLAEVTAQRDNLEQE--SLAEKERYDALEKEVTSLRADNEAA 577
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 578 NSKISELEEKLSTLKQTMRIMEVENQVAVGLEFEFEAHKKSSKL-----------RVDDLLSALLEKESTIESLQKSLDN 646
Cdd:COG4717 145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLateeelqdlaeELEELQQRLAELEEELEEAQEELEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 647 LTRDVLRNSKEGHMLSIAPEQEDI---------------AGDSICNKCEELEKLIA-----------DLESKKNSCECDQ 700
Cdd:COG4717 225 LEEELEQLENELEAAALEERLKEArlllliaaallallgLGGSLLSLILTIAGVLFlvlgllallflLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 701 LRLEIVSVRDKLESVE-----SAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYD--ALDQQWQA--QQAGITTL 771
Cdd:COG4717 305 EELQALPALEELEEEEleellAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQleELEQEIAAllAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 772 HE--KHEHVQEKYQKLQEEYEQLESRARSASSAEFQRLQndntkfQADIASLNERLEEAQnmlTEVQNSESTVEKLRIQN 849
Cdd:COG4717 385 EElrAALEQAEEYQELKEELEELEEQLEELLGELEELLE------ALDEEELEEELEELE---EELEELEEELEELREEL 455
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 442627454 850 HELTAKIKELETN--FEEMQREYDCLSNQLMESVQENDALR 888
Cdd:COG4717 456 AELEAELEQLEEDgeLAELLQELEELKAELRELAEEWAALK 496
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
764-1571 |
2.92e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 764 QQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVE 843
Cdd:PTZ00121 1068 QDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARK 1147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 844 KLRIQNHELTAKIKELEtNFEEMQREYDCLSNQLMESVQENDALREEIKQRPTSHVEESMRSSGISSDFDEQKQDINLLH 923
Cdd:PTZ00121 1148 AEDAKRVEIARKAEDAR-KAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKA 1226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 924 QFVQLSESVQQIELQHHSGISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIKRLSQE 1003
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE 1306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1004 HVDMGEEKRLLDIISQLEQEIEEKSalmeatEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVY 1083
Cdd:PTZ00121 1307 AKKKAEEAKKADEAKKKAEEAKKKA------DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA 1380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1084 EELQDRVTRESSMSEslLRVPPDEDTLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKD-GNIARL 1162
Cdd:PTZ00121 1381 DAAKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKkAEEAKK 1458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1163 QTDFEEMSERCLSMEvRLAELDEDTKQKQELLDR--QAQKLSDDLCLIDQLQKKNAQL--VEQYHKATESLSLADAKPDQ 1238
Cdd:PTZ00121 1459 AEEAKKKAEEAKKAD-EAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEAKKKADEAkkAEEAKKADEAKKAEEAKKAD 1537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1239 ILLSSQYDSQIEKLNQLLNAAKDE----LHDVRRIKDDEISALR-MEFLLQIETNEKENQAKFYAElqetkdryesnvae 1313
Cdd:PTZ00121 1538 EAKKAEEKKKADELKKAEELKKAEekkkAEEAKKAEEDKNMALRkAEEAKKAEEARIEEVMKLYEE-------------- 1603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1314 lkEKLLQVEETLSSVTVRCQAElealksahkeNISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQSKMEDAFRAE 1393
Cdd:PTZ00121 1604 --EKKMKAEEAKKAEEAKIKAE----------ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1394 INEVRAtlmEQLNQTKEDRDKGASKL---EEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDnielEKQCSK 1470
Cdd:PTZ00121 1672 EDKKKA---EEAKKAEEDEKKAAEALkkeAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE----AEEDKK 1744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1471 TQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIE-LEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKL 1549
Cdd:PTZ00121 1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDS 1824
|
810 820
....*....|....*....|....*.
gi 442627454 1550 QELQ----AEMKVLSNRNEKEKCDFE 1571
Cdd:PTZ00121 1825 KEMEdsaiKEVADSKNMQLEEADAFE 1850
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1298-1773 |
4.04e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1298 AELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELE--ALKSAHKENISQAVEERNNLIVQHQAEMETIRETLK-- 1373
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAeaGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQah 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1374 NKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRDKGASKLEEVKK---TLEQMINGGRV----MSDTIAELEKT 1446
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEeieELRERFGDAPVdlgnAEDFLEELREE 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1447 KAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLElivaSSKKRIIELEEkcdqqvlELDKCRL 1526
Cdd:PRK02224 421 RDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIE----EDRERVEELEA-------ELEDLEE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1527 EKLSLESEIQKAnsehsctmEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQ----HKVILYDDLV 1602
Cdd:PRK02224 490 EVEEVEERLERA--------EDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAeleaEAEEKREAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1603 SQHERLKICLAEANELSSNLQKkvmslHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERM 1682
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAE-----LKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERK 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1683 ANQAEKFTREAanlkgsINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSL 1762
Cdd:PRK02224 637 RELEAEFDEAR------IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEAL 710
|
490
....*....|.
gi 442627454 1763 EqQLRDNKSEI 1773
Cdd:PRK02224 711 E-ALYDEAEEL 720
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1717-2182 |
4.11e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1717 LESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRdnKSEIYQRHTELTKEVELGRNRIGELTK 1796
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1797 KCEELCSDLENSDQIRLDLQETKEQLKKTLEN-NLGWQQKVDEVTRECEKLRFDMQSKEV---QNESKVQELISECEELR 1872
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEeleEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1873 STLKSKEASFQSEKESMDRTISSLLEDKRNLEEKLCSANDIVAKLETEIAALRPRKSLDRNPVPRKSITFESEIRKNRRI 1952
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1953 SVHDERRQSYWNDVREFGIMTDPvdnncncaELNSKLQDCQRELFIRESQVTALKMELDHHPLKDENAQLTKRVIEEQDK 2032
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSP--------EELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 2033 AKVEQKRLKMKLQDLNARINDLTtasakepesNQMAQAAKPATVAAQTQTESDLETILEKTNVKYQEAVRMLRYRYHLIQ 2112
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELE---------EQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627454 2113 ELKEKLRQNENSDTsnITSLSAgQTSALKAQCESQKKEILAIKYKYEAAKRIL-AIRNDDLDALREKLAKY 2182
Cdd:COG4717 457 ELEAELEQLEEDGE--LAELLQ-ELEELKAELRELAEEWAALKLALELLEEAReEYREERLPPVLERASEY 524
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1017-1260 |
4.22e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 4.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1017 ISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSViinKVEDYQRQIESLEKQNAEMTMVYEELQDRV-TRESS 1095
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA---ELEALQAEIDKLQAEIAEAEAEIEERREELgERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1096 MSESLLRVPPDEDTLPGcpTSPS---RREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDfeemser 1172
Cdd:COG3883 95 LYRSGGSVSYLDVLLGS--ESFSdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1173 clsMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKL 1252
Cdd:COG3883 166 ---LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
....*...
gi 442627454 1253 NQLLNAAK 1260
Cdd:COG3883 243 AASAAGAG 250
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
751-1092 |
5.63e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 751 QERYDALDQQWQAQQAGITTLHEKHEHVQEKyQKLQEEYEQLESRARSASSAEfqRLQNDNTKFQADIASLNERLEEaQN 830
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAE-SDLEQDYQAASDHLNLVQTAL--RQQEKIERYQADLEELEERLEE-QN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 831 MLTEVQNSESTveklriqnheltakikELETNFEEMQREYDCLSNQLMESVQENDAL-REEIKQRPTSHVEESMRSSGIS 909
Cdd:PRK04863 369 EVVEEADEQQE----------------ENEARAEAAEEEVDELKSQLADYQQALDVQqTRAIQYQQAVQALERAKQLCGL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 910 SDFDEQKQDiNLLHQFVQLSESVQQIELQhhsgISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEpicLKGF 989
Cdd:PRK04863 433 PDLTADNAE-DWLEEFQAKEQEATEELLS----LEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARE---LLRR 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 990 LKRHRFQIKRLSQEHVDMGEEKRLLDIISQLEQ---EIEEKSALMEATEATINEMR-EQMTNLESALLEKSVIINKVEDY 1065
Cdd:PRK04863 505 LREQRHLAEQLQQLRMRLSELEQRLRQQQRAERllaEFCKRLGKNLDDEDELEQLQeELEARLESLSESVSEARERRMAL 584
|
330 340 350
....*....|....*....|....*....|
gi 442627454 1066 QRQIESLEKQNAEMTM---VYEELQDRVTR 1092
Cdd:PRK04863 585 RQQLEQLQARIQRLAArapAWLAAQDALAR 614
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1020-1433 |
5.74e-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: 45.33 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1020 LEQEIEEKSALMEATEATINEMREQMTNLESALLEKsviiNKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRessmses 1099
Cdd:COG3096 311 MARELEELSARESDLEQDYQAASDHLNLVQTALRQQ----EKIERYQEDLEELTERLEEQEEVVEEAAEQLAE------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1100 llrvppdedtlpgCPTSPSRREQEVATLKtsitelqSQVSDLKAEL-ENHLRQIQ----LKDGNIARLQTDFEEMSERcl 1174
Cdd:COG3096 380 -------------AEARLEAAEEEVDSLK-------SQLADYQQALdVQQTRAIQyqqaVQALEKARALCGLPDLTPE-- 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1175 SMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKnAQLVEQYHKATESlSLADAKPDQILlsSQYDSQiEKLNQ 1254
Cdd:COG3096 438 NAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKA-YELVCKIAGEVER-SQAWQTARELL--RRYRSQ-QALAQ 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1255 LLNAAKDELHDVRRIKDDEISALRM--EFLLQI--ETNEKENQAKFYAELQETKDRYESNVAELKEKLLQveetlssvtv 1330
Cdd:COG3096 513 RLQQLRAQLAELEQRLRQQQNAERLleEFCQRIgqQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSE---------- 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1331 rCQAELEALKSAHKENISQAVEERnnlivQHQAEMETIREtlknklaeastqQSKMEDAFRAEINEVRATLMEQLNQTKE 1410
Cdd:COG3096 583 -LRQQLEQLRARIKELAARAPAWL-----AAQDALERLRE------------QSGEALADSQEVTAAMQQLLEREREATV 644
|
410 420
....*....|....*....|...
gi 442627454 1411 DRDKGASKLEEVKKTLEQMINGG 1433
Cdd:COG3096 645 ERDELAARKQALESQIERLSQPG 667
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
530-865 |
5.81e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 5.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 530 EEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRIMEVENQVAVGLE 609
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETI 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 610 FEFEAhkkssklRVDDLLSALLEKESTIESLQKSLDNLTRdvlrnskeghmlsiAPEQEDIAgDSICNKCEELEKLIADl 689
Cdd:PRK02224 471 EEDRE-------RVEELEAELEDLEEEVEEVEERLERAED--------------LVEAEDRI-ERLEERREDLEELIAE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 690 esKKNSCECDQLRLEivSVRDKLESVES----------AFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQ 759
Cdd:PRK02224 528 --RRETIEEKRERAE--ELRERAAELEAeaeekreaaaEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIAD 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 760 QWQAqqagITTLHEKHEHVQEK----YQKLQEEYEQLESRARSASSAEFQRLQNDNTKFQADIASLNERLEEA------- 828
Cdd:PRK02224 604 AEDE----IERLREKREALAELnderRERLAEKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELreerddl 679
|
330 340 350
....*....|....*....|....*....|....*..
gi 442627454 829 QNMLTEVQNSESTVEKLRIQNHELTAKIKELETNFEE 865
Cdd:PRK02224 680 QAEIGAVENELEELEELRERREALENRVEALEALYDE 716
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
699-936 |
6.10e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 6.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 699 DQLRLEIVSVRDKLESVESAfnlaSSEIiqkatdcERLSKELStsqnafgQLQERYDALDQQWQAQQAGITTLHEKHEHV 778
Cdd:COG4913 664 ASAEREIAELEAELERLDAS----SDDL-------AALEEQLE-------ELEAELEELEEELDELKGEIGRLEKELEQA 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 779 QEKYQKLQEEYEQLESRARSASSAEF--QRLQNDNTKFQADI-ASLNERLEEAQnmlTEVQNSESTVEKLRIQ-NHELTA 854
Cdd:COG4913 726 EEELDELQDRLEAAEDLARLELRALLeeRFAAALGDAVERELrENLEERIDALR---ARLNRAEEELERAMRAfNREWPA 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 855 KIKELETNFEEMqREYDCLSNQLmesvqENDAL---REEIKQRPTSHVEESMrsSGISSDFDEQKQDINllHQFVQLSES 931
Cdd:COG4913 803 ETADLDADLESL-PEYLALLDRL-----EEDGLpeyEERFKELLNENSIEFV--ADLLSKLRRAIREIK--ERIDPLNDS 872
|
....*
gi 442627454 932 VQQIE 936
Cdd:COG4913 873 LKRIP 877
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1603-1801 |
6.32e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1603 SQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERM 1682
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1683 ANQAEKFTREAANL--KGSINELLLKLNS-----MQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKL 1755
Cdd:COG4942 100 EAQKEELAELLRALyrLGRQPPLALLLSPedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442627454 1756 EDAKTSLEQQLRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEEL 1801
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1632-1928 |
6.47e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1632 ELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVE-ERmaNQAEKF---TREAANLKGSinELLLKL 1707
Cdd:TIGR02169 157 KIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRrER--EKAERYqalLKEKREYEGY--ELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1708 NSMQETKDMLESGNEELKEQLRNSQNLRNMLDEEskmcisLKEKLVKLEDaktsLEQQLRDNKSEIYQRHTEltkevelg 1787
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKR------LEEIEQLLEE----LNKKIKDLGEEEQLRVKE-------- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1788 rnRIGELTKKCEELCSDLENSDQIRLDLQET----KEQLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQE 1863
Cdd:TIGR02169 295 --KIGELEAEIASLERSIAEKERELEDAEERlaklEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627454 1864 LISECEELRST------LKSKEASFQSEKESMDRTISSLLEDKRNLEEKLCSANDIVAKLETEIAALRPRK 1928
Cdd:TIGR02169 373 LEEVDKEFAETrdelkdYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
778-1738 |
6.55e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.04 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 778 VQEKYQKLQEEyeQLESRARSASSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQNHELTAKIK 857
Cdd:TIGR00606 195 RQTQGQKVQEH--QMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 858 ELETNFEEMQREYDCLSNQLMESVQENDALREEIKQRPTSHVEESMRS-SGISSDFDEQKQDINLLHQfvqlsesvQQIE 936
Cdd:TIGR00606 273 ALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERElVDCQRELEKLNKERRLLNQ--------EKTE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 937 LQHHsgISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFlkrHRFQIKRLSQEhvdmgeekrlLDI 1016
Cdd:TIGR00606 345 LLVE--QGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNF---HTLVIERQEDE----------AKT 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1017 ISQLEQEIEEKSALmeaTEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESlEKQNAEMTMvyeelQDRVTRESSM 1096
Cdd:TIGR00606 410 AAQLCADLQSKERL---KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIK-ELQQLEGSS-----DRILELDQEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1097 SESLLRVPPDEdtlpgcptspsrREQEVATLKTSITELQSQvsdlKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSM 1176
Cdd:TIGR00606 481 RKAERELSKAE------------KNSLTETLKKEVKSLQNE----KADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDK 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1177 EVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQlVEQYHKATESLSLADAKPDQilLSSQYDSQIEKLNQLL 1256
Cdd:TIGR00606 545 MDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKE-INQTRDRLAKLNKELASLEQ--NKNHINNELESKEEQL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1257 NAAKDELHDVRRIKDDEISALRMEfllqietNEKENQAKFYAELQETKDRYESNVAELKEK-----------------LL 1319
Cdd:TIGR00606 622 SSYEDKLFDVCGSQDEESDLERLK-------EEIEKSSKQRAMLAGATAVYSQFITQLTDEnqsccpvcqrvfqteaeLQ 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1320 QVEETLSSVTVRCQAELEALKS------AHKENISQAVEERNNLIVQHQAEMETIRET----------LKNKLAEASTQ- 1382
Cdd:TIGR00606 695 EFISDLQSKLRLAPDKLKSTESelkkkeKRRDEMLGLAPGRQSIIDLKEKEIPELRNKlqkvnrdiqrLKNDIEEQETLl 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1383 QSKMEDAFRAEINEVRATLMEQLNQtkedrdkgasKLEEVKKTLEQMIN--GGRVMSDTIAELEKTKAEQDLAVNKLTKD 1460
Cdd:TIGR00606 775 GTIMPEEESAKVCLTDVTIMERFQM----------ELKDVERKIAQQAAklQGSDLDRTVQQVNQEKQEKQHELDTVVSK 844
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1461 NIELEKQCSKTQEQLQMESLTRDQISFEieahikklELIVASSKKRIIELEEKCDQQVLELDKCRleklsleSEIQKANS 1540
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNELKSE--------KLQIGTNLQRRQQFEEQLVELSTEVQSLI-------REIKDAKE 909
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1541 EHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKVilYDDLVSQHERLKICLAEANELSS 1620
Cdd:TIGR00606 910 QDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKI--QDGKDDYLKQKETELNTVNAQLE 987
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1621 NLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQmTLVTQLKDV-EERMANQAEKFTREAANLKGS 1699
Cdd:TIGR00606 988 ECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEE-ELKQHLKEMgQMQVLQMKQEHQKLEENIDLI 1066
|
970 980 990 1000
....*....|....*....|....*....|....*....|.
gi 442627454 1700 INELLLKLNSMQETKDMLESGNEELKE-QLRNSQ-NLRNML 1738
Cdd:TIGR00606 1067 KRNHVLALGRQKGYEKEIKHFKKELREpQFRDAEeKYREMM 1107
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1455-1691 |
6.62e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1455 NKLTKDNIElekqcsKTQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLESE 1534
Cdd:PHA02562 169 DKLNKDKIR------ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1535 IQKANSEH---SCTMEKLQELQAEMKvlsnrNEKEKCDFETK--------------LETFTFKITDLEEVLKEAQHKvil 1597
Cdd:PHA02562 243 LLNLVMDIedpSAALNKLNTAAAKIK-----SKIEQFQKVIKmyekggvcptctqqISEGPDRITKIKDKLKELQHS--- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1598 YDDLVSQHERLKICLAEANElssnLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKD 1677
Cdd:PHA02562 315 LEKLDTAIDELEEIMDEFNE----QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
250
....*....|....*
gi 442627454 1678 VEERMANQA-EKFTR 1691
Cdd:PHA02562 391 IVKTKSELVkEKYHR 405
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
506-897 |
6.84e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 506 DKIKKEIQDL-QMFTSLEKHFEVECEEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISEL 584
Cdd:TIGR04523 214 KSLESQISELkKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 585 EEKLSTLKqtmrimeveNQVAVGLEFEFEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDvlRNSKEGHMLSIA 664
Cdd:TIGR04523 294 KSEISDLN---------NQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE--LTNSESENSEKQ 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 665 PEQEDiagdsicnKCEELEKLIADLESKKNSCEcdQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQ 744
Cdd:TIGR04523 363 RELEE--------KQNEIEKLKKENQSYKQEIK--NLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 745 NAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASsaefQRLQNDNTKFQADIASLNER 824
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQ----KELKSKEKELKKLNEEKKEL 508
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627454 825 LEEAQNMLTEVQNSESTVEKLRIQNHELTAKIKELETNFEEMqrEYDCLSNQLMESVQENDALREEIKQRPTS 897
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKD--DFELKKENLEKEIDEKNKEIEELKQTQKS 579
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
680-869 |
7.26e-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: 44.37 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 680 EELEKLIADLESKKNSC--ECDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELST--------------- 742
Cdd:COG4942 37 AELEKELAALKKEEKALlkQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAqkeelaellralyrl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 743 ----------SQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLEsRARSASSAEFQRLQNDNT 812
Cdd:COG4942 117 grqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE-ALLAELEEERAALEALKA 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442627454 813 KFQADIASLNERLEEAQNMLTEVQNSEStveklriqnhELTAKIKELETNFEEMQRE 869
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAE----------ELEALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1613-1806 |
7.54e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1613 AEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTRE 1692
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1693 AANLK---GSINELLLKLNSmqetkdmlesgnEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQ---L 1766
Cdd:COG3883 92 ARALYrsgGSVSYLDVLLGS------------ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKlaeL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442627454 1767 RDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLE 1806
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
618-879 |
8.02e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 618 SSKLRVDDLLSAL--LEKEstIESLQKSLDNLTRDvLRNSKEGHMLSIAPEQEDIagdsicnkceeLEKLIADLESKKNs 695
Cdd:COG3206 165 NLELRREEARKALefLEEQ--LPELRKELEEAEAA-LEEFRQKNGLVDLSEEAKL-----------LLQQLSELESQLA- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 696 cecdQLRLEIVSVRDKLESVESAFNLASSEIIQKATDcerlskelstsqNAFGQLQERYDALDQQWQAQQAgitTLHEKH 775
Cdd:COG3206 230 ----EARAELAEAEARLAALRAQLGSGPDALPELLQS------------PVIQQLRAQLAELEAELAELSA---RYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 776 EhvqeKYQKLQEEYEQLESRARSASSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSEstveklriqnheltAK 855
Cdd:COG3206 291 P----DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE--------------AE 352
|
250 260
....*....|....*....|....
gi 442627454 856 IKELETNFEEMQREYDCLSNQLME 879
Cdd:COG3206 353 LRRLEREVEVARELYESLLQRLEE 376
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1748-1948 |
8.06e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1748 LKEKLVKLEDAKTSLE-QQLRDNKSEIYQRHTE---LTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQE------ 1817
Cdd:COG4913 257 IRELAERYAAARERLAeLEYLRAALRLWFAQRRlelLEAELEELRAELARLEAELERLEARLDALREELDELEAqirgng 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1818 --TKEQLKKTLENnlgWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELisecEELRSTLKSKEASFQSEKESMDRTISS 1895
Cdd:COG4913 337 gdRLEQLEREIER---LERELEERERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEELEALEEALAE 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442627454 1896 LLEDKRNLEEKLcsandivAKLETEIAALRPRKSLdrnpVPRKSITFESEIRK 1948
Cdd:COG4913 410 AEAALRDLRREL-------RELEAEIASLERRKSN----IPARLLALRDALAE 451
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1603-1928 |
8.62e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.51 E-value: 8.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1603 SQHERLKICLAEANELSSNLQKKVMSLH----TELIDSQKGISSRDveinELREELKAaMDAKATASAEQMTLVTQLKDV 1678
Cdd:PLN02939 121 DGEQLSDFQLEDLVGMIQNAEKNILLLNqarlQALEDLEKILTEKE----ALQGKINI-LEMRLSETDARIKLAAQEKIH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1679 EERMANQAEKFTRE----AANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNlrnmldeeskmcisLKEKLVK 1754
Cdd:PLN02939 196 VEILEEQLEKLRNEllirGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAE--------------TEERVFK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1755 LEDAKTSLEQQLRDNKSEIYQRHTELTK-----------EVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLK 1823
Cdd:PLN02939 262 LEKERSLLDASLRELESKFIVAQEDVSKlsplqydcwweKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLK 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1824 KTLENNLG------WQQKVDEVtreceKLRFDMQSKEVQNESKV-QELISECEELRSTLKSkeasfQSEKESMDRTISS- 1895
Cdd:PLN02939 342 EANVSKFSsykvelLQQKLKLL-----EERLQASDHEIHSYIQLyQESIKEFQDTLSKLKE-----ESKKRSLEHPADDm 411
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 442627454 1896 ---------LLEDKRNLEEKLcSANDivAKLETEIAALRPRK 1928
Cdd:PLN02939 412 psefwsrilLLIDGWLLEKKI-SNND--AKLLREMVWKRDGR 450
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1701-1925 |
9.63e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 9.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1701 NELLLKLNSMQETKDMLESGNEELKEQLRNSQ----------NLRNMLDEESKMCI-----SLKEKLVKLEDAKTSLEQQ 1765
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLErqaekaerykELKAELRELELALLvlrleELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1766 LRDNKSEIyqrhTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEK 1845
Cdd:TIGR02168 255 LEELTAEL----QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1846 LRFDMQSKEVQNESKVQELISECEELRSTLKSKEASFQSEKESMdrtisslledkRNLEEKLCSANDIVAKLETEIAALR 1925
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-----------EELEEQLETLRSKVAQLELQIASLN 399
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1009-1633 |
9.68e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 9.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1009 EEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESA--LLEKSV--IINKVEDYQRQIESLekqNAEMTMVYE 1084
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKikILEQQIkdLNDKLKKNKDKINKL---NSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1085 EL----QDRVTRESSMSESLLRVPPDEDTLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIA 1160
Cdd:TIGR04523 111 EIkndkEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1161 RLQ----------TDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLS 1230
Cdd:TIGR04523 191 KIKnkllklelllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1231 ladakpDQILLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDDEISALRMEFLLQIEtNEKENQAKFYAELQETKDRYESN 1310
Cdd:TIGR04523 271 ------EKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQE-KKLEEIQNQISQNNKIISQLNEQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1311 VAELKEKLLQVEETLSSVTVRCQAELEALKSAHKENISQaVEERNNLIVQHQAEMETIR--ETLKNKLAEASTQQSKMED 1388
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY-KQEIKNLESQINDLESKIQnqEKLNQQKDEQIKKLQQEKE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1389 AFRAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQC 1468
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1469 SKTQEQLQMESLTRDQISfEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLesEIQKANSEHSCTMEK 1548
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKIS-SLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEID--EKNKEIEELKQTQKS 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1549 LQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKvilyddlvsqHERLKICLAEANELSSNLQKKVMS 1628
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE----------NEKLSSIIKNIKSKKNKLKQEVKQ 649
|
....*
gi 442627454 1629 LHTEL 1633
Cdd:TIGR04523 650 IKETI 654
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1612-1827 |
9.74e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1612 LAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMAN---QAEK 1688
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1689 FTREAANLKGSINELLLKLNSM-QETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQ-- 1765
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAEra 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627454 1766 -LRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLE 1827
Cdd:COG4942 175 eLEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1531-1907 |
1.10e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1531 LESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKVILYDDLVSQHERLKI 1610
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1611 CLAEANELSSNLQKKVMSLHTELIDSQKGISSR----DVEINELREELKAAMDAKATASAEQMTLVTQL----------- 1675
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRvlerETELERMKERAKKAGAQRKEEEAERKQLQAKLqqteeelrsls 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1676 KDVEERMANQAEKFTrEAANLKGSINELLLKLNSMQETkdmlESGNEELKEQLRnsqnlrnmldeeskmciSLKEKLVKL 1755
Cdd:pfam07888 192 KEFQELRNSLAQRDT-QVLQLQDTITTLTQKLTTAHRK----EAENEALLEELR-----------------SLQERLNAS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1756 EDAKTSLEQQLRDNKSEIYQRHTELTK---EVELGRNRIGELTKKC-EELCSDLENSDQIRLDLQETKEQLKKTLENNLG 1831
Cdd:pfam07888 250 ERKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQLADASLALrEGRARWAQERETLQQSAEADKDRIEKLSAELQR 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627454 1832 WQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISECEELRSTLKSkeasFQSEKESMDRTISSLLEDKRNLEEKL 1907
Cdd:pfam07888 330 LEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV----AQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1433-1884 |
1.10e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1433 GRVMSDTIAELEKTKAEQDLAVNKlTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELE- 1511
Cdd:COG4717 63 GRKPELNLKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEl 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1512 EKCDQQVLELDKCRLEKLSLESEIQKANSEHsctMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEA 1591
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAEL---AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1592 QHKVilyDDLVSQHERLKICLAEANELSSNLQKKVMSLhteLIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTL 1671
Cdd:COG4717 219 QEEL---EELEEELEQLENELEAAALEERLKEARLLLL---IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1672 VTQLKDVEERMANQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEK 1751
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1752 LVKLEDAKTSLEQQLRdNKSEIYQRHTELTKEVELGRNRIGELTKKCEELcSDLENSDQIRLDLQETKEQLKKTlennlg 1831
Cdd:COG4717 373 AALLAEAGVEDEEELR-AALEQAEEYQELKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEEL------ 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 442627454 1832 wQQKVDEVTRECEKLRFDMqsKEVQNESKVQELISECEELRSTLKSKEASFQS 1884
Cdd:COG4717 445 -EEELEELREELAELEAEL--EQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1257-1585 |
1.10e-03 |
|
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: 44.18 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1257 NAAKDELHDVRRIKDDEISALRMEFLLQIETNEKENQAKFYAELQETKDRYESNV---AELKEKLLQVEETLSSVTVRCQ 1333
Cdd:COG5185 205 NSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVeqnTDLRLEKLGENAESSKRLNENA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1334 AELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRD 1413
Cdd:COG5185 285 NNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1414 --KGASKLEEVKKTLEQminggrvMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQlQMESLTRD--QISFEI 1489
Cdd:COG5185 365 niVGEVELSKSSEELDS-------FKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADR-QIEELQRQieQATSSN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1490 EAHIKKLELIVASSKKRIIELEEKCDQQVLEldKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCD 1569
Cdd:COG5185 437 EEVSKLLNELISELNKVMREADEESQSRLEE--AYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEG 514
|
330
....*....|....*.
gi 442627454 1570 FETKLETFTFKITDLE 1585
Cdd:COG5185 515 VRSKLDQVAESLKDFM 530
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
510-920 |
1.20e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 510 KEIQDLQMFTSLEKHFEVECEEVQGLKEKLAEVTAQRDnleqESLAEKERYDALEKEVTSLRADNEAANSKISELEEKLS 589
Cdd:PRK01156 302 KYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYN----DYIKKKSRYDDLNNQILELEGYEMDYNSYLKSIESLKK 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 590 TLKQTMRIMEVENQVAVGLEFEFEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSKEGHMLSiapeqed 669
Cdd:PRK01156 378 KIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLN------- 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 670 iaGDSICNKC------EELEKLIADLESKKNSCECDQlrleivsvrDKLESVESAFNlasSEIIQKATDCERLSKELSts 743
Cdd:PRK01156 451 --GQSVCPVCgttlgeEKSNHIINHYNEKKSRLEEKI---------REIEIEVKDID---EKIVDLKKRKEYLESEEI-- 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 744 qnafgqlqERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKlqeeYEQLESRARSASSAEFQRLQNDNTKFQADIASLne 823
Cdd:PRK01156 515 --------NKSINEYNKIESARADLEDIKIKINELKDKHDK----YEEIKNRYKSLKLEDLDSKRTSWLNALAVISLI-- 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 824 rleeaqnmltEVQNSESTVEKLRIQNHELTAKIKELETNFE-----------EMQREYDCLSNQLMEsVQENDALREEIK 892
Cdd:PRK01156 581 ----------DIETNRSRSNEIKKQLNDLESRLQEIEIGFPddksyidksirEIENEANNLNNKYNE-IQENKILIEKLR 649
|
410 420
....*....|....*....|....*...
gi 442627454 893 QRPTSHVEESMRSSGISSDFDEQKQDIN 920
Cdd:PRK01156 650 GKIDNYKKQIAEIDSIIPDLKEITSRIN 677
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1646-1887 |
1.32e-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: 43.60 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1646 EINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEK---FTREAANLKGSINELLLKLNSMQETkdmLESGNE 1722
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAE---LEAQKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1723 ELKEQLRNSQnlRNMLDEESKMCISlkeklvkledaktsleqqlRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELc 1802
Cdd:COG4942 105 ELAELLRALY--RLGRQPPLALLLS-------------------PEDFLDAVRRLQYLKYLAPARREQAEELRADLAEL- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1803 sdlensDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISECEELRSTLKSKEASF 1882
Cdd:COG4942 163 ------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
....*
gi 442627454 1883 QSEKE 1887
Cdd:COG4942 237 AAAAE 241
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1033-1555 |
1.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1033 ATEATINEMREQMTNLESALLEksviinkVEDYQRQIESLEKQNAEmtmvYEELQDRVTRESSMSESLLRVPP--DEDTL 1110
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEA-------LEDAREQIELLEPIREL----AERYAAARERLAELEYLRAALRLwfAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1111 PGCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNiarlqtdfeemserclsmevRLAELDEDTKQK 1190
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD--------------------RLEQLEREIERL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1191 QELLDRQAQKLsddlclidqlqkknaqlvEQYHKATESLSLADAKPDQIL---------LSSQYDSQIEKLNQLLNAAKD 1261
Cdd:COG4913 351 ERELEERERRR------------------ARLEALLAALGLPLPASAEEFaalraeaaaLLEALEEELEALEEALAEAEA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1262 ELHDVRR---IKDDEISALR----------MEFLLQI--ETNEKENQAKFYAELQETK---------------------- 1304
Cdd:COG4913 413 ALRDLRRelrELEAEIASLErrksniparlLALRDALaeALGLDEAELPFVGELIEVRpeeerwrgaiervlggfaltll 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1305 --DRYESNVAE------LKEKL--LQVEETLSSVT---------------------------------VRCQAELEALK- 1340
Cdd:COG4913 493 vpPEHYAAALRwvnrlhLRGRLvyERVRTGLPDPErprldpdslagkldfkphpfrawleaelgrrfdYVCVDSPEELRr 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1341 ---------------SAHKENISQAVEERNNLIVQHQAEMETIRE---TLKNKLAEASTQQSKMEDAfRAEINEVRATLM 1402
Cdd:COG4913 573 hpraitragqvkgngTRHEKDDRRRIRSRYVLGFDNRAKLAALEAelaELEEELAEAEERLEALEAE-LDALQERREALQ 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1403 EQLNQTKEDRDKGA--SKLEEVKKTLEQMINGgrvmSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQmesl 1480
Cdd:COG4913 652 RLAEYSWDEIDVASaeREIAELEAELERLDAS----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE---- 723
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627454 1481 trdQISFEIEAHIKKLElivASSKKRIIELEEKCDQQVLELDKCRLEK---LSLESEIQKANSEHSCTMEKLQELQAE 1555
Cdd:COG4913 724 ---QAEEELDELQDRLE---AAEDLARLELRALLEERFAAALGDAVERelrENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
826-1366 |
1.39e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 826 EEAQNMLTEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLME----------SVQENDALREEI--KQ 893
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPElreeleklekEVKELEELKEEIeeLE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 894 RPTSHVEESMRS-----SGISSDFDEQKQDINLLHQFVQLSESVQQIELQHhsgisrlfranqmkldqsepgLKLCLESA 968
Cdd:PRK03918 245 KELESLEGSKRKleekiRELEERIEELKKEIEELEEKVKELKELKEKAEEY---------------------IKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 969 EYIEEDNRqsdatepicLKGFLKRHRFQIKRLSQEHVDMGEEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNL 1048
Cdd:PRK03918 304 EYLDELRE---------IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1049 ESalLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRV----TRESSMSESLLRVPPDEDTLPGC--PTSPSRREQ 1122
Cdd:PRK03918 375 ER--LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIgelkKEIKELKKAIEELKKAKGKCPVCgrELTEEHRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1123 -------EVATLKTSITELQSQVSDLKAELENhLRQIQLKDGNIARLQTDFEEMSERCLSME-VRLAELDEDTKQKQELL 1194
Cdd:PRK03918 453 lleeytaELKRIEKELKEIEEKERKLRKELRE-LEKVLKKESELIKLKELAEQLKELEEKLKkYNLEELEKKAEEYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1195 DR------QAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKPDQILLSSQYD-----SQIEKLNQLLNAAKDEL 1263
Cdd:PRK03918 532 EKliklkgEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEleerlKELEPFYNEYLELKDAE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1264 HDVRRIKdDEISALRMEFLLQIETNEKENQA--KFYAELQETKDRY-ESNVAELKEKLLQVEETLSSVTvrcqAELEALK 1340
Cdd:PRK03918 612 KELEREE-KELKKLEEELDKAFEELAETEKRleELRKELEELEKKYsEEEYEELREEYLELSRELAGLR----AELEELE 686
|
570 580
....*....|....*....|....*.
gi 442627454 1341 SAHKENISQAVEERNNLIVQHQAEME 1366
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1046-1262 |
1.59e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1046 TNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTressmsesllrvppdedtlpgcptspsRREQEVA 1125
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE---------------------------ALQAEID 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1126 TLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQ-----TDFEEMSERCLSMEV---RLAELDEDTKQKQELLDRQ 1197
Cdd:COG3883 69 KLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDvllgsESFSDFLDRLSALSKiadADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442627454 1198 AQKLSDDLcliDQLQKKNAQLVEQYHKATESLSLADAKPDQilLSSQYDSQIEKLNQLLNAAKDE 1262
Cdd:COG3883 149 KAELEAKL---AELEALKAELEAAKAELEAQQAEQEALLAQ--LSAEEAAAEAQLAELEAELAAA 208
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1017-1201 |
1.61e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1017 ISQLEQEIEEKSALMEATEATINEMREQmTNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSM 1096
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEEFRQK-NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1097 SESLLRVPPDEDTLpgcpTSPSRREQEVATLKT-------SITELQSQVSDLKAELENHLRQIQLK--------DGNIAR 1161
Cdd:COG3206 256 LPELLQSPVIQQLR----AQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASleaelealQAREAS 331
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442627454 1162 LQTDFEEMSERCLSM---EVRLAELDEDTKQKQELLDRQAQKL 1201
Cdd:COG3206 332 LQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRL 374
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
526-924 |
2.35e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 526 EVECEEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRIMEVENQVA 605
Cdd:PRK03918 227 EKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 606 VGL-EFEFEAHKKSSKLR-VDDLLSALLEKESTIESLQKSLDNLTRDVLRnSKEGHML--SIAPEQEDIAGDSICNKCEE 681
Cdd:PRK03918 307 DELrEIEKRLSRLEEEINgIEERIKELEEKEERLEELKKKLKELEKRLEE-LEERHELyeEAKAKKEELERLKKRLTGLT 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 682 LEKLIADLES-KKNSCECDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDC-----------------------ERLS 737
Cdd:PRK03918 386 PEKLEKELEElEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelteehrkelleeytaelKRIE 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 738 KELSTSQNAFGQLQERYDALDQQwQAQQAGITTLHEKHEHVQEKYQKLQE-EYEQLESRARsassaEFQRLQNDNTKFQA 816
Cdd:PRK03918 466 KELKEIEEKERKLRKELRELEKV-LKKESELIKLKELAEQLKELEEKLKKyNLEELEKKAE-----EYEKLKEKLIKLKG 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 817 DIASLNERLEEAQNMLTEVQNSESTVEKLRIQNHELTAKIKELE-TNFEEMQREYDCLS------NQLMESVQENDALRE 889
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEpfyneyLELKDAEKELEREEK 619
|
410 420 430
....*....|....*....|....*....|....*
gi 442627454 890 EIKQRPTSHVEESMRSSGISSDFDEQKQDINLLHQ 924
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
502-1412 |
3.36e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 502 PLTTDK-IKKEIQDLQMFTSLEKHFEVECEEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSK 580
Cdd:TIGR00606 164 PLSEGKaLKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSY 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 581 ISELEEklstLKQTMRIMEvenqvavglefefeaHKKSSKLRVDDLLSALLEKESTIESLQKSLDNL-------TRDVLR 653
Cdd:TIGR00606 244 ENELDP----LKNRLKEIE---------------HNLSKIMKLDNEIKALKSRKKQMEKDNSELELKmekvfqgTDEQLN 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 654 NSKEGHMLSIAPEQEDIAgdSICNKCEELEKLIADLESKKNSCECDQLRLEIVSVRDKLESvesafnlasseiiqKATDC 733
Cdd:TIGR00606 305 DLYHNHQRTVREKERELV--DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHI--------------RARDS 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 734 ERLSKELSTSQNAFgqlqERYDALDQQWQAqqaGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASSAEFQRLQNDNTK 813
Cdd:TIGR00606 369 LIQSLATRLELDGF----ERGPFSERQIKN---FHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRT 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 814 FQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQNHELTAKIKEL-----ETNFEEMQREYDCLSNQLMESVQENDALR 888
Cdd:TIGR00606 442 IELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELskaekNSLTETLKKEVKSLQNEKADLDRKLRKLD 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 889 EEIKQ--RPTSHVEESMRSSGISSDFDEQKQDINLLHQFV------------QLSESVQQIELQHHSGISRLFRANQ--M 952
Cdd:TIGR00606 522 QEMEQlnHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDEltsllgyfpnkkQLEDWLHSKSKEINQTRDRLAKLNKelA 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 953 KLDQSEPGLKLCLESAEyiEEDNRQSDATEPIC----LKGFLKRHRFQIKRLSQEHVDMGEEKRLLD-IISQLEQEIEEK 1027
Cdd:TIGR00606 602 SLEQNKNHINNELESKE--EQLSSYEDKLFDVCgsqdEESDLERLKEEIEKSSKQRAMLAGATAVYSqFITQLTDENQSC 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1028 SALMEATEATINEMREQMTNLESALLeksVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTREssmsesllrvppdE 1107
Cdd:TIGR00606 680 CPVCQRVFQTEAELQEFISDLQSKLR---LAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK-------------E 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1108 DTLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAELENhLRQIQLKDGNIARLQTDFEEMSERCLSMEVRL------- 1180
Cdd:TIGR00606 744 KEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEES-AKVCLTDVTIMERFQMELKDVERKIAQQAAKLqgsdldr 822
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1181 --AELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHK-ATESLSLADAKPDQILLSSQYDSQIEKLNQLLN 1257
Cdd:TIGR00606 823 tvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIR 902
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1258 AAKDelhdvrriKDDEISALRMEFLLQIETNEKENQAKfyaelQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELE 1337
Cdd:TIGR00606 903 EIKD--------AKEQDSPLETFLEKDQQEKEELISSK-----ETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKD 969
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1338 ALKSaHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQSKMEDAF-----RAEINEVRATLMEQLNQTKEDR 1412
Cdd:TIGR00606 970 DYLK-QKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLtlrkrENELKEVEEELKQHLKEMGQMQ 1048
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1290-1556 |
3.45e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1290 KENQAKFYAELQETKDRYESNVAELKEKLLQVEetlssvtvrcqAELEALKSAHKeniSQAVEERNNLIVQHQAEMETIR 1369
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAE-----------AALEEFRQKNG---LVDLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1370 ETLKNKLAEASTQQskmeDAFRAEINEVRATLMEQLNQTkedrdkgaskleevkktleqminggrVMSDTIAELEKTKAE 1449
Cdd:COG3206 229 AEARAELAEAEARL----AALRAQLGSGPDALPELLQSP--------------------------VIQQLRAQLAELEAE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1450 QDLAVNKLTKDN---IELEKQCSKTQEQLQMESltrDQISFEIEAHIKKLELIVASSKKRIIELEekcdQQVLELDKCRL 1526
Cdd:COG3206 279 LAELSARYTPNHpdvIALRAQIAALRAQLQQEA---QRILASLEAELEALQAREASLQAQLAQLE----ARLAELPELEA 351
|
250 260 270
....*....|....*....|....*....|
gi 442627454 1527 EKLSLESEIQKANSEHSCTMEKLQELQAEM 1556
Cdd:COG3206 352 ELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
530-907 |
3.74e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 530 EEVQGLKEKLAEVTAQRDNLE-------------QESLAEKERYDALEKEVTSLRADNEAANSKIS-------ELEEKLS 589
Cdd:pfam10174 178 EEDWERTRRIAEAEMQLGHLEvlldqkekenihlREELHRRNQLQPDPAKTKALQTVIEMKDTKISslernirDLEDEVQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 590 TLKQTMRIMEVENQVAVGLEFEFEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTR---------DVLRNSKEGHM 660
Cdd:pfam10174 258 MLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNqnsdckqhiEVLKESLTAKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 661 LSIAPEQEDIagDSICNKCEELEKLIADLESK--KNSCECDQLRLEIVSVRDKLESVESAFNLASSEIiqkatdcERLSK 738
Cdd:pfam10174 338 QRAAILQTEV--DALRLRLEEKESFLNKKTKQlqDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKI-------ENLQE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 739 ELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEqLESRARSASSAEFQRlQNDNTKFQADi 818
Cdd:pfam10174 409 QLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQRE-REDRERLEELESLKK-ENKDLKEKVS- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 819 aSLNERLEEAQNMLTEVQNSESTvekLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALR--EEI----- 891
Cdd:pfam10174 486 -ALQPELTEKESSLIDLKEHASS---LASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnPEIndrir 561
|
410
....*....|....*...
gi 442627454 892 --KQRPTSHVEESMRSSG 907
Cdd:pfam10174 562 llEQEVARYKEESGKAQA 579
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
557-935 |
3.94e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 557 KERYDALEKEVTSLRADNEAANSKISELEEKLSTLKQtmrIMEVENQVAvglEFEFEahkkssKLRVDDLLSALLEKEST 636
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQE---RREALQRLA---EYSWD------EIDVASAEREIAELEAE 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 637 IESLQKSLDNLtrdvlrnskeghmlsiapeqediagdsicnkcEELEKLIADLESKKnscecDQLRLEIVSVRDKLESVE 716
Cdd:COG4913 677 LERLDASSDDL--------------------------------AALEEQLEELEAEL-----EELEEELDELKGEIGRLE 719
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 717 SAFNLASSEIIQKATDCERLSKELSTSQNAfgQLQERYDALDQQwqaqqagittlhekhEHVQEKYQKLQEEYEQLESRA 796
Cdd:COG4913 720 KELEQAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGD---------------AVERELRENLEERIDALRARL 782
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 797 RSASSaEFQRLQND-NTKFQADIASLN---ERLEEAQNMLTEVQNSEstvekLriqnHELTAKIKELETNFEEMQREYdc 872
Cdd:COG4913 783 NRAEE-ELERAMRAfNREWPAETADLDadlESLPEYLALLDRLEEDG-----L----PEYEERFKELLNENSIEFVAD-- 850
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 873 LSNQLMESVQE--------NDALRE-----------EIKQRPTSHV----EESMRSSGISSDFDEQKQDinllHQFVQLS 929
Cdd:COG4913 851 LLSKLRRAIREikeridplNDSLKRipfgpgrylrlEARPRPDPEVrefrQELRAVTSGASLFDEELSE----ARFAALK 926
|
....*.
gi 442627454 930 ESVQQI 935
Cdd:COG4913 927 RLIERL 932
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1339-1497 |
3.94e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1339 LKSAHKENISQAVEERNNLIVQHQAEMETIRetlKNKLAEASTQQSKMEDAFRAEINEVRATLM----------EQLNQT 1408
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIK---KEALLEAKEEIHKLRNEFEKELRERRNELQklekrllqkeENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1409 KEDRDKGASKLEEVKKTLEQMINggrvmsdtiaELEKTKAEQDLAVNKLTKdniELEKQCSKTQE---QLQMESLtRDQI 1485
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQ----------ELEKKEEELEELIEEQLQ---ELERISGLTAEeakEILLEKV-EEEA 167
|
170
....*....|..
gi 442627454 1486 SFEIEAHIKKLE 1497
Cdd:PRK12704 168 RHEAAVLIKEIE 179
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
666-880 |
4.35e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 666 EQEDIAGDSICNKCEELEKLIAdlESKKNSCECDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELStsqn 745
Cdd:PHA02562 206 EQRKKNGENIARKQNKYDELVE--EAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIK---- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 746 aFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSAS--SAEFQRLQNDNTKFQADIASLNE 823
Cdd:PHA02562 280 -MYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNeqSKKLLELKNKISTNKQSLITLVD 358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627454 824 RLEEAQNMLTEVQ----NSESTVEKLriqNHELTAKIKELeTNFEEMQREYDCLSNQLMES 880
Cdd:PHA02562 359 KAKKVKAAIEELQaefvDNAEELAKL---QDELDKIVKTK-SELVKEKYHRGIVTDLLKDS 415
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
519-802 |
4.51e-03 |
|
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: 42.35 E-value: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 519 TSLEKHFEVECEEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRIM 598
Cdd:TIGR02168 757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT 836
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 599 EVENQVAVGLEFEFEAHKKSSKLRVDDLLSALLEKESTIESLQKsldnltrdvLRNSKEGHMLSIAPEQediagdsicnk 678
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN---------ERASLEEALALLRSEL----------- 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 679 cEELEKLIADLESKKnscecDQLRLEIVSVRDKLESVESAFNLASSEIIQKAtdcERLSKELSTSQNAFGQLQERYDALD 758
Cdd:TIGR02168 897 -EELSEELRELESKR-----SELRRELEELREKLAQLELRLEGLEVRIDNLQ---ERLSEEYSLTLEEAEALENKIEDDE 967
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 442627454 759 QQWQAQ----QAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASSA 802
Cdd:TIGR02168 968 EEARRRlkrlENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEA 1015
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1283-1697 |
5.68e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 5.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1283 LQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQA-ELEALKSAHKENISQAVEERNNLivqh 1361
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERLEEL---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1362 QAEMETIREtLKNKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQminggrvmsdtiA 1441
Cdd:COG4717 152 EERLEELRE-LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE------------A 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1442 ELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMES-----------------------LTRDQISFEIEAHIKKLEL 1498
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllsliltiagvlFLVLGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1499 IVASSKKRIIELEEKCDQQVLELDKcRLEKLSLESEIQKAN-SEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETF 1577
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEE-LLAALGLPPDLSPEElLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1578 TFKITDLEEVLKEAQHKVIlYDDLVSQHERLKICLAEANELSSNLQKKVM--SLHTELIDSQKGISSRDVEINELREELK 1655
Cdd:COG4717 378 EAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 442627454 1656 AAmdAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLK 1697
Cdd:COG4717 457 EL--EAELEQLEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
530-730 |
5.85e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 5.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 530 EEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISELEEKLST----LKQTMRIMEVENQVA 605
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreeLGERARALYRSGGSV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 606 VGLEFEFEAhkKSsklrVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSKEGHMLSIAPEQEDIAGDSICNKCEELEKL 685
Cdd:COG3883 103 SYLDVLLGS--ES----FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442627454 686 IADLESKKNscecdQLRLEIVSVRDKLESVESAFNLASSEIIQKA 730
Cdd:COG3883 177 QAEQEALLA-----QLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1308-1476 |
7.01e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 7.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1308 ESNVAELKEKLLQVEETLSSVtvrcQAELEALKSAH---KENISQAVEERNNL---IVQHQAEMETIRETLKNKLAEAST 1381
Cdd:COG3883 22 QKELSELQAELEAAQAELDAL----QAELEELNEEYnelQAELEALQAEIDKLqaeIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1382 Q-----------QSKMEDAF--RAE-INEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTK 1447
Cdd:COG3883 98 SggsvsyldvllGSESFSDFldRLSaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180
....*....|....*....|....*....
gi 442627454 1448 AEQDLAVNKLTKDNIELEKQCSKTQEQLQ 1476
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1328-1730 |
7.12e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1328 VTVRCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQ-----QSKMEDAFRAEINEVRATLm 1402
Cdd:PLN02939 31 LAVSCRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMElpqksTSSDDDHNRASMQRDEAIA- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1403 eqlNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQmESLTR 1482
Cdd:PLN02939 110 ---AIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLS-ETDAR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1483 DQISFEIEAHIKKLELIVASSKKRII---ELEEKCDQQ-VLELDKCRLEKLSLESEIQKANSEhsctMEKLQELQAEMKV 1558
Cdd:PLN02939 186 IKLAAQEKIHVEILEEQLEKLRNELLirgATEGLCVHSlSKELDVLKEENMLLKDDIQFLKAE----LIEVAETEERVFK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1559 LsnrnEKEKCDFETKLETFTFK-ITDLEEVLKEAQHKvilYDDLVSQHERLKICLAEAnelSSNLQKKVMSL--HTELID 1635
Cdd:PLN02939 262 L----EKERSLLDASLRELESKfIVAQEDVSKLSPLQ---YDCWWEKVENLQDLLDRA---TNQVEKAALVLdqNQDLRD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1636 sqkgissrdvEINELREELKAAMDAKatASAEQMTLVTQ-LKDVEERM-ANQAEKFTreaanlkgsinELLLKLNSMQET 1713
Cdd:PLN02939 332 ----------KVDKLEASLKEANVSK--FSSYKVELLQQkLKLLEERLqASDHEIHS-----------YIQLYQESIKEF 388
|
410
....*....|....*..
gi 442627454 1714 KDMLESGNEELKEQLRN 1730
Cdd:PLN02939 389 QDTLSKLKEESKKRSLE 405
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
530-828 |
7.73e-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: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 530 EEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEK--EVTSLRADNEAANSKISELEEKLSTLKQTmrimeveNQVAVG 607
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDAS-------SDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 608 LEFEFEAHKKssklRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNskeghmlsiAPEQEDIAGDSICNKCEELEKLIA 687
Cdd:COG4913 690 LEEQLEELEA----ELEELEEELDELKGEIGRLEKELEQAEEELDEL---------QDRLEAAEDLARLELRALLEERFA 756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 688 DLESKKNScecDQLRLEIvsvRDKLESVESAFNLASSEIIqkatdcerlskelstsqNAFGQLQERYDALDQQWQAQQAG 767
Cdd:COG4913 757 AALGDAVE---RELRENL---EERIDALRARLNRAEEELE-----------------RAMRAFNREWPAETADLDADLES 813
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442627454 768 IttlhekhEHVQEKYQKLQE----EYEQlesrarsassaEFQRLQNDNTkfQADIASLNERLEEA 828
Cdd:COG4913 814 L-------PEYLALLDRLEEdglpEYEE-----------RFKELLNENS--IEFVADLLSKLRRA 858
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
530-1090 |
8.33e-03 |
|
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: 41.16 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 530 EEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRIMEVE----NQVA 605
Cdd:TIGR04523 40 KKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEikndKEQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 606 VGLEFEF---EAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSKEGHMLS--IAPEQEDIagDSICNKCE 680
Cdd:TIGR04523 120 NKLEVELnklEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEkeKLNIQKNI--DKIKNKLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 681 ELEKLIADLESKKNscecdqlrlEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQ 760
Cdd:TIGR04523 198 KLELLLSNLKKKIQ---------KNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQ 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 761 WQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESrarsassaefQRLQNDNTKFQADIASLNERLEEAQNMLTevqNSES 840
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQLKSEISDLNN----------QKEQDWNKELKSELKNQEKKLEEIQNQIS---QNNK 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 841 TVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQRPTShveesmrSSGISSDFDEQKQDIN 920
Cdd:TIGR04523 336 IISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ-------INDLESKIQNQEKLNQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 921 LLHQFVQLSESVQQIELQHHSGIS--RLFRANQMK-LDQSEPGLKLCLESAE-YIEEDNRQSDATEPIC--LKGFLKRHR 994
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKetIIKNNSEIKdLTNQDSVKELIIKNLDnTRESLETQLKVLSRSInkIKQNLEQKQ 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 995 FQIKRLSQEHVDMGEEKRLLD-IISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINK------VEDYQR 1067
Cdd:TIGR04523 489 KELKSKEKELKKLNEEKKELEeKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekeIDEKNK 568
|
570 580
....*....|....*....|...
gi 442627454 1068 QIESLEKQNAEMTMVYEELQDRV 1090
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELI 591
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1619-1906 |
8.46e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.56 E-value: 8.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1619 SSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAaMDAKATASaeqmtlvtqlkdVEERMANQAEKFTREAANLKG 1698
Cdd:pfam15905 68 NLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEK-VEAKLNAA------------VREKTSLSASVASLEKQLLEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1699 S-INELLLKLNSMQETKDMLESGNEELKEqlrnsqnLRNMLDEESKMCISLKEKL-VKLEDAKTSLEQ------QLRDNK 1770
Cdd:pfam15905 135 TrVNELLKAKFSEDGTQKKMSSLSMELMK-------LRNKLEAKMKEVMAKQEGMeGKLQVTQKNLEHskgkvaQLEEKL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1771 SEIYQRHTELTKEVElgrnrigELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRFDM 1850
Cdd:pfam15905 208 VSTEKEKIEEKSETE-------KLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDL 280
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627454 1851 qskevqnESKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEK 1906
Cdd:pfam15905 281 -------NEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1747-1927 |
9.38e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1747 SLKEKLVKLEDAKTSLEQQLRDNKSE---IYQRHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLK 1823
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEekaLLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1824 KTLENNLGWQQKVDEVTRecekLRFDMQSKEVQNESKV-----------QELISECEELRSTLKSKEASFQSEKESMDRT 1892
Cdd:COG4942 104 EELAELLRALYRLGRQPP----LALLLSPEDFLDAVRRlqylkylaparREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190
....*....|....*....|....*....|....*
gi 442627454 1893 ISSLLEDKRNLEEKLCSANDIVAKLETEIAALRPR 1927
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1176-1413 |
9.39e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1176 MEVRLAELDEDTKQKQELLDRQAQKLSDDLcliDQLQKKnaqlVEQYHKATESLSLADAkpdqillSSQYDSQIEKLNQL 1255
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKEL---EEAEAA----LEEFRQKNGLVDLSEE-------AKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1256 LNAAKDELHDVRRikddEISALRMEFLLQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLssvtVRCQAE 1335
Cdd:COG3206 228 LAEARAELAEAEA----RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDV----IALRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 1336 LEALKSAHKENISQAVEERNNLIVQHQAEMETIR---ETLKNKLAEASTQQSKMEDAFR-AEIN-EVRATLMEQLNQTKE 1410
Cdd:COG3206 300 IAALRAQLQQEAQRILASLEAELEALQAREASLQaqlAQLEARLAELPELEAELRRLEReVEVArELYESLLQRLEEARL 379
|
...
gi 442627454 1411 DRD 1413
Cdd:COG3206 380 AEA 382
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
838-1099 |
9.97e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 838 SESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQrptshveesmrssgISSDFDEQKQ 917
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA--------------LEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 918 DINLLHQfvQLSESVQQIELQHHSgISRLFRANQMKLDQSEPGLKLcleSAEYIEEDNRQSDAtepicLKGFLKRHRFQI 997
Cdd:COG4942 84 ELAELEK--EIAELRAELEAQKEE-LAELLRALYRLGRQPPLALLL---SPEDFLDAVRRLQY-----LKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627454 998 KRLSQEhvdmgeekrlLDIISQLEQEIEEKSAlmeATEATINEMREQMTNLESALLEKSVIINKVE----DYQRQIESLE 1073
Cdd:COG4942 153 EELRAD----------LAELAALRAELEAERA---ELEALLAELEEERAALEALKAERQKLLARLEkelaELAAELAELQ 219
|
250 260
....*....|....*....|....*.
gi 442627454 1074 KQNAEMTMVYEELQDRVTRESSMSES 1099
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAERTPA 245
|
|
| |
