|
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 |
2.60e-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: 2.60e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 8 SIQVCIKVRPCEPGLT-----SLWQVKERrSIHLADSHAEPYVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIFAY 82
Cdd:cd01374 1 KITVTVRVRPLNSREIgineqVAWEIDND-TIYLVEPPSTSFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 83 GQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISSETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHE-SGNGIVNVNC 161
Cdd:cd01374 80 GQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDLLSPTSQNLKIRDdVEKGVYVAGL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 162 EECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSDDDAVIQSVLNLVDLAGSERADQTGARG 241
Cdd:cd01374 160 TEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGTVRVSTLNLIDLAGSERAAQTGAAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 242 ARLKEGGHINKSLLFLSNVIKSLSENADNRFTNYRDSKLTRILQASLGGNAFTSIICTIKP--SIMEESQSTLSFATRAK 319
Cdd:cd01374 240 VRRKEGSHINKSLLTLGTVISKLSEGKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPaeSHVEETLNTLKFASRAK 319
|
..
gi 442627456 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: 384.62 E-value: 1.12e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 8 SIQVCIKVRP-----CEPGLTSLWQV--KERRSIHLADSHAEP----YVFDYVFDEGASNQEVFDRMAKHIVHACMQGFN 76
Cdd:smart00129 1 NIRVVVRVRPlnkreKSRKSPSVVPFpdKVGKTLTVRSPKNRQgekkFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 77 GTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISS-ETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNG 155
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKrEEGWQFSVKVSYLEIYNEKIRDLLNPSSKKLEIREDEKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 156 IVNV-NCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDhSDDDAVIQSVLNLVDLAGSERA 234
Cdd:smart00129 161 GVYVkGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKN-SSSGSGKASKLNLVDLAGSERA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 235 DQTGARGARLKEGGHINKSLLFLSNVIKSLSENADNRFTNYRDSKLTRILQASLGGNAFTSIICTIKPSI--MEESQSTL 312
Cdd:smart00129 240 KKTGAEGDRLKEAGNINKSLSALGNVINALAQHSKSRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPSSsnLEETLSTL 319
|
330
....*....|....*.
gi 442627456 313 SFATRAKKIRIKPQVN 328
Cdd:smart00129 320 RFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
2-321 |
7.27e-118 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 376.53 E-value: 7.27e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 2 SAKNASSIQVCIKVRPCEPGLTSLWQVKERRSihladshaepYVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIFA 81
Cdd:pfam00225 10 KERGSSVIVSVESVDSETVESSHLTNKNRTKT----------FTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 82 YGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISSETERD-FLLRVGYIEIYNEKIYDLLNKKNQD---LKIHESGNGIV 157
Cdd:pfam00225 80 YGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTKERSeFSVKVSYLEIYNEKIRDLLSPSNKNkrkLRIREDPKKGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 158 NV-NCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSDDDAVIQSVLNLVDLAGSERADQ 236
Cdd:pfam00225 160 YVkGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEESVKTGKLNLVDLAGSERASK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 237 TG-ARGARLKEGGHINKSLLFLSNVIKSLSENADNrFTNYRDSKLTRILQASLGGNAFTSIICTIKPSI--MEESQSTLS 313
Cdd:pfam00225 240 TGaAGGQRLKEAANINKSLSALGNVISALADKKSK-HIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSsnYEETLSTLR 318
|
....*...
gi 442627456 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 |
1.45e-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: 1.45e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 8 SIQVCIKVRP----CEPGLTSLWQVKERRSIHL---ADSHAEP--YVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGT 78
Cdd:cd00106 1 NVRVAVRVRPlngrEARSAKSVISVDGGKSVVLdppKNRVAPPktFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYNGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 79 IFAYGQTSSGKTYTMMGDEQN-PGVMVLAAKEIFQQISS--ETERDFLLRVGYIEIYNEKIYDLLNKKNQ-DLKIHESGN 154
Cdd:cd00106 81 IFAYGQTGSGKTYTMLGPDPEqRGIIPRALEDIFERIDKrkETKSSFSVSASYLEIYNEKIYDLLSPVPKkPLSLREDPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 155 -GIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDhSDDDAVIQSVLNLVDLAGSER 233
Cdd:cd00106 161 rGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNRE-KSGESVTSSKLNLVDLAGSER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 234 ADQTGARGARLKEGGHINKSLLFLSNVIKSLSENaDNRFTNYRDSKLTRILQASLGGNAFTSIICTIKPSIM--EESQST 311
Cdd:cd00106 240 AKKTGAEGDRLKEGGNINKSLSALGKVISALADG-QNKHIPYRDSKLTRLLQDSLGGNSKTIMIACISPSSEnfEETLST 318
|
....*...
gi 442627456 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 |
3.70e-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: 3.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 44 YVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISS-ETERDF 122
Cdd:cd01370 63 YVFDRVFDETSTQEEVYEETTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIESlKDEKEF 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 123 LLRVGYIEIYNEKIYDLLNKKNQDLKIHE-SGNGIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIF 201
Cdd:cd01370 143 EVSMSYLEIYNETIRDLLNPSSGPLELREdAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 202 KIIIESRKSDHSDDDAVIQSVLNLVDLAGSERADQTGARGARLKEGGHINKSLLFLSNVIKSLSENA-DNRFTNYRDSKL 280
Cdd:cd01370 223 QITVRQQDKTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGkKNKHIPYRDSKL 302
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 442627456 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 |
1.16e-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: 1.16e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 7 SSIQVCIKVRPcEPGLT------SLWQVKERRSIHLADSHAE-PYVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTI 79
Cdd:cd01369 2 CNIKVVCRFRP-LNELEvlqgskSIVKFDPEDTVVIATSETGkTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 80 FAYGQTSSGKTYTMMG---DEQNPGVMVLAAKEIFQQISSETERD-FLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNG 155
Cdd:cd01369 81 FAYGQTSSGKTYTMEGklgDPESMGIIPRIVQDIFETIYSMDENLeFHVKVSYFEIYMEKIRDLLDVSKTNLSVHEDKNR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 156 IVNV-NCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRksdHSDDDAVIQSVLNLVDLAGSERA 234
Cdd:cd01369 161 GPYVkGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQE---NVETEKKKSGKLYLVDLAGSEKV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 235 DQTGARGARLKEGGHINKSLLFLSNVIKSLSENADNrFTNYRDSKLTRILQASLGGNAFTSIICTIKPSIMEESQ--STL 312
Cdd:cd01369 238 SKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKT-HIPYRDSKLTRILQDSLGGNSRTTLIICCSPSSYNESEtlSTL 316
|
....*....
gi 442627456 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 |
2.88e-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: 2.88e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 7 SSIQVCIKVRP------CEPGLTSLWQVKERRSIHLADSHAepYVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIF 80
Cdd:cd01372 1 SSVRVAVRVRPllpkeiIEGCRICVSFVPGEPQVTVGTDKS--FTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 81 AYGQTSSGKTYTMMG------DEQNPGVMVLAAKEIFQQIS-SETERDFLLRVGYIEIYNEKIYDLLN---KKNQDLKIH 150
Cdd:cd01372 79 AYGQTGSGKTYTMGTaytaeeDEEQVGIIPRAIQHIFKKIEkKKDTFEFQLKVSFLEIYNEEIRDLLDpetDKKPTISIR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 151 ESGNG-IVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRK-------SDHSDDDAVIQSV 222
Cdd:cd01372 159 EDSKGgITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKkngpiapMSADDKNSTFTSK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 223 LNLVDLAGSERADQTGARGARLKEGGHINKSLLFLSNVIKSL-SENADNRFTNYRDSKLTRILQASLGGNAFTSIICTIK 301
Cdd:cd01372 239 FHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALgDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVS 318
|
330 340
....*....|....*....|...
gi 442627456 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 |
5.60e-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: 5.60e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 7 SSIQVCIKVRP-----CEPGLTSLWQVKERRSIHLADSHAE-----------PYVFDYVFDE-------GASNQEVFDRM 63
Cdd:cd01365 1 ANVKVAVRVRPfnsreKERNSKCIVQMSGKETTLKNPKQADknnkatrevpkSFSFDYSYWShdsedpnYASQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 64 AKHIVHACMQGFNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQI--SSETERDFLLRVGYIEIYNEKIYDLLN 141
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIadTTNQNMSYSVEVSYMEIYNEKVRDLLN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 142 KKN----QDLKIHES-GNGIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSD-HSDD 215
Cdd:cd01365 161 PKPkknkGNLKVREHpVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKRHDaETNL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 216 DAVIQSVLNLVDLAGSERADQTGARGARLKEGGHINKSLLFLSNVIKSLSENAD------NRFTNYRDSKLTRILQASLG 289
Cdd:cd01365 241 TTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkkSSFIPYRDSVLTWLLKENLG 320
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 442627456 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 |
7.24e-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: 7.24e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 9 IQVCIKVRPCEPGLT----SLWQVKE--RRSIHLADSHAEPYVF--DYVFDEGASNQEVFdRMAKHIVHACMQGFNGTIF 80
Cdd:cd01366 4 IRVFCRVRPLLPSEEnedtSHITFPDedGQTIELTSIGAKQKEFsfDKVFDPEASQEDVF-EEVSPLVQSALDGYNVCIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 81 AYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISSETERD--FLLRVGYIEIYNEKIYDLLNK---KNQDLKI-HESGN 154
Cdd:cd01366 83 AYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKELKEKGwsYTIKASMLEIYNETIRDLLAPgnaPQKKLEIrHDSEK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 155 GIVNV-NCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRksdHSDDDAVIQSVLNLVDLAGSER 233
Cdd:cd01366 163 GDTTVtNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGR---NLQTGEISVGKLNLVDLAGSER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 234 ADQTGARGARLKEGGHINKSLLFLSNVIKSLSENadNRFTNYRDSKLTRILQASLGGNAFTSIICTIKP--SIMEESQST 311
Cdd:cd01366 240 LNKSGATGDRLKETQAINKSLSALGDVISALRQK--QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPaeSNLNETLNS 317
|
330
....*....|..
gi 442627456 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 |
5.05e-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: 5.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 8 SIQVCIKVRPC-----EPGLTSLWQVKE-RRSIHL----ADSHAEP--YVFDYVFDEGASNQEVFDRMAKHIVHACMQGF 75
Cdd:cd01371 2 NVKVVVRCRPLngkekAAGALQIVDVDEkRGQVSVrnpkATANEPPktFTFDAVFDPNSKQLDVYDETARPLVDSVLEGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 76 NGTIFAYGQTSSGKTYTMMG---DEQNPGVMVLAAKEIFQQISSETE-RDFLLRVGYIEIYNEKIYDLLNK-KNQDLKIH 150
Cdd:cd01371 82 NGTIFAYGQTGTGKTYTMEGkreDPELRGIIPNSFAHIFGHIARSQNnQQFLVRVSYLEIYNEEIRDLLGKdQTKRLELK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 151 ES-GNGIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSDDDAVIQSVLNLVDLA 229
Cdd:cd01371 162 ERpDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITIECSEKGEDGENHIRVGKLNLVDLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 230 GSERADQTGARGARLKEGGHINKSLLFLSNVIKSLsenADNRFTN--YRDSKLTRILQASLGGNAFTSIICTIKP--SIM 305
Cdd:cd01371 242 GSERQSKTGATGERLKEATKINLSLSALGNVISAL---VDGKSTHipYRDSKLTRLLQDSLGGNSKTVMCANIGPadYNY 318
|
330
....*....|....*.
gi 442627456 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 |
9.89e-80 |
|
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: 268.04 E-value: 9.89e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 7 SSIQVCIKVRP---------------CEPgltSLWQVKERRSIHLADSHAEPYVFDYVFDEGASNQEVFDRMAKHIVHAC 71
Cdd:cd01364 2 KNIQVVVRCRPfnlrerkasshsvveVDP---VRKEVSVRTGGLADKSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 72 MQGFNGTIFAYGQTSSGKTYTMMGD---------EQNP--GVMVLAAKEIFQQISSeTERDFLLRVGYIEIYNEKIYDLL 140
Cdd:cd01364 79 LMGYNCTIFAYGQTGTGKTYTMEGDrspneeytwELDPlaGIIPRTLHQLFEKLED-NGTEYSVKVSYLEIYNEELFDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 141 ---NKKNQDLKIHES---GNGIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSD 214
Cdd:cd01364 158 spsSDVSERLRMFDDprnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 215 DDAVIQSVLNLVDLAGSERADQTGARGARLKEGGHINKSLLFLSNVIKSLSENADNrfTNYRDSKLTRILQASLGGNAFT 294
Cdd:cd01364 238 EELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVERAPH--VPYRESKLTRLLQDSLGGRTKT 315
|
330 340 350
....*....|....*....|....*....|....*..
gi 442627456 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 |
1.03e-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: 1.03e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 9 IQVCIKVRPCEPGLTSL---WQVKERRSIHLAdSHAEP---YVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIFAY 82
Cdd:cd01373 3 VKVFVRIRPPAEREGDGeygQCLKKLSSDTLV-LHSKPpktFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 83 GQTSSGKTYTMMG----DEQNPGVMVLAAKEIFQQISSETERD---------FLLRVGYIEIYNEKIYDLLNKKNQDLKI 149
Cdd:cd01373 82 GQTGSGKTYTMWGpsesDNESPHGLRGVIPRIFEYLFSLIQREkekagegksFLCKCSFLEIYNEQIYDLLDPASRNLKL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 150 HES-GNGIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESrKSDHSDDDAVIQSVLNLVDL 228
Cdd:cd01373 162 REDiKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIES-WEKKACFVNIRTSRLNLVDL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 229 AGSERADQTGARGARLKEGGHINKSLLFLSNVIKSLSENAD--NRFTNYRDSKLTRILQASLGGNAFTSIICTIKPSI-- 304
Cdd:cd01373 241 AGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHgkQRHVCYRDSKLTFLLRDSLGGNAKTAIIANVHPSSkc 320
|
330 340
....*....|....*....|....*
gi 442627456 305 MEESQSTLSFATRAKKIRIKPQVNE 329
Cdd:cd01373 321 FGETLSTLRFAQRAKLIKNKAVVNE 345
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
2-359 |
7.29e-72 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 252.74 E-value: 7.29e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 2 SAKNASSIQVCIKVRPCEPGLTsLWQVKERRSIHLADSHAEPYVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIFA 81
Cdd:COG5059 17 NEKSVSDIKSTIRIIPGELGER-LINTSKKSHVSLEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 82 YGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQIS-SETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNGIVNV- 159
Cdd:COG5059 96 YGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLEdLSMTKDFAVSISYLEIYNEKIYDLLSPNEESLNIREDSLLGVKVa 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 160 NCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSDDdavIQSVLNLVDLAGSERADQTGA 239
Cdd:COG5059 176 GLTEKHVSSKEEILDLLRKGEKNRTTASTEINDESSRSHSIFQIELASKNKVSGTS---ETSKLSLVDLAGSERAARTGN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 240 RGARLKEGGHINKSLLFLSNVIKSLSENADNRFTNYRDSKLTRILQASLGGNAFTSIICTIKPS--IMEESQSTLSFATR 317
Cdd:COG5059 253 RGTRLKEGASINKSLLTLGNVINALGDKKKSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSsnSFEETINTLKFASR 332
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 442627456 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 |
2.48e-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: 2.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 9 IQVCIKVRPCEPGL-----TSLWQVKERRSIHLAD--SHAEP--YVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTI 79
Cdd:cd01376 2 VRVAVRVRPFVDGTagasdPSCVSGIDSCSVELADprNHGETlkYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNATV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 80 FAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFqQISSETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNG---I 156
Cdd:cd01376 82 FAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-QMTRKEAWALSFTMSYLEIYQEKILDLLEPASKELVIREDKDGnilI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 157 VNVNCEEciITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSdhSDDDAVIQSVLNLVDLAGSERADQ 236
Cdd:cd01376 161 PGLSSKP--IKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRER--LAPFRQRTGKLNLIDLAGSEDNRR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 237 TGARGARLKEGGHINKSLLFLSNVIKSLSENAdnRFTNYRDSKLTRILQASLGGNAFTSIICTIKPSI--MEESQSTLSF 314
Cdd:cd01376 237 TGNEGIRLKESGAINSSLFVLSKVVNALNKNL--PRIPYRDSKLTRLLQDSLGGGSRCIMVANIAPERtfYQDTLSTLNF 314
|
....*
gi 442627456 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 |
8.09e-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: 8.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 9 IQVCIKVRPCE--------------PGLTSLWQVKERRSIHLADSH-AEPYVFDYVFDEGASNQEVFDRMAKHIVHACMQ 73
Cdd:cd01367 2 IKVCVRKRPLNkkevakkeidvvsvPSKLTLIVHEPKLKVDLTKYIeNHTFRFDYVFDESSSNETVYRSTVKPLVPHIFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 74 GFNGTIFAYGQTSSGKTYTMMGD----EQNPGVMVLAAKEIFQQISSETERDFL-LRVGYIEIYNEKIYDLLNKKnQDLK 148
Cdd:cd01367 82 GGKATCFAYGQTGSGKTYTMGGDfsgqEESKGIYALAARDVFRLLNKLPYKDNLgVTVSFFEIYGGKVFDLLNRK-KRVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 149 IHESGNGIVNV-NCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSdddaviQSVLNLVD 227
Cdd:cd01367 161 LREDGKGEVQVvGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTNKL------HGKLSFVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 228 LAGSER-ADQTGARGARLKEGGHINKSLLFLSNVIKSLSENadNRFTNYRDSKLTRILQASL-GGNAFTSIICTIKPSI- 304
Cdd:cd01367 235 LAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQN--KAHIPFRGSKLTQVLKDSFiGENSKTCMIATISPGAs 312
|
330
....*....|....*.
gi 442627456 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 |
1.89e-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: 1.89e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 8 SIQVCIKVRPCEP---GLTSLWQVKERRSIHLADSHAEPYV----------FDYVFDEgASNQEVFDRMAKHIVHACMQG 74
Cdd:cd01375 1 KVQAFVRVRPTDDfahEMIKYGEDGKSISIHLKKDLRRGVVnnqqedwsfkFDGVLHN-ASQELVYETVAKDVVSSALAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 75 FNGTIFAYGQTSSGKTYTMMGDEQN---PGVMVLAAKEIFQQISSETERDFLLRVGYIEIYNEKIYDLLNKKNQDLK--- 148
Cdd:cd01375 80 YNGTIFAYGQTGAGKTFTMTGGTENykhRGIIPRALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLSTLPYVGPsvt 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 149 ----IHESGNGIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSdDDAVIQSVLN 224
Cdd:cd01375 160 pmtiLEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLS-SEKYITSKLN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 225 LVDLAGSERADQTGARGARLKEGGHINKSLLFLSNVIKSLSENaDNRFTNYRDSKLTRILQASLGGNAFTSIICTI--KP 302
Cdd:cd01375 239 LVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIALSDK-DRTHVPFRQSKLTHVLRDSLGGNCNTVMVANIygEA 317
|
330
....*....|....*..
gi 442627456 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 |
2.09e-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: 214.95 E-value: 2.09e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 27 QVKERRSIHLADSHAEPYVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLA 106
Cdd:cd01368 40 GSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPLVQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 107 AKEIFQQISseterDFLLRVGYIEIYNEKIYDLL-------NKKNQDLKIHESGNGIVNV-NCEECIITSEVDLLRLLCL 178
Cdd:cd01368 120 LDVIFNSIG-----GYSVFVSYIEIYNEYIYDLLepspsspTKKRQSLRLREDHNGNMYVaGLTEIEVKSTEEARKVLKR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 179 GNKERTVGETNMNERSSRSHAIFKIII-----ESRKSDHSDDDAVIQSVLNLVDLAGSERADQTGARGARLKEGGHINKS 253
Cdd:cd01368 195 GQKNRSVAGTKLNRESSRSHSVFTIKLvqapgDSDGDVDQDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTS 274
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627456 254 LLFLSNVIKSLSENADNRFTN---YRDSKLTRILQASLGGNAFTSIICTIKPSI--MEESQSTLSFATRAK 319
Cdd:cd01368 275 LMTLGTCIEVLRENQLQGTNKmvpFRDSKLTHLFQNYFDGEGKASMIVNVNPCAsdYDETLHVMKFSAIAQ 345
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
7-351 |
8.13e-51 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 198.62 E-value: 8.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 7 SSIQVCIKVRPCEPGLTSLWQVKERRSIHLADShAEPYVFDYVFDEGASNQEVFDRMAKHIVHACMQGFNGTIFAYGQTS 86
Cdd:PLN03188 98 SGVKVIVRMKPLNKGEEGEMIVQKMSNDSLTIN-GQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTG 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 87 SGKTYTMMG------------DEQnpGVMVLAAKEIFQQISSE----TER--DFLLRVGYIEIYNEKIYDLLNKKNQDLK 148
Cdd:PLN03188 177 SGKTYTMWGpanglleehlsgDQQ--GLTPRVFERLFARINEEqikhADRqlKYQCRCSFLEIYNEQITDLLDPSQKNLQ 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 149 IHE---SGNGIVNVNcEECIITSEvDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSDDDAVIQ-SVLN 224
Cdd:PLN03188 255 IREdvkSGVYVENLT-EEYVKTMK-DVTQLLIKGLSNRRTGATSINAESSRSHSVFTCVVESRCKSVADGLSSFKtSRIN 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 225 LVDLAGSERADQTGARGARLKEGGHINKSLLFLSNVIKSL---SENADNRFTNYRDSKLTRILQASLGGNAFTSIICTIK 301
Cdd:PLN03188 333 LVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILaeiSQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAIS 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 442627456 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 ... |
505-1297 |
3.14e-18 |
|
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: 92.04 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 505 YDALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRIMEVENQVAVGlefefeahkkssklRVDDLLSALLEKESTIES 584
Cdd:TIGR02168 241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK--------------ELYALANEISRLEQQKQI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 585 LQKSLDNLTRDVlrnskeghmlsiapeqediagdsicnkcEELEKLIADLESKKnscecDQLRLEIVSVRDKLESVESAF 664
Cdd:TIGR02168 307 LRERLANLERQL----------------------------EELEAQLEELESKL-----DELAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 665 NLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLEsraRSA 744
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL---KKL 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 745 SSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNS----ESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSN 820
Cdd:TIGR02168 431 EEAELKELQAELEELEEELEELQEELERLEEALEELREEleeaEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 821 QLMESVQEND---ALREEIKQRP--TSHVEESMRSSG---ISSDFDEQKQDINLLHQfvQLSESVQQIELQHHSGisRLF 892
Cdd:TIGR02168 511 LLKNQSGLSGilgVLSELISVDEgyEAAIEAALGGRLqavVVENLNAAKKAIAFLKQ--NELGRVTFLPLDSIKG--TEI 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 893 RANQMKLDQSEPGLKLCLESAEYIEED---------------------NRQSDATEP----ICLKGFLKRHRFQI--KRL 945
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvlvvddldnaLELAKKLRPgyriVTLDGDLVRPGGVItgGSA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 946 SQEHVDMGEEKRlldiISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIInkvEDYQRQIESLEKQNAEMT 1025
Cdd:TIGR02168 667 KTNSSILERRRE----IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL---EELSRQISALRKDLARLE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1026 MVYEELQDRVTRESSMSESLL-RVPPDEDTLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNI 1104
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEaEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1105 ARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQyhKATESLSLADAKPDQI 1184
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE--RASLEEALALLRSELE 897
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1185 LLSSQ---YDSQIEKLNQLLNAAKDELHDVRRikddEISALRMEfLLQIETNEKENQAKFYAELQETKDRYESNVAELKE 1261
Cdd:TIGR02168 898 ELSEElreLESKRSELRRELEELREKLAQLEL----RLEGLEVR-IDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR 972
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 442627456 1262 KLLQVEETLSS---VTVRCQAELEALK------SAHKENISQAVE 1297
Cdd:TIGR02168 973 RLKRLENKIKElgpVNLAAIEEYEELKerydflTAQKEDLTEAKE 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
954-1718 |
6.44e-18 |
|
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: 90.89 E-value: 6.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 954 EEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEdyqRQIESLEKQNAEMTMVYEELQD 1033
Cdd:TIGR02168 247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE---QQKQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1034 RVTRESSMSESLLrvppdedtlpgcpTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEE 1113
Cdd:TIGR02168 324 QLEELESKLDELA-------------EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1114 MSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLvEQYHKATESLSLADAKPDQILLSSQYDSQ 1193
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1194 IEKLNQLLNAAKDELHDVRRikddeisalRMEFLLQIETNekenqakfyaelQETKDRYESNVAELKEKLLQVEETLSSV 1273
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQA---------RLDSLERLQEN------------LEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1274 tVRCQAELEALKSAHKENISQAVEERNN----LIVQHQAEMETIRETL-------KNKLAEASTQQSKMEDAFRAEINEV 1342
Cdd:TIGR02168 529 -ISVDEGYEAAIEAALGGRLQAVVVENLnaakKAIAFLKQNELGRVTFlpldsikGTEIQGNDREILKNIEGFLGVAKDL 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1343 RaTLMEQLNQTKEDR-------DKGASKLEEVKKTLEQ---------------MINGGRVMSDT--------IAELEKTK 1392
Cdd:TIGR02168 608 V-KFDPKLRKALSYLlggvlvvDDLDNALELAKKLRPGyrivtldgdlvrpggVITGGSAKTNSsilerrreIEELEEKI 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1393 AEQDLAVNKLTKDNIELEKQcsktQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLE 1472
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1473 KLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKekcdFETKLETFTFKITDLEEvlkEAQHKVILYDDLVSQHER 1552
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA----LREALDELRAELTLLNE---EAANLRERLESLERRIAA 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1553 LKICLAEANELSSNLQKKVMSLHTELIDSQkgissrdVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAE 1632
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELE-------ELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1633 KFTReaanLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLrnMLDEeskmcisLKEKLVKLEDAKTSLEQQLR 1712
Cdd:TIGR02168 909 KRSE----LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL--TLEE-------AEALENKIEDDEEEARRRLK 975
|
....*.
gi 442627456 1713 DNKSEI 1718
Cdd:TIGR02168 976 RLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
648-1396 |
8.37e-18 |
|
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: 90.50 E-value: 8.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 648 LEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKY 727
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 728 QKLQEEYEQLEsrarsassAEFQRLQNDNTKFQADIASLNERLEEAQNmltEVQNSESTVEKLRIQNHELTAKIKELETN 807
Cdd:TIGR02168 312 ANLERQLEELE--------AQLEELESKLDELAEELAELEEKLEELKE---ELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 808 FEEMQREYDCLSNQ---LMESVQENDALREEIKQRPTSHVEE--SMRSSGISSDFDEQKQDINLLHQ-FVQLSESVQQIE 881
Cdd:TIGR02168 381 LETLRSKVAQLELQiasLNNEIERLEARLERLEDRRERLQQEieELLKKLEEAELKELQAELEELEEeLEELQEELERLE 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 882 LQHHSgISRLFRANQMKLDQSEPGLKLcLESAEYIEEDNRQSDATEPICLKgFLKRHRFQIK----RLSQE-HVDMGEEK 956
Cdd:TIGR02168 461 EALEE-LREELEEAEQALDAAERELAQ-LQARLDSLERLQENLEGFSEGVK-ALLKNQSGLSgilgVLSELiSVDEGYEA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 957 RL-------------------LDIISQLEQEIEEKSALMEATEATINEM----REQMTNLESALLEKSVIINKVEDYQRQ 1013
Cdd:TIGR02168 538 AIeaalggrlqavvvenlnaaKKAIAFLKQNELGRVTFLPLDSIKGTEIqgndREILKNIEGFLGVAKDLVKFDPKLRKA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1014 IESLEKQnaemTMVYEELQDRVTRESSMSESLLRVPPDEDTLPGC--------PTSPSR--REQEVATLKTSITELQSQV 1083
Cdd:TIGR02168 618 LSYLLGG----VLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGgvitggsaKTNSSIleRRREIEELEEKIEELEEKI 693
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1084 SDLKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDdlclidqLQKKNAQL 1163
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTE-------LEAEIEEL 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1164 VEQYHKATESLSLADAKpdqillssqydsqIEKLNQLLNAAKDELHDVRRIKD---DEISALRMEFLLQieTNEKENQAK 1240
Cdd:TIGR02168 767 EERLEEAEEELAEAEAE-------------IEELEAQIEQLKEELKALREALDelrAELTLLNEEAANL--RERLESLER 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1241 FYAELQETKDRYESNVAELKEKLLQVEETLSSVTVRC---QAELEAL---KSAHKENISQAVEERNNLIVQhQAEMETIR 1314
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIeelESELEALlneRASLEEALALLRSELEELSEE-LRELESKR 910
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1315 ETLKNKLAEASTQQSKME---DAFRAEINEVRATLMEQLNQTKED-------RDKGASKLEEVKKTLEQMING-GRVMSD 1383
Cdd:TIGR02168 911 SELRRELEELREKLAQLElrlEGLEVRIDNLQERLSEEYSLTLEEaealenkIEDDEEEARRRLKRLENKIKElGPVNLA 990
|
810
....*....|...
gi 442627456 1384 TIAELEKTKAEQD 1396
Cdd:TIGR02168 991 AIEEYEELKERYD 1003
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
528-1376 |
8.81e-18 |
|
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: 90.50 E-value: 8.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 528 ELEEKLSTLKQTMRIMEVEnqvavglEFEFEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVlrnSKEGHMLS 607
Cdd:TIGR02168 236 ELREELEELQEELKEAEEE-------LEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI---SRLEQQKQ 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 608 IAPEQEDIAGDSIcnkcEELEKLIADLESKKnscecDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELST 687
Cdd:TIGR02168 306 ILRERLANLERQL----EELEAQLEELESKL-----DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 688 SQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLEsraRSASSAEFQRLQNDNTKFQADIASLN 767
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL---KKLEEAELKELQAELEELEEELEELQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 768 ERLEEAQNMLTEVQNS----ESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQEND---ALREEIKQRP 840
Cdd:TIGR02168 454 EELERLEEALEELREEleeaEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGilgVLSELISVDE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 841 --TSHVEESMRSSG---ISSDFDEQKQDINLLHQfvQLSESVQQIELQHHSGisRLFRANQMKLDQSEPGLKLCLESAEY 915
Cdd:TIGR02168 534 gyEAAIEAALGGRLqavVVENLNAAKKAIAFLKQ--NELGRVTFLPLDSIKG--TEIQGNDREILKNIEGFLGVAKDLVK 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 916 IEED---------------------NRQSDATEP----ICLKGFLKRHRFQIKRlsqehvdmGEEKRLLDIISQlEQEIE 970
Cdd:TIGR02168 610 FDPKlrkalsyllggvlvvddldnaLELAKKLRPgyriVTLDGDLVRPGGVITG--------GSAKTNSSILER-RREIE 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 971 EKSALMEATEATINEMREQMTNLESALLEksvIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSMSESLlrvpp 1050
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEE---LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQL----- 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1051 dedtlpgcptspsrrEQEVATLKTSITELQSQVSDLKAELENHLRQIQlkdgniaRLQTDFEEMSERCLSMEVRLAELDE 1130
Cdd:TIGR02168 753 ---------------SKELTELEAEIEELEERLEEAEEELAEAEAEIE-------ELEAQIEQLKEELKALREALDELRA 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1131 DTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAkpdqillssqydsQIEKLNQLLNAAKDELhd 1210
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA-------------EIEELEELIEELESEL-- 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1211 vrrikdDEISALRMEFLLQIETNEKEnqakfYAELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQaELEALKSAHKE 1290
Cdd:TIGR02168 876 ------EALLNERASLEEALALLRSE-----LEELSEELRELESKRSELRRELEELREKLAQLELRLE-GLEVRIDNLQE 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1291 NISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQqskmedafRAEINEVRATLMEQLNQTKEDRD---KGASKLEEV 1367
Cdd:TIGR02168 944 RLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENK--------IKELGPVNLAAIEEYEELKERYDfltAQKEDLTEA 1015
|
....*....
gi 442627456 1368 KKTLEQMIN 1376
Cdd:TIGR02168 1016 KETLEEAIE 1024
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
45-263 |
2.63e-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: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 45 VFDYVFDEGASNQEVFdRMAKHIVHACMQGFNG-TIFAYGQTSSGKTYTMMGdeqnpgvmvlaakeIFQQIsseterdfl 123
Cdd:cd01363 21 VFYRGFRRSESQPHVF-AIADPAYQSMLDGYNNqSIFAYGESGAGKTETMKG--------------VIPYL--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 124 lrvgyIEIYNEKIYDLLNKKNQdlkihesgngivnvNCEECIITSEVDLLRLLCLGNKERTvGETNMNERSSRSHAIFKI 203
Cdd:cd01363 77 -----ASVAFNGINKGETEGWV--------------YLTEITVTLEDQILQANPILEAFGN-AKTTRNENSSRFGKFIEI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 204 iiesrksdhsdddaviqsvlnLVDLAGSERadqtgargarlkegghINKSLLFLSNVIKS 263
Cdd:cd01363 137 ---------------------LLDIAGFEI----------------INESLNTLMNVLRA 159
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
956-1773 |
5.80e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 87.80 E-value: 5.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 956 KRLLDIISQLEQEIEEKSALMEATEATInEMREQMTNLEsalleKSVIINKVEDYQRQIESLEKQNAEMtmvyEELQDRV 1035
Cdd:TIGR02168 189 DRLEDILNELERQLKSLERQAEKAERYK-ELKAELRELE-----LALLVLRLEELREELEELQEELKEA----EEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1036 TRESSMSESLLrvppdedtlpgcptspSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMS 1115
Cdd:TIGR02168 259 TAELQELEEKL----------------EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1116 ErclsmevRLAELDEDTKQKQELLDRQAQKlsddlclIDQLQKKNAQLVEqyhkateslsladakpdqillssqydsQIE 1195
Cdd:TIGR02168 323 A-------QLEELESKLDELAEELAELEEK-------LEELKEELESLEA---------------------------ELE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1196 KLNQLLNAAKDELHDVRRikddeisalrmefllqietnEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVTV 1275
Cdd:TIGR02168 362 ELEAELEELESRLEELEE--------------------QLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1276 RCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKnKLAEASTQQSKMEDAFRAEINEVRA--TLMEQLNQT 1353
Cdd:TIGR02168 422 EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALE-ELREELEEAEQALDAAERELAQLQArlDSLERLQEN 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1354 KEDRDKGASKLEEVKKTLEQMINggrVMSDTI-------AELEKTKAE--QDLAVNKLT--KDNIELEKQCSKTQEQLQM 1422
Cdd:TIGR02168 501 LEGFSEGVKALLKNQSGLSGILG---VLSELIsvdegyeAAIEAALGGrlQAVVVENLNaaKKAIAFLKQNELGRVTFLP 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1423 ESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCdQQVLE--LDKCRLEKlSLESEIQKANSEHSCTM------EKL 1494
Cdd:TIGR02168 578 LDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKL-RKALSylLGGVLVVD-DLDNALELAKKLRPGYRivtldgDLV 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1495 --------QELQAEMKVLSNRNEKEKCdfETKLETFTFKITDLEEVLKEAQHKVILY----DDLVSQHERLKICLAEANE 1562
Cdd:TIGR02168 656 rpggvitgGSAKTNSSILERRREIEEL--EEKIEELEEKIAELEKALAELRKELEELeeelEQLRKELEELSRQISALRK 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1563 LSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFT---REAA 1639
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDelrAELT 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1640 NLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQ----NLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNK 1715
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSedieSLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627456 1716 SEIYqrhtELTKEVELGRNRIGELTKKCEELCSDLEnsdQIRLDLQETKEQLKKTLEN 1773
Cdd:TIGR02168 894 SELE----ELSEELRELESKRSELRRELEELREKLA---QLELRLEGLEVRIDNLQER 944
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1082-1870 |
1.71e-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: 86.26 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1082 QVSDLKAELENHLRQIQLKdgniARLQTDFEEMSErclsmEVRLAELDEDTKQKQELLDRqaqklsddlclIDQLQKKNA 1161
Cdd:TIGR02168 190 RLEDILNELERQLKSLERQ----AEKAERYKELKA-----ELRELELALLVLRLEELREE-----------LEELQEELK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1162 QLVEQYHKATESLSLADAKPDQIllssqyDSQIEKLNQLLNAAKDELHDVRRikddEISALRMEflLQIETNEKENQAKF 1241
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEEL------RLEVSELEEEIEELQKELYALAN----EISRLEQQ--KQILRERLANLERQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1242 YAELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELEALKSAHKEniSQAVEERNnlivqhqAEMETIRETLKNKL 1321
Cdd:TIGR02168 318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAE--LEELESRL-------EELEEQLETLRSKV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1322 AEASTQqskmEDAFRAEINEVRATLmEQLNQTKEDRDKGASKLEEVKKTLEqminggrvMSDTIAELEKTKAEQDlavnK 1401
Cdd:TIGR02168 389 AQLELQ----IASLNNEIERLEARL-ERLEDRRERLQQEIEELLKKLEEAE--------LKELQAELEELEEELE----E 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1402 LTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIvasskKRIIELEEKCDQQVLELDKCRLEK---LSLES 1478
Cdd:TIGR02168 452 LQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSL-----ERLQENLEGFSEGVKALLKNQSGLsgiLGVLS 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1479 EIQKANSEHSCTMEK-LQE-LQAemkVLSNRNEKEKCDFETKLETFTFKITDLE--------------EVLKEAQHKVIL 1542
Cdd:TIGR02168 527 ELISVDEGYEAAIEAaLGGrLQA---VVVENLNAAKKAIAFLKQNELGRVTFLPldsikgteiqgndrEILKNIEGFLGV 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1543 YDDLVSQHERLKIC-------------LAEANELSSNLQKKVM--SLHTELI-----------DSQKGISSRDVEINELR 1596
Cdd:TIGR02168 604 AKDLVKFDPKLRKAlsyllggvlvvddLDNALELAKKLRPGYRivTLDGDLVrpggvitggsaKTNSSILERRREIEELE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1597 EELKAAMDAKATASAEQMTLVTQLKDVEER-----------------MANQAEKFTREAANLKGSINELLLKL----NSM 1655
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEEleqlrkeleelsrqisaLRKDLARLEAEVEQLEERIAQLSKELteleAEI 763
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1656 QETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNKSeiyqRHTELTKEVELGRNR 1735
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRE----RLESLERRIAATERR 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1736 IGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLEnnlGWQQKVDEVTRECEKLRFDMQSKEVQN---ESKVQELISE 1812
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELE---ALLNERASLEEALALLRSELEELSEELrelESKRSELRRE 916
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627456 1813 CEELRSTLKSKEASFQSEKESMDRTISSLLED-KRNLEEKLCSANDIV---AKLETEIAALR 1870
Cdd:TIGR02168 917 LEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEddeEEARRRLKRLE 978
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1111-1876 |
2.45e-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: 82.47 E-value: 2.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1111 FEEMSERCLSMEVRLAELDE-DTKQK----QELLDRQA--QKLSDDLCLIDQLQKKNAQ----LVEQYHKATESLSLADA 1179
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNElHEKQKfylrQSVIDLQTklQEMQMERDAMADIRRRESQsqedLRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1180 KPDQILLSSqyDSQIEKLNQLLNAAKDELHDVRRIKDD--EISALRMEFLLQIETNEKENQAKFYAELQETKDryeSNVA 1257
Cdd:pfam15921 160 LKEDMLEDS--NTQIEQLRKMMLSHEGVLQEIRSILVDfeEASGKKIYEHDSMSTMHFRSLGSAISKILRELD---TEIS 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1258 ELKEKLLQVEETLSSVTVRCQAELEALKSAHKENISQaveernnLIVQHQAEMETIRETLKNKLAEASTQQSKMEdAFRA 1337
Cdd:pfam15921 235 YLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQ-------LISEHEVEITGLTEKASSARSQANSIQSQLE-IIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1338 EINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEqminggrvmsDTIAELEKTKAeqdLAVNKLTKDNIElekqcsktQ 1417
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE----------DKIEELEKQLV---LANSELTEARTE--------R 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1418 EQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEK-------CDQQVLELDKCRLEKLSLESEIQKANSEHSCT 1490
Cdd:pfam15921 366 DQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRdtgnsitIDHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1491 MEKlqelqaEMKVLSNRNEKEKcdfetKLETFTFKITDLEEVLKeaqhKVIlyDDLVSQHERLKICLAEANELSSNLQKK 1570
Cdd:pfam15921 446 MER------QMAAIQGKNESLE-----KVSSLTAQLESTKEMLR----KVV--EELTAKKMTLESSERTVSDLTASLQEK 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1571 VMSLHTELIDSQKGISSRDVEINELrEELKAAMDAKATASAEQMTLVTQLKD---VEERMANQAEKFTR----------- 1636
Cdd:pfam15921 509 ERAIEATNAEITKLRSRVDLKLQEL-QHLKNEGDHLRNVQTECEALKLQMAEkdkVIEILRQQIENMTQlvgqhgrtaga 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1637 ---EAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNsqnlrnmldeeskmcisLKEKLVKLEDAKTSLEQQLRD 1713
Cdd:pfam15921 588 mqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD-----------------LELEKVKLVNAGSERLRAVKD 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1714 nkseIYQRHTELTKEVELGRNRIGELTKKCEELCSDLEN--------SDQIRLDLQETKEQLKKT--------------L 1771
Cdd:pfam15921 651 ----IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNkseemettTNKLKMQLKSAQSELEQTrntlksmegsdghaM 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1772 ENNLGWQQKVDEVTRECEKLRFDMQSKE--VQNESKVQELIsecEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLE 1849
Cdd:pfam15921 727 KVAMGMQKQITAKRGQIDALQSKIQFLEeaMTNANKEKHFL---KEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLK 803
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 442627456 1850 EKLCS--------------ANDIVAKLETEIAALRPRKSLD 1876
Cdd:pfam15921 804 EKVANmevaldkaslqfaeCQDIIQRQEQESVRLKLQHTLD 844
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1006-1847 |
3.05e-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: 78.96 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1006 KVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSMSESLLRVppDEDTLPGCPTSPSRREQEVATLKTSITELQSQVSD 1085
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERY--QALLKEKREYEGYELLKEKEALERQKEAIERQLAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1086 LKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSM----EVRLAELDEDTKQKQELLDRQAQKLSDDLcliDQLQKKNA 1161
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeQLRVKEKIGELEAEIASLERSIAEKEREL---EDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1162 QLVEQYHKATESL-----SLADAKPDQILLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDdEISALRMEflLQIETNEKE 1236
Cdd:TIGR02169 326 KLEAEIDKLLAEIeelerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRD-ELKDYREK--LEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1237 NQAKFYAELQETKDRYESNVAELKEKLLQVEETLssvtvrcqAELEALKSAHKENISQAVEERNNLivqhQAEMETIRET 1316
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKI--------NELEEEKEDKALEIKKQEWKLEQL----AADLSKYEQE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1317 LKNKLAEASTQQSKMEDAfRAEINEVRATLmeqlnQTKEDRDKGASKLEEVKKTLEQMINGgrvmsdTIAELEKTKAEQD 1396
Cdd:TIGR02169 471 LYDLKEEYDRVEKELSKL-QRELAEAEAQA-----RASEERVRGGRAVEEVLKASIQGVHG------TVAQLGSVGERYA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1397 LAV-----NKLTKDNIELEKQCSKTQEQLQMESLTRdqISFEIEAHIKKLELIVASSKKR--------IIELEEKC---- 1459
Cdd:TIGR02169 539 TAIevaagNRLNNVVVEDDAVAKEAIELLKRRKAGR--ATFLPLNKMRDERRDLSILSEDgvigfavdLVEFDPKYepaf 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1460 -----DQQVLE--------LDKCRLekLSLESEIQK--------ANSEHSCTM------EKLQELQAE---MKVLSNRNE 1509
Cdd:TIGR02169 617 kyvfgDTLVVEdieaarrlMGKYRM--VTLEGELFEksgamtggSRAPRGGILfsrsepAELQRLRERlegLKRELSSLQ 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1510 KEKCDFETKLETFTFKITDLEEVLKEAQHKVILYDDlvsQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRD 1589
Cdd:TIGR02169 695 SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQ---EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1590 VEINELREELkaamdakatASAEQMTLVTQLKDVEermaNQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGNEEL 1669
Cdd:TIGR02169 772 EDLHKLEEAL---------NDLEARLSHSRIPEIQ----AELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1670 KEQLRNSQNLRNMLDEESKmciSLKEKLVKLEDAKTSLEQQLRDNKSeiyqRHTELTKEVELGRNRIGELTKKCEELCSD 1749
Cdd:TIGR02169 839 QEQRIDLKEQIKSIEKEIE---NLNGKKEELEEELEELEAALRDLES----RLGDLKKERDELEAQLRELERKIEELEAQ 911
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1750 LENSDQIRLDLQETKEQLK---KTLENNLGWQQKV-------DEVTRECEKLRFDMQSKEVQNESKVQELiSECEELRST 1819
Cdd:TIGR02169 912 IEKKRKRLSELKAKLEALEeelSEIEDPKGEDEEIpeeelslEDVQAELQRVEEEIRALEPVNMLAIQEY-EEVLKRLDE 990
|
890 900
....*....|....*....|....*...
gi 442627456 1820 LKSKEASFQSEKESMDRTISSLLEDKRN 1847
Cdd:TIGR02169 991 LKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
711-1554 |
5.39e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.17 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 711 AGITTLHEKHEHVQEKYQKLQEEYE-----------QLESRARSASSAE-FQRLQNDntKFQADIASLNERLEEAQNmlt 778
Cdd:TIGR02168 165 AGISKYKERRKETERKLERTRENLDrledilnelerQLKSLERQAEKAErYKELKAE--LRELELALLVLRLEELRE--- 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 779 EVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIkqrptshveesmrssgisSDFD 858
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI------------------SRLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 859 EQKQdinllHQFVQLSESVQQIElqhhsgisrlfranqmkldqsepglklclESAEYIEEDNRQSDatepiCLKGFLKRH 938
Cdd:TIGR02168 302 QQKQ-----ILRERLANLERQLE-----------------------------ELEAQLEELESKLD-----ELAEELAEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 939 RFQIKRLSQEHVDmgeekrlldiisqLEQEIEEKSALMEATEATINEMREQMTNLESALLEKsviinkvedyQRQIESLE 1018
Cdd:TIGR02168 343 EEKLEELKEELES-------------LEAELEELEAELEELESRLEELEEQLETLRSKVAQL----------ELQIASLN 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1019 KQNAEMTMVYEELQDRVTRESSMSESLLRVPPDEDTlpgcptspSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQ 1098
Cdd:TIGR02168 400 NEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL--------KELQAELEELEEELEELQEELERLEEALEELREELE 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1099 LKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQ--------------------- 1157
Cdd:TIGR02168 472 EAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISvdegyeaaieaalggrlqavv 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1158 -------KKNAQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKLNQLLNAAKDELHDVR------------RIKDDE 1218
Cdd:TIGR02168 552 venlnaaKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalsyllggvLVVDDL 631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1219 ISALRMEFLLQIETN-------------------EKENQAKFY-----AELQETKDRYESNVAELKEKLLQVEETLSSVt 1274
Cdd:TIGR02168 632 DNALELAKKLRPGYRivtldgdlvrpggvitggsAKTNSSILErrreiEELEEKIEELEEKIAELEKALAELRKELEEL- 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1275 vrcQAELEALKSAhKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEastqqskmedafRAEINEVRATLMEQLNQTK 1354
Cdd:TIGR02168 711 ---EEELEQLRKE-LEELSRQISALRKDLARLEAEVEQLEERIAQLSKE------------LTELEAEIEELEERLEEAE 774
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1355 EDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEI 1434
Cdd:TIGR02168 775 EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1435 E---AHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKE 1511
Cdd:TIGR02168 855 EslaAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 442627456 1512 KCDFETKLETFTFKITDLEEVLKEaqHKVILYDDLVSQHERLK 1554
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLEEAEA--LENKIEDDEEEARRRLK 975
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
957-1787 |
1.02e-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: 77.40 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 957 RLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKS----VIINKVEDYQRQIESLEKQNAEMTMVYEELQ 1032
Cdd:TIGR02168 243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQkelyALANEISRLEQQKQILRERLANLERQLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1033 DRVTRESSMSESLLrvppdedtlpgcpTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFE 1112
Cdd:TIGR02168 323 AQLEELESKLDELA-------------EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1113 EMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLvEQYHKATESLSLADAKPDQILLSSQYDS 1192
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEEALEELRE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1193 QIEKLNQLLNAAKDELHDVRRikddeisalRMEFLLQIETNekenqakfyaelQETKDRYESNVAELKEKLLQVEETLSS 1272
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQA---------RLDSLERLQEN------------LEGFSEGVKALLKNQSGLSGILGVLSE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1273 VtVRCQAELEALKSAHKENISQAVEERNN----LIVQHQAEMETIRETL-------KNKLAEASTQQSKMEDAFRAEINE 1341
Cdd:TIGR02168 528 L-ISVDEGYEAAIEAALGGRLQAVVVENLnaakKAIAFLKQNELGRVTFlpldsikGTEIQGNDREILKNIEGFLGVAKD 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1342 VRaTLMEQLNQTKEDR-------DKGASKLEEVKKTLEQ---------------MINGGRVMSDT--------IAELEKT 1391
Cdd:TIGR02168 607 LV-KFDPKLRKALSYLlggvlvvDDLDNALELAKKLRPGyrivtldgdlvrpggVITGGSAKTNSsilerrreIEELEEK 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1392 KAEQDLAVNKLTKDNIELEKQcsktQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRL 1471
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKE----LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1472 EKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKekcdfetkletftfkitdLEEVLKEAQhkvilyddlvSQHE 1551
Cdd:TIGR02168 762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA------------------LREALDELR----------AELT 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1552 RLKICLAEANELSSNLQKKVMSLHTELIDSQKgissrdvEINELREELKAA------MDAKATASAEQMTLVTQLKDVEE 1625
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEE-------QIEELSEDIESLaaeieeLEELIEELESELEALLNERASLE 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1626 RMANQAEKftrEAANLKGSINELLLKLN----SMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMcisLKEKLVKLE 1701
Cdd:TIGR02168 887 EALALLRS---ELEELSEELRELESKRSelrrELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL---TLEEAEALE 960
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1702 DAKTSLEQQLRDnkseiyqRHTELTKEV-ELGR---NRIGELtkkcEELCSDLENSDQIRLDLQETKEQLKKTLEnnlgw 1777
Cdd:TIGR02168 961 NKIEDDEEEARR-------RLKRLENKIkELGPvnlAAIEEY----EELKERYDFLTAQKEDLTEAKETLEEAIE----- 1024
|
890
....*....|
gi 442627456 1778 qqKVDEVTRE 1787
Cdd:TIGR02168 1025 --EIDREARE 1032
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1233-1812 |
3.87e-13 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 75.10 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1233 NEKENQAKFYAELQETKDRYESNVAELKEKLLQVEEtLSSVTVRCQAELEALKS------AHKENISQAvEERNNLIVQH 1306
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREINE-ISSELPELREELEKLEKevkeleELKEEIEEL-EKELESLEGS 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1307 QAEMETIRETLKNKLAEASTQQSKMEDAfRAEINEVR--ATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGgrvMSDT 1384
Cdd:PRK03918 254 KRKLEEKIRELEERIEELKKEIEELEEK-VKELKELKekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING---IEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1385 IAELEKTKAEqdlaVNKLTKDNIELEKQCSKTQEQL-----------QMESLTRDQISFEIEAHIKKLELiVASSKKRII 1453
Cdd:PRK03918 330 IKELEEKEER----LEELKKKLKELEKRLEELEERHelyeeakakkeELERLKKRLTGLTPEKLEKELEE-LEKAKEEIE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1454 ELEEKCDQQVLELDKCRLEKLSLESEIQKANSE-----HSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITD 1528
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1529 LEEVLKEaQHKVI----LYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMD 1604
Cdd:PRK03918 485 LEKVLKK-ESELIklkeLAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1605 AKATASAEQMTLVTQL--------KDVEERMaNQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNS 1676
Cdd:PRK03918 564 KLDELEEELAELLKELeelgfesvEELEERL-KELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1677 QNLRNMLDEeskmcislKEKLVKLEDAKtsleqqlrdnksEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLEnsdqi 1756
Cdd:PRK03918 643 EELRKELEE--------LEKKYSEEEYE------------ELREEYLELSRELAGLRAELEELEKRREEIKKTLE----- 697
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627456 1757 rlDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISE 1812
Cdd:PRK03918 698 --KLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASE 751
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1191-1832 |
5.76e-12 |
|
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: 71.54 E-value: 5.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1191 DSQIEKLNQLLNAAKDELHDVRRIKDDEISALRMEfllQIETNEKENQAKFYAELQETKDRYE-------SNVAELKEKL 1263
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA---LQQTQQSHAYLTQKREAQEEQLKKQqllkqlrARIEELRAQE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1264 LQVEETLSSVTVRCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEAST---QQSKMEDAFRAEI- 1339
Cdd:TIGR00618 277 AVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSieeQRRLLQTLHSQEIh 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1340 ----NEVRATLMEQLNQTKEDRDKgASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCsk 1415
Cdd:TIGR00618 357 irdaHEVATSIREISCQQHTLTQH-IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQ-- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1416 tqeQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEK-L 1494
Cdd:TIGR00618 434 ---ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGsC 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1495 QELQAEMKVLSN---------RNEKEKCDFETKLETFTFKITDLEEVLKEAQHKVILYDDLVSqheRLKICLAEANELSS 1565
Cdd:TIGR00618 511 IHPNPARQDIDNpgpltrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFS---ILTQCDNRSKEDIP 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1566 NLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATA------SAEQMTLVTQLKDVEERMANQAEK----FT 1635
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRlhlqqcSQELALKLTALHALQLTLTQERVRehalSI 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1636 REAANLKGSINELLL-----KLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQ 1710
Cdd:TIGR00618 668 RVLPKELLASRQLALqkmqsEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKE 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1711 LRDNKSEIYQrHTELTKEVELGRNRIGELTKKCEElcsDLENSDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTR--EC 1788
Cdd:TIGR00618 748 LMHQARTVLK-ARTEAHFNNNEEVTAALQTGAELS---HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILnlQC 823
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 442627456 1789 EKLRFDMQSKEVQNESKVQELIS---ECEELRSTLKSKEASFQSEKE 1832
Cdd:TIGR00618 824 ETLVQEEEQFLSRLEEKSATLGEithQLLKYEECSKQLAQLTQEQAK 870
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
8-140 |
2.00e-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: 2.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 8 SIQVCIKVRPCEPGLTSLWQVKERRSIHLADSHAEPYVFDYVFDEGASNQEVFDRMaKHIVHACMQGFNGTIFAYGQTSS 87
Cdd:pfam16796 21 NIRVFARVRPELLSEAQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQEI-SQLVQSCLDGYNVCIFAYGQTGS 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 442627456 88 GKtytmmgdeqNPGVMVLAAKEIFQQISS-ETERDFLLRVGYIEIYNEKIYDLL 140
Cdd:pfam16796 100 GS---------NDGMIPRAREQIFRFISSlKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1204-1877 |
3.85e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.01 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1204 AKDELHDVRRIKDdeisALRMEFLLQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELEA 1283
Cdd:PTZ00121 1120 AKKKAEDARKAEE----ARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRK 1195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1284 LKSAHKENISQAVEERNNLIVQHQAEMETIRETLKnklaEASTQQSKMEDAFRAEI--NEVRATLMEQLNQTKEDRDKGA 1361
Cdd:PTZ00121 1196 AEDARKAEAARKAEEERKAEEARKAEDAKKAEAVK----KAEEAKKDAEEAKKAEEerNNEEIRKFEEARMAHFARRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1362 SKLEEVKKTLEQMINGGRVMSDTIAELE--------KTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQmESLTRDQISfE 1433
Cdd:PTZ00121 1272 IKAEEARKADELKKAEEKKKADEAKKAEekkkadeaKKKAEEAKKADEAKKKAEEAKKKADAAKKKAE-EAKKAAEAA-K 1349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1434 IEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMK----VLSNRNE 1509
Cdd:PTZ00121 1350 AEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKkadeAKKKAEE 1429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1510 KEKCDFETKLETFTFKITDL----------EEVLKEAQHKVILyDDLVSQHERLKIClAEANELSSNLQKKVMSLHTELI 1579
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAkkkaeeakkaEEAKKKAEEAKKA-DEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAAE 1507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1580 DSQKGISSRDVEINELREELKAAMDAKAT---------ASAEQMTLVTQLKDVEERMANQAEKFTREAANLKGSINELLL 1650
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKAdeakkaeekKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAK 1587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1651 KLnsmqETKDMLESGNEELKEQLRNSQNLRNMLDEESKmcislKEKLVKLEDAKTSLEQqLRDNKSEIYQRHTELTKEVE 1730
Cdd:PTZ00121 1588 KA----EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK-----AEELKKAEEEKKKVEQ-LKKKEAEEKKKAEELKKAEE 1657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1731 LGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQ---KVDEVTRECEKLRfdmqSKEVQNESKVQ 1807
Cdd:PTZ00121 1658 ENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkKEAEEKKKAEELK----KAEEENKIKAE 1733
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1808 ELISECEElrstlKSKEASFQSEKESMDRTISSLLEDKRNLEEKLCSANDIVAKLETEIAALRPRKSLDR 1877
Cdd:PTZ00121 1734 EAKKEAEE-----DKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
625-1122 |
3.89e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 68.53 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 625 EELEKLIADLESKKNSCEC--DQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDAL 702
Cdd:PRK02224 254 ETLEAEIEDLRETIAETERerEELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEC 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 703 DQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASSAEFQRlQNDNTKFQADIASLNERLEEAQnmlTEVQN 782
Cdd:PRK02224 334 RVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR-REEIEELEEEIEELRERFGDAP---VDLGN 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 783 SESTVEKLRIQNHELTAKIKELETNFEEMQreydclsnqlmESVQENDALREEIKQrPT--SHVEESMRSSGISSDfDEQ 860
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATLRTAR-----------ERVEEAEALLEAGKC-PEcgQPVEGSPHVETIEED-RER 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 861 KQDinllhqfvqLSESVQQIELQHHSGISRLFRANQMKldQSEPGLKLCLESAEYIEEDNRQSDATepiclkgfLKRHRF 940
Cdd:PRK02224 477 VEE---------LEAELEDLEEEVEEVEERLERAEDLV--EAEDRIERLEERREDLEELIAERRET--------IEEKRE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 941 QIKRL---SQEHVDMGEEKRllDIISQLEQEIE---EKSALMEATEATINEMREQMTNLESALLEksviinkVEDYQRQI 1014
Cdd:PRK02224 538 RAEELrerAAELEAEAEEKR--EAAAEAEEEAEearEEVAELNSKLAELKERIESLERIRTLLAA-------IADAEDEI 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1015 ESLEKQNAEMTMVYEE----LQDRVTRESSMSESLlrvppDEDTLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAE- 1089
Cdd:PRK02224 609 ERLREKREALAELNDErrerLAEKRERKRELEAEF-----DEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEi 683
|
490 500 510
....*....|....*....|....*....|....*
gi 442627456 1090 --LENHLRQiqlkdgnIARLQTDFEEMSERCLSME 1122
Cdd:PRK02224 684 gaVENELEE-------LEELRERREALENRVEALE 711
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
562-1367 |
5.15e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.56 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 562 KSSKLRVDDLLSALLEKESTI-----ESLQKSLDNLTRDVlrNSKEGHMLSIAPEQEDIAgdsicNKCEELEKLIADLE- 635
Cdd:TIGR02169 207 REKAERYQALLKEKREYEGYEllkekEALERQKEAIERQL--ASLEEELEKLTEEISELE-----KRLEEIEQLLEELNk 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 636 --SKKNSCECDQLRLEIVSVRDKLESVESAFNL--------------ASSEIIQKATDCERLSKELSTSQNAFGQLQERY 699
Cdd:TIGR02169 280 kiKDLGEEEQLRVKEKIGELEAEIASLERSIAEkereledaeerlakLEAEIDKLLAEIEELEREIEEERKRRDKLTEEY 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 700 DALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRaRSASSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTE 779
Cdd:TIGR02169 360 AELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE-INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 780 VqnsESTVEKLRiqnheltAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEI--KQRPTSHVEESMRSSGISSDF 857
Cdd:TIGR02169 439 L---EEEKEDKA-------LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELskLQRELAEAEAQARASEERVRG 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 858 DEQKQDInllhqfvqLSESVQQIelqhHSGISRLFRAnqmkldqsEPGLKLCLESAEYIEEDN--RQSDATEPICLKgFL 935
Cdd:TIGR02169 509 GRAVEEV--------LKASIQGV----HGTVAQLGSV--------GERYATAIEVAAGNRLNNvvVEDDAVAKEAIE-LL 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 936 KRHR------FQIKRLSQEHVDMGEEKR------LLDIIsQLEQEIEE-------KSALMEATEATINEM-REQMTNLES 995
Cdd:TIGR02169 568 KRRKagratfLPLNKMRDERRDLSILSEdgvigfAVDLV-EFDPKYEPafkyvfgDTLVVEDIEAARRLMgKYRMVTLEG 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 996 ALLEKSviinkvedyqrqieslekqnAEMTMVYEELQDRVTRESSMSESLLRVPPDEDTLpgcptspsrrEQEVATLKTS 1075
Cdd:TIGR02169 647 ELFEKS--------------------GAMTGGSRAPRGGILFSRSEPAELQRLRERLEGL----------KRELSSLQSE 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1076 ITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSErclsmevRLAELDEDTKQKQelldrqaQKLSDDLCLIDQ 1155
Cdd:TIGR02169 697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKE-------RLEELEEDLSSLE-------QEIENVKSELKE 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1156 LQKKNAQLVEQYHKATESLSLADAKPDQillssqydSQIEKLNQLLNAAKDELHDVR-RIKDDEISALRMEFLLQIETNE 1234
Cdd:TIGR02169 763 LEARIEELEEDLHKLEEALNDLEARLSH--------SRIPEIQAELSKLEEEVSRIEaRLREIEQKLNRLTLEKEYLEKE 834
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1235 KENQAKFYAELQETKDRYESNVAEL---KEKLLQVEETLSSVTVRCQAELEALKSAHKENISQ--AVEERNNLIVQHQAE 1309
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQlrELERKIEELEAQIEK 914
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 442627456 1310 METIRETLKNKLAEASTQQSKMEDAFRAEINEVRATL-MEQLNQTKEDRDKGASKLEEV 1367
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELsLEDVQAELQRVEEEIRALEPV 973
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1337-1850 |
5.33e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.17 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1337 AEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMinggrvmSDTIAELEKTKAEqdlaVNKLTKDNIELEKQCSKT 1416
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKL-------EKEVKELEELKEE----IEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1417 QEQLQMeslTRDQISfEIEAHIKKLELIVasskKRIIELEEKCDQqVLELDKCRLEKLSLESEIQKANSEHSctmEKLQE 1496
Cdd:PRK03918 258 EEKIRE---LEERIE-ELKKEIEELEEKV----KELKELKEKAEE-YIKLSEFYEEYLDELREIEKRLSRLE---EEING 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1497 LQAEMKVLSNRNEKekcdfetkLETFTFKITDLEEVLKEAQHKVILYDD---LVSQHERLKICLA-----EANELSSNLQ 1568
Cdd:PRK03918 326 IEERIKELEEKEER--------LEELKKKLKELEKRLEELEERHELYEEakaKKEELERLKKRLTgltpeKLEKELEELE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1569 KKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATA-----------SAEQMTLVT-QLKDVEERMA---NQAEK 1633
Cdd:PRK03918 398 KAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelteehRKELLEEYTaELKRIEKELKeieEKERK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1634 FTREAANLKGSINEL--LLKLNSMQETKDMLES-----GNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLED---A 1703
Cdd:PRK03918 478 LRKELRELEKVLKKEseLIKLKELAEQLKELEEklkkyNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEElkkK 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1704 KTSLEQQLRDNKSEIYQRHTELTkevELGRNRIGELTKKCEELCS------DLENSDQirlDLQETKEQLKKTLENNLGW 1777
Cdd:PRK03918 558 LAELEKKLDELEEELAELLKELE---ELGFESVEELEERLKELEPfyneylELKDAEK---ELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627456 1778 QQKVDEVTRECEKLRFDMQSKEVQ-NESKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEE 1850
Cdd:PRK03918 632 FEELAETEKRLEELRKELEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1229-2069 |
5.72e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.16 E-value: 5.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1229 QIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSsvtvRCQAELEALKSAH--KENISQAVEERNNLIVQH 1306
Cdd:TIGR02168 221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQ----ELEEKLEELRLEVseLEEEIEELQKELYALANE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1307 QAEMETIRETLKNKLAEASTQQskmedafrAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIA 1386
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQL--------EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1387 ELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQL-----QMESLT--RDQISFEIEAHIKKL-ELIVASSKKRIIELEEK 1458
Cdd:TIGR02168 369 ELESRLEELEEQLETLRSKVAQLELQIASLNNEIerleaRLERLEdrRERLQQEIEELLKKLeEAELKELQAELEELEEE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1459 CDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRnekekcdfETKLETFTFKITDLEEVLKEAQH 1538
Cdd:TIGR02168 449 LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL--------QENLEGFSEGVKALLKNQSGLSG 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1539 KVILYDDLVSQHERLKICLAEAneLSSNLQKKVMslhtelidsqKGISSRDVEINELREELKAamdaKATASAEQMTLVT 1618
Cdd:TIGR02168 521 ILGVLSELISVDEGYEAAIEAA--LGGRLQAVVV----------ENLNAAKKAIAFLKQNELG----RVTFLPLDSIKGT 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1619 QLKDVEERMANQAEKFTREAANLKGSINELLLKLNSMqetkdmleSGNEELKEQLRNSQNLRNMLDEESkMCISLKEKLV 1698
Cdd:TIGR02168 585 EIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYL--------LGGVLVVDDLDNALELAKKLRPGY-RIVTLDGDLV 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1699 kledaktsleqqlrdNKSEIYQRHTELTKEVELGRNR-IGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLEnnlGW 1777
Cdd:TIGR02168 656 ---------------RPGGVITGGSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELE---QL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1778 QQKVDEVTRECEKLRFDMQSKEvQNESKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEKLCSAND 1857
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLE-AEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1858 IVAKLETEIAALRPRKSLDRNPVPRKSITFESEIRKNRRISVHDERRQSYWNDVREfgimtdpvdnncNCAELNSKLQDC 1937
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE------------DIESLAAEIEEL 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1938 QRELfiresqvTALKMELDHHplkdenaqltkrvIEEQDKAKVEQKRLKMKLQDLNARINDLTTASAKEPESNQMAQAAK 2017
Cdd:TIGR02168 865 EELI-------EELESELEAL-------------LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL 924
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627456 2018 PATVAAQTQTESDLETILEKTNVKYQ----EAVRMLRYRYHLIQELKEKLRQNENS 2069
Cdd:TIGR02168 925 AQLELRLEGLEVRIDNLQERLSEEYSltleEAEALENKIEDDEEEARRRLKRLENK 980
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1012-1346 |
1.07e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1012 RQIESLEKQnAEMTMVYEELQDRVtRESSMSESLLRVppdedtlpgcptspSRREQEVATLKTSITELQSQVSDLKAELE 1091
Cdd:COG1196 200 RQLEPLERQ-AEKAERYRELKEEL-KELEAELLLLKL--------------RELEAELEELEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1092 NHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQyhKAT 1171
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE--LEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1172 ESLSLADAKPDQILLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDDEISALRMEFLLQIETNEKENQAkfyAELQETKDR 1251
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE---EALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1252 YESNVAELKEKLLQVEETLSSV--TVRCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQS 1329
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEeeALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
330
....*....|....*..
gi 442627456 1330 kMEDAFRAEINEVRATL 1346
Cdd:COG1196 499 -AEADYEGFLEGVKAAL 514
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
625-989 |
1.40e-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: 67.00 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 625 EELEKLIADLESKknsceCDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQ 704
Cdd:TIGR02168 680 EELEEKIEELEEK-----IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 705 QWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLE------SRARSASSAEFQRLQNDNTKFQADIASLNERLEEAQNML- 777
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEaqieqlKEELKALREALDELRAELTLLNEEAANLRERLESLERRIa 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 778 ---TEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQrptshVEESMRSsgIS 854
Cdd:TIGR02168 835 ateRRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE-----LSEELRE--LE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 855 SDFDEQKQDINLL-HQFVQLSESVQQIELQHHSGISRLfrANQMKLDQSEPglklcLESAEYIEEDNRQsdatepicLKG 933
Cdd:TIGR02168 908 SKRSELRRELEELrEKLAQLELRLEGLEVRIDNLQERL--SEEYSLTLEEA-----EALENKIEDDEEE--------ARR 972
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627456 934 FLKRHRFQIKRLSQehVDMG-------EEKRLLDIISQLEQEIEEKSALMEATEATINEMREQ 989
Cdd:TIGR02168 973 RLKRLENKIKELGP--VNLAaieeyeeLKERYDFLTAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1261-2065 |
2.48e-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: 66.22 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1261 EKLLQVEETLSSVTVRCQAELEALKsahkENISQAVEERNNlIVQHQAEMETIRETLKNKLAEASTQQSKMEdafraEIN 1340
Cdd:TIGR00606 189 ETLRQVRQTQGQKVQEHQMELKYLK----QYKEKACEIRDQ-ITSKEAQLESSREIVKSYENELDPLKNRLK-----EIE 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1341 EVRATLME------QLNQTKEDRDKGASKLEEVKK-----TLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIEL 1409
Cdd:TIGR00606 259 HNLSKIMKldneikALKSRKKQMEKDNSELELKMEkvfqgTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1410 EKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKAN----- 1484
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQLcadlq 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1485 SEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVlkEAQHKVILYDDLVSQHERLKICLAEANELS 1564
Cdd:TIGR00606 419 SKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQL--EGSSDRILELDQELRKAERELSKAEKNSLT 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1565 SNLQKKVMSLHTELIDSQKGISSRDVEINELREElKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLKGS 1644
Cdd:TIGR00606 497 ETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHH-TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQL 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1645 INELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKL---EDAKTSLEQqLRDNKSEIYQR 1721
Cdd:TIGR00606 576 EDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgsQDEESDLER-LKEEIEKSSKQ 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1722 HTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQ 1801
Cdd:TIGR00606 655 RAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPG 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1802 NESKVQELISECEELRSTLKSKEASFQSEKESMDR------TISSLLEDKRNLE------EKLCSANDIVAKLETEIAAL 1869
Cdd:TIGR00606 735 RQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEqetllgTIMPEEESAKVCLtdvtimERFQMELKDVERKIAQQAAK 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1870 RPRKSLDRNPVP---------RKSITFESEIRKNRRISV-HDERRQSYWNDVREFGIMTDPVDNNCNCA--------ELN 1931
Cdd:TIGR00606 815 LQGSDLDRTVQQvnqekqekqHELDTVVSKIELNRKLIQdQQEQIQHLKSKTNELKSEKLQIGTNLQRRqqfeeqlvELS 894
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1932 SKLQDCQRELFIRESQVTALKMELDHhpLKDENAQLTKRVIEEQDKAKVEQKRLKMKLQDLNARINDLTTASAKEPESNQ 2011
Cdd:TIGR00606 895 TEVQSLIREIKDAKEQDSPLETFLEK--DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYL 972
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442627456 2012 MAQAAKPATVAAQ--------TQTESDLETILEKTNVKYQEAVRM-----LRYRYHLIQELKEKLRQ 2065
Cdd:TIGR00606 973 KQKETELNTVNAQleecekhqEKINEDMRLMRQDIDTQKIQERWLqdnltLRKRENELKEVEEELKQ 1039
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1465-1767 |
2.55e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1465 ELDKcRLEKLSLESEiqKAnsehsctmEKLQELQAEMKVLSNR---NEKEkcDFETKLETFTFKITDLEEVLKEAQHKVi 1541
Cdd:COG1196 197 ELER-QLEPLERQAE--KA--------ERYRELKEELKELEAElllLKLR--ELEAELEELEAELEELEAELEELEAEL- 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1542 lyDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLK 1621
Cdd:COG1196 263 --AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1622 DVEERMANQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLE 1701
Cdd:COG1196 341 ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627456 1702 DAKTSLEQQLRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQL 1767
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
935-1680 |
4.32e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.47 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 935 LKRHRFQIKRLSQEHVDMGEEKRLLDI-ISQLEQEIEEKSALMEATEATI-----NEMREQMTNLESALLEKSVIINKVE 1008
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEeISELEKRLEEIEQLLEELNKKIkdlgeEEQLRVKEKIGELEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1009 DYQRQIESLEKQNAEMTMVY-------EELQDRVTRESSMSESLL-RVPPDEDTLPGCPTSPSRREQEVATLKTSITELQ 1080
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIdkllaeiEELEREIEEERKRRDKLTeEYAELKEELEDLRAELEEVDKEFAETRDELKDYR 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1081 SQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLS---DDLCLIDQ-- 1155
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEqlaADLSKYEQel 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1156 --LQKKNAQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKL------------NQLLN-----------AAKDELHD 1210
Cdd:TIGR02169 472 ydLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVlkasiqgvhgtvAQLGSvgeryataievAAGNRLNN 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1211 VrRIKDDEISALRMEFLLQ--------IETNE-----------KENQAKFYA-ELQETKDRYESNVAELKEKLLQVEETL 1270
Cdd:TIGR02169 552 V-VVEDDAVAKEAIELLKRrkagratfLPLNKmrderrdlsilSEDGVIGFAvDLVEFDPKYEPAFKYVFGDTLVVEDIE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1271 SSVTVRCQAELEAL------KS--------AHKENISQAVEERNNLI-VQHQAE-METIRETLKNKLAEASTQQSKMEDA 1334
Cdd:TIGR02169 631 AARRLMGKYRMVTLegelfeKSgamtggsrAPRGGILFSRSEPAELQrLRERLEgLKRELSSLQSELRRIENRLDELSQE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1335 FRAEINEVRaTLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCS 1414
Cdd:TIGR02169 711 LSDASRKIG-EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1415 ktQEQLQmesltrdqisfEIEAHIKKLELIVASSKKRIIELEEKcdqqvleLDKCRLEKLSLESEIqkansehsctmekl 1494
Cdd:TIGR02169 790 --HSRIP-----------EIQAELSKLEEEVSRIEARLREIEQK-------LNRLTLEKEYLEKEI-------------- 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1495 QELQAEMKVLSNRnekeKCDFETKLETFTFKITDLEEVLKEAQHKVilyDDLVSQHERLKICLAEANELSSNLQKKVMSL 1574
Cdd:TIGR02169 836 QELQEQRIDLKEQ----IKSIEKEIENLNGKKEELEEELEELEAAL---RDLESRLGDLKKERDELEAQLRELERKIEEL 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1575 HTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLKG--SINELLLKL 1652
Cdd:TIGR02169 909 EAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAiqEYEEVLKRL 988
|
810 820
....*....|....*....|....*...
gi 442627456 1653 NSMQETKDMLESGNEELKEQLRNSQNLR 1680
Cdd:TIGR02169 989 DELKEKRAKLEEERKAILERIEEYEKKK 1016
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
506-1268 |
4.99e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.09 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 506 DALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRIMEVENQVAVGLEFEfEAHKKSSKLRvddllSALLEKESTIESL 585
Cdd:TIGR02169 247 ASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIG-ELEAEIASLE-----RSIAEKERELEDA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 586 QKSLDNLtrDVLRNSKEGHMLSIAPEQEDIAG------DSICNKCEELEKLIADLESKknSCECDQLRLEIVSVRDKLES 659
Cdd:TIGR02169 321 EERLAKL--EAEIDKLLAEIEELEREIEEERKrrdkltEEYAELKEELEDLRAELEEV--DKEFAETRDELKDYREKLEK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 660 VESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLEs 739
Cdd:TIGR02169 397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLK- 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 740 rarsassAEFQRLQNDNTKFQADIASLNERLEEAQnmlTEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYD-CL 818
Cdd:TIGR02169 476 -------EEYDRVEKELSKLQRELAEAEAQARASE---ERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEvAA 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 819 SNQLMESVQENDALREE----IKQR--------PTSHVEESMRSSGISS------------DFDEQKQdiNLLHQFVQLS 874
Cdd:TIGR02169 546 GNRLNNVVVEDDAVAKEaielLKRRkagratflPLNKMRDERRDLSILSedgvigfavdlvEFDPKYE--PAFKYVFGDT 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 875 ESVQQIE-------------------------------LQHHSGISRLFRANQMKLDQSEPGLKLCLES--AEYIEEDNR 921
Cdd:TIGR02169 624 LVVEDIEaarrlmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSlqSELRRIENR 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 922 QSDATEPIC-LKGFLKRHRFQIKRLSQEHVDMGEE-KRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESAL-- 997
Cdd:TIGR02169 704 LDELSQELSdASRKIGEIEKEIEQLEQEEEKLKERlEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALnd 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 998 LEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVtressmsesllrvppdedtlpgcptspSRREQEVATLKTSIT 1077
Cdd:TIGR02169 784 LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKL---------------------------NRLTLEKEYLEKEIQ 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1078 ELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQ 1157
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1158 KKNAQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKLNQllnaakdelhdVRRIKDDEISALRMEFLLQIEtnEKEN 1237
Cdd:TIGR02169 917 KRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQA-----------ELQRVEEEIRALEPVNMLAIQ--EYEE 983
|
810 820 830
....*....|....*....|....*....|.
gi 442627456 1238 QAKFYAELQETKDRYESNVAELKEKLLQVEE 1268
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1182-1869 |
5.96e-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: 64.70 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1182 DQILLSSQYDSQIEKlnqllnaAKDELHDVRRiKDDEISALRMEFLLQIETNEKE-NQAKFYAELQETKDRYE-----SN 1255
Cdd:TIGR02169 160 DEIAGVAEFDRKKEK-------ALEELEEVEE-NIERLDLIIDEKRQQLERLRRErEKAERYQALLKEKREYEgyellKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1256 VAELKEKLLQVEETLSSVTvRCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQSKMEDAF 1335
Cdd:TIGR02169 232 KEALERQKEAIERQLASLE-EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1336 RAEINEVRaTLMEQLNQTKEDRDKGASKLEEVKKTLEQ-----------MINGGRVMSDTIAELEKTKAEQDLAVNKLTK 1404
Cdd:TIGR02169 311 AEKERELE-DAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklteeYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1405 DNIELEK----------QCSKTQEQLQMESLTRDQISFEI---EAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRL 1471
Cdd:TIGR02169 390 YREKLEKlkreinelkrELDRLQEELQRLSEELADLNAAIagiEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1472 EKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKcdfetkletftfkitDLEEVLKEAQHKVI-LYDDLVSQH 1550
Cdd:TIGR02169 470 ELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGR---------------AVEEVLKASIQGVHgTVAQLGSVG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1551 ERLKICL----------------AEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMD--------AK 1606
Cdd:TIGR02169 535 ERYATAIevaagnrlnnvvveddAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDlvefdpkyEP 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1607 ATASAEQMTLVTQLKDVEERMANQAEKFTREAanlkgsinELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEE 1686
Cdd:TIGR02169 615 AFKYVFGDTLVVEDIEAARRLMGKYRMVTLEG--------ELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGL 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1687 SKMCISLKEKLVKLEDAKTSLEQQLRDNK---SEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQET 1763
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASrkiGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1764 KEQLKKTLENnlgWQQKVDEVTRECEKLRFDmqskEVQNE-SKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLL 1842
Cdd:TIGR02169 767 IEELEEDLHK---LEEALNDLEARLSHSRIP----EIQAElSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ 839
|
730 740
....*....|....*....|....*..
gi 442627456 1843 EDKRNLEEKLCSANDIVAKLETEIAAL 1869
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKEEL 866
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
625-839 |
8.35e-10 |
|
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: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 625 EELEKLIADLESKKNscECDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQ 704
Cdd:COG1196 253 AELEELEAELAELEA--ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 705 QWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASSAEFQRLQNDNTKFQADIASLNERLEEAQ---NMLTEVQ 781
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqleELEEAEE 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627456 782 NSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQR 839
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
769-1447 |
5.81e-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: 61.78 E-value: 5.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 769 RLEEAQNMLTEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVqenDALREEIKQRptshveesm 848
Cdd:pfam12128 235 GIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLL---RTLDDQWKEK--------- 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 849 rssgissdFDEQKQDINLLHQFVQLSES-VQQIELQHhsGISRLFRANQMKLDQS------------EPGLKLCLESAEY 915
Cdd:pfam12128 303 --------RDELNGELSAADAAVAKDRSeLEALEDQH--GAFLDADIETAAADQEqlpswqselenlEERLKALTGKHQD 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 916 IEE--DNRQSDATEpiclkgflkRHRFQIKRLSQEHVDMGEEK-RLLDIISQLEQEIEekSALMEATEATINEMREQMTN 992
Cdd:pfam12128 373 VTAkyNRRRSKIKE---------QNNRDIAGIKDKLAKIREARdRQLAVAEDDLQALE--SELREQLEAGKLEFNEEEYR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 993 LESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSMSESLLRVPPDEDTLPGCPTSPSRREQEVatl 1072
Cdd:pfam12128 442 LKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEER--- 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1073 KTSITELQSQVSDLKAELENHLR-QIQLKDGNIARL-------QTDFE-EMSERCLSMEVRLAELDEDTKQKQ------- 1136
Cdd:pfam12128 519 QSALDELELQLFPQAGTLLHFLRkEAPDWEQSIGKVispellhRTDLDpEVWDGSVGGELNLYGVKLDLKRIDvpewaas 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1137 -ELLDRQAQKLSDDL----CLIDQLQKKNAQLVEQYHKATESLSLA-----DAKPDQILLSSQYDSQIEKLNQLLNAAKD 1206
Cdd:pfam12128 599 eEELRERLDKAEEALqsarEKQAAAEEQLVQANGELEKASREETFArtalkNARLDLRRLFDEKQSEKDKKNKALAERKD 678
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1207 ELHDVRRikddeisalrmefllQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELEALKS 1286
Cdd:pfam12128 679 SANERLN---------------SLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRS 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1287 AHKENISQAVEERNNLIV------QHQAEMETIRETLKNKLAEASTQQSKMEDAFR------AEINEVRATLMEQLNQTK 1354
Cdd:pfam12128 744 GAKAELKALETWYKRDLAslgvdpDVIAKLKREIRTLERKIERIAVRRQEVLRYFDwyqetwLQRRPRLATQLSNIERAI 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1355 EDRDKGASKLEEVKKTLEQMINGGRVMSDTIA-----ELEKTKAEQD-LAVNKLTKDNIELEKQCSKTQEQLQMESLTRD 1428
Cdd:pfam12128 824 SELQQQLARLIADTKLRRAKLEMERKASEKQQvrlseNLRGLRCEMSkLATLKEDANSEQAQGSIGERLAQLEDLKLKRD 903
|
730
....*....|....*....
gi 442627456 1429 QISFEIEAHIKKLELIVAS 1447
Cdd:pfam12128 904 YLSESVKKYVEHFKNVIAD 922
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1305-2026 |
6.85e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 6.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1305 QHQAEMETIRETLKNKLAEASTQQSKME-DAFRAEINEVRatlmEQLNQTKEDRDKGASKLEEVKKTLEQMInggrvmsD 1383
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELALLVLRlEELREELEELQ----EELKEAEEELEELTAELQELEEKLEELR-------L 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1384 TIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLEL---IVASSKKRIIELEEKCD 1460
Cdd:TIGR02168 275 EVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDElaeELAELEEKLEELKEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1461 QQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSN---RNEKEKCDFETKLETFTFKITDLEEVLKEAQ 1537
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNeieRLEARLERLEDRRERLQQEIEELLKKLEEAE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1538 HKVI---------LYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQ-------------------------- 1582
Cdd:TIGR02168 435 LKELqaeleeleeELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslerlqenlegfsegvkallkn 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1583 ----KGISSRDVEINELREELKAAMDAkATASAEQMTLVTQLKDVEERMANQAEKFTREAANL----------KGSINEL 1648
Cdd:TIGR02168 515 qsglSGILGVLSELISVDEGYEAAIEA-ALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLpldsikgteiQGNDREI 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1649 LLKLNSMQETKDMLESGNEELK-------------EQLRNSQNLRNMLDEESkMCISLKEKLVKLE------DAKTSLEQ 1709
Cdd:TIGR02168 594 LKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvDDLDNALELAKKLRPGY-RIVTLDGDLVRPGgvitggSAKTNSSI 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1710 QLRDNKSEiyqrhtELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNlgwQQKVDEVTRECE 1789
Cdd:TIGR02168 673 LERRREIE------ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL---RKDLARLEAEVE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1790 KLRFDMQSKEVQNES---KVQELISECEELRSTLKSKEAsfqsEKESMDRTISSLLEDKRNLEEKLCSANDIVAKLETEI 1866
Cdd:TIGR02168 744 QLEERIAQLSKELTEleaEIEELEERLEEAEEELAEAEA----EIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1867 AALRPRKSLDRNPVPRKSITFESEIRKNRRISVHDERRQSYWNDVREFgimtdpvdnncnCAELNSKLQDCQRELFIRES 1946
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEEL------------IEELESELEALLNERASLEE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1947 QVTALKMELDHhpLKDENAQLTKRVIEEQDKAKVEQKRL---KMKLQDLNARINDLTTASAKEPESNQMAQAAKPATVAA 2023
Cdd:TIGR02168 888 ALALLRSELEE--LSEELRELESKRSELRRELEELREKLaqlELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965
|
...
gi 442627456 2024 QTQ 2026
Cdd:TIGR02168 966 DEE 968
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
958-1852 |
1.37e-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: 60.19 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 958 LLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTR 1037
Cdd:pfam01576 73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1038 ESSMSEsllrvppdeDTLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSER 1117
Cdd:pfam01576 153 ERKLLE---------ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQ 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1118 CLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKpdqillSSQYDSQIEKL 1197
Cdd:pfam01576 224 IAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAA------RNKAEKQRRDL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1198 NQLLNAAKDELHDV--RRIKDDEISALRMEFLLQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEetlssvtv 1275
Cdd:pfam01576 298 GEELEALKTELEDTldTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAK-------- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1276 RCQAELEALKSA-HKENISQAVEERnnLIVQHQAEMETIRETLKNKLAEAstqQSKMEDAFRAeinevRATLMEQLNqtk 1354
Cdd:pfam01576 370 RNKANLEKAKQAlESENAELQAELR--TLQQAKQDSEHKRKKLEGQLQEL---QARLSESERQ-----RAELAEKLS--- 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1355 edrdKGASKLEEVKKTLEqminggrvmsdtiaelektkaEQDLAVNKLTKDNIELEKQCSKTQEQLQMEslTRDQISfeI 1434
Cdd:pfam01576 437 ----KLQSELESVSSLLN---------------------EAEGKNIKLSKDVSSLESQLQDTQELLQEE--TRQKLN--L 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1435 EAHIKKLELIVASSKKRIIELEEKcdqqvleldkcrleKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCD 1514
Cdd:pfam01576 488 STRLRQLEDERNSLQEQLEEEEEA--------------KRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1515 FETKLETFTFKITDLEEVLKEAQHKVILYDDLVSQHERLKiclaeanELSSNLQKKVMSLHTELIDsQKGISSRDVEINE 1594
Cdd:pfam01576 554 LEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQR-------QLVSNLEKKQKKFDQMLAE-EKAISARYAEERD 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1595 LREELKAAMDAKATASAEQMTLVTQLKDVEERmANQAEKftREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLr 1674
Cdd:pfam01576 626 RAEAEAREKETRALSLARALEEALEAKEELER-TNKQLR--AEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQL- 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1675 nsqnlrnmldEEskmcisLKEKLVKLEDAKTSLEQQLRDNKSeiyQRHTELTKEVELGRNRIGELTKKCEELCSDLENSD 1754
Cdd:pfam01576 702 ----------EE------LEDELQATEDAKLRLEVNMQALKA---QFERDLQARDEQGEEKRRQLVKQVRELEAELEDER 762
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1755 QIR-----------LDLQETKEQLKKT-------LENNLGWQQKVDEVTRECEKLRFD-----MQSKEVQNESK------ 1805
Cdd:pfam01576 763 KQRaqavaakkkleLDLKELEAQIDAAnkgreeaVKQLKKLQAQMKDLQRELEEARASrdeilAQSKESEKKLKnleael 842
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 442627456 1806 --VQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEKL 1852
Cdd:pfam01576 843 lqLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARI 891
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
960-1764 |
1.43e-08 |
|
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: 60.52 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 960 DIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKsviinkvedyqrqieslekqnaemtmVYEELQDRVTRES 1039
Cdd:pfam15921 163 DMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASGKK--------------------------IYEHDSMSTMHFR 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1040 SMSESLLRVPPDEDTlpgcptspsrreqEVATLKTSITELQSQVSDLKAELENHLRQIqlkdgniarLQTDFEEMSERCL 1119
Cdd:pfam15921 217 SLGSAISKILRELDT-------------EISYLKGRIFPVEDQLEALKSESQNKIELL---------LQQHQDRIEQLIS 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1120 SMEVRLAELDEDTKQKQElldrQAQKLSDDLCLIdQLQKKNAQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKLNQ 1199
Cdd:pfam15921 275 EHEVEITGLTEKASSARS----QANSIQSQLEII-QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEK 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1200 LLNAAKDELHDVRRIKDDeisalrmefLLQIETNEKENQAKFYAELQetKDRYESNVAELKEKLLQVEETLSSVTV---- 1275
Cdd:pfam15921 350 QLVLANSELTEARTERDQ---------FSQESGNLDDQLQKLLADLH--KREKELSLEKEQNKRLWDRDTGNSITIdhlr 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1276 -----------RCQAELEALKSAHKENISQ---AVEERN---NLIVQHQAEMETIRETLKNKLAEASTQQSKMEDAFRAe 1338
Cdd:pfam15921 419 relddrnmevqRLEALLKAMKSECQGQMERqmaAIQGKNeslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERT- 497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1339 INEVRATLMEQ---LNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTK---AEQDLAVNKLTK---DNIEL 1409
Cdd:pfam15921 498 VSDLTASLQEKeraIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKlqmAEKDKVIEILRQqieNMTQL 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1410 EKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQqvLELDKCRLEKLSLE--SEIQKANSEH 1487
Cdd:pfam15921 578 VGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD--LELEKVKLVNAGSErlRAVKDIKQER 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1488 SCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKVILYDDLVSQHE-----RLKICLAEANE 1562
Cdd:pfam15921 656 DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdghAMKVAMGMQKQ 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1563 LSSN------LQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQA---EK 1633
Cdd:pfam15921 736 ITAKrgqidaLQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEvalDK 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1634 FTREAANLKGSINE-----LLLKLNSMQETKDMLESG---NEELKEQL-------------RNSQNLRNMLDEESKMCIS 1692
Cdd:pfam15921 816 ASLQFAECQDIIQRqeqesVRLKLQHTLDVKELQGPGytsNSSMKPRLlqpasftrthsnvPSSQSTASFLSHHSRKTNA 895
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1693 LKeklvklEDAKTSLEQQLRDNKSEIYQRHT-ELTKEVELGRN----RIGELTKKC---EELCSDLENSDQIRLDLQETK 1764
Cdd:pfam15921 896 LK------EDPTRDLKQLLQELRSVINEEPTvQLSKAEDKGRApslgALDDRVRDCiieSSLRSDICHSSSNSLQTEGSK 969
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
625-988 |
1.94e-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: 60.08 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 625 EELEKLIADLESKKNscECDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQ 704
Cdd:TIGR02169 674 AELQRLRERLEGLKR--ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 705 QWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASSAEFQRLQNDNTKFQADI--------ASLNERLEEAQNM 776
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIearlreieQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 777 LTEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQRptshvEESMRSsgISSD 856
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDEL-----EAQLRE--LERK 904
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 857 FDEQKQDINLLHQFVQLSESVQQIELQHHSGISRLFRAnqmklDQSEPGLKLCLES-AEYIEEDNRQSDATEPICLKGFl 935
Cdd:TIGR02169 905 IEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-----DEEIPEEELSLEDvQAELQRVEEEIRALEPVNMLAI- 978
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 442627456 936 krhrfqikrlsQEHVDmgEEKRLLDIISQLEQEIEEKSALMEATEATINEMRE 988
Cdd:TIGR02169 979 -----------QEYEE--VLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1337-2128 |
3.09e-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: 3.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1337 AEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMinggrvmsdtiaELEKTKAE---------QDLAVNKLTKDNI 1407
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERL------------RREREKAEryqallkekREYEGYELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1408 ELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELdKCRLEKLSLE-SEIQKANSE 1486
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIGELEAEiASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1487 HSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKvilYDDLVSQHERLKICLAEANELSSN 1566
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE---LEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1567 LQKKVMSLHTElidsqkgissrdveINELREELKAAMDAKATASAEQMTLVTQLKDVEERMAnqaekftreaanlkgsin 1646
Cdd:TIGR02169 390 YREKLEKLKRE--------------INELKRELDRLQEELQRLSEELADLNAAIAGIEAKIN------------------ 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1647 elllklnsmqETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLrdnkseiyqrhTELT 1726
Cdd:TIGR02169 438 ----------ELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL-----------AEAE 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1727 KEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQKV-----DEVTRECEKLRFDMQS---- 1797
Cdd:TIGR02169 497 AQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNNvvvedDAVAKEAIELLKRRKAgrat 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1798 ----KEVQNESKVQELIS------------ECEE---------LRSTLKSKeaSFQSEKESMD----------------- 1835
Cdd:TIGR02169 577 flplNKMRDERRDLSILSedgvigfavdlvEFDPkyepafkyvFGDTLVVE--DIEAARRLMGkyrmvtlegelfeksga 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1836 -----RTISSLLEDKRNLEEKLCSANDIVAKLETEIAALRPRKSLDRNPVPRKSITFESEIRKNRRISVHDERRQSYWND 1910
Cdd:TIGR02169 655 mtggsRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1911 VREfgimtdpvdnncNCAELNSKLQDCQRELFIRESQVTAL-----KMELDHHPLKDENAQLTKRVIEEQ--------DK 1977
Cdd:TIGR02169 735 LKE------------RLEELEEDLSSLEQEIENVKSELKELearieELEEDLHKLEEALNDLEARLSHSRipeiqaelSK 802
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1978 AKVEQKRLKMKLQDLNARINDLTTASAKEPESNQMAQAAKPAT---VAAQTQTESDLETILEKTNVKYQEAVRMLRyryH 2054
Cdd:TIGR02169 803 LEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEELEAALR---D 879
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627456 2055 LIQELKEKLRQNENsdtsnitslsagqtsaLKAQCESQKKEILAIKYKYEAAKRILAIRNDDLDALREKLAKYE 2128
Cdd:TIGR02169 880 LESRLGDLKKERDE----------------LEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1297-1825 |
4.96e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 58.51 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1297 EERNNLIVQHQAEMETIRET-LKNKLAEASTQQSKMEDAFRaEINEVRATLMEQLNQTKEDRDKGASKLEEVKkTLEQMI 1375
Cdd:PRK02224 183 SDQRGSLDQLKAQIEEKEEKdLHERLNGLESELAELDEEIE-RYEEQREQARETRDEADEVLEEHEERREELE-TLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1376 NGGRvmsDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEahikklelivasskkriiEL 1455
Cdd:PRK02224 261 EDLR---ETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARRE------------------EL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1456 EEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLsnrnEKEKCDFETKLETFTFKITDLEEVLKE 1535
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAEL----ESELEEAREAVEDRREEIEELEEEIEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1536 AQHKVilyDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQK----------------------------GISS 1587
Cdd:PRK02224 396 LRERF---GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARErveeaealleagkcpecgqpvegsphveTIEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1588 RDVEINELREELkAAMDAKATASAEQMTLVTQLKDVE---ERMANQAEKFTREAANLKGSINELLLKLNSMQETKDMLES 1664
Cdd:PRK02224 473 DRERVEELEAEL-EDLEEEVEEVEERLERAEDLVEAEdriERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1665 GNEELKEQLR----NSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLE--QQLRDNKSEIYQRHTELTKEVELGRNRIGE 1738
Cdd:PRK02224 552 EAEEKREAAAeaeeEAEEAREEVAELNSKLAELKERIESLERIRTLLAaiADAEDEIERLREKREALAELNDERRERLAE 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1739 LTKKCEELCSDLENSdqiRLD-LQETKEQLKKTLENnlgwqqkVDEVTRECEKLRFDMQSKEVQNESKVQELisecEELR 1817
Cdd:PRK02224 632 KRERKRELEAEFDEA---RIEeAREDKERAEEYLEQ-------VEEKLDELREERDDLQAEIGAVENELEEL----EELR 697
|
....*...
gi 442627456 1818 STLKSKEA 1825
Cdd:PRK02224 698 ERREALEN 705
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
504-1203 |
5.55e-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: 58.53 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 504 TYDALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRIMEVENQVAVGLEFEFEAHKKSSKLRVDDLLSALLEKESTIE 583
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 584 SLQKSLDNltrdvLRNSKEGHMLSIAPEQEDIAGDSICNKCEELEKLIADLESKKNSCECDQLRLEivSVRDKLESVESA 663
Cdd:TIGR02168 397 SLNNEIER-----LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELE--RLEEALEELREE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 664 FNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQ--AGITTLHEKHEHVQEKYQKLQEEYeqLESRA 741
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSglSGILGVLSELISVDEGYEAAIEAA--LGGRL 547
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 742 RSAssaefqrLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVEK---LRIQNHELTAKI-KELETNFEEMQREYDC 817
Cdd:TIGR02168 548 QAV-------VVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGndrEILKNIEGFLGVaKDLVKFDPKLRKALSY 620
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 818 LSNQLM--ESVQENDALREEIKQRPTSHVE--ESMRSSGISSdFDEQKQDINLLHQFVQLSESVQQIELQhhsgisrlfr 893
Cdd:TIGR02168 621 LLGGVLvvDDLDNALELAKKLRPGYRIVTLdgDLVRPGGVIT-GGSAKTNSSILERRREIEELEEKIEEL---------- 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 894 anQMKLDQSEPGLKLCLESAEYIEEDNRQSDAtEPICLKGFLKRHRFQIKRLSQEHVDMGEEKRLLDI-ISQLEQEIEEK 972
Cdd:TIGR02168 690 --EEKIAELEKALAELRKELEELEEELEQLRK-ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKeLTELEAEIEEL 766
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 973 SALMEATEATINEMREQMTNLESalleksviinKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSMSESLlrvppdE 1052
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEA----------QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESL------E 830
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1053 DTLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDT 1132
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627456 1133 KQKQELLDRQAQKLSDdlcLIDQLQKKNAQLVEQYHKATESLSL----ADAKPDQILLSSQY-DSQIEKLNQLLNA 1203
Cdd:TIGR02168 911 SELRRELEELREKLAQ---LELRLEGLEVRIDNLQERLSEEYSLtleeAEALENKIEDDEEEaRRRLKRLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1423-1742 |
6.44e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1423 ESLTR-DQISFEIEAHIKKLEL--IVASSKKRIIELEEKCDQQ--VLELDKCRLEKLSLESEIQKANsehsctmEKLQEL 1497
Cdd:COG1196 186 ENLERlEDILGELERQLEPLERqaEKAERYRELKEELKELEAEllLLKLRELEAELEELEAELEELE-------AELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1498 QAEMKVLsnrnekekcdfETKLETFTFKITDLEEVLKEAQHKvilYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTE 1577
Cdd:COG1196 259 EAELAEL-----------EAELEELRLELEELELELEEAQAE---EYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1578 LIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLKGSINELLLKLNSMQE 1657
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1658 TKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNKSEIYQRHTELTKEVELGRNRIG 1737
Cdd:COG1196 405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
....*
gi 442627456 1738 ELTKK 1742
Cdd:COG1196 485 ELAEA 489
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
694-1267 |
8.26e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.00 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 694 QLQERYDALDQQWQAQQAGITTLHekHEHVQEKYQKLQEEYEQLEsrarsassAEFQRLQNDNTKFQADIASLNERLEEA 773
Cdd:COG4913 259 ELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELR--------AELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 774 QNMLTEVQNSEstVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQRPTSHVEESMRssgI 853
Cdd:COG4913 329 EAQIRGNGGDR--LEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEA---L 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 854 SSDFDEQKQDI-NLLHQFVQLSESVQQIElQHHSGISR---LFR---ANQMKLDQSEP---------------------- 904
Cdd:COG4913 404 EEALAEAEAALrDLRRELRELEAEIASLE-RRKSNIPArllALRdalAEALGLDEAELpfvgelievrpeeerwrgaier 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 905 ---GLKLCLesaeyIEEDNRQSDATEpiclkgFLKRHRFQiKRLSQEHVDMGEEKRLLDIISQ----------------- 964
Cdd:COG4913 483 vlgGFALTL-----LVPPEHYAAALR------WVNRLHLR-GRLVYERVRTGLPDPERPRLDPdslagkldfkphpfraw 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 965 LEQEIEEKSALM--EATEATINE----MREQMT---------NLESALLEKSVI----INKVEDYQRQIESLEKQNAEMT 1025
Cdd:COG4913 551 LEAELGRRFDYVcvDSPEELRRHpraiTRAGQVkgngtrhekDDRRRIRSRYVLgfdnRAKLAALEAELAELEEELAEAE 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1026 MVYEELQ---DRVTRESSMSESLLRVPPDEDTLPGCPTSPSRREQEVATLKTS---ITELQSQVSDLKAELENHLRQIQL 1099
Cdd:COG4913 631 ERLEALEaelDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASsddLAALEEQLEELEAELEELEEELDE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1100 KDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQ-ELLDRQAQKLSDDLC---LIDQLQKKNAQLVEQYHKATESL- 1174
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDAVereLRENLEERIDALRARLNRAEEELe 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1175 -SLADAKPDQILLSSQYDSQIEKLNQLLnaakdELHDvrRIKDDEISALRMEFLLQIETNEKENQAKFYAELQETKDRYE 1253
Cdd:COG4913 791 rAMRAFNREWPAETADLDADLESLPEYL-----ALLD--RLEEDGLPEYEERFKELLNENSIEFVADLLSKLRRAIREIK 863
|
650
....*....|....
gi 442627456 1254 SNVAELKEKLLQVE 1267
Cdd:COG4913 864 ERIDPLNDSLKRIP 877
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
936-1373 |
2.30e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.93 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 936 KRHRFQIKRLSQEHVDMGEEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLEsALLEKSVIINKVEDYQRQIE 1015
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLE-KLLQLLPLYQELEALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1016 SLEKQNAEMTMVYEELQDRVTRESSMSESLLRVPPDEDTLpgCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLR 1095
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEEL--LEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1096 QIQLKDGNIARLQTDFEEMSERC---------------LSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKN 1160
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEErlkearlllliaaalLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1161 AQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKlnqllNAAKDELHDVRRIKDDEISALRMEFLLQIETNEKENQAK 1240
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSP-----EELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1241 FYAELQETKDRYESNvAELKEKLLQVEETLSSVTVRCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNK 1320
Cdd:COG4717 376 LAEAGVEDEEELRAA-LEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREE 454
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 442627456 1321 LAEASTQQSKMEDAFR-AEINEVRATLMEQLNQTKEDRDK---GASKLEEVKKTLEQ 1373
Cdd:COG4717 455 LAELEAELEQLEEDGElAELLQELEELKAELRELAEEWAAlklALELLEEAREEYRE 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1528-1825 |
3.16e-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: 3.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1528 DLEEVLKEAQHKVILYDDLVSQHErlkicLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKA 1607
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAE-----LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1608 TASAEQMTLVTQLKDVEERMANQAEkftrEAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEEs 1687
Cdd:COG1196 292 ELLAELARLEQDIARLEERRRELEE----RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA- 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1688 kmcislKEKLVKLEDAKTSLEQQLRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQL 1767
Cdd:COG1196 367 ------LLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627456 1768 KKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISECEELRSTLKSKEA 1825
Cdd:COG1196 441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1378-1852 |
3.42e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1378 GRVMSDTIAELEKTKA------EQDL--AVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLElivassk 1449
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAqieekeEKDLheRLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE------- 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1450 kRIIELEEKCDQQVLELDKCRLEKLSLESEIQkansEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDL 1529
Cdd:PRK02224 252 -ELETLEAEIEDLRETIAETEREREELAEEVR----DLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1530 EEVLKEAQHKVilyDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATA 1609
Cdd:PRK02224 327 RDRLEECRVAA---QAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1610 SaeqmtlvTQLKDVEERMANQAEkftrEAANLKGSINELLLKL----NSMQETKDMLESGN--------------EELKE 1671
Cdd:PRK02224 404 P-------VDLGNAEDFLEELRE----ERDELREREAELEATLrtarERVEEAEALLEAGKcpecgqpvegsphvETIEE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1672 QLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQ--QLRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELCSD 1749
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRieRLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1750 LEnsdQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRfdmqskevqNESKVQELISECEELRSTLKSKEASFQS 1829
Cdd:PRK02224 553 AE---EKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLE---------RIRTLLAAIADAEDEIERLREKREALAE 620
|
490 500
....*....|....*....|...
gi 442627456 1830 EKESMDRTISSLLEDKRNLEEKL 1852
Cdd:PRK02224 621 LNDERRERLAEKRERKRELEAEF 643
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
935-1502 |
4.84e-07 |
|
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: 55.11 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 935 LKRHRFQIKRLSQEHVDMGEEKR-----LLDIISQLEQEIEEKSALMEATEATINEMRE----QMTNLESALLEKSVIIN 1005
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDKEkqvslLLIQITEKENKMKDLTFLLEESRDKANQLEEktklQDENLKELIEKKDHLTK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1006 KVEDYQRqieSLEKQNAEMTMVYEELQDRVTRESSMSESllrvppDEDTLPGCPTSPSRREQEVATLKTSITELQSQVSD 1085
Cdd:pfam05483 297 ELEDIKM---SLQRSMSTQKALEEDLQIATKTICQLTEE------KEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1086 LKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLD--RQAQKLSDDLC-----LIDQLQK 1158
Cdd:pfam05483 368 EQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDekKQFEKIAEELKgkeqeLIFLLQA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1159 KNAQL-------------VEQYHKATESL--SLADAKPDQILLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDDEISALR 1223
Cdd:pfam05483 448 REKEIhdleiqltaiktsEEHYLKEVEDLktELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKK 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1224 ME--FLLQIETNEkENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELEALKSAHKE--NISQAVEER 1299
Cdd:pfam05483 528 QEerMLKQIENLE-EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKcnNLKKQIENK 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1300 NNLIVQHQAEmetiretlKNKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMinggr 1379
Cdd:pfam05483 607 NKNIEELHQE--------NKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKL----- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1380 vmsdtIAELEKTKAEQDLAVnKLTKdniELEKQCS-KTQEQLQMESLTRDQISFEIEAHIKKLELIvassKKRIIELEEK 1458
Cdd:pfam05483 674 -----LEEVEKAKAIADEAV-KLQK---EIDKRCQhKIAEMVALMEKHKHQYDKIIEERDSELGLY----KNKEQEQSSA 740
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 442627456 1459 CDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMK 1502
Cdd:pfam05483 741 KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILK 784
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
966-1815 |
5.55e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 54.98 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 966 EQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTM----VYEELQDRVTRESSM 1041
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLdylkLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1042 SESLLRVPPDEDTLpgcPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKdgniARLQTDFEEMSERCLSM 1121
Cdd:pfam02463 249 EQEEIESSKQEIEK---EEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLK----LERRKVDDEEKLKESEK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1122 EVRLAElDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKLNQLL 1201
Cdd:pfam02463 322 EKKKAE-KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1202 NAAKDELHDVRRIKDDEISALRMEFLLQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSvtVRCQAEL 1281
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE--DLLKETQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1282 EALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRDKGA 1361
Cdd:pfam02463 479 LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATAD 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1362 SKLEEVKKTLEqmINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTqEQLQMESLTRDQISFEIEAHIKKL 1441
Cdd:pfam02463 559 EVEERQKLVRA--LTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA-TLEADEDDKRAKVVEGILKDTELT 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1442 ELIVaSSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLET 1521
Cdd:pfam02463 636 KLKE-SAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKK 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1522 FTFKITDLEEVLKEAQHKVILYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKA 1601
Cdd:pfam02463 715 LKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1602 AMDAKATASAEqmtLVTQLKDVEERMANQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRN 1681
Cdd:pfam02463 795 KLKAQEEELRA---LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1682 MLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQ 1761
Cdd:pfam02463 872 LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKE 951
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 442627456 1762 ETKeqLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISECEE 1815
Cdd:pfam02463 952 ENN--KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEE 1003
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1337-1680 |
6.00e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1337 AEINEVRATLMEQLNQTKEDRDKgASKLEEVKKTLEQMinGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKT 1416
Cdd:COG1196 189 ERLEDILGELERQLEPLERQAEK-AERYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1417 QEQLQMESLTRDQISFEIEAHIKKLELIVAsskkRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQE 1496
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLA----ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1497 LQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKVILYDDLVSQHERLKICLAEANELSSNLQKKVMSLHT 1576
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1577 ELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEkftrEAANLKGSINELLLKLNSMQ 1656
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA----ALAELLEELAEAAARLLLLL 497
|
330 340
....*....|....*....|....
gi 442627456 1657 ETKDMLESGNEELKEQLRNSQNLR 1680
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRG 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
506-1037 |
6.99e-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: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 506 DALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRIMEVENQVAVGLEFEFEAHKKSSKLRVDDLLSALLEKESTIESL 585
Cdd:COG1196 242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 586 QKSLDNLTRDVLRNSKEghMLSIAPEQEDIAgdsicnkcEELEKLIADLESKKnscecdQLRLEIVSVRDKLESVESAFN 665
Cdd:COG1196 322 EEELAELEEELEELEEE--LEELEEELEEAE--------EELEEAEAELAEAE------EALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 666 LASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSAS 745
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 746 SA---EFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQN---------HELTAKIKELETNFEEmqR 813
Cdd:COG1196 466 AElleEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAglrglagavAVLIGVEAAYEAALEA--A 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 814 EYDCLSNQLMESVQENDALREEIKQRPTSHVEESMRSSGISSDFDEQKQDINLLHQFVQLSESvqqiELQHHSGISRLFR 893
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVAS----DLREADARYYVLG 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 894 ANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIKRLSQEHVDMGEEKRLLDIISQLEQEIEEKS 973
Cdd:COG1196 620 DTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEAL 699
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627456 974 ALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQ--------NAEMTMVYEELQDRVTR 1037
Cdd:COG1196 700 LAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEElleeealeELPEPPDLEELERELER 771
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1236-1851 |
8.47e-07 |
|
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: 54.34 E-value: 8.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1236 ENQAKFYAELQETKDRYESNVAELKEKLLQVEEtlssvtVRCQAELEALKSAHKenISQAVEERNNLIVQHQAEMETIRE 1315
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNNIEKMILAFEE------LRVQAENARLEMHFK--LKEDHEKIQHLEEEYKKEINDKEK 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1316 TLKNKLAEASTQQSKMED-AFRAEINEVRATLMEQ--------LNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIA 1386
Cdd:pfam05483 241 QVSLLLIQITEKENKMKDlTFLLEESRDKANQLEEktklqdenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQ 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1387 ------------------ELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIVASS 1448
Cdd:pfam05483 321 iatkticqlteekeaqmeELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1449 KKRIIELEEkcdqqvleLDKCRLEKLSLESEiqkaNSEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTfkiTD 1528
Cdd:pfam05483 401 NNKEVELEE--------LKKILAEDEKLLDE----KKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIK---TS 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1529 LEEVLKEAQhkvilydDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKAT 1608
Cdd:pfam05483 466 EEHYLKEVE-------DLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1609 ASAEQMTLVTQLKDVEERMANQAE----KFTREAANLKGSINELLLKLNSMQET-------KDMLESGNEELKEQLRNSQ 1677
Cdd:pfam05483 539 LEEKEMNLRDELESVREEFIQKGDevkcKLDKSEENARSIEYEVLKKEKQMKILenkcnnlKKQIENKNKNIEELHQENK 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1678 NLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDnKSEIYQRHTELTKEVElgRNRIGELTKKCEELCSDLENSDQIR 1757
Cdd:pfam05483 619 ALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEE-IIDNYQKEIEDKKISE--EKLLEEVEKAKAIADEAVKLQKEID 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1758 LDLQETKEQLKKTLENNlgwQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISECEELRSTLKSKEASFQSEKESMDRT 1837
Cdd:pfam05483 696 KRCQHKIAEMVALMEKH---KHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKL 772
|
650
....*....|....
gi 442627456 1838 ISSLLEDKRNLEEK 1851
Cdd:pfam05483 773 KMEAKENTAILKDK 786
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
694-1284 |
9.16e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 9.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 694 QLQERYDALDQQ-----WQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASsAEFQRLQNDNTKFQADIASLNE 768
Cdd:COG1196 217 ELKEELKELEAEllllkLRELEAELEELEAELEELEAELEELEAELAELEAELEELR-LELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 769 RLEEAQNMLT----EVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQrptshv 844
Cdd:COG1196 296 ELARLEQDIArleeRRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------ 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 845 EESMRSSGISSDFDEQKQDINLLHQFVQLSESVQQIELQHHSGISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSD 924
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 925 AtepiclkgfLKRHRFQIKRLSQEHVDMGEEKRLLDiisQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVII 1004
Cdd:COG1196 450 E---------EAELEEEEEALLELLAELLEEAALLE---AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1005 NkvedyQRQIESLEKQNAEMTMVYEelqdRVTRESSMSESLLRVPPDEDTLPGCptspsrREQEVATLKTSITELQSQVS 1084
Cdd:COG1196 518 G-----LRGLAGAVAVLIGVEAAYE----AALEAALAAALQNIVVEDDEVAAAA------IEYLKAAKAGRATFLPLDKI 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1085 DLKAELENHLRQIQLKDGnIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLV 1164
Cdd:COG1196 583 RARAALAAALARGAIGAA-VDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1165 EQYHKATESLSLADAKpdQILLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDDEISALRMEFLLQIETNEKENQAKFYAE 1244
Cdd:COG1196 662 LTGGSRRELLAALLEA--EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLE 739
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 442627456 1245 LQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELEAL 1284
Cdd:COG1196 740 ELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1615-1870 |
1.03e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1615 TLVTQLKDVE-ERMANQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKmciSL 1693
Cdd:COG1196 217 ELKEELKELEaELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEY---EL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1694 KEKLVKLEDAKTSLEQQLRDNKSEIyqrhTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLEN 1773
Cdd:COG1196 294 LAELARLEQDIARLEERRRELEERL----EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1774 NLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELisecEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEKLC 1853
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEEL----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250
....*....|....*..
gi 442627456 1854 SANDIVAKLETEIAALR 1870
Cdd:COG1196 446 EAAEEEAELEEEEEALL 462
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1063-1290 |
1.60e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1063 SRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQ 1142
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1143 AQKLSDdlcLIDQLQKKNAQlveqyhkATESLSLADAKPDQILLSSQYdsqiekLNQLLNAAKDELHDVRRIKdDEISAL 1222
Cdd:COG4942 103 KEELAE---LLRALYRLGRQ-------PPLALLLSPEDFLDAVRRLQY------LKYLAPARREQAEELRADL-AELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627456 1223 RMEFllqieTNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVtvrcQAELEALKSAHKE 1290
Cdd:COG4942 166 RAEL-----EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAEL----AAELAELQQEAEE 224
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1229-1869 |
1.60e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1229 QIETNEKE-NQAKFYAELQETKDRYESNVAELKEKLLQveetlssvtvrcqAELEALKSAHKENisqavEERNNLIVQHQ 1307
Cdd:COG1196 201 QLEPLERQaEKAERYRELKEELKELEAELLLLKLRELE-------------AELEELEAELEEL-----EAELEELEAEL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1308 AEMETIRETLKNKLAEASTQQSKMEDAFRAEINEVrATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAE 1387
Cdd:COG1196 263 AELEAELEELRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1388 LEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLelivASSKKRIIELEEKCDQQVLELD 1467
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA----AELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1468 KCRLEKLSLESEIQKANSEhsctmeKLQELQAEMKVLSNRNEKEkcdfeTKLETFTFKITDLEEVLKEAQHKVILYDDLV 1547
Cdd:COG1196 418 RLEEELEELEEALAELEEE------EEEEEEALEEAAEEEAELE-----EEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1548 SQHERLKICLAEANELSSNLQKKVMSLHteLIDSQKGISSRDVEINELREELKAAMDAKATASAEQmtlvtqlkDVEERM 1627
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAAL--LLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQN--------IVVEDD 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1628 ANQAEKFTREAANLKGSINELLLklnsmqetkDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSL 1707
Cdd:COG1196 557 EVAAAAIEYLKAAKAGRATFLPL---------DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1708 EQQLRDNKSEIYQRHTELTKEVELGRnrigeltkkceelcsdlensDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRE 1787
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEG--------------------EGGSAGGSLTGGSRRELLAALLEAEAELEELAER 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1788 CEKLRFDMQSKEVQNESKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEKLCSANDI--------- 1858
Cdd:COG1196 688 LAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEppdleeler 767
|
650
....*....|..
gi 442627456 1859 -VAKLETEIAAL 1869
Cdd:COG1196 768 eLERLEREIEAL 779
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
503-1278 |
1.99e-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: 53.30 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 503 LTYDALEKEVTSLRADNEAANSKI----SELEEKLSTLKQTMRIMEVENQVAvGLEFEFEAhKKSSKLRVDDLLSALLEK 578
Cdd:pfam12128 193 GKFRDVKSMIVAILEDDGVVPPKSrlnrQQVEHWIRDIQAIAGIMKIRPEFT-KLQQEFNT-LESAELRLSHLHFGYKSD 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 579 ESTIESLQKSLDNLTRDVlrnskeghmlsiaPEQEDIAGDSICNKCEELEKLIADLESKKNSCECDQLRLEIVSVRDKLE 658
Cdd:pfam12128 271 ETLIASRQEERQETSAEL-------------NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 659 SVESAfNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQ-QAGITTLHEKHEHVQEKYQKLQEE---- 733
Cdd:pfam12128 338 DIETA-AADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVaedd 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 734 YEQLESRARSassaefqRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQR 813
Cdd:pfam12128 417 LQALESELRE-------QLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVER 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 814 EYDCLSNQLMESVQENDALReeikqrptshvEESMRSSGISSDFDEQKQDI----NLLHQFVQ-----LSESVQQI---E 881
Cdd:pfam12128 490 LQSELRQARKRRDQASEALR-----------QASRRLEERQSALDELELQLfpqaGTLLHFLRkeapdWEQSIGKVispE 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 882 LQHHSGISRLFRANQMKLDQSEPGLKLCLEsaeyieednrQSDATEPICLKGFLKRHRFQIKRLSQEHVDMgeEKRLLDI 961
Cdd:pfam12128 559 LLHRTDLDPEVWDGSVGGELNLYGVKLDLK----------RIDVPEWAASEEELRERLDKAEEALQSAREK--QAAAEEQ 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 962 ISQLEQEIEEKSALMEATEATI-----------NEMREQMTNLESALLEKsviINKVEDYQRQIESLEKQNAEMTMVYEE 1030
Cdd:pfam12128 627 LVQANGELEKASREETFARTALknarldlrrlfDEKQSEKDKKNKALAER---KDSANERLNSLEAQLKQLDKKHQAWLE 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1031 LQDRVTRESSMS--ESLLRVPPDEDTLPGC--PTSPSRREQEVATLKTSITELQSQ----------VSDLKAELENHLRQ 1096
Cdd:pfam12128 704 EQKEQKREARTEkqAYWQVVEGALDAQLALlkAAIAARRSGAKAELKALETWYKRDlaslgvdpdvIAKLKREIRTLERK 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1097 IQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCL-IDQLQKKNAQLVEQYHKATESLS 1175
Cdd:pfam12128 784 IERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLrRAKLEMERKASEKQQVRLSENLR 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1176 LADAKPDQiLLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDDEISALRMEfllqIETNEKENQAKFYAELQETKDRYESN 1255
Cdd:pfam12128 864 GLRCEMSK-LATLKEDANSEQAQGSIGERLAQLEDLKLKRDYLSESVKKY----VEHFKNVIADHSGSGLAETWESLREE 938
|
810 820
....*....|....*....|...
gi 442627456 1256 VAELKEKLLQVEETLSSVTVRCQ 1278
Cdd:pfam12128 939 DHYQNDKGIRLLDYRKLVPYLEQ 961
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
962-1181 |
2.02e-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: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 962 ISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVED----YQRQIESLEKQNAEMTMVYEELQDRVTR 1037
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQelaaLEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1038 ESSMSESLLRVPPDEDTLPgcPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSER 1117
Cdd:COG4942 109 LLRALYRLGRQPPLALLLS--PEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627456 1118 clsmevrLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKP 1181
Cdd:COG4942 187 -------RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
515-816 |
2.75e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 515 LRADNEAANSKISELEEKLSTLKQTMRIMEVEnqvavglefefeahkkssklrVDDLLSALLEKESTIESLQKSLDNLTR 594
Cdd:COG1196 237 LEAELEELEAELEELEAELEELEAELAELEAE---------------------LEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 595 DVLRNSKEghmlsIAPEQEDIAGDSicnkcEELEKLIADLESKKNscECDQLRLEIVSVRDKLESVESAFNLASSEIIQK 674
Cdd:COG1196 296 ELARLEQD-----IARLEERRRELE-----ERLEELEEELAELEE--ELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 675 ATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASSAEfQRLQN 754
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE-EEEEE 442
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627456 755 DNTKFQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYD 816
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
570-832 |
3.22e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.61 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 570 DLLSALLEKESTIESLQKSLDNLTRDVLRNSKEGHMLSiAPEQEDIAgdsicnkcEELEKL-IADLESKKNScecdqlrl 648
Cdd:PRK11281 70 ALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALK-DDNDEETR--------ETLSTLsLRQLESRLAQ-------- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 649 eivsVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQ------------NAFGQLQERYDALDqQWQAQQAGITTL 716
Cdd:PRK11281 133 ----TLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSqrlqqirnllkgGKVGGKALRPSQRV-LLQAEQALLNAQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 717 HEKHEHVQEKYQKLQEeyeqLESRARSASSAEFQRLQNDNTKFQADIASlnERLEEAQNMLTEVQNSESTVeklRIQNHE 796
Cdd:PRK11281 208 NDLQRKSLEGNTQLQD----LLQKQRDYLTARIQRLEHQLQLLQEAINS--KRLTLSEKTVQEAQSQDEAA---RIQANP 278
|
250 260 270
....*....|....*....|....*....|....*.
gi 442627456 797 LTAkiKELETNFEemqreydcLSNQLMESVQENDAL 832
Cdd:PRK11281 279 LVA--QELEINLQ--------LSQRLLKATEKLNTL 304
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
506-838 |
4.51e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 506 DALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRIMEVENQvavglefEFEAHKKSSKLRVDDLLSALLEKESTIESL 585
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLG-------NAEDFLEELREERDELREREAELEATLRTA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 586 QKSLDNlTRDVLRNSKeghmlsiAPE-QEDIAGDSICNKCEELEKLIADLESkknscECDQLRLEIVSVRDKLESVESAF 664
Cdd:PRK02224 439 RERVEE-AEALLEAGK-------CPEcGQPVEGSPHVETIEEDRERVEELEA-----ELEDLEEEVEEVEERLERAEDLV 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 665 NLAS--SEIIQKATDCERLSKE----LSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLE 738
Cdd:PRK02224 506 EAEDriERLEERREDLEELIAErretIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELK 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 739 SRARSASSAEfqRLQNDNTKFQADIASLNERLEEAQNMLTEVQN----------------SESTVEKLRIQNHELTAKIK 802
Cdd:PRK02224 586 ERIESLERIR--TLLAAIADAEDEIERLREKREALAELNDERRErlaekrerkreleaefDEARIEEAREDKERAEEYLE 663
|
330 340 350
....*....|....*....|....*....|....*....
gi 442627456 803 ELETNFEEMQREYDCLSNQ---LMESVQENDALREEIKQ 838
Cdd:PRK02224 664 QVEEKLDELREERDDLQAEigaVENELEELEELRERREA 702
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1142-1769 |
5.41e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.83 E-value: 5.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1142 QAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKPDQIllsSQYDSQIEKLNQLLnaakDELHDVRRIKDDEISA 1221
Cdd:PRK01156 150 QRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKL---KSSNLELENIKKQI----ADDEKSHSITLKEIER 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1222 LRMEFllQIETNEKEN---QAKFYAELQETKDRYESNVAELKEKLLQVEETLSsvtvrcqaELEALKSAHKENISQAVEE 1298
Cdd:PRK01156 223 LSIEY--NNAMDDYNNlksALNELSSLEDMKNRYESEIKTAESDLSMELEKNN--------YYKELEERHMKIINDPVYK 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1299 RNNLIVQH---QAEMETIRETLKNKLAEASTQQSKMEdafRAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMI 1375
Cdd:PRK01156 293 NRNYINDYfkyKNDIENKKQILSNIDAEINKYHAIIK---KLSVLQKDYNDYIKKKSRYDDLNNQILELEGYEMDYNSYL 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1376 NGGRVMSDTIAELEKTKAEQDLAVNKLTK----DNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIvaSSKKR 1451
Cdd:PRK01156 370 KSIESLKKKIEEYSKNIERMSAFISEILKiqeiDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDEL--SRNME 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1452 IIELEEKC--------DQQVLELDKCRLEKLS-LESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETF 1522
Cdd:PRK01156 448 MLNGQSVCpvcgttlgEEKSNHIINHYNEKKSrLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESA 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1523 TFKITDLEEVLKEAQHKVILYDDLVSQHERLKICLAEANelssnlqkkvmslHTELIDSQKGISSRDVEINELREELKAa 1602
Cdd:PRK01156 528 RADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSK-------------RTSWLNALAVISLIDIETNRSRSNEIK- 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1603 mdakatasaeqmtlvTQLKDVEERMANQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGN---EELKEQLRNSQNL 1679
Cdd:PRK01156 594 ---------------KQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKiliEKLRGKIDNYKKQ 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1680 RNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNKSEIYqrhtELTKEVELGRNRIGELTKKCEELCSDLENSDQIRL- 1758
Cdd:PRK01156 659 IAEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRA----RLESTIEILRTRINELSDRINDINETLESMKKIKKa 734
|
650
....*....|...
gi 442627456 1759 --DLQETKEQLKK 1769
Cdd:PRK01156 735 igDLKRLREAFDK 747
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1338-1851 |
6.38e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1338 EINEVRATLMEQLNQTKEDRDKGASKLEEVKK----------TLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNI 1407
Cdd:TIGR04523 163 DLKKQKEELENELNLLEKEKLNIQKNIDKIKNkllklelllsNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEIN 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1408 ELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLElivaSSKKRIIELEEKCDQQVLELDKCRLEKL------------S 1475
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELE----QNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkelkselkN 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1476 LESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKVILYDDLVSQHERLKI 1555
Cdd:TIGR04523 319 QEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLES 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1556 CLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKAtasaEQMTLVTQLKDVEERMANQAEKFT 1635
Cdd:TIGR04523 399 KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS----VKELIIKNLDNTRESLETQLKVLS 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1636 REAANLKgsinelllklNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNK 1715
Cdd:TIGR04523 475 RSINKIK----------QNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1716 SEIYQRHTELTKevELGRNRIGELTKKCEELCSDLENSdqirLDLQETKEQLKKTLEnnlgwqQKVDEVTRECEKLRFDM 1795
Cdd:TIGR04523 545 DELNKDDFELKK--ENLEKEIDEKNKEIEELKQTQKSL----KKKQEEKQELIDQKE------KEKKDLIKEIEEKEKKI 612
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627456 1796 QSKEvQNESKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEK 1851
Cdd:TIGR04523 613 SSLE-KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKK 667
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
667-838 |
7.85e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 7.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 667 ASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEE----YEQLESRAR 742
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEieerREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 743 SA-----------------SSAEF-------QRLQNDNTKFQADIASLNERLEEAQNMLtevqnsESTVEKLRIQNHELT 798
Cdd:COG3883 94 ALyrsggsvsyldvllgseSFSDFldrlsalSKIADADADLLEELKADKAELEAKKAEL------EAKLAELEALKAELE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442627456 799 AKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQ 838
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1348-2067 |
1.03e-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: 51.13 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1348 EQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQD----LAVNKLTKDNIELEKQCSKTQEQLQME 1423
Cdd:pfam02463 176 KKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEyllyLDYLKLNEERIDLLQELLRDEQEEIES 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1424 SLTRDQISFEIEAHIKKL----ELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEhsctMEKLQELQA 1499
Cdd:pfam02463 256 SKQEIEKEEEKLAQVLKEnkeeEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE----KKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1500 EMKVLSNRNEKEKCDFETKLETFTFKITDLEEV-LKEAQHKVILYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTEL 1578
Cdd:pfam02463 332 KEKEEIEELEKELKELEIKREAEEEEEEELEKLqEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1579 IDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLKgsinELLLKLNSMQET 1658
Cdd:pfam02463 412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK----ETQLVKLQEQLE 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1659 KDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLV--KLEDAKTSLEQQLRDNKSEIYQRHTELTKEVELGRNRI 1736
Cdd:pfam02463 488 LLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAhgRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLV 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1737 GELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISECEEL 1816
Cdd:pfam02463 568 RALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESG 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1817 RSTLKSKEASFQSEKEsmDRTISSLLEDKRNLEEKLCSANDIVAKLETEIAALRPRKSLDRNPVPRKSITFESEIRKNRR 1896
Cdd:pfam02463 648 LRKGVSLEEGLAEKSE--VKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLAD 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1897 ISVHDERRQSYWNDVREFGIMtdpvDNNCNCAELNSKLQDCQRELFIRESQVTALKMELDHHPLKDENAQLTKRVIEEQD 1976
Cdd:pfam02463 726 RVQEAQDKINEELKLLKQKID----EEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1977 KAKVEQKRLKMKLQDLNARINDLTTASAKEPESNQMAQAAKPATVAAQTQTESDLETILEKTNVKYQEAVRMLRYRYHLI 2056
Cdd:pfam02463 802 ELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEE 881
|
730
....*....|.
gi 442627456 2057 QELKEKLRQNE 2067
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 ... |
1245-1868 |
1.21e-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: 50.56 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1245 LQETKDRYESNVAELKEKLLQVEETLSsvtvRCQAELEALKSAHKENISQAVEER------NNLIVQHQAEMETIRETLK 1318
Cdd:pfam01576 122 LQLEKVTTEAKIKKLEEDILLLEDQNS----KLSKERKLLEERISEFTSNLAEEEekakslSKLKNKHEAMISDLEERLK 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1319 nKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLeqminggrvmsdtiAELEKTKAEQDLA 1398
Cdd:pfam01576 198 -KEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL--------------ARLEEETAQKNNA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1399 VNKLTkdniELEKQCSKTQEQLQMESLTRDQ-------ISFEIEAHIKKLELIVASSKKRIiELEEKCDQQVLELDKC-R 1470
Cdd:pfam01576 263 LKKIR----ELEAQISELQEDLESERAARNKaekqrrdLGEELEALKTELEDTLDTTAAQQ-ELRSKREQEVTELKKAlE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1471 LEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKvilYDDLVSQH 1550
Cdd:pfam01576 338 EETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHK---RKKLEGQL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1551 ERLKICLAEANELSSNLQKKVMSLHTELiDSQKGIssrdveINELreELKAAMDAKATASAEqmtlvTQLKDVEERMANQ 1630
Cdd:pfam01576 415 QELQARLSESERQRAELAEKLSKLQSEL-ESVSSL------LNEA--EGKNIKLSKDVSSLE-----SQLQDTQELLQEE 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1631 aekfTREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLrnsQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQ 1710
Cdd:pfam01576 481 ----TRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQL---STLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRE 553
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1711 LrDNKSEIYQRHTELTKEVELGRNRigeLTKKCEELCSDLENSDQIRLDLQETKEQLKKTLEnnlgwQQKVDEVTRECEK 1790
Cdd:pfam01576 554 L-EALTQQLEEKAAAYDKLEKTKNR---LQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLA-----EEKAISARYAEER 624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1791 LRFDMQSKEvqNESKVQELISECEELRSTLKSKEASFQSEKESMDRTISS----------LLEDKRNLEEKLCSANDIVA 1860
Cdd:pfam01576 625 DRAEAEARE--KETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSkddvgknvheLERSKRALEQQVEEMKTQLE 702
|
....*...
gi 442627456 1861 KLETEIAA 1868
Cdd:pfam01576 703 ELEDELQA 710
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
730-1053 |
1.34e-05 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 50.31 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 730 LQEEYEQLESRARSASSAEFQRL-QNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQNHELTAK--IKELET 806
Cdd:PRK05771 14 LKSYKDEVLEALHELGVVHIEDLkEELSNERLRKLRSLLTKLSEALDKLRSYLPKLNPLREEKKKVSVKSLEelIKDVEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 807 NFEEMQREYDCLSNQLMEsvqendaLREEIKqrptshveesmrssgissdfdEQKQDINLLHQFVQLSESVqqIELQHHS 886
Cdd:PRK05771 94 ELEKIEKEIKELEEEISE-------LENEIK---------------------ELEQEIERLEPWGNFDLDL--SLLLGFK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 887 GISRlfRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIKRLSQEHVDMGEEKRLLDIISQLE 966
Cdd:PRK05771 144 YVSV--FVGTVPEDKLEELKLESDVENVEYISTDKGYVYVVVVVLKELSDEVEEELKKLGFERLELEEEGTPSELIREIK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 967 QEIEEKSALMEATEATINEMREQMTNLESALLEK-SVIINKVEDYQRQIESlekqnaEMTMV---------YEELQDRVT 1036
Cdd:PRK05771 222 EELEEIEKERESLLEELKELAKKYLEELLALYEYlEIELERAEALSKFLKT------DKTFAiegwvpedrVKKLKELID 295
|
330
....*....|....*..
gi 442627456 1037 RESSMSESLLRVPPDED 1053
Cdd:PRK05771 296 KATGGSAYVEFVEPDEE 312
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1446-1648 |
1.72e-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: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1446 ASSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLS---NRNEKEKCDFETKLETf 1522
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEaelAELEKEIAELRAELEA- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1523 tfKITDLEEVLKEAQH-------KVILYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINEL 1595
Cdd:COG4942 102 --QKEELAELLRALYRlgrqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442627456 1596 REELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLKGSINEL 1648
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
768-1281 |
2.41e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 768 ERLEEAQNMLTEVQNSESTVEklriqnhELTAKIKELETNFEEMQREYDCLSnqlmESVQENDALREEIKQRPTSHVEES 847
Cdd:PRK02224 234 ETRDEADEVLEEHEERREELE-------TLEAEIEDLRETIAETEREREELA----EEVRDLRERLEELEEERDDLLAEA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 848 MRSSGISSDFDEQKQDinLLHQFVQLSESVQQ--IELQHHSGISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDA 925
Cdd:PRK02224 303 GLDDADAEAVEARREE--LEDRDEELRDRLEEcrVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 926 TEPICLKGFLKRHRFQIKRLSQEHVDMGEEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESA--------L 997
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqP 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 998 LEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSMSESLLRVPPDEDTLpgcptspSRREQEVATLKTSIT 1077
Cdd:PRK02224 461 VEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERR-------EDLEELIAERRETIE 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1078 ELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAqKLSDDLCLIDQLQ 1157
Cdd:PRK02224 534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA-AIADAEDEIERLR 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1158 KKNAQLVEQYHKATESLSLADAKPDQiLLSSQYDSQIEKLNQLLNAAKDELHDVrrikDDEISALRMEF-LLQIETNEKE 1236
Cdd:PRK02224 613 EKREALAELNDERRERLAEKRERKRE-LEAEFDEARIEEAREDKERAEEYLEQV----EEKLDELREERdDLQAEIGAVE 687
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 442627456 1237 NQAKFYAELQETKDRYESNVAELkEKLLQVEETLSSVTVRCQAEL 1281
Cdd:PRK02224 688 NELEELEELRERREALENRVEAL-EALYDEAEELESMYGDLRAEL 731
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
725-1360 |
3.52e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 49.31 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 725 EKYQKLQEEYEQLESRARSASSAEFQRLQNDNTKF-----QADIASLNERLEEAQNMLTEVQNSESTVEKLRIQNHELTA 799
Cdd:COG5022 827 KREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFsllkkETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELES 906
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 800 KIKELetnfeemqreydclSNQLMESVQENDALREEIKQRPTSHVEESMRSSGISSDFDEQKQDINLLHQFVQLSESVQQ 879
Cdd:COG5022 907 EIIEL--------------KKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETSEE 972
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 880 IEL---QHHSGISRLFRAN-QMKLDQSEPGLKLCLESAeyIEEDNRQSDATEPIclkgfLKRHRFQIKRLSQEHVDMGEE 955
Cdd:COG5022 973 YEDllkKSTILVREGNKANsELKNFKKELAELSKQYGA--LQESTKQLKELPVE-----VAELQSASKIISSESTELSIL 1045
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 956 KRLLDIISQLEQEIEEKSALMEA-----------------------TEATINEMREQMTNLESALLEKSVIINKVE---- 1008
Cdd:COG5022 1046 KPLQKLKGLLLLENNQLQARYKAlklrrensllddkqlyqlestenLLKTINVKDLEVTNRNLVKPANVLQFIVAQmikl 1125
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1009 DYQRQIESLEKQNAE----MTMVYEELQDRVtressmsESLLRVPPDEDTLPGCP---TSPSRrEQEVATLKTSITELQS 1081
Cdd:COG5022 1126 NLLQEISKFLSQLVNtlepVFQKLSVLQLEL-------DGLFWEANLEALPSPPPfaaLSEKR-LYQSALYDEKSKLSSS 1197
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1082 QVSDLKAELENHLRQIQlKDGNIARLQTDF--EEMSERCLSMEVRLAELDEDTKQKQEllDRQAQKLSDDLCLIDQLQKK 1159
Cdd:COG5022 1198 EVNDLKNELIALFSKIF-SGWPRGDKLKKLisEGWVPTEYSTSLKGFNNLNKKFDTPA--SMSNEKLLSLLNSIDNLLSS 1274
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1160 NAQLVEQYHKateslsladakpdqillssqydsqieKLNQLLNAAKDELHDVRRIKDdeiSALRMEFLLQIETNEKENQA 1239
Cdd:COG5022 1275 YKLEEEVLPA--------------------------TINSLLQYINVGLFNALRTKA---SSLRWKSATEVNYNSEELDD 1325
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1240 KF--------YAELQETKDRyeSNVAELKEK-LLQVEETLSSVTVRCQAELEALKSAHkenisQAVEERNNLIVQHQAEM 1310
Cdd:COG5022 1326 WCrefeisdvDEELEELIQA--VKVLQLLKDdLNKLDELLDACYSLNPAEIQNLKSRY-----DPADKENNLPKEILKKI 1398
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 442627456 1311 ETirETLKNKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRDKG 1360
Cdd:COG5022 1399 EA--LLIKQELQLSLEGKDETEVHLSEIFSEEKSLISLDRNSIYKEEVLS 1446
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
679-1713 |
4.32e-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: 49.02 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 679 ERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASSAEfQRLQNDNTK 758
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELEEILHELESRLEEEEERS-QQLQNEKKK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 759 FQADIASLNERLEEaqnmltevqnSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSnqlmesvQENDALREEIKQ 838
Cdd:pfam01576 101 MQQHIQDLEEQLDE----------EEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLS-------KERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 839 RPTSHVEEsmrssgissdfdEQKqdinllhqfvqlSESVQQIELQHHSGISRLfranqmkldqsEPGLKLCLESAEYIEE 918
Cdd:pfam01576 164 FTSNLAEE------------EEK------------AKSLSKLKNKHEAMISDL-----------EERLKKEEKGRQELEK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 919 DNRQSDAtEPICLKGFLKRHRFQIKRLSQEHVDmgEEKRLLDIISQLEQEIEEKSALMEAteatINEMREQMTNLESALL 998
Cdd:pfam01576 209 AKRKLEG-ESTDLQEQIAELQAQIAELRAQLAK--KEEELQAALARLEEETAQKNNALKK----IRELEAQISELQEDLE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 999 EKSVIINKVEDYQRQIESlekqnaEMTMVYEELQDrvTRESSMSESLLRvppdedtlpgcptspSRREQEVATLKTSITE 1078
Cdd:pfam01576 282 SERAARNKAEKQRRDLGE------ELEALKTELED--TLDTTAAQQELR---------------SKREQEVTELKKALEE 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1079 ----LQSQVSDLKA-------ELENHLRQIQLKDGNIARLQTDFEEMSERcLSMEVR-LAELDEDTKQKQELLDRQAQKL 1146
Cdd:pfam01576 339 etrsHEAQLQEMRQkhtqaleELTEQLEQAKRNKANLEKAKQALESENAE-LQAELRtLQQAKQDSEHKRKKLEGQLQEL 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1147 SDDLcliDQLQKKNAQLVEQYHKATESLSLADAkpdqilLSSQYDSQIEKLNQLLNAAKDELHDVRRikddeisalrmef 1226
Cdd:pfam01576 418 QARL---SESERQRAELAEKLSKLQSELESVSS------LLNEAEGKNIKLSKDVSSLESQLQDTQE------------- 475
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1227 LLQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVtvrcQAELEALKSAHKE---NISQAVEERNNLi 1303
Cdd:pfam01576 476 LLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTL----QAQLSDMKKKLEEdagTLEALEEGKKRL- 550
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1304 vqhQAEMETIRETLKNKLAEAstqqSKMEDAFRAEINEVRATLMEQLNQTKEdrdkgASKLEEVKKTLEQMINGGRVMSD 1383
Cdd:pfam01576 551 ---QRELEALTQQLEEKAAAY----DKLEKTKNRLQQELDDLLVDLDHQRQL-----VSNLEKKQKKFDQMLAEEKAISA 618
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1384 TIAElEKTKAEQD--------LAVNKLTKDNIELEKQCSKTQEQLQ--MESL--TRDQIS---FEIEAHIKKLELIVASS 1448
Cdd:pfam01576 619 RYAE-ERDRAEAEareketraLSLARALEEALEAKEELERTNKQLRaeMEDLvsSKDDVGknvHELERSKRALEQQVEEM 697
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1449 KKRIIELEEKCdqQVLELDKCRLE------KLSLESEIQ----KANSEHSCTMEKLQELQAEMK----------VLSNRN 1508
Cdd:pfam01576 698 KTQLEELEDEL--QATEDAKLRLEvnmqalKAQFERDLQardeQGEEKRRQLVKQVRELEAELEderkqraqavAAKKKL 775
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1509 EKEKCDFETKLETFTFKITDLEEVLKEAQHKVILY----DDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKG 1584
Cdd:pfam01576 776 ELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLqrelEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERA 855
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1585 ISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQA-------EKFTREAANLKGSINELLLKLNSMQE 1657
Cdd:pfam01576 856 RRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQsntellnDRLRKSTLQVEQLTTELAAERSTSQK 935
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1658 T---KDMLESGNEELKEQLrnsQNLRNMLDEESKMCIS-LKEKLVKLEDaktSLEQQLRD 1713
Cdd:pfam01576 936 SesaRQQLERQNKELKAKL---QEMEGTVKSKFKSSIAaLEAKIAQLEE---QLEQESRE 989
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
955-1531 |
5.34e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 955 EKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDR 1034
Cdd:PRK03918 164 YKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1035 VTRESSmsesllrvppdedtlpgcptspsrREQEVATLKTSITELQSQVSDLKAELEN------HLRQIQLKDGNIARLQ 1108
Cdd:PRK03918 244 EKELES------------------------LEGSKRKLEEKIRELEERIEELKKEIEEleekvkELKELKEKAEEYIKLS 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1109 TDFEEMSERCLSMEVRLAELDEDTKQKQELLdrqaQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSL---ADAKPDQI- 1184
Cdd:PRK03918 300 EFYEEYLDELREIEKRLSRLEEEINGIEERI----KELEEKEERLEELKKKLKELEKRLEELEERHELyeeAKAKKEELe 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1185 -LLSSQYDSQIEKLNQLLNA---AKDELHDVRRIKDDEISALRmefllqietNEKENQAKFYAELQETKDR--------Y 1252
Cdd:PRK03918 376 rLKKRLTGLTPEKLEKELEElekAKEEIEEEISKITARIGELK---------KEIKELKKAIEELKKAKGKcpvcgrelT 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1253 ESNVAELKEKLLQVEETLSSVTVRCQAELEALKsAHKENISQAVEERNNLIVQHQA--EMETIRETLKNKLAEASTQQSK 1330
Cdd:PRK03918 447 EEHRKELLEEYTAELKRIEKELKEIEEKERKLR-KELRELEKVLKKESELIKLKELaeQLKELEEKLKKYNLEELEKKAE 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1331 MEDAFRAEINEVRATL------MEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMS-DTIAELEKTKAEQDLAVNK-L 1402
Cdd:PRK03918 526 EYEKLKEKLIKLKGEIkslkkeLEKLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEyL 605
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1403 TKDNIELEKQcsKTQEQLQMESLTRDQISFEIEAHIKKLELIvassKKRIIELEEKCDQQvlELDKCRLEKLSLESEIQK 1482
Cdd:PRK03918 606 ELKDAEKELE--REEKELKKLEEELDKAFEELAETEKRLEEL----RKELEELEKKYSEE--EYEELREEYLELSRELAG 677
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 442627456 1483 ANSEHSCTMEKLQELQAEMKVLSNRNEKEKcDFETKLETFTFKITDLEE 1531
Cdd:PRK03918 678 LRAELEELEKRREEIKKTLEKLKEELEERE-KAKKELEKLEKALERVEE 725
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1054-1330 |
5.59e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1054 TLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTK 1133
Cdd:COG3883 3 ALALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1134 QKQELLD---RQAQKLSDDLCLIDQLqkknaqlveqyhkaTESLSLADakpdqillssqYDSQIEKLNQLLNAAKDELHD 1210
Cdd:COG3883 83 ERREELGeraRALYRSGGSVSYLDVL--------------LGSESFSD-----------FLDRLSALSKIADADADLLEE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1211 VRRIKDdeisalrmefllQIETNEKENQAKFyAELQETKDRYESNVAELKEKllqveetlssvtvrcQAELEALKSAHKE 1290
Cdd:COG3883 138 LKADKA------------ELEAKKAELEAKL-AELEALKAELEAAKAELEAQ---------------QAEQEALLAQLSA 189
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 442627456 1291 NISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQSK 1330
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
515-1145 |
6.25e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 6.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 515 LRADNEAANSKISELEEKLSTLKQtmRIMEVENQVavglefefEAHKKSSKLRVDDLLSALLEK-ESTIESLQKSLDNLT 593
Cdd:pfam15921 215 FRSLGSAISKILRELDTEISYLKG--RIFPVEDQL--------EALKSESQNKIELLLQQHQDRiEQLISEHEVEITGLT 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 594 RDVlrNSKEGHMLSIAPEQEdIAGDSICNKCEELEKLIADLESKknsceCDQLRLEIVSVR----DKLESVESAFNLASS 669
Cdd:pfam15921 285 EKA--SSARSQANSIQSQLE-IIQEQARNQNSMYMRQLSDLEST-----VSQLRSELREAKrmyeDKIEELEKQLVLANS 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 670 EIIQKATDCERLSKElstSQNAFGQLQ---------ERYDALDQQ-----WQAQQAGITTLHEKHEHVQEK---YQKLQE 732
Cdd:pfam15921 357 ELTEARTERDQFSQE---SGNLDDQLQklladlhkrEKELSLEKEqnkrlWDRDTGNSITIDHLRRELDDRnmeVQRLEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 733 EYEQLESRARSASSAEFQRLQNDNTKFQaDIASLNERLEEAQNMLTEVQnSESTVEKLRIQNHE-----LTAKIKELETN 807
Cdd:pfam15921 434 LLKAMKSECQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVV-EELTAKKMTLESSErtvsdLTASLQEKERA 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 808 FEEMQREYDCLSNQLMESVQENDALREEIKQRPTSHVEesmrSSGISSDFDEQKQDINLLHQFVqlsESVQQIELQH--H 885
Cdd:pfam15921 512 IEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTE----CEALKLQMAEKDKVIEILRQQI---ENMTQLVGQHgrT 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 886 SGISRLFRA------NQMKLDQSEPGLKLCLESAEYIEEDNRQSD-ATEPICLKGFLKRHRFQIKRLSQEHVDMGEE--- 955
Cdd:pfam15921 585 AGAMQVEKAqlekeiNDRRLELQEFKILKDKKDAKIRELEARVSDlELEKVKLVNAGSERLRAVKDIKQERDQLLNEvkt 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 956 -KRLLDIISQ----LEQEIEEKSalmEATEATINEMREQMTNLESALleksviinkvEDYQRQIESLEKQNAEMTMVYEE 1030
Cdd:pfam15921 665 sRNELNSLSEdyevLKRNFRNKS---EEMETTTNKLKMQLKSAQSEL----------EQTRNTLKSMEGSDGHAMKVAMG 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1031 LQDRVTRESSMSESLlrvppdEDTLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAElENHLRqiqlkdGNIARLQTD 1110
Cdd:pfam15921 732 MQKQITAKRGQIDAL------QSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATE-KNKMA------GELEVLRSQ 798
|
650 660 670
....*....|....*....|....*....|....*
gi 442627456 1111 FEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQK 1145
Cdd:pfam15921 799 ERRLKEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
655-1117 |
7.00e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 655 DKLESVESAFNLASS---EIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQ--AGITTLHEKHEHVQEKYQK 729
Cdd:COG4717 71 KELKELEEELKEAEEkeeEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 730 LQEEYEQLESRarsassaefqrlqndntkfQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQnheltakikELETNFE 809
Cdd:COG4717 151 LEERLEELREL-------------------EEELEELEAELAELQEELEELLEQLSLATEEELQ---------DLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 810 EMQREYDCLSNQLMESVQENDALREEIKQRPTSHVEEsmrssgissdfdEQKQDINLLHQFVQLSESVQQIELQHHSGIS 889
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAA------------ALEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 890 RLFRAnqMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIKRLSQEHvdMGEEKRLLDIISQLEQEI 969
Cdd:COG4717 271 LILTI--AGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL--GLPPDLSPEELLELLDRI 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 970 EEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNaEMTMVYEELQDRVTRESSMSESLLRVP 1049
Cdd:COG4717 347 EELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEAL 425
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627456 1050 PDEDTlpgcptspsrrEQEVATLKTSITELQSQVSDL---KAELENHLRQIQlKDGNIARLQTDFEEMSER 1117
Cdd:COG4717 426 DEEEL-----------EEELEELEEELEELEEELEELreeLAELEAELEQLE-EDGELAELLQELEELKAE 484
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
649-838 |
7.35e-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: 7.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 649 EIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQ 728
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 729 KLQEEY-EQLESRARSA---------SSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVE----KLRIQN 794
Cdd:COG4942 101 AQKEELaELLRALYRLGrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEaeraELEALL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442627456 795 HELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQ 838
Cdd:COG4942 181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1227-1451 |
1.17e-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: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1227 LLQIETNEKENQAKFyAELQETKDRYESNVAELKEKLLQVEETLSSVtvrcQAELEALKSAHKENISQAVEERNNLIVQH 1306
Cdd:COG4942 29 LEQLQQEIAELEKEL-AALKKEEKALLKQLAALERRIAALARRIRAL----EQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1307 QAEMETIRETLKNKLAEAST---QQSKMEDAFRA-----EINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGg 1378
Cdd:COG4942 104 EELAELLRALYRLGRQPPLAlllSPEDFLDAVRRlqylkYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE- 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627456 1379 rvMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQmesltrdqisfEIEAHIKKLELIVASSKKR 1451
Cdd:COG4942 183 --LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE-----------ELEALIARLEAEAAAAAER 242
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
625-1451 |
1.38e-04 |
|
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: 47.27 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 625 EELEKLIADLESKKNSCECDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQ 704
Cdd:pfam02463 221 LEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKS 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 705 QWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESrarsassaEFQRLQNDNTKFQADIASLNERLEE-AQNMLTEVQNS 783
Cdd:pfam02463 301 ELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE--------EIEELEKELKELEIKREAEEEEEEElEKLQEKLEQLE 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 784 ESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQRPTSHVEESmrssgissdfdEQKQD 863
Cdd:pfam02463 373 EELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEE-----------ESIEL 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 864 INLLHQFVQLSESVQQIELQHHSGISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIK 943
Cdd:pfam02463 442 KQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 944 RLSQehvdmGEEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNAE 1023
Cdd:pfam02463 522 GRII-----SAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAV 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1024 MTMVYEELQDRVTRESSMSESLLRVPPDEDTLPGCPTSPSRREQEVATlktsITELQSQVSDLKAELENHLRQIQLKDGN 1103
Cdd:pfam02463 597 LEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK----ESGLRKGVSLEEGLAEKSEVKASLSELT 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1104 IARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKPDQ 1183
Cdd:pfam02463 673 KELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1184 ILLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDDEISALRMEFLLQIETNEKENQAKFYAELQETKDRYESNVAELKEKL 1263
Cdd:pfam02463 753 EKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKE 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1264 LQVEETLSSVTVRCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEA-STQQSKMEDAFRAEINEV 1342
Cdd:pfam02463 833 EELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEkEKEEKKELEEESQKLNLL 912
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1343 RATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQM 1422
Cdd:pfam02463 913 EEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNK 992
|
810 820
....*....|....*....|....*....
gi 442627456 1423 ESLTRDQISFEIEAHIKKLELIVASSKKR 1451
Cdd:pfam02463 993 DELEKERLEEEKKKLIRAIIEETCQRLKE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
943-1516 |
2.38e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 943 KRLSQEHVDMGEEKRLLDIISQLEQEIEEKSalmeatEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNA 1022
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKA------DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKE 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1023 EMTMVYEELQDRVTRESSMSEslLRVPPDEDTLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKD- 1101
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADE--AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKk 1452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1102 GNIARLQTDFEEMSERCLSMEvRLAELDEDTKQKQELLDR--QAQKLSDDLCLIDQLQKKNAQL--VEQYHKATESLSLA 1177
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKKAD-EAKKKAEEAKKADEAKKKaeEAKKKADEAKKAAEAKKKADEAkkAEEAKKADEAKKAE 1531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1178 DAKPDQILLSSQYDSQIEKLNQLLNAAKDE----LHDVRRIKDDEISALR-MEFLLQIETNEKENQAKFYAElqetkdry 1252
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEekkkAEEAKKAEEDKNMALRkAEEAKKAEEARIEEVMKLYEE-------- 1603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1253 esnvaelkEKLLQVEETLSSVTVRCQAElealksahkeNISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQSKME 1332
Cdd:PTZ00121 1604 --------EKKMKAEEAKKAEEAKIKAE----------ELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE 1665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1333 DAFRAEINEVRAtlmEQLNQTKEDRDKGASKL---EEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDniel 1409
Cdd:PTZ00121 1666 EAKKAEEDKKKA---EEAKKAEEDEKKAAEALkkeAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKE---- 1738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1410 EKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIE-LEEKCDQQVLELDKCRLEKLSLESEIQKANSEHS 1488
Cdd:PTZ00121 1739 AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGN 1818
|
570 580 590
....*....|....*....|....*....|..
gi 442627456 1489 CTMEKLQELQ----AEMKVLSNRNEKEKCDFE 1516
Cdd:PTZ00121 1819 LVINDSKEMEdsaiKEVADSKNMQLEEADAFE 1850
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1243-1772 |
2.62e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1243 AELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELE--ALKSAHKENISQAVEERNNLIVQHQAEMETIRETLK-- 1318
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAeaGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQah 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1319 NKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEqminggrvmsdtiaELEKTKAEQDLA 1398
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIE--------------ELRERFGDAPVD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1399 VNKLTKDNIELEKQCSKTQEQLQmesltrdqisfEIEAHIKKLElivasskKRIIEleekcDQQVLELDKCRleklslES 1478
Cdd:PRK02224 407 LGNAEDFLEELREERDELREREA-----------ELEATLRTAR-------ERVEE-----AEALLEAGKCP------EC 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1479 EIQKANSEHSCTMEKLQElqaemkvlsnrnekekcdfetkletftfKITDLEEVLKEAQHKVilyDDLVSQHERLKICLA 1558
Cdd:PRK02224 458 GQPVEGSPHVETIEEDRE----------------------------RVEELEAELEDLEEEV---EEVEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1559 EANELSSNLQKKvmSLHTELIDSQK-GISSRDVEINELRE---ELKAAMDAKATASAEQMtlvtqlkDVEERMANQAEKF 1634
Cdd:PRK02224 507 AEDRIERLEERR--EDLEELIAERReTIEEKRERAEELREraaELEAEAEEKREAAAEAE-------EEAEEAREEVAEL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1635 TREAANLKGSInELLLKLNSMQETKDMLESGNEELKEQLrnsQNLRNMLDEEskmcislKEKLVKLEDAKTSLEQQLRDN 1714
Cdd:PRK02224 578 NSKLAELKERI-ESLERIRTLLAAIADAEDEIERLREKR---EALAELNDER-------RERLAEKRERKRELEAEFDEA 646
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442627456 1715 K-SEIYQRHTELTKEVELGRNRIGELTKKCEELCSD---LENSDQIRLDLQETKEQLKKTLE 1772
Cdd:PRK02224 647 RiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigaVENELEELEELRERREALENRVE 708
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1662-2127 |
2.85e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1662 LESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRdnKSEIYQRHTELTKEVELGRNRIGELTK 1741
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ--LLPLYQELEALEAELAELPERLEELEE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1742 KCEELCSDLENSDQIRLDLQETKEQLKKTLEN-NLGWQQKVDEVTRECEKLRFDMQSKEV---QNESKVQELISECEELR 1817
Cdd:COG4717 154 RLEELRELEEELEELEAELAELQEELEELLEQlSLATEEELQDLAEELEELQQRLAELEEeleEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1818 STLKSKEASFQSEKESMDRTISSLLEDKRNLEEKLCSANDIVAKLETEIAALRPRKSLDRNPVPRKSITFESEIRKNRRI 1897
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1898 SVHDERRQSYWNDVREFGIMTDPvdnncncaELNSKLQDCQRELFIRESQVTALKMELDHHPLKDENAQLTKRVIEEQDK 1977
Cdd:COG4717 314 EELEEEELEELLAALGLPPDLSP--------EELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEE 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1978 AKVEQKRLKMKLQDLNARINDLTtasakepesNQMAQAAKPATVAAQTQTESDLETILEKTNVKYQEAVRMLRYRYHLIQ 2057
Cdd:COG4717 386 ELRAALEQAEEYQELKEELEELE---------EQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627456 2058 ELKEKLRQNENSDTsnITSLSAgQTSALKAQCESQKKEILAIKYKYEAAKRIL-AIRNDDLDALREKLAKY 2127
Cdd:COG4717 457 ELEAELEQLEEDGE--LAELLQ-ELEELKAELRELAEEWAALKLALELLEEAReEYREERLPPVLERASEY 524
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
561-1175 |
2.90e-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: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 561 KKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSkegHMLSIAPEQEDIAGdsiCNKceELEKLIADLESKKNS 640
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRAR---KAAPLAAHIKAVTQ---IEQ--QAQRIHTELQSKMRS 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 641 cecdqlRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKElSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKH 720
Cdd:TIGR00618 323 ------RAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDA-HEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKL 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 721 EHVQEKYQKLQEEYEQLESRArSASSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQNHELTAK 800
Cdd:TIGR00618 396 QSLCKELDILQREQATIDTRT-SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 801 IKELEtNFEEMQREYDCLSNQLMESVQENDALREEikqrPTSHVEESMRSSGISSDfdEQKQDINLLHQFVQLSESVQQI 880
Cdd:TIGR00618 475 LQTKE-QIHLQETRKKAVVLARLLELQEEPCPLCG----SCIHPNPARQDIDNPGP--LTRRMQRGEQTYAQLETSEEDV 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 881 ELQHHSGISRLFR-ANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIKRLSQEHVDMGEEKRLL 959
Cdd:TIGR00618 548 YHQLTSERKQRASlKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 960 DIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRES 1039
Cdd:TIGR00618 628 QDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLR 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1040 SMSESLLRVPPD-EDTLPGCPTSPSRREQEVATLKTSITELQSQV-SDLKAELENHLRQIQLKdgnIARLQTDfEEMSER 1117
Cdd:TIGR00618 708 ELETHIEEYDREfNEIENASSSLGSDLAAREDALNQSLKELMHQArTVLKARTEAHFNNNEEV---TAALQTG-AELSHL 783
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627456 1118 CLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLS 1175
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKS 841
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
723-1683 |
2.98e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 2.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 723 VQEKYQKLQEEyeQLESRARSASSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQNHELTAKIK 802
Cdd:TIGR00606 195 RQTQGQKVQEH--QMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 803 ELETNFEEMQREYDCLSNQLMESVQENDALREEIKQRPTSHVEESMRS-SGISSDFDEQKQDINLLHQfvqlsesvQQIE 881
Cdd:TIGR00606 273 ALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERElVDCQRELEKLNKERRLLNQ--------EKTE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 882 LQHHsgISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFlkrHRFQIKRLSQEhvdmgeekrlLDI 961
Cdd:TIGR00606 345 LLVE--QGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNF---HTLVIERQEDE----------AKT 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 962 ISQLEQEIEEKSALmeaTEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESlEKQNAEMTMvyeelQDRVTRESSM 1041
Cdd:TIGR00606 410 AAQLCADLQSKERL---KQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIK-ELQQLEGSS-----DRILELDQEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1042 SESLLRVPPDEdtlpgcptspsrREQEVATLKTSITELQSQvsdlKAELENHLRQIQLKDGNIARLQTDFEEMSERCLSM 1121
Cdd:TIGR00606 481 RKAERELSKAE------------KNSLTETLKKEVKSLQNE----KADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDK 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1122 EVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQlVEQYHKATESLSLADAKPDQilLSSQYDSQIEKLNQLL 1201
Cdd:TIGR00606 545 MDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKE-INQTRDRLAKLNKELASLEQ--NKNHINNELESKEEQL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1202 NAAKDELHDVRRIKDDEISALRMEFLLQ-------------------IETNEKENQA---------KFYAELQETKDRYE 1253
Cdd:TIGR00606 622 SSYEDKLFDVCGSQDEESDLERLKEEIEksskqramlagatavysqfITQLTDENQSccpvcqrvfQTEAELQEFISDLQ 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1254 SNVAELKEKLLQVEETLSSVTVRcqAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQ-QSKME 1332
Cdd:TIGR00606 702 SKLRLAPDKLKSTESELKKKEKR--RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLlGTIMP 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1333 DAFRAEINEVRATLMEQLNQtkedrdkgasKLEEVKKTLEQMIN--GGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELE 1410
Cdd:TIGR00606 780 EEESAKVCLTDVTIMERFQM----------ELKDVERKIAQQAAklQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNR 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1411 KQCSKTQEQLQMESLTRDQISFEieahikklELIVASSKKRIIELEEKCDQQVLELDKCRleklsleSEIQKANSEHSCT 1490
Cdd:TIGR00606 850 KLIQDQQEQIQHLKSKTNELKSE--------KLQIGTNLQRRQQFEEQLVELSTEVQSLI-------REIKDAKEQDSPL 914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1491 MEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKVilYDDLVSQHERLKICLAEANELSSNLQKK 1570
Cdd:TIGR00606 915 ETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKI--QDGKDDYLKQKETELNTVNAQLEECEKH 992
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1571 VMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQmTLVTQLKDV-EERMANQAEKFTREAANLKGSINELL 1649
Cdd:TIGR00606 993 QEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEE-ELKQHLKEMgQMQVLQMKQEHQKLEENIDLIKRNHV 1071
|
970 980 990
....*....|....*....|....*....|....*.
gi 442627456 1650 LKLNSMQETKDMLESGNEELKE-QLRNSQ-NLRNML 1683
Cdd:TIGR00606 1072 LALGRQKGYEKEIKHFKKELREpQFRDAEeKYREMM 1107
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
962-1205 |
3.67e-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: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 962 ISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSViinKVEDYQRQIESLEKQNAEMTMVYEELQDRV-TRESS 1040
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQA---ELEALQAEIDKLQAEIAEAEAEIEERREELgERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1041 MSESLLRVPPDEDTLPGcpTSPS---RREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQTDfeemser 1117
Cdd:COG3883 95 LYRSGGSVSYLDVLLGS--ESFSdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1118 clsMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKL 1197
Cdd:COG3883 166 ---LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
....*...
gi 442627456 1198 NQLLNAAK 1205
Cdd:COG3883 243 AASAAGAG 250
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
620-1148 |
3.83e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 620 ICNKCEELEKLIADLESKKNscecdqlrlEIVSVRDKLESVESAFNLASSEIIQKATDCERLSK---ELSTSQNAFGQLQ 696
Cdd:PRK03918 174 IKRRIERLEKFIKRTENIEE---------LIKEKEKELEEVLREINEISSELPELREELEKLEKevkELEELKEEIEELE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 697 ERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSASS-AEFQRLQNDNTKFQADI----ASLNERLE 771
Cdd:PRK03918 245 KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyIKLSEFYEEYLDELREIekrlSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 772 EAQNMLTEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQReydclsnqLMESVQENDALREEIKQRPTSHVEESM--- 848
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE--------AKAKKEELERLKKRLTGLTPEKLEKELeel 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 849 --RSSGISSDFDEQKQDINLLHQFV-QLSESVqqIELQHHSGISRLFRAnqmKLDQSEPGLKLclesAEYIEEDNR-QSD 924
Cdd:PRK03918 397 ekAKEEIEEEISKITARIGELKKEIkELKKAI--EELKKAKGKCPVCGR---ELTEEHRKELL----EEYTAELKRiEKE 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 925 ATEPICLKGFLKRHRFQIKRLSQEHVDMGEEKRLLDIISQLE--------QEIEEKSALMEATEATINEMREQMTNLESA 996
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEeklkkynlEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 997 LLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSMSESLLRVPPDE-DTLPGCPTSPSRREQEVATLKTS 1075
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEyLELKDAEKELEREEKELKKLEEE 627
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627456 1076 ITELQSQVSDLKAELENhLRQiQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSD 1148
Cdd:PRK03918 628 LDKAFEELAETEKRLEE-LRK-ELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
954-1378 |
4.12e-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: 45.71 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 954 EEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESAlleksviiNKVEDYQRQIESLEKQNAEMTMVYEELQD 1033
Cdd:COG3096 304 EQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALRQQ--------EKIERYQEDLEELTERLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1034 RVTRessmsesllrvppdedtlpgCPTSPSRREQEVATLKtsitelqSQVSDLKAEL-ENHLRQIQ----LKDGNIARLQ 1108
Cdd:COG3096 376 QLAE--------------------AEARLEAAEEEVDSLK-------SQLADYQQALdVQQTRAIQyqqaVQALEKARAL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1109 TDFEEMSERclSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKnAQLVEQYHKATESlSLADAKPDQILlsS 1188
Cdd:COG3096 429 CGLPDLTPE--NAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKA-YELVCKIAGEVER-SQAWQTARELL--R 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1189 QYDSQiEKLNQLLNAAKDELHDVRRIKDDEISALRM--EFLLQI--ETNEKENQAKFYAELQETKDRYESNVAELKEKLL 1264
Cdd:COG3096 503 RYRSQ-QALAQRLQQLRAQLAELEQRLRQQQNAERLleEFCQRIgqQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1265 QveetlssvtvrCQAELEALKSAHKENISQAVEERnnlivQHQAEMETIREtlknklaeastqQSKMEDAFRAEINEVRA 1344
Cdd:COG3096 582 E-----------LRQQLEQLRARIKELAARAPAWL-----AAQDALERLRE------------QSGEALADSQEVTAAMQ 633
|
410 420 430
....*....|....*....|....*....|....
gi 442627456 1345 TLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGG 1378
Cdd:COG3096 634 QLLEREREATVERDELAARKQALESQIERLSQPG 667
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1577-1873 |
4.65e-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: 45.44 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1577 ELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVE-ERmaNQAEKF---TREAANLKGSinELLLKL 1652
Cdd:TIGR02169 157 KIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRrER--EKAERYqalLKEKREYEGY--ELLKEK 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1653 NSMQETKDMLESGNEELKEQLRNSQNLRNMLDEEskmcisLKEKLVKLEDaktsLEQQLRDNKSEIYQRHTEltkevelg 1732
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKR------LEEIEQLLEE----LNKKIKDLGEEEQLRVKE-------- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1733 rnRIGELTKKCEELCSDLENSDQIRLDLQET----KEQLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQE 1808
Cdd:TIGR02169 295 --KIGELEAEIASLERSIAEKERELEDAEERlaklEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627456 1809 LISECEELRST------LKSKEASFQSEKESMDRTISSLLEDKRNLEEKLCSANDIVAKLETEIAALRPRK 1873
Cdd:TIGR02169 373 LEEVDKEFAETrdelkdYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEK 443
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
696-1037 |
4.75e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.72 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 696 QERYDALDQQWQAQQAGITTLHEKHEHVQEKyQKLQEEYEQLESRARSASSAEfqRLQNDNTKFQADIASLNERLEEaQN 775
Cdd:PRK04863 293 RELYTSRRQLAAEQYRLVEMARELAELNEAE-SDLEQDYQAASDHLNLVQTAL--RQQEKIERYQADLEELEERLEE-QN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 776 MLTEVQNSESTveklriqnheltakikELETNFEEMQREYDCLSNQLMESVQENDAL-REEIKQRPTSHVEESMRSSGIS 854
Cdd:PRK04863 369 EVVEEADEQQE----------------ENEARAEAAEEEVDELKSQLADYQQALDVQqTRAIQYQQAVQALERAKQLCGL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 855 SDFDEQKQDiNLLHQFVQLSESVQQIELQhhsgISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEpicLKGF 934
Cdd:PRK04863 433 PDLTADNAE-DWLEEFQAKEQEATEELLS----LEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARE---LLRR 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 935 LKRHRFQIKRLSQEHVDMGEEKRLLDIISQLEQ---EIEEKSALMEATEATINEMR-EQMTNLESALLEKSVIINKVEDY 1010
Cdd:PRK04863 505 LREQRHLAEQLQQLRMRLSELEQRLRQQQRAERllaEFCKRLGKNLDDEDELEQLQeELEARLESLSESVSEARERRMAL 584
|
330 340 350
....*....|....*....|....*....|
gi 442627456 1011 QRQIESLEKQNAEMTM---VYEELQDRVTR 1037
Cdd:PRK04863 585 RQQLEQLQARIQRLAArapAWLAAQDALAR 614
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
644-881 |
4.89e-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: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 644 DQLRLEIVSVRDKLESVESAfnlaSSEIiqkatdcERLSKELStsqnafgQLQERYDALDQQWQAQQAGITTLHEKHEHV 723
Cdd:COG4913 664 ASAEREIAELEAELERLDAS----SDDL-------AALEEQLE-------ELEAELEELEEELDELKGEIGRLEKELEQA 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 724 QEKYQKLQEEYEQLESRARSASSAEF--QRLQNDNTKFQADI-ASLNERLEEAQnmlTEVQNSESTVEKLRIQ-NHELTA 799
Cdd:COG4913 726 EEELDELQDRLEAAEDLARLELRALLeeRFAAALGDAVERELrENLEERIDALR---ARLNRAEEELERAMRAfNREWPA 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 800 KIKELETNFEEMqREYDCLSNQLmesvqENDAL---REEIKQRPTSHVEESMrsSGISSDFDEQKQDINllHQFVQLSES 876
Cdd:COG4913 803 ETADLDADLESL-PEYLALLDRL-----EEDGLpeyEERFKELLNENSIEFV--ADLLSKLRRAIREIK--ERIDPLNDS 872
|
....*
gi 442627456 877 VQQIE 881
Cdd:COG4913 873 LKRIP 877
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
954-1578 |
4.99e-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: 45.40 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 954 EEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESA--LLEKSV--IINKVEDYQRQIESLekqNAEMTMVYE 1029
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKikILEQQIkdLNDKLKKNKDKINKL---NSDLSKINS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1030 EL----QDRVTRESSMSESLLRVPPDEDTLPGCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNIA 1105
Cdd:TIGR04523 111 EIkndkEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNID 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1106 RLQ----------TDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLS 1175
Cdd:TIGR04523 191 KIKnkllklelllSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1176 ladakpDQILLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDDEISALRMEFLLQIEtNEKENQAKFYAELQETKDRYESN 1255
Cdd:TIGR04523 271 ------EKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQE-KKLEEIQNQISQNNKIISQLNEQ 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1256 VAELKEKLLQVEETLSSVTVRCQAELEALKSAHKENISQaVEERNNLIVQHQAEMETIR--ETLKNKLAEASTQQSKMED 1333
Cdd:TIGR04523 344 ISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY-KQEIKNLESQINDLESKIQnqEKLNQQKDEQIKKLQQEKE 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1334 AFRAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQC 1413
Cdd:TIGR04523 423 LLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLN 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1414 SKTQEQLQMESLTRDQISfEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLesEIQKANSEHSCTMEK 1493
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKIS-SLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEID--EKNKEIEELKQTQKS 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1494 LQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKvilyddlvsqHERLKICLAEANELSSNLQKKVMS 1573
Cdd:TIGR04523 580 LKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE----------NEKLSSIIKNIKSKKNKLKQEVKQ 649
|
....*
gi 442627456 1574 LHTEL 1578
Cdd:TIGR04523 650 IKETI 654
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1548-1746 |
5.49e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1548 SQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERM 1627
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1628 ANQAEKFTREAANL--KGSINELLLKLNS-----MQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKL 1700
Cdd:COG4942 100 EAQKEELAELLRALyrLGRQPPLALLLSPedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442627456 1701 EDAKTSLEQQLRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEEL 1746
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1400-1636 |
5.72e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1400 NKLTKDNIElekqcsKTQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLESE 1479
Cdd:PHA02562 169 DKLNKDKIR------ELNQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTDE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1480 IQKANSEH---SCTMEKLQELQAEMKvlsnrNEKEKCDFETK--------------LETFTFKITDLEEVLKEAQHKvil 1542
Cdd:PHA02562 243 LLNLVMDIedpSAALNKLNTAAAKIK-----SKIEQFQKVIKmyekggvcptctqqISEGPDRITKIKDKLKELQHS--- 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1543 YDDLVSQHERLKICLAEANElssnLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKD 1622
Cdd:PHA02562 315 LEKLDTAIDELEEIMDEFNE----QSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDK 390
|
250
....*....|....*
gi 442627456 1623 VEERMANQA-EKFTR 1636
Cdd:PHA02562 391 IVKTKSELVkEKYHR 405
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
625-814 |
5.89e-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: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 625 EELEKLIADLESKKNSC--ECDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELST--------------- 687
Cdd:COG4942 37 AELEKELAALKKEEKALlkQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAqkeelaellralyrl 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 688 ----------SQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLEsRARSASSAEFQRLQNDNT 757
Cdd:COG4942 117 grqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE-ALLAELEEERAALEALKA 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442627456 758 KFQADIASLNERLEEAQNMLTEVQNSEStveklriqnhELTAKIKELETNFEEMQRE 814
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAE----------ELEALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1558-1751 |
6.50e-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: 6.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1558 AEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTRE 1637
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1638 AANLK---GSINELLLKLNSmqetkdmlesgnEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQ---L 1711
Cdd:COG3883 92 ARALYrsgGSVSYLDVLLGS------------ESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKlaeL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442627456 1712 RDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLE 1751
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLA 199
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1548-1873 |
6.51e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 6.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1548 SQHERLKICLAEANELSSNLQKKVMSLH----TELIDSQKGISSRDveinELREELKAaMDAKATASAEQMTLVTQLKDV 1623
Cdd:PLN02939 121 DGEQLSDFQLEDLVGMIQNAEKNILLLNqarlQALEDLEKILTEKE----ALQGKINI-LEMRLSETDARIKLAAQEKIH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1624 EERMANQAEKFTRE----AANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNlrnmldeeskmcisLKEKLVK 1699
Cdd:PLN02939 196 VEILEEQLEKLRNEllirGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAE--------------TEERVFK 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1700 LEDAKTSLEQQLRDNKSEIYQRHTELTK-----------EVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLK 1768
Cdd:PLN02939 262 LEKERSLLDASLRELESKFIVAQEDVSKlsplqydcwweKVENLQDLLDRATNQVEKAALVLDQNQDLRDKVDKLEASLK 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1769 KTLENNLG------WQQKVDEVtreceKLRFDMQSKEVQNESKV-QELISECEELRSTLKSkeasfQSEKESMDRTISS- 1840
Cdd:PLN02939 342 EANVSKFSsykvelLQQKLKLL-----EERLQASDHEIHSYIQLyQESIKEFQDTLSKLKE-----ESKKRSLEHPADDm 411
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 442627456 1841 ---------LLEDKRNLEEKLcSANDivAKLETEIAALRPRK 1873
Cdd:PLN02939 412 psefwsrilLLIDGWLLEKKI-SNND--AKLLREMVWKRDGR 450
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1693-1893 |
6.91e-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: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1693 LKEKLVKLEDAKTSLE-QQLRDNKSEIYQRHTE---LTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQE------ 1762
Cdd:COG4913 257 IRELAERYAAARERLAeLEYLRAALRLWFAQRRlelLEAELEELRAELARLEAELERLEARLDALREELDELEAqirgng 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1763 --TKEQLKKTLENnlgWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELisecEELRSTLKSKEASFQSEKESMDRTISS 1840
Cdd:COG4913 337 gdRLEQLEREIER---LERELEERERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEELEALEEALAE 409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442627456 1841 LLEDKRNLEEKLcsandivAKLETEIAALRPRKSLdrnpVPRKSITFESEIRK 1893
Cdd:COG4913 410 AEAALRDLRREL-------RELEAEIASLERRKSN----IPARLLALRDALAE 451
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
771-1311 |
7.29e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 771 EEAQNMLTEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLME----------SVQENDALREEI--KQ 838
Cdd:PRK03918 165 KNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPElreeleklekEVKELEELKEEIeeLE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 839 RPTSHVEESMRS-----SGISSDFDEQKQDINLLHQFVQLSESVQQIELQHhsgisrlfranqmkldqsepgLKLCLESA 913
Cdd:PRK03918 245 KELESLEGSKRKleekiRELEERIEELKKEIEELEEKVKELKELKEKAEEY---------------------IKLSEFYE 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 914 EYIEEDNRqsdatepicLKGFLKRHRFQIKRLSQEHVDMGEEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNL 993
Cdd:PRK03918 304 EYLDELRE---------IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 994 ESalLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRV----TRESSMSESLLRVPPDEDTLPGC--PTSPSRREQ 1067
Cdd:PRK03918 375 ER--LKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIgelkKEIKELKKAIEELKKAKGKCPVCgrELTEEHRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1068 -------EVATLKTSITELQSQVSDLKAELENhLRQIQLKDGNIARLQTDFEEMSERCLSME-VRLAELDEDTKQKQELL 1139
Cdd:PRK03918 453 lleeytaELKRIEKELKEIEEKERKLRKELRE-LEKVLKKESELIKLKELAEQLKELEEKLKkYNLEELEKKAEEYEKLK 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1140 DR------QAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKPDQILLSSQYD-----SQIEKLNQLLNAAKDEL 1208
Cdd:PRK03918 532 EKliklkgEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEleerlKELEPFYNEYLELKDAE 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1209 HDVRRIKdDEISALRMEFLLQIETNEKENQA--KFYAELQETKDRY-ESNVAELKEKLLQVEETLSSVTvrcqAELEALK 1285
Cdd:PRK03918 612 KELEREE-KELKKLEEELDKAFEELAETEKRleELRKELEELEKKYsEEEYEELREEYLELSRELAGLR----AELEELE 686
|
570 580
....*....|....*....|....*.
gi 442627456 1286 SAHKENISQAVEERNNLIVQHQAEME 1311
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKE 712
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
563-824 |
7.73e-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: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 563 SSKLRVDDLLSAL--LEKEstIESLQKSLDNLTRDvLRNSKEGHMLSIAPEQEDIagdsicnkceeLEKLIADLESKKNs 640
Cdd:COG3206 165 NLELRREEARKALefLEEQ--LPELRKELEEAEAA-LEEFRQKNGLVDLSEEAKL-----------LLQQLSELESQLA- 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 641 cecdQLRLEIVSVRDKLESVESAFNLASSEIIQKATDcerlskelstsqNAFGQLQERYDALDQQWQAQQAgitTLHEKH 720
Cdd:COG3206 230 ----EARAELAEAEARLAALRAQLGSGPDALPELLQS------------PVIQQLRAQLAELEAELAELSA---RYTPNH 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 721 EhvqeKYQKLQEEYEQLESRARSASSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSEstveklriqnheltAK 800
Cdd:COG3206 291 P----DVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELE--------------AE 352
|
250 260
....*....|....*....|....
gi 442627456 801 IKELETNFEEMQREYDCLSNQLME 824
Cdd:COG3206 353 LRRLEREVEVARELYESLLQRLEE 376
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1202-1530 |
7.84e-04 |
|
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: 44.56 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1202 NAAKDELHDVRRIKDDEISALRMEFLLQIETNEKENQAKFYAELQETKDRYESNV---AELKEKLLQVEETLSSVTVRCQ 1278
Cdd:COG5185 205 NSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVeqnTDLRLEKLGENAESSKRLNENA 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1279 AELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRD 1358
Cdd:COG5185 285 NNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1359 --KGASKLEEVKKTLEQminggrvMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQlQMESLTRD--QISFEI 1434
Cdd:COG5185 365 niVGEVELSKSSEELDS-------FKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADR-QIEELQRQieQATSSN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1435 EAHIKKLELIVASSKKRIIELEEKCDQQVLEldKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCD 1514
Cdd:COG5185 437 EEVSKLLNELISELNKVMREADEESQSRLEE--AYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEG 514
|
330
....*....|....*.
gi 442627456 1515 FETKLETFTFKITDLE 1530
Cdd:COG5185 515 VRSKLDQVAESLKDFM 530
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1378-1829 |
7.97e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 7.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1378 GRVMSDTIAELEKTKAEQDLAVNKlTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELE- 1456
Cdd:COG4717 63 GRKPELNLKELKELEEELKEAEEK-EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEl 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1457 EKCDQQVLELDKCRLEKLSLESEIQKANSEHsctMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEA 1536
Cdd:COG4717 142 AELPERLEELEERLEELRELEEELEELEAEL---AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1537 QHKVilyDDLVSQHERLKICLAEANELSSNLQKKVMSLhteLIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTL 1616
Cdd:COG4717 219 QEEL---EELEEELEQLENELEAAALEERLKEARLLLL---IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLL 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1617 VTQLKDVEERMANQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEK 1696
Cdd:COG4717 293 LAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1697 LVKLEDAKTSLEQQLRdNKSEIYQRHTELTKEVELGRNRIGELTKKCEELcSDLENSDQIRLDLQETKEQLKKTlennlg 1776
Cdd:COG4717 373 AALLAEAGVEDEEELR-AALEQAEEYQELKEELEELEEQLEELLGELEEL-LEALDEEELEEELEELEEELEEL------ 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 442627456 1777 wQQKVDEVTRECEKLRFDMqsKEVQNESKVQELISECEELRSTLKSKEASFQS 1829
Cdd:COG4717 445 -EEELEELREELAELEAEL--EQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1646-1870 |
8.12e-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: 8.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1646 NELLLKLNSMQETKDMLESGNEELKEQLRNSQ----------NLRNMLDEESKMCI-----SLKEKLVKLEDAKTSLEQQ 1710
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLErqaekaerykELKAELRELELALLvlrleELREELEELQEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1711 LRDNKSEIyqrhTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEK 1790
Cdd:TIGR02168 255 LEELTAEL----QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1791 LRFDMQSKEVQNESKVQELISECEELRSTLKSKEASFQSEKESMdrtisslledkRNLEEKLCSANDIVAKLETEIAALR 1870
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL-----------EELEEQLETLRSKVAQLELQIASLN 399
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1557-1772 |
8.25e-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: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1557 LAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMAN---QAEK 1633
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1634 FTREAANLKGSINELLLKLNSM-QETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQ-- 1710
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAEra 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442627456 1711 -LRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLE 1772
Cdd:COG4942 175 eLEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1476-1852 |
8.42e-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: 44.12 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1476 LESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKVILYDDLVSQHERLKI 1555
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1556 CLAEANELSSNLQKKVMSLHTELIDSQKGISSR----DVEINELREELKAAMDAKATASAEQMTLVTQL----------- 1620
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKTLTQRvlerETELERMKERAKKAGAQRKEEEAERKQLQAKLqqteeelrsls 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1621 KDVEERMANQAEKFTrEAANLKGSINELLLKLNSMQETkdmlESGNEELKEQLRnsqnlrnmldeeskmciSLKEKLVKL 1700
Cdd:pfam07888 192 KEFQELRNSLAQRDT-QVLQLQDTITTLTQKLTTAHRK----EAENEALLEELR-----------------SLQERLNAS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1701 EDAKTSLEQQLRDNKSEIYQRHTELTK---EVELGRNRIGELTKKC-EELCSDLENSDQIRLDLQETKEQLKKTLENNLG 1776
Cdd:pfam07888 250 ERKVEGLGEELSSMAAQRDRTQAELHQarlQAAQLTLQLADASLALrEGRARWAQERETLQQSAEADKDRIEKLSAELQR 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442627456 1777 WQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISECEELRSTLKSkeasFQSEKESMDRTISSLLEDKRNLEEKL 1852
Cdd:pfam07888 330 LEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRV----AQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
978-1500 |
9.69e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 978 ATEATINEMREQMTNLESALLEksviinkVEDYQRQIESLEKQNAEmtmvYEELQDRVTRESSMSESLLRVPP--DEDTL 1055
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEA-------LEDAREQIELLEPIREL----AERYAAARERLAELEYLRAALRLwfAQRRL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1056 PGCPTSPSRREQEVATLKTSITELQSQVSDLKAELENHLRQIQLKDGNiarlqtdfeemserclsmevRLAELDEDTKQK 1135
Cdd:COG4913 291 ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGD--------------------RLEQLEREIERL 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1136 QELLDRQAQKLsddlclidqlqkknaqlvEQYHKATESLSLADAKPDQIL---------LSSQYDSQIEKLNQLLNAAKD 1206
Cdd:COG4913 351 ERELEERERRR------------------ARLEALLAALGLPLPASAEEFaalraeaaaLLEALEEELEALEEALAEAEA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1207 ELHDVRR---IKDDEISALR----------MEFLLQI--ETNEKENQAKFYAELQETK---------------------- 1249
Cdd:COG4913 413 ALRDLRRelrELEAEIASLErrksniparlLALRDALaeALGLDEAELPFVGELIEVRpeeerwrgaiervlggfaltll 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1250 --DRYESNVAE------LKEKL--LQVEETLSSVT---------------------------------VRCQAELEALK- 1285
Cdd:COG4913 493 vpPEHYAAALRwvnrlhLRGRLvyERVRTGLPDPErprldpdslagkldfkphpfrawleaelgrrfdYVCVDSPEELRr 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1286 ---------------SAHKENISQAVEERNNLIVQHQAEMETIRE---TLKNKLAEASTQQSKMEDAfRAEINEVRATLM 1347
Cdd:COG4913 573 hpraitragqvkgngTRHEKDDRRRIRSRYVLGFDNRAKLAALEAelaELEEELAEAEERLEALEAE-LDALQERREALQ 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1348 EQLNQTKEDRDKGA--SKLEEVKKTLEQMINGgrvmSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQmesl 1425
Cdd:COG4913 652 RLAEYSWDEIDVASaeREIAELEAELERLDAS----SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE---- 723
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627456 1426 trdQISFEIEAHIKKLElivASSKKRIIELEEKCDQQVLELDKCRLEK---LSLESEIQKANSEHSCTMEKLQELQAE 1500
Cdd:COG4913 724 ---QAEEELDELQDRLE---AAEDLARLELRALLEERFAAALGDAVERelrENLEERIDALRARLNRAEEELERAMRA 795
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1591-1832 |
1.07e-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: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1591 EINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAekftREAANLKGSINELLLKLNSMQETKDMLESGNEELK 1670
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALA----RRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1671 EQLrnSQNLRNMldeeskmcislkEKLVKLEDAKTSLEQqlrDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELcsdl 1750
Cdd:COG4942 104 EEL--AELLRAL------------YRLGRQPPLALLLSP---EDFLDAVRRLQYLKYLAPARREQAEELRADLAEL---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1751 ensDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISECEELRSTLKSKEASFQSE 1830
Cdd:COG4942 163 ---AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
..
gi 442627456 1831 KE 1832
Cdd:COG4942 240 AE 241
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
991-1207 |
1.42e-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: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 991 TNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTressmsesllrvppdedtlpgcptspsRREQEVA 1070
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELE---------------------------ALQAEID 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1071 TLKTSITELQSQVSDLKAELENHLRQIQLKDGNIARLQ-----TDFEEMSERCLSMEV---RLAELDEDTKQKQELLDRQ 1142
Cdd:COG3883 69 KLQAEIAEAEAEIEERREELGERARALYRSGGSVSYLDvllgsESFSDFLDRLSALSKiadADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442627456 1143 AQKLSDDLcliDQLQKKNAQLVEQYHKATESLSLADAKPDQilLSSQYDSQIEKLNQLLNAAKDE 1207
Cdd:COG3883 149 KAELEAKL---AELEALKAELEAAKAELEAQQAEQEALLAQ--LSAEEAAAEAQLAELEAELAAA 208
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
962-1146 |
1.56e-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: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 962 ISQLEQEIEEKSALMEATEATINEMREQmTNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSM 1041
Cdd:COG3206 177 LEFLEEQLPELRKELEEAEAALEEFRQK-NGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1042 SESLLRVPPDEDTLpgcpTSPSRREQEVATLKT-------SITELQSQVSDLKAELENHLRQIQLK--------DGNIAR 1106
Cdd:COG3206 256 LPELLQSPVIQQLR----AQLAELEAELAELSArytpnhpDVIALRAQIAALRAQLQQEAQRILASleaelealQAREAS 331
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442627456 1107 LQTDFEEMSERCLSM---EVRLAELDEDTKQKQELLDRQAQKL 1146
Cdd:COG3206 332 LQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRL 374
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1284-1442 |
3.29e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1284 LKSAHKENISQAVEERNNLIVQHQAEMETIRetlKNKLAEASTQQSKMEDAFRAEINEVRATLM----------EQLNQT 1353
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIK---KEALLEAKEEIHKLRNEFEKELRERRNELQklekrllqkeENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1354 KEDRDKGASKLEEVKKTLEQMINggrvmsdtiaELEKTKAEQDLAVNKLTKdniELEKQCSKTQE---QLQMESLtRDQI 1430
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQ----------ELEKKEEELEELIEEQLQ---ELERISGLTAEeakEILLEKV-EEEA 167
|
170
....*....|..
gi 442627456 1431 SFEIEAHIKKLE 1442
Cdd:PRK12704 168 RHEAAVLIKEIE 179
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1235-1501 |
3.33e-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: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1235 KENQAKFYAELQETKDRYESNVAELKEKLLQVEetlssvtvrcqAELEALKSAHKeniSQAVEERNNLIVQHQAEMETIR 1314
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAE-----------AALEEFRQKNG---LVDLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1315 ETLKNKLAEASTQQskmeDAFRAEINEVRATLMEQLNQTkedrdkgaskleevkktleqminggrVMSDTIAELEKTKAE 1394
Cdd:COG3206 229 AEARAELAEAEARL----AALRAQLGSGPDALPELLQSP--------------------------VIQQLRAQLAELEAE 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1395 QDLAVNKLTKDN---IELEKQCSKTQEQLQMESltrDQISFEIEAHIKKLELIVASSKKRIIELEekcdQQVLELDKCRL 1471
Cdd:COG3206 279 LAELSARYTPNHpdvIALRAQIAALRAQLQQEA---QRILASLEAELEALQAREASLQAQLAQLE----ARLAELPELEA 351
|
250 260 270
....*....|....*....|....*....|
gi 442627456 1472 EKLSLESEIQKANSEHSCTMEKLQELQAEM 1501
Cdd:COG3206 352 ELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
504-754 |
3.36e-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: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 504 TYDALEKEVTSLRAdneaansKISELEEKLSTLKQTMRIMEVENQVAVGLEfefeahkkssklRVDDLLSALLEKESTIE 583
Cdd:COG3206 176 ALEFLEEQLPELRK-------ELEEAEAALEEFRQKNGLVDLSEEAKLLLQ------------QLSELESQLAEARAELA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 584 SLQKSLDNLTRDVLRNSKEGHMLSIAPEQediagdsicnkcEELEKLIADLESKKnscecDQLRL-------EIVSVRDK 656
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSPVI------------QQLRAQLAELEAEL-----AELSArytpnhpDVIALRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 657 LESVESAFNLASSEIIQKA-TDCERLSKELSTSQNAFGQLQERYDALDQQwQAQQAGIttlhekhehvQEKYQKLQEEYE 735
Cdd:COG3206 300 IAALRAQLQQEAQRILASLeAELEALQAREASLQAQLAQLEARLAELPEL-EAELRRL----------EREVEVARELYE 368
|
250
....*....|....*....
gi 442627456 736 QLESRARSASSAEFQRLQN 754
Cdd:COG3206 369 SLLQRLEEARLAEALTVGN 387
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1228-1642 |
3.41e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1228 LQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQA-ELEALKSAHKENISQAVEERNNLivqh 1306
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERLEEL---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1307 QAEMETIREtLKNKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQminggrvmsdtiA 1386
Cdd:COG4717 152 EERLEELRE-LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE------------A 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1387 ELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMES-----------------------LTRDQISFEIEAHIKKLEL 1443
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllsliltiagvlFLVLGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1444 IVASSKKRIIELEEKCDQQVLELDKcRLEKLSLESEIQKAN-SEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETF 1522
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEE-LLAALGLPPDLSPEElLELLDRIEELQELLREAEELEEELQLEELEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1523 TFKITDLEEVLKEAQHKVIlYDDLVSQHERLKICLAEANELSSNLQKKVM--SLHTELIDSQKGISSRDVEINELREELK 1600
Cdd:COG4717 378 EAGVEDEEELRAALEQAEE-YQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 442627456 1601 AAmdAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLK 1642
Cdd:COG4717 457 EL--EAELEQLEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
611-825 |
3.76e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 611 EQEDIAGDSICNKCEELEKLIAdlESKKNSCECDQLRLEIVSVRDKLESVESAFNLASSEIIQKATDCERLSKELStsqn 690
Cdd:PHA02562 206 EQRKKNGENIARKQNKYDELVE--EAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIK---- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 691 aFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSAS--SAEFQRLQNDNTKFQADIASLNE 768
Cdd:PHA02562 280 -MYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNeqSKKLLELKNKISTNKQSLITLVD 358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442627456 769 RLEEAQNMLTEVQ----NSESTVEKLriqNHELTAKIKELeTNFEEMQREYDCLSNQLMES 825
Cdd:PHA02562 359 KAKKVKAAIEELQaefvDNAEELAKL---QDELDKIVKTK-SELVKEKYHRGIVTDLLKDS 415
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
506-880 |
4.61e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 506 DALEKEVTSLRADNEAANSKISELEEKLSTLKQtmrIMEVENQVAvglEFEFEahkkssKLRVDDLLSALLEKESTIESL 585
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQE---RREALQRLA---EYSWD------EIDVASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 586 QKSLDNLtrdvlrnskeghmlsiapeqediagdsicnkcEELEKLIADLESKKnscecDQLRLEIVSVRDKLESVESAFN 665
Cdd:COG4913 681 DASSDDL--------------------------------AALEEQLEELEAEL-----EELEEELDELKGEIGRLEKELE 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 666 LASSEIIQKATDCERLSKELSTSQNAfgQLQERYDALDQQwqaqqagittlhekhEHVQEKYQKLQEEYEQLESRARSAS 745
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRA--LLEERFAAALGD---------------AVERELRENLEERIDALRARLNRAE 786
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 746 SaEFQRLQND-NTKFQADIASLN---ERLEEAQNMLTEVQNSEstvekLriqnHELTAKIKELETNFEEMQREYdcLSNQ 821
Cdd:COG4913 787 E-ELERAMRAfNREWPAETADLDadlESLPEYLALLDRLEEDG-----L----PEYEERFKELLNENSIEFVAD--LLSK 854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 822 LMESVQE--------NDALRE-----------EIKQRPTSHV----EESMRSSGISSDFDEQKQDinllHQFVQLSESVQ 878
Cdd:COG4913 855 LRRAIREikeridplNDSLKRipfgpgrylrlEARPRPDPEVrefrQELRAVTSGASLFDEELSE----ARFAALKRLIE 930
|
..
gi 442627456 879 QI 880
Cdd:COG4913 931 RL 932
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1564-1851 |
5.57e-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: 41.34 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1564 SSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAaMDAKATASaeqmtlvtqlkdVEERMANQAEKFTREAANLKG 1643
Cdd:pfam15905 68 NLKESKDQKELEKEIRALVQERGEQDKRLQALEEELEK-VEAKLNAA------------VREKTSLSASVASLEKQLLEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1644 S-INELLLKLNSMQETKDMLESGNEELKEqlrnsqnLRNMLDEESKMCISLKEKL-VKLEDAKTSLEQ------QLRDNK 1715
Cdd:pfam15905 135 TrVNELLKAKFSEDGTQKKMSSLSMELMK-------LRNKLEAKMKEVMAKQEGMeGKLQVTQKNLEHskgkvaQLEEKL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1716 SEIYQRHTELTKEVElgrnrigELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRFDM 1795
Cdd:pfam15905 208 VSTEKEKIEEKSETE-------KLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDL 280
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 442627456 1796 qskevqnESKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEK 1851
Cdd:pfam15905 281 -------NEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
1273-1675 |
5.65e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 41.81 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1273 VTVRCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQ-----QSKMEDAFRAEINEVRATLm 1347
Cdd:PLN02939 31 LAVSCRARRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMElpqksTSSDDDHNRASMQRDEAIA- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1348 eqlNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQmESLTR 1427
Cdd:PLN02939 110 ---AIDNEQQTNSKDGEQLSDFQLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRLS-ETDAR 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1428 DQISFEIEAHIKKLELIVASSKKRII---ELEEKCDQQ-VLELDKCRLEKLSLESEIQKANSEhsctMEKLQELQAEMKV 1503
Cdd:PLN02939 186 IKLAAQEKIHVEILEEQLEKLRNELLirgATEGLCVHSlSKELDVLKEENMLLKDDIQFLKAE----LIEVAETEERVFK 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1504 LsnrnEKEKCDFETKLETFTFK-ITDLEEVLKEAQHKvilYDDLVSQHERLKICLAEAnelSSNLQKKVMSL--HTELID 1580
Cdd:PLN02939 262 L----EKERSLLDASLRELESKfIVAQEDVSKLSPLQ---YDCWWEKVENLQDLLDRA---TNQVEKAALVLdqNQDLRD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1581 sqkgissrdvEINELREELKAAMDAKatASAEQMTLVTQ-LKDVEERM-ANQAEKFTreaanlkgsinELLLKLNSMQET 1658
Cdd:PLN02939 332 ----------KVDKLEASLKEANVSK--FSSYKVELLQQkLKLLEERLqASDHEIHS-----------YIQLYQESIKEF 388
|
410
....*....|....*..
gi 442627456 1659 KDMLESGNEELKEQLRN 1675
Cdd:PLN02939 389 QDTLSKLKEESKKRSLE 405
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1253-1421 |
5.84e-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: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1253 ESNVAELKEKLLQVEETLSSVtvrcQAELEALKSAH---KENISQAVEERNNL---IVQHQAEMETIRETLKNKLAEAST 1326
Cdd:COG3883 22 QKELSELQAELEAAQAELDAL----QAELEELNEEYnelQAELEALQAEIDKLqaeIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1327 Q-----------QSKMEDAF--RAE-INEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTK 1392
Cdd:COG3883 98 SggsvsyldvllGSESFSDFldRLSaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180
....*....|....*....|....*....
gi 442627456 1393 AEQDLAVNKLTKDNIELEKQCSKTQEQLQ 1421
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELA 206
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
888-1663 |
6.25e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 888 ISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIKRLSQEHVDMGEEKRLLDIISQLEQ 967
Cdd:TIGR00618 188 KKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 968 EIEEKSALMEATEATiNEMREQMTnlesalleksviinKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSMSESLLR 1047
Cdd:TIGR00618 268 RIEELRAQEAVLEET-QERINRAR--------------KAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1048 VppdedtlpgcptspSRREQEVATLKTSITELQSQvsdlkaelENHLRQiqlkdgnIARLQTDFEEMSERCLSMEVRLAE 1127
Cdd:TIGR00618 333 H--------------VKQQSSIEEQRRLLQTLHSQ--------EIHIRD-------AHEVATSIREISCQQHTLTQHIHT 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1128 LdedtKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAkpdQILLSSQYDSQ----IEKLNQLLNA 1203
Cdd:TIGR00618 384 L----QQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKK---QQELQQRYAELcaaaITCTAQCEKL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1204 AKDELHDVRRIKDDEISALR-MEFLLQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEEtLSSVTVRCQAELE 1282
Cdd:TIGR00618 457 EKIHLQESAQSLKEREQQLQtKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQ 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1283 ALKSAHK--ENISQAVEERNNLIVQHQAEMETIRETLKnKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQtkEDRDKG 1360
Cdd:TIGR00618 536 TYAQLETseEDVYHQLTSERKQRASLKEQMQEIQQSFS-ILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA--EDMLAC 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1361 ASKLEEVKKTLEQMinggrvMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQ----CSKTQEQLQMESLTRDQISFEIEA 1436
Cdd:TIGR00618 613 EQHALLRKLQPEQD------LQDVRLHLQQCSQELALKLTALHALQLTLTQErvreHALSIRVLPKELLASRQLALQKMQ 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1437 HIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLE-KLSLESEIQKANSEHSCTMEKLQELQAEmkvlsnrnekekcdF 1515
Cdd:TIGR00618 687 SEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEiENASSSLGSDLAAREDALNQSLKELMHQ--------------A 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1516 ETKLETFTFKitdlEEVLKEAQHKVILYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGIssRDVEINEL 1595
Cdd:TIGR00618 753 RTVLKARTEA----HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDI--LNLQCETL 826
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442627456 1596 REELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTREAanlkgSINELLLKLNSMQETKDMLE 1663
Cdd:TIGR00618 827 VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQA-----KIIQLSDKLNGINQIKIQFD 889
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1516-2129 |
6.63e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1516 ETKLETFTFKITDLEEVLKEAQHKVILYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINEL 1595
Cdd:PRK03918 199 EKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1596 REELK--AAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLKGSINELllklnsmqetkdmlESGNEELKEQL 1673
Cdd:PRK03918 279 EEKVKelKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL--------------EEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1674 RNSQNLRNMLDEeskmcisLKEKLVKLEDAKtSLEQQLRDNKSEIYQRHTE-LTKEVELGRNRIGELTKKCEELCSDLEN 1752
Cdd:PRK03918 345 KKLKELEKRLEE-------LEERHELYEEAK-AKKEELERLKKRLTGLTPEkLEKELEELEKAKEEIEEEISKITARIGE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1753 SDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVqnESKVQELISECEELRSTLKSKEASFqsEKE 1832
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRI--EKELKEIEEKERKLRKELRELEKVL--KKE 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1833 SMDRTISSLLEDKRNLEEKLCSANdiVAKLEteiaalrpRKSLDRNPVPRKSITFESEIRknrriSVHDERRQSywndvr 1912
Cdd:PRK03918 493 SELIKLKELAEQLKELEEKLKKYN--LEELE--------KKAEEYEKLKEKLIKLKGEIK-----SLKKELEKL------ 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1913 efgimtdpvdnncncAELNSKLQDCQRELFIRESQVTALKMELDHHPLKDENAqlTKRVIEEQDKAKVEQKRLKMKLQDL 1992
Cdd:PRK03918 552 ---------------EELKKKLAELEKKLDELEEELAELLKELEELGFESVEE--LEERLKELEPFYNEYLELKDAEKEL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1993 NARINDLttasAKEPESNQMAQAAKPATVAAQTQTESDLETILEKTNVK-YQEAVRMLRYRYHLIQELKEKLRQNENSDT 2071
Cdd:PRK03918 615 EREEKEL----KKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEeYEELREEYLELSRELAGLRAELEELEKRRE 690
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 442627456 2072 SNITSLSAgqtsaLKAQCESQKKEILAIKyKYEAAKrilairnDDLDALREKLAKYET 2129
Cdd:PRK03918 691 EIKKTLEK-----LKEELEEREKAKKELE-KLEKAL-------ERVEELREKVKKYKA 735
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1132-1869 |
7.39e-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: 41.57 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1132 TKQKQELLDRQ-AQKLSDDLCLIDQLQKKNAQLVEQYHKATESL-SLADAKPDQILLSSQYDSQIEKLNQLLNAAKDELH 1209
Cdd:TIGR00606 228 SKEAQLESSREiVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIkALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLY 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1210 DVRRIKDDEISALRMEFLLQIETNEKENQakfyaELQETKDRYESNVAELKEKLLQVEETL---SSVTVRCQAELEALKS 1286
Cdd:TIGR00606 308 HNHQRTVREKERELVDCQRELEKLNKERR-----LLNQEKTELLVEQGRLQLQADRHQEHIrarDSLIQSLATRLELDGF 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1287 AHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQSKMEDAFRAEINEVRATLMEQlnqtKEDRDKGASKLEE 1366
Cdd:TIGR00606 383 ERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELK----KEILEKKQEELKF 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1367 VKKTLEQMINGgrvmSDTIAELEK--TKAEQDLAV---NKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKL 1441
Cdd:TIGR00606 459 VIKELQQLEGS----SDRILELDQelRKAERELSKaekNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTR 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1442 ELIVASSKK------RIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLS------NRNE 1509
Cdd:TIGR00606 535 TQMEMLTKDkmdkdeQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEqnknhiNNEL 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1510 KEKCDFETKLETFTF----------KITDLEEVLKEAQH-------KVILYDDLVSQH-----------ERLKICLAEAN 1561
Cdd:TIGR00606 615 ESKEEQLSSYEDKLFdvcgsqdeesDLERLKEEIEKSSKqramlagATAVYSQFITQLtdenqsccpvcQRVFQTEAELQ 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1562 ELSSNLQKKVMSLHTELIDSQKGISSRDVEINElreelkaaMDAKATASAEQMTL-VTQLKDVEERMANQAEKFTREAAN 1640
Cdd:TIGR00606 695 EFISDLQSKLRLAPDKLKSTESELKKKEKRRDE--------MLGLAPGRQSIIDLkEKEIPELRNKLQKVNRDIQRLKND 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1641 LkgSINELLLklnsmqETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSleQQLRDNKSEIYQ 1720
Cdd:TIGR00606 767 I--EEQETLL------GTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTV--QQVNQEKQEKQH 836
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1721 RHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEklrfDMQSKEV 1800
Cdd:TIGR00606 837 ELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIK----DAKEQDS 912
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1801 QNESKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEKLCSA-NDIVAKLETEIAAL 1869
Cdd:TIGR00606 913 PLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGkDDYLKQKETELNTV 982
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
679-883 |
7.65e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 679 ERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQekyqkLQEEYEQLESRARSASSaEFQRLQNDNTK 758
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELES-QLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 759 FQADIASLNERLEEAQNMLTEVQNSeSTVEKLRIQNHELTAKIKELETNF------------------EEMQREYDCLSN 820
Cdd:COG3206 238 AEARLAALRAQLGSGPDALPELLQS-PVIQQLRAQLAELEAELAELSARYtpnhpdvialraqiaalrAQLQQEAQRILA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442627456 821 QLMESVQENDALREEIKQRPTSHVEESMRSSGISSDFDEQKQDINLLHQ-FVQLSESVQQIELQ 883
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARElYESLLQRLEEARLA 380
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
625-805 |
7.77e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 625 EELEKLIADLESKKNscECDQLRLEIVSVRDKLESVESAFNLASSEI--IQKATDCERLSKELStsqnafgQLQERYDAL 702
Cdd:COG4717 74 KELEEELKEAEEKEE--EYAELQEELEELEEELEELEAELEELREELekLEKLLQLLPLYQELE-------ALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 703 DQQWQAQQAGITTLHEKH---EHVQEKYQKLQEEYEQLESRARSASSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTE 779
Cdd:COG4717 145 PERLEELEERLEELRELEeelEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
|
170 180
....*....|....*....|....*.
gi 442627456 780 VQNSESTVEKlRIQNHELTAKIKELE 805
Cdd:COG4717 225 LEEELEQLEN-ELEAAALEERLKEAR 249
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1692-1872 |
7.82e-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: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1692 SLKEKLVKLEDAKTSLEQQLRDNKSE---IYQRHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLK 1768
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEekaLLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1769 KTLENNLGWQQKVDEVTRecekLRFDMQSKEVQNESKV-----------QELISECEELRSTLKSKEASFQSEKESMDRT 1837
Cdd:COG4942 104 EELAELLRALYRLGRQPP----LALLLSPEDFLDAVRRlqylkylaparREQAEELRADLAELAALRAELEAERAELEAL 179
|
170 180 190
....*....|....*....|....*....|....*
gi 442627456 1838 ISSLLEDKRNLEEKLCSANDIVAKLETEIAALRPR 1872
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLARLEKELAELAAE 214
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1494-1826 |
7.94e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 41.36 E-value: 7.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1494 LQELQAEMKVLSNRNEKEKC--DFETkLETFTFKITDLEEVLKEAQhkvilyddlVSQHERLKIClaeaNELSSNLQKKV 1571
Cdd:pfam12128 227 IRDIQAIAGIMKIRPEFTKLqqEFNT-LESAELRLSHLHFGYKSDE---------TLIASRQEER----QETSAELNQLL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1572 MSLHTELIDSqkgissrdveINELREELKAAMDAKATASAEQMTLVTQLK-----DVEERMANQ--AEKFTREAANLKGS 1644
Cdd:pfam12128 293 RTLDDQWKEK----------RDELNGELSAADAAVAKDRSELEALEDQHGafldaDIETAAADQeqLPSWQSELENLEER 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1645 INELLLKLNSMQETKDMLEsgneelkeQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNKSEIYQRHTE 1724
Cdd:pfam12128 363 LKALTGKHQDVTAKYNRRR--------SKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1725 LTKEVELGRNRIGELTKK------CEELCSDLENSDQIRLDLQETKEQLKKtlennlgwqqKVDEVTRECEKLR--FDMQ 1796
Cdd:pfam12128 435 FNEEEYRLKSRLGELKLRlnqataTPELLLQLENFDERIERAREEQEAANA----------EVERLQSELRQARkrRDQA 504
|
330 340 350
....*....|....*....|....*....|.
gi 442627456 1797 SKEVQNES-KVQELISECEELRSTLKSKEAS 1826
Cdd:pfam12128 505 SEALRQASrRLEERQSALDELELQLFPQAGT 535
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
783-1044 |
8.30e-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: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 783 SESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLSNQLMESVQENDALREEIKQrptshveesmrssgISSDFDEQKQ 862
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA--------------LEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 863 DINLLHQfvQLSESVQQIELQHHSgISRLFRANQMKLDQSEPGLKLcleSAEYIEEDNRQSDAtepicLKGFLKRHRFQI 942
Cdd:COG4942 84 ELAELEK--EIAELRAELEAQKEE-LAELLRALYRLGRQPPLALLL---SPEDFLDAVRRLQY-----LKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 943 KRLSQEhvdmgeekrlLDIISQLEQEIEEKSAlmeATEATINEMREQMTNLESALLEKSVIINKVE----DYQRQIESLE 1018
Cdd:COG4942 153 EELRAD----------LAELAALRAELEAERA---ELEALLAELEEERAALEALKAERQKLLARLEkelaELAAELAELQ 219
|
250 260
....*....|....*....|....*.
gi 442627456 1019 KQNAEMTMVYEELQDRVTRESSMSES 1044
Cdd:COG4942 220 QEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
666-839 |
8.75e-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: 8.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 666 LASSEIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHEKHEHVQEKYQKLQEEYEQLESRARSAs 745
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 746 SAEFQRLQNDNTKFQADIASLNERL---------------EEAQNMLTEVQNSESTVEKLRIQNHELTAKIKELETNFEE 810
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180
....*....|....*....|....*....
gi 442627456 811 MQREYDCLSNQLMESVQENDALREEIKQR 839
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAER 197
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1121-1358 |
9.06e-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: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1121 MEVRLAELDEDTKQKQELLDRQAQKLSDDLcliDQLQKKnaqlVEQYHKATESLSLADAkpdqillSSQYDSQIEKLNQL 1200
Cdd:COG3206 162 LEQNLELRREEARKALEFLEEQLPELRKEL---EEAEAA----LEEFRQKNGLVDLSEE-------AKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1201 LNAAKDELHDVRRikddEISALRMEFLLQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLssvtVRCQAE 1280
Cdd:COG3206 228 LAEARAELAEAEA----RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDV----IALRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1281 LEALKSAHKENISQAVEERNNLIVQHQAEMETIR---ETLKNKLAEASTQQSKMEDAFR-AEIN-EVRATLMEQLNQTKE 1355
Cdd:COG3206 300 IAALRAQLQQEAQRILASLEAELEALQAREASLQaqlAQLEARLAELPELEAELRRLEReVEVArELYESLLQRLEEARL 379
|
...
gi 442627456 1356 DRD 1358
Cdd:COG3206 380 AEA 382
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1352-1505 |
9.58e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.17 E-value: 9.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 1352 QTKEDRDKgasKLEEVKKTLEQMINggRVMSDtIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDQIS 1431
Cdd:pfam05667 324 ETEEELQQ---QREEELEELQEQLE--DLESS-IQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKVKKKTLDLLP 397
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442627456 1432 fEIEAHIKKLELIVASSKKRIIELEEKCDQ-QVLELDKCRleklSLESEIQKANSEHSCTMEKLQELQAEMKVLS 1505
Cdd:pfam05667 398 -DAEENIAKLQALVDASAQRLVELAGQWEKhRVPLIEEYR----ALKEAKSNKEDESQRKLEEIKELREKIKEVA 467
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
644-765 |
9.84e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.22 E-value: 9.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442627456 644 DQLRLEIVSVRDKLESVESAFNLASSEiiqKAtdcERLSKELStsqnafgQLQERYDALDQQWQAQQAGITTLHEKHEHV 723
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFE---RL---AELRDELA-------ELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 442627456 724 QEKYQKLQEEYEQLESrARSASSAEFQRLQNDNTKfqADIAS 765
Cdd:COG0542 481 EQRYGKIPELEKELAE-LEEELAELAPLLREEVTE--EDIAE 519
|
|
| |
