|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
4-342 |
0e+00 |
|
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: 597.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 4 IPVKVAVRIRPLLCKEVLHNHQVCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 84 GQTGSGKTYTIGGGHIASVVEGQKGIIPRAIQEIFQSISEHPS-IEFNVKVSYIEVYKEDLRDLLELET-SMKDLHIRED 161
Cdd:cd01372 81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKDtFEFQLKVSFLEIYNEEIRDLLDPETdKKPTISIRED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 162 EKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNVEAAEDGSWYSPRHIVSKFH 241
Cdd:cd01372 161 SKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNSTFTSKFH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 242 FVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPS 321
Cdd:cd01372 241 FVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPA 320
|
330 340
....*....|....*....|.
gi 1622873320 322 SSNFDESLNSLKYANRARNIR 342
Cdd:cd01372 321 DSNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
5-348 |
1.02e-145 |
|
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: 443.55 E-value: 1.02e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 5 PVKVAVRIRPLLCKEVLHNHQVCVRVIPNSQQVII-------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTvrspknrQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 78 ATVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISEH-PSIEFNVKVSYIEVYKEDLRDLLEleTSMKDL 156
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLLN--PSSKKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 157 HIREDEKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNVEaaedgswySPRHI 236
Cdd:smart00129 153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSS--------SGSGK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 237 VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRrKSSHIPYRDAKITRLLKDSLGGSAKTVMIT 316
Cdd:smart00129 225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS-KSRHIPYRDSKLTRLLQDSLGGNSKTLMIA 303
|
330 340 350
....*....|....*....|....*....|..
gi 1622873320 317 CVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:smart00129 304 NVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
11-341 |
1.56e-139 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 426.99 E-value: 1.56e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 11 RIRPLLCKEVLHNHQVCVRVIPNSQQVII-------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 84 GQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISEHPS-IEFNVKVSYIEVYKEDLRDLLELETSMKD-LHIRED 161
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKErSEFSVKVSYLEIYNEKIRDLLSPSNKNKRkLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 162 EKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNVEAAEDGSwysprHIVSKFH 241
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQ--RNRSTGGEES-----VKTGKLN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 242 FVDLAGSERVTKTGN-TGERFKESIQINSGLLALGNVISALGDPrrKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSP 320
Cdd:pfam00225 228 LVDLAGSERASKTGAaGGQRLKEAANINKSLSALGNVISALADK--KSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISP 305
|
330 340
....*....|....*....|.
gi 1622873320 321 SSSNFDESLNSLKYANRARNI 341
Cdd:pfam00225 306 SSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
5-339 |
9.77e-130 |
|
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: 401.25 E-value: 9.77e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 5 PVKVAVRIRPLlcKEVLHNHQVCVRVIPNSQQVIIG-------RDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd00106 1 NVRVAVRVRPL--NGREARSAKSVISVDGGKSVVLDppknrvaPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 78 ATVFAYGQTGSGKTYTIGGGHiasvvEGQKGIIPRAIQEIFQSISE--HPSIEFNVKVSYIEVYKEDLRDLLELETSmKD 155
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKrkETKSSFSVSASYLEIYNEKIYDLLSPVPK-KP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 156 LHIREDEKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTIsicQVHKNVEAAEDGSWYSprh 235
Cdd:cd00106 153 LSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTI---HVKQRNREKSGESVTS--- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 236 ivSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKssHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd00106 227 --SKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMI 302
|
330 340
....*....|....*....|....
gi 1622873320 316 TCVSPSSSNFDESLNSLKYANRAR 339
Cdd:cd00106 303 ACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
6-341 |
8.91e-113 |
|
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: 356.65 E-value: 8.91e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 6 VKVAVRIRPLLCKEVLHNHQVCVRVI----------------------PNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNT 63
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMdnhmlvfdpkdeedgffhggsnNRDRRKRRNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 64 CIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISE-HPSIEFNVKVSYIEVYKED 142
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGT------PQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 143 LRDLLEleTSMKDLHIREDEKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNV 222
Cdd:cd01370 156 IRDLLN--PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 223 EAAEDgswysprHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLL 302
Cdd:cd01370 234 SINQQ-------VRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLL 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 1622873320 303 KDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNI 341
Cdd:cd01370 307 KDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
6-341 |
4.22e-112 |
|
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: 353.95 E-value: 4.22e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 6 VKVAVRIRPLLCKEVLHNHQVCVRVIPNSqqvIIGRDRV---FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFA 82
Cdd:cd01374 2 ITVTVRVRPLNSREIGINEQVAWEIDNDT---IYLVEPPstsFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 83 YGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISEHPSIEFNVKVSYIEVYKEDLRDLleLETSMKDLHIREDE 162
Cdd:cd01374 79 YGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDL--LSPTSQNLKIRDDV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 163 KGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknvEAAEDGSWYSPRHIVSKFHF 242
Cdd:cd01374 151 EKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITI-------ESSERGELEEGTVRVSTLNL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 243 VDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDpRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSS 322
Cdd:cd01374 224 IDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAE 302
|
330
....*....|....*....
gi 1622873320 323 SNFDESLNSLKYANRARNI 341
Cdd:cd01374 303 SHVEETLNTLKFASRAKKI 321
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
6-341 |
4.40e-110 |
|
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or KIF3_like proteins. Subgroup of kinesins, which form heterotrimers composed of 2 kinesins and one non-motor accessory subunit. Kinesins II play important roles in ciliary transport, and have been implicated in neuronal transport, melanosome transport, the secretory pathway, and mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this group the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276822 [Multi-domain] Cd Length: 334 Bit Score: 349.07 E-value: 4.40e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 6 VKVAVRIRPLLCKEVLHNHQVCVRVIPNSQQVII--GRD------RVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 78 ATVFAYGQTGSGKTYTIGGghiASVVEGQKGIIPRAIQEIFQSISEHPS-IEFNVKVSYIEVYKEDLRDLLELETSmKDL 156
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEG---KREDPELRGIIPNSFAHIFGHIARSQNnQQFLVRVSYLEIYNEEIRDLLGKDQT-KRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 157 HIREDEKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTISIcqvhKNVEAAEDGSwyspRHI 236
Cdd:cd01371 159 ELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI----ECSEKGEDGE----NHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 237 -VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPrrKSSHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd01371 231 rVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMC 308
|
330 340
....*....|....*....|....*.
gi 1622873320 316 TCVSPSSSNFDESLNSLKYANRARNI 341
Cdd:cd01371 309 ANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
11-343 |
5.22e-109 |
|
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: 345.73 E-value: 5.22e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 11 RIRPLLCKEVLHNHQVCVRVIPNSQQVII----GRDRVFTFDFVFGKNSTQDEVYNTcIKPLVLSLIEGYNATVFAYGQT 86
Cdd:cd01366 9 RVRPLLPSEENEDTSHITFPDEDGQTIELtsigAKQKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIFAYGQT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 87 GSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISE--HPSIEFNVKVSYIEVYKEDLRDLL-ELETSMKDLHIRED-E 162
Cdd:cd01366 88 GSGKTYTMEG------PPESPGIIPRALQELFNTIKElkEKGWSYTIKASMLEIYNETIRDLLaPGNAPQKKLEIRHDsE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 163 KGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNVEAAEDGswysprhivsKFHF 242
Cdd:cd01366 162 KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHISGRNLQTGEISVG----------KLNL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 243 VDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALgdpRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSS 322
Cdd:cd01366 232 VDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL---RQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAE 308
|
330 340
....*....|....*....|.
gi 1622873320 323 SNFDESLNSLKYANRARNIRN 343
Cdd:cd01366 309 SNLNETLNSLRFASKVNSCEL 329
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
6-341 |
3.95e-104 |
|
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup. Members of this group have been associated with organelle transport. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276820 [Multi-domain] Cd Length: 325 Bit Score: 332.37 E-value: 3.95e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 6 VKVAVRIRPLLCKEVLHNHQVCVRvIPNSQQVIIGRD---RVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFA 82
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVK-FDPEDTVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 83 YGQTGSGKTYTIGGGHIAsvvEGQKGIIPRAIQEIFQSISEHPS-IEFNVKVSYIEVYKEDLRDLleLETSMKDLHIRED 161
Cdd:cd01369 83 YGQTSSGKTYTMEGKLGD---PESMGIIPRIVQDIFETIYSMDEnLEFHVKVSYFEIYMEKIRDL--LDVSKTNLSVHED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 162 EKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNVeaaEDGSWYSprhivSKFH 241
Cdd:cd01369 158 KNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ--ENV---ETEKKKS-----GKLY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 242 FVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDprRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPS 321
Cdd:cd01369 228 LVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD--GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPS 305
|
330 340
....*....|....*....|
gi 1622873320 322 SSNFDESLNSLKYANRARNI 341
Cdd:cd01369 306 SYNESETLSTLRFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
6-348 |
8.00e-102 |
|
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: 327.36 E-value: 8.00e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 6 VKVAVRIRPLLCKEVLHNHQVCVRVIPNSQQVII--------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 78 ATVFAYGQTGSGKTYTIGGGHiaSVVEGQK-------GIIPRAIQEIFQSISEHpSIEFNVKVSYIEVYKEDLRDLLELE 150
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMEGDR--SPNEEYTweldplaGIIPRTLHQLFEKLEDN-GTEYSVKVSYLEIYNEELFDLLSPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 151 TS-MKDLHIRED--EKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNVEAAEd 227
Cdd:cd01364 161 SDvSERLRMFDDprNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 228 gswyspRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDprrKSSHIPYRDAKITRLLKDSLG 307
Cdd:cd01364 240 ------LVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLG 310
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1622873320 308 GSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01364 311 GRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
6-348 |
1.55e-101 |
|
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: 327.00 E-value: 1.55e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 6 VKVAVRIRPLLCKEV---------LHNHQVCVRVIPNSQQVIIGRDRV---FTFDFVF------GKN-STQDEVYNTCIK 66
Cdd:cd01365 3 VKVAVRVRPFNSREKernskcivqMSGKETTLKNPKQADKNNKATREVpksFSFDYSYwshdseDPNyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 67 PLVLSLIEGYNATVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSI--SEHPSIEFNVKVSYIEVYKEDLR 144
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMG------TQEQPGIIPRLCEDLFSRIadTTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 145 DLLELETSMKD--LHIREDEKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNV 222
Cdd:cd01365 157 DLLNPKPKKNKgnLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQ--KRH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 223 EAAEDGSwyspRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRR-----KSSHIPYRDAK 297
Cdd:cd01365 235 DAETNLT----TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1622873320 298 ITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01365 311 LTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
5-337 |
2.97e-84 |
|
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: 278.03 E-value: 2.97e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 5 PVKVAVRIRPLLCKEVLHNHQVCVRVIPNSQQVI-IGRDRV----------FTFDFVFGKNSTQDEVYNTCIKPLVLSLI 73
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVhEPKLKVdltkyienhtFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 74 EGYNATVFAYGQTGSGKTYTIGGGHiaSVVEGQKGIIPRAIQEIFQSISEHPSIE-FNVKVSYIEVYKEDLRDLLEletS 152
Cdd:cd01367 81 EGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKLPYKDnLGVTVSFFEIYGGKVFDLLN---R 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 153 MKDLHIREDEKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknvEAAEDGSwys 232
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-------RDRGTNK--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 233 prhIVSKFHFVDLAGSER-VTKTGNTGERFKESIQINSGLLALGNVISALGDPrrkSSHIPYRDAKITRLLKDSL-GGSA 310
Cdd:cd01367 226 ---LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQN---KAHIPFRGSKLTQVLKDSFiGENS 299
|
330 340
....*....|....*....|....*..
gi 1622873320 311 KTVMITCVSPSSSNFDESLNSLKYANR 337
Cdd:cd01367 300 KTCMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
5-348 |
6.12e-84 |
|
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: 277.85 E-value: 6.12e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 5 PVKVAVRIRPLLCKEVLHNHQVCVRVIPNSQQVIIG-RDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 84 GQTGSGKTYTIGG--GHIASVVEGQKGIIPRAIQEIFQSISEH-----PSIEFNVKVSYIEVYKEDLRDLleLETSMKDL 156
Cdd:cd01373 82 GQTGSGKTYTMWGpsESDNESPHGLRGVIPRIFEYLFSLIQREkekagEGKSFLCKCSFLEIYNEQIYDL--LDPASRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 157 HIREDEKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknvEAAEDGSWYSpRHI 236
Cdd:cd01373 160 KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI-------ESWEKKACFV-NIR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 237 VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGD-PRRKSSHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd01373 232 TSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAII 311
|
330 340 350
....*....|....*....|....*....|...
gi 1622873320 316 TCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01373 312 ANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
5-335 |
1.16e-82 |
|
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: 274.27 E-value: 1.16e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 5 PVKVAVRIRPLLCKEVLHNHQVCVRVIpNSQQV----------------IIGRDRVFTFDFVFGKNSTQDEVYNTCIKPL 68
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVI-NSTTVvlhppkgsaanksernGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 69 VLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISehpsiEFNVKVSYIEVYKEDLRDLLE 148
Cdd:cd01368 81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGS------PGDGGILPRSLDVIFNSIG-----GYSVFVSYIEIYNEYIYDLLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 149 LETS-----MKDLHIREDEKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNVE 223
Cdd:cd01368 150 PSPSsptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 224 AAEDGSWYSPRhiVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISAL--GDPRRKSSHIPYRDAKITRL 301
Cdd:cd01368 230 GDVDQDKDQIT--VSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLreNQLQGTNKMVPFRDSKLTHL 307
|
330 340 350
....*....|....*....|....*....|....
gi 1622873320 302 LKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYA 335
Cdd:cd01368 308 FQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
45-388 |
2.04e-82 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 281.24 E-value: 2.04e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 45 FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISEH 124
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGT------EEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 125 PSI-EFNVKVSYIEVYKEDLRDLLELETsmKDLHIREDEKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEH 203
Cdd:COG5059 132 SMTkDFAVSISYLEIYNEKIYDLLSPNE--ESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 204 SSRSHAIFTISICQVHKNveaaedgswySPRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGD 283
Cdd:COG5059 210 SSRSHSIFQIELASKNKV----------SGTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 284 PRrKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVNFSPESDR-IDEMEFE 362
Cdd:COG5059 280 KK-KSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReIEEIKFD 358
|
330 340
....*....|....*....|....*..
gi 1622873320 363 IKLLREALQSQQAN-VSQTSQINREGS 388
Cdd:COG5059 359 LSEDRSEIEILVFReQSQLSQSSLSGI 385
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
5-339 |
1.02e-80 |
|
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: 267.83 E-value: 1.02e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 5 PVKVAVRIRPLLCKEVLHNHQVCVRVIpNSQQVIIGRDRV------FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNA 78
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELADPRNhgetlkYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 79 TVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQsISEHPSIEFNVKVSYIEVYKEDLRDLLELETsmKDLHI 158
Cdd:cd01376 80 TVFAYGSTGAGKTFTMLG------SPEQPGLMPLTVMDLLQ-MTRKEAWALSFTMSYLEIYQEKILDLLEPAS--KELVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 159 REDEKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNVeaaedgswySPRHIVS 238
Cdd:cd01376 151 REDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLA---------PFRQRTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 239 KFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISAL--GDPRrksshIPYRDAKITRLLKDSLGGSAKTVMIT 316
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALnkNLPR-----IPYRDSKLTRLLQDSLGGGSRCIMVA 296
|
330 340
....*....|....*....|...
gi 1622873320 317 CVSPSSSNFDESLNSLKYANRAR 339
Cdd:cd01376 297 NIAPERTFYQDTLSTLNFAARSR 319
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
33-339 |
6.75e-73 |
|
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: 246.34 E-value: 6.75e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 33 NSQQviigRDRVFTFDFVFgKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGHIASvveGQKGIIPR 112
Cdd:cd01375 42 NNQQ----EDWSFKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENY---KHRGIIPR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 113 AIQEIFQSISEHPSIEFNVKVSYIEVYKEDLRDLL----ELETSMKDLHIREDEKGNTVIVGAKECHVESADEVMSLLET 188
Cdd:cd01375 114 ALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 189 GNAARHTGTTQMNEHSSRSHAIFTIsicqvHKNVEAAEDGswySPRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQIN 268
Cdd:cd01375 194 GETNRIIASHTMNKNSSRSHCIFTI-----HLEAHSRTLS---SEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYIN 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622873320 269 SGLLALGNVISALGDPRRksSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRAR 339
Cdd:cd01375 266 KSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
6-397 |
3.81e-62 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 233.29 E-value: 3.81e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 6 VKVAVRIRPLLCKEvlhNHQVCVRVIPNSQQVIIGRdrVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQ 85
Cdd:PLN03188 100 VKVIVRMKPLNKGE---EGEMIVQKMSNDSLTINGQ--TFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 86 TGSGKTYTIGGGHIASVVEG----QKGIIPRAIQEIFQSISEHP------SIEFNVKVSYIEVYKEDLRDLLEleTSMKD 155
Cdd:PLN03188 175 TGSGKTYTMWGPANGLLEEHlsgdQQGLTPRVFERLFARINEEQikhadrQLKYQCRCSFLEIYNEQITDLLD--PSQKN 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 156 LHIREDEKGNTVIVGAKECHVESADEVMSLLETGNAARHTGTTQMNEHSSRSHAIFTisiCQVHKNVEAAEDG-SWYSpr 234
Cdd:PLN03188 253 LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT---CVVESRCKSVADGlSSFK-- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 235 hiVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRR--KSSHIPYRDAKITRLLKDSLGGSAKT 312
Cdd:PLN03188 328 --TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAKL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 313 VMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVNFSPESDrIDEMEFEIKLLREALQSQQANVSQTSQINREGSPDTN 392
Cdd:PLN03188 406 AMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDD-VNFLREVIRQLRDELQRVKANGNNPTNPNVAYSTAWN 484
|
....*
gi 1622873320 393 RIHSL 397
Cdd:PLN03188 485 ARRSL 489
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
26-280 |
1.36e-24 |
|
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: 101.65 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 26 VCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTCiKPLVLSLIEGYN-ATVFAYGQTGSGKTYTIggghiasvve 104
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGESGAGKTETM---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 105 gqKGIIPRAIQEIFqsisehpsiefnvkvSYIEVYKEDLRDLLEletsmkdlhiredekgntvivgakECHVESADEVMS 184
Cdd:cd01363 70 --KGVIPYLASVAF---------------NGINKGETEGWVYLT------------------------EITVTLEDQILQ 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 185 LLETGNAARhTGTTQMNEHSSRSHAIFTIsicqvhknveaaedgswysprhivskfhFVDLAGSERvtktgntgerfkes 264
Cdd:cd01363 109 ANPILEAFG-NAKTTRNENSSRFGKFIEI----------------------------LLDIAGFEI-------------- 145
|
250
....*....|....*.
gi 1622873320 265 iqINSGLLALGNVISA 280
Cdd:cd01363 146 --INESLNTLMNVLRA 159
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
6-147 |
1.58e-18 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 83.42 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 6 VKVAVRIRPLLckevLHNHQVCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTcIKPLVLSLIEGYNATVFAYGQ 85
Cdd:pfam16796 22 IRVFARVRPEL----LSEAQIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQE-ISQLVQSCLDGYNVCIFAYGQ 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622873320 86 TGSGKTytiggghiasvvegqKGIIPRAIQEIFQSISE-HPSIEFNVKVSYIEVYKEDLRDLL 147
Cdd:pfam16796 97 TGSGSN---------------DGMIPRAREQIFRFISSlKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
726-1258 |
2.81e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.26 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 726 YLQESQELNLQKLKNSERILTEAK--QKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELTE 803
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKkaEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 804 TQKQLQELENKdlsdvAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLS-IQNEKRANELEQSVDHMKYQKIQLQ 882
Cdd:PTZ00121 1300 EKKKADEAKKK-----AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKKE 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 883 RKLREENEKRKQLDAVIKRDQQKIKELQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDQLQKLDEQKKWLDEEVEKVL 962
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAE 1454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 963 NQRQELEELEEDLKKREAIVSKKEAllQEKSHLENKKLRSSQAlntdnlkiSTRLNLLEQELSEKNVQLQTSTAEEKIKI 1042
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKKADEAKKKA--EEAKKADEAKKKAEEA--------KKKADEAKKAAEAKKKADEAKKAEEAKKA 1524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1043 SEQVEVLQKEK-DQLQKrrnsVDEKLKNGRVLSPEEehvLFQLEEGIEALEAAIEYKNESIQRRRNSLRASFHNLSRSEA 1121
Cdd:PTZ00121 1525 DEAKKAEEAKKaDEAKK----AEEKKKADELKKAEE---LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1122 NVLEQIACLSPVEIRAILFRYFNKVVNLREAERKQQLYnEEMKMKVLERDNMVRELESALDHLKLqcdRRLTLQQKEHEQ 1201
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-EQLKKKEAEEKKKAEELKKAEEENKI---KAAEEAKKAEED 1673
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1202 KMQLLLHHFKEQDEEGIMETFKTYED---KIQQLEKDLYFYKKTSRDLKKKLKELIMRLE 1258
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAAEALKKEAEeakKAEELKKKEAEEKKKAEELKKAEEENKIKAE 1733
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
789-1146 |
2.61e-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: 68.54 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 789 KLEHDAEQAKVELTETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELE 868
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 869 QsvdhmkyQKIQLQRKLREENEKRKQLDAVIKRDQQKIKELQLKTGQ-EEGLKPKAEDLDACNLKRRKGSFGSIDQLQKL 947
Cdd:TIGR02168 761 A-------EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlREALDELRAELTLLNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 948 DEQKKWLDEEVEKVLNQRQELEELEEDLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDNLKISTRLNLLEQELSEK 1027
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1028 NVQLQtSTAEEKIKISEQVEVLQKEKDQLQKRRNS-------VDEKLKNGRVLSPEE-EHVLFQLEEGIEAL----EAAI 1095
Cdd:TIGR02168 914 RRELE-ELREKLAQLELRLEGLEVRIDNLQERLSEeysltleEAEALENKIEDDEEEaRRRLKRLENKIKELgpvnLAAI 992
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1622873320 1096 -EYknESIQRRRNSLRASFHNLSRSEANVLEQIACLSpVEIRAILFRYFNKV 1146
Cdd:TIGR02168 993 eEY--EELKERYDFLTAQKEDLTEAKETLEEAIEEID-REARERFKDTFDQV 1041
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
703-1253 |
2.36e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 703 VELNDTQDETQKSNLENEDLKIDYLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQ 782
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 783 YSLKVTKLEHDAEQAKVELTETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEK 862
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 863 RANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKELQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSID 942
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 943 QLQKLDEQKKWLDEEVEKVLNQRQELEELEEDLKKREAIVSKKEALLQEKSHLENKKLRSS-QALNTDNLKISTRLNLLE 1021
Cdd:COG1196 502 DYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAiEYLKAAKAGRATFLPLDK 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1022 QELSEKNVQLQTSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYKNES 1101
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGS 661
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1102 IQRRRNSLRASfhnlSRSEANVLEQIAclspveirailfryfnkvvnlREAERKQQLYNEEMKMKVLERDNMVRELESAL 1181
Cdd:COG1196 662 LTGGSRRELLA----ALLEAEAELEEL---------------------AERLAEEELELEEALLAEEEEERELAEAEEER 716
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622873320 1182 DHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDEEGIMEtfKTYEDKIQQLEKDLyfykktsRDLKKKLKEL 1253
Cdd:COG1196 717 LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE--LPEPPDLEELEREL-------ERLEREIEAL 779
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
711-1253 |
5.48e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.93 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 711 ETQKSNLENEDLKIDYLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQY------- 783
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelkeei 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 784 ---SLKVTKLEHDAEQAKVELTETQKQLQELEnKDLSDVAMKVKLQKEFRKKMDA----AKLRVQVLQKKQQDSKKLASL 856
Cdd:PRK03918 241 eelEKELESLEGSKRKLEEKIRELEERIEELK-KEIEELEEKVKELKELKEKAEEyiklSEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 857 siqnEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLdAVIKRDQQKIKELQLKTGQEEGLKPKAEDLDACNLKRrkg 936
Cdd:PRK03918 320 ----EEEINGIEERIKELEEKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEK--- 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 937 sfgsidQLQKLDEQKKWLDEEVEKVLNQRQELEELEEDLKKreAIVSKKEAL-----------------LQEKSHLENKK 999
Cdd:PRK03918 392 ------ELEELEKAKEEIEEEISKITARIGELKKEIKELKK--AIEELKKAKgkcpvcgrelteehrkeLLEEYTAELKR 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1000 LRSSQALNTDNL-KISTRLNLLEQELS-EKNVQLQTSTAEEKIKISEQVEVLQKEKdqLQKRRNSVDEKLKNGRVLSPEE 1077
Cdd:PRK03918 464 IEKELKEIEEKErKLRKELRELEKVLKkESELIKLKELAEQLKELEEKLKKYNLEE--LEKKAEEYEKLKEKLIKLKGEI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1078 EHVLFQLEEgIEALE---AAIEYKNESIQRRRNSLRASFHNLS-RSEANVLEQIACLSPveiraiLFRYFNKVVN----L 1149
Cdd:PRK03918 542 KSLKKELEK-LEELKkklAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEP------FYNEYLELKDaekeL 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1150 REAERKQQLYNEEMKM---KVLERDNMVRELESALDHLKLQCDrrltlqQKEHEQKMQLLLHhfKEQDEEGIMETFKTYE 1226
Cdd:PRK03918 615 EREEKELKKLEEELDKafeELAETEKRLEELRKELEELEKKYS------EEEYEELREEYLE--LSRELAGLRAELEELE 686
|
570 580
....*....|....*....|....*..
gi 1622873320 1227 DKIQQLEKDLYFYKKTSRDLKKKLKEL 1253
Cdd:PRK03918 687 KRREEIKKTLEKLKEELEEREKAKKEL 713
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
875-1190 |
3.74e-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: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 875 KYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKELQLKTGQEE---GLKPKAEDLDACNLKRRKGSFgsIDQLQKLDEQK 951
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAErykELKAELRELELALLVLRLEEL--REELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 952 KWLDEEVEKVLNQRQELEELEEDLKKREAIVSKKEALLQEKSHLENKKLrssQALNTDNLKISTRLNLLEQELSEKNVQL 1031
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI---SRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1032 QTStAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKngrvlspEEEHVLFQLEEGIEALEAAIEYKN----------ES 1101
Cdd:TIGR02168 326 EEL-ESKLDELAEELAELEEKLEELKEELESLEAELE-------ELEAELEELESRLEELEEQLETLRskvaqlelqiAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1102 IQRRRNSLRASFHNLSRSEANVLEQIACLSPVEIRAILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESAL 1181
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
....*....
gi 1622873320 1182 DHLKLQCDR 1190
Cdd:TIGR02168 478 DAAERELAQ 486
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
747-1068 |
1.39e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 59.69 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 747 EAKQKMRELTINIKMKEDLIKELIKTGN----DAKSVSKQYSLKVTKLEHDAEQAKVELTETQKQLQELEnkdlSDVAMK 822
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKslerQAEKAERYKELKAELRELELALLVLRLEELREELEELQ----EELKEA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 823 VKLQKEFRKKMDAAKLRVQVLQ-KKQQDSKKLASLsiqnEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKR 901
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRlEVSELEEEIEEL----QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 902 DQQKIKELQLK----TGQEEGLKPKAEDLDACNLKRRKGSFGSIDQLQKLDEQKKWLDEEVEKVLNQRQELEELEEDLKK 977
Cdd:TIGR02168 328 LESKLDELAEElaelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 978 R-EAIVSKKEALLQEKSHLEnkklrsSQALNTDNLKISTRLNLLEQELSEKNVQLQTsTAEEKIKISEQVEVLQKEKDQL 1056
Cdd:TIGR02168 408 RlERLEDRRERLQQEIEELL------KKLEEAELKELQAELEELEEELEELQEELER-LEEALEELREELEEAEQALDAA 480
|
330
....*....|..
gi 1622873320 1057 QKRRNSVDEKLK 1068
Cdd:TIGR02168 481 ERELAQLQARLD 492
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
731-1260 |
1.65e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 731 QELNLQKL----KNSERILTEAKQKMRELTINIKMKEDlIKELIKTgndaksvskqyslkvtklehdaeqAKVELTETQK 806
Cdd:PRK03918 153 QILGLDDYenayKNLGEVIKEIKRRIERLEKFIKRTEN-IEELIKE------------------------KEKELEEVLR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 807 QLQELEnkdlsdvamkvKLQKEFRKKMDAAKLRVQVLqkkqqdskklaslsiqnEKRANELEQSvdhmKYQKIQLQRKLR 886
Cdd:PRK03918 208 EINEIS-----------SELPELREELEKLEKEVKEL-----------------EELKEEIEEL----EKELESLEGSKR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 887 EENEKRKQLDAVIKRDQQKIKELQLKTGQEEGLKPKAEDLDACNLKRRKgsfgSIDQLQKLDEQKKWLDEE---VEKVLN 963
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE----YLDELREIEKRLSRLEEEingIEERIK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 964 QRQELEELEEDLKKREAIVSKKEALLqEKSHLENKKLRSSQAlNTDNLKisTRLNLLEQELSEKNVQlqtSTAEEKIKIS 1043
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEEL-EERHELYEEAKAKKE-ELERLK--KRLTGLTPEKLEKELE---ELEKAKEEIE 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1044 EQVEVLQKEKDQLQKRRNSVD---EKLKNGRVLSP------EEEHVLFQLEEGIEALEaAIEYKNESIQRRRNSLRASFH 1114
Cdd:PRK03918 405 EEISKITARIGELKKEIKELKkaiEELKKAKGKCPvcgrelTEEHRKELLEEYTAELK-RIEKELKEIEEKERKLRKELR 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1115 NLSRSEANVLEQIACLSPVE-IRAILFRYfnKVVNLREAERKQQLYnEEMKMKVLERDNMVRELESALDHLKLQCDRRLT 1193
Cdd:PRK03918 484 ELEKVLKKESELIKLKELAEqLKELEEKL--KKYNLEELEKKAEEY-EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE 560
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622873320 1194 LQQKEHEQKMQLLLHHfKEQDEEGiMETFKTYEDKIQQLEKdlyFYKK--TSRDLKKKLKELIMRLEME 1260
Cdd:PRK03918 561 LEKKLDELEEELAELL-KELEELG-FESVEELEERLKELEP---FYNEylELKDAEKELEREEKELKKL 624
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
704-1261 |
7.86e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.90 E-value: 7.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 704 ELNDTQDETQKSN--LENEDLKIDYLQESQELNLQKLKNSERiltEAKQKMRELTINIKMKEDLiKELIKTGNDAKSVSK 781
Cdd:pfam02463 245 LLRDEQEEIESSKqeIEKEEEKLAQVLKENKEEEKEKKLQEE---ELKLLAKEEEELKSELLKL-ERRKVDDEEKLKESE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 782 QyslKVTKLEHDAEQAKVELTETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNE 861
Cdd:pfam02463 321 K---EKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 862 KRANELEQSVDhmkyQKIQLQRKLREENEKRKQLDAVIKRDQQKIKELQLKTGQEEGLKpkaedldacnlkrrkgsfgsi 941
Cdd:pfam02463 398 ELKSEEEKEAQ----LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE--------------------- 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 942 DQLQKLDEQKKWLDEEVEKVLNQRQELEELEEDLKKREAIVSKKEALLQEKSHLENKKLRssqaLNTDNLKISTRLNLLE 1021
Cdd:pfam02463 453 LEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL----LALIKDGVGGRIISAH 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1022 QELSEKNVQLQTSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRVLSPEEEHVLFQL-----------EEGIEA 1090
Cdd:pfam02463 529 GRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLksiavleidpiLNLAQL 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1091 LEAAIEYKNESIQRRRNSLRASFHNLSRSEANVLEQIACLSPVEIRAILFRYFNKVVNLREAERKQQLYNEEMKMKvLER 1170
Cdd:pfam02463 609 DKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK-AES 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1171 DNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDEEgIMETFKTYEDKIQQLEKDlyfYKKTSRDLKKKL 1250
Cdd:pfam02463 688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDK-INEELKLLKQKIDEEEEE---EEKSRLKKEEKE 763
|
570
....*....|.
gi 1622873320 1251 KELIMRLEMES 1261
Cdd:pfam02463 764 EEKSELSLKEK 774
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
729-1206 |
9.95e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 56.52 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 729 ESQELNLQKLKNSERILTE-AKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEhDAEQAKVELTETQKQ 807
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE-EQLKKQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 808 LQELEN--KDLSDVAMKVKLQkefRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMK------YQKI 879
Cdd:TIGR00618 269 IEELRAqeAVLEETQERINRA---RKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKqqssieEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 880 QLQRKLREENEKRKQLDAVIKRDQQKIKELQLktgqEEGLKPKAEDLDAcnlkrrkgsfgSIDQLQKLDEQKKWLDEEVE 959
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAHEVATSIREISCQQHTL----TQHIHTLQQQKTT-----------LTQKLQSLCKELDILQREQA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 960 KVLNQRQELEELEEDLKKREA-IVSKKEALLQEKSHLENkKLRSSQALNTDNLKISTRLNLLEQELseKNVQLQTSTAEE 1038
Cdd:TIGR00618 411 TIDTRTSAFRDLQGQLAHAKKqQELQQRYAELCAAAITC-TAQCEKLEKIHLQESAQSLKEREQQL--QTKEQIHLQETR 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1039 KIKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIE---YKNESIQRRRNSLRASFHN 1115
Cdd:TIGR00618 488 KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEdvyHQLTSERKQRASLKEQMQE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1116 LSRSEANVLEQIAclspvEIRAILFRYFNKVVNLREAERKQqlyNEEMKMKVLERDNMVRELESALDHLKLqcdrRLTLQ 1195
Cdd:TIGR00618 568 IQQSFSILTQCDN-----RSKEDIPNLQNITVRLQDLTEKL---SEAEDMLACEQHALLRKLQPEQDLQDV----RLHLQ 635
|
490
....*....|.
gi 1622873320 1196 QKEHEQKMQLL 1206
Cdd:TIGR00618 636 QCSQELALKLT 646
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
707-1261 |
1.96e-07 |
|
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: 55.89 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 707 DTQDETQKSNLENedlKIDYLQESQELNLQKLKNSERI----LTEAKQKMRELTINIKMKEDLIKEliktgnDAKSVSKQ 782
Cdd:pfam15921 244 EDQLEALKSESQN---KIELLLQQHQDRIEQLISEHEVeitgLTEKASSARSQANSIQSQLEIIQE------QARNQNSM 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 783 YSLKVTKLEHDAEQAKVELTETQK----QLQELE------NKDLSDVAMKvklQKEFRKKMDAAKLRVQVLQKKQQDSKK 852
Cdd:pfam15921 315 YMRQLSDLESTVSQLRSELREAKRmyedKIEELEkqlvlaNSELTEARTE---RDQFSQESGNLDDQLQKLLADLHKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 853 LASLSIQNEKRANELEQ----SVDHmkyqkiqLQRKLREENEKRKQLDAVIKRDQQKIKelqlktGQEEGlkpkaedlda 928
Cdd:pfam15921 392 ELSLEKEQNKRLWDRDTgnsiTIDH-------LRRELDDRNMEVQRLEALLKAMKSECQ------GQMER---------- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 929 cNLKRRKGSFGSIDQLQKLDEQKKWLDEEVEKVLnqrQELEELEEDLKKREAIVSKKEALLQEKShlenkklRSSQALNT 1008
Cdd:pfam15921 449 -QMAAIQGKNESLEKVSSLTAQLESTKEMLRKVV---EELTAKKMTLESSERTVSDLTASLQEKE-------RAIEATNA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1009 DNLKISTRLNLLEQELSE--------KNVQ-------LQTSTAEEKIKI-SEQVE--------------VLQKEKDQLQK 1058
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHlknegdhlRNVQtecealkLQMAEKDKVIEIlRQQIEnmtqlvgqhgrtagAMQVEKAQLEK 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1059 RRNSVDEKLKNGRVLSPEEEHVLFQLEEGIEALE-AAIEYKN---------ESIQRRRNSLRASFHNlSRSEANVLEqia 1128
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDAKIRELEARVSDLElEKVKLVNagserlravKDIKQERDQLLNEVKT-SRNELNSLS--- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1129 clspvEIRAILFRYF-NKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDH---LKLQCDRRLTLQQKE---HEQ 1201
Cdd:pfam15921 674 -----EDYEVLKRNFrNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHamkVAMGMQKQITAKRGQidaLQS 748
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622873320 1202 KMQLLLH---------HFKEQDEEGIMETFKTYEDKIQQLEKDLYFYKKTSRDLKKKLKELIMRLEMES 1261
Cdd:pfam15921 749 KIQFLEEamtnankekHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
710-1104 |
4.01e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 54.76 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 710 DETQKSNlenEDLKIDYLQESQEL----NLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSL 785
Cdd:PTZ00121 1537 DEAKKAE---EKKKADELKKAEELkkaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 786 KVTKLEHDAEQAKVElTETQKQLQELENKDlsdvAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLAS-LSIQNEKRA 864
Cdd:PTZ00121 1614 KAEEAKIKAEELKKA-EEEKKKVEQLKKKE----AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeAKKAEEDEK 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 865 NELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKELQLKTGQEEGlKPKAEDldacnLKRRKGSFGSIDQL 944
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED-KKKAEE-----AKKDEEEKKKIAHL 1762
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 945 QKLDEqkkwldeevekvlnqrqeleeleedlKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDNLKiSTRLNLLEQEl 1024
Cdd:PTZ00121 1763 KKEEE--------------------------KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF-DNFANIIEGG- 1814
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1025 SEKNVQLQTSTAEEKIKISEQVE---VLQKEKDQLQK---RRNSVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYK 1098
Cdd:PTZ00121 1815 KEGNLVINDSKEMEDSAIKEVADsknMQLEEADAFEKhkfNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKID 1894
|
....*.
gi 1622873320 1099 NESIQR 1104
Cdd:PTZ00121 1895 KDDIER 1900
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
711-1253 |
4.62e-07 |
|
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: 54.26 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 711 ETQKSNLENEDLKIDYLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKEL----------IKTGNDAKSVS 780
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLnsdlskinseIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 781 KQYSLK------------------VTKLEHDAEQAKVELTETQKQLQELENKDLSDVAMKVKLQKEF---RKKMDAAKLR 839
Cdd:TIGR04523 123 EVELNKlekqkkenkknidkflteIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIdkiKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 840 VQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLreeNEKRKQLDAVIKRDQQKIKELQLKTGQEEGL 919
Cdd:TIGR04523 203 LSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI---SNTQTQLNQLKDEQNKIKKQLSEKQKELEQN 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 920 KPKAEDLDA---------CNLKRRKGSFGSIDQLQKLDEQKKWLDEEVEKVLNQRQELEELEEDLKKREAIVSKKEALLQ 990
Cdd:TIGR04523 280 NKKIKELEKqlnqlkseiSDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENS 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 991 EKSHLENKKLRSSQALNTDNLKISTRLNLLEQELSEKNVQLQTSTAEEKIKiSEQVEVLQKEKDQLQKRRnsvdEKLKNG 1070
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQK-DEQIKKLQQEKELLEKEI----ERLKET 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1071 RVLSPEE----EHVLFQLEEGIEALEAAIEYKNESIQRRRNSLRASFHNLSRSEANVLEQIACLSPVEIRAILFRYFNKV 1146
Cdd:TIGR04523 435 IIKNNSEikdlTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1147 VNLREAERKQQLynEEMKMKVLERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLLLHH-----FKEQDEegIMET 1221
Cdd:TIGR04523 515 LTKKISSLKEKI--EKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQtqkslKKKQEE--KQEL 590
|
570 580 590
....*....|....*....|....*....|..
gi 1622873320 1222 FKTYEDKIQQLEKDLYFYKKTSRDLKKKLKEL 1253
Cdd:TIGR04523 591 IDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
838-1258 |
5.12e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 838 LRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVikrdQQKIKELQlktgqee 917
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL----EAELEELR------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 918 glkpkaEDLDAcnLKRRKGSFGSIDQLQKLDEQKKWLDEEVEKVLNQRQELEELEEDLKKREA-IVSKKEALLQEKSHLE 996
Cdd:COG4717 116 ------EELEK--LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAeLAELQEELEELLEQLS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 997 NKKLRSSQALNTDNLKISTRLNLLEQELSEKNVQLQtsTAEEKIKISEQVEVLQKEKDQLQKRRNS------VDEKLKNG 1070
Cdd:COG4717 188 LATEEELQDLAEELEELQQRLAELEEELEEAQEELE--ELEEELEQLENELEAAALEERLKEARLLlliaaaLLALLGLG 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1071 RVLSPEEEHV--LFQLEEGIEALEAAIEYKNESIQRRRNSLRASFHNLSRSEANVLEQIAC---LSPVEIRAILFRYFNK 1145
Cdd:COG4717 266 GSLLSLILTIagVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalgLPPDLSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1146 VVNLREAERKQQLYNEEMKMKVL--ERDNMVREL----ESALDHLKLQCDRRLTLQQKEHEQKMQLLLhHFKEQDEEGIM 1219
Cdd:COG4717 346 IEELQELLREAEELEEELQLEELeqEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEE-LLGELEELLEA 424
|
410 420 430
....*....|....*....|....*....|....*....
gi 1622873320 1220 ETFKTYEDKIQQLEKDLYFYKKTSRDLKKKLKELIMRLE 1258
Cdd:COG4717 425 LDEEELEEELEELEEELEELEEELEELREELAELEAELE 463
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
705-1050 |
6.43e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 54.15 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 705 LNDTQ---DETQKSNLENEDLKIDYLQESQEL-----NLQKLKNSEriLTEAKQKMRELTInikmkEDLIKELIKTGNDA 776
Cdd:PRK11281 65 LEQTLallDKIDRQKEETEQLKQQLAQAPAKLrqaqaELEALKDDN--DEETRETLSTLSL-----RQLESRLAQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 777 KSVSK---QYSLKVTKLEHDAEQAKVELTETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAaklrvqvlqkkqqdskKL 853
Cdd:PRK11281 138 QNAQNdlaEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQA----------------EQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 854 ASLSIQNEKRANELEQSVdhmkyqkiQLQRKLreeNEKRKQLDAVIKRDQQKIKELQlktgqeeglkpkaedlDACNLKR 933
Cdd:PRK11281 202 ALLNAQNDLQRKSLEGNT--------QLQDLL---QKQRDYLTARIQRLEHQLQLLQ----------------EAINSKR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 934 RKGSfgsidqlqkldEQKkwldeeVEKVLNQRQELEELEEDLKKREAIVSKKeallqekshLENKKLRSSQALNT---DN 1010
Cdd:PRK11281 255 LTLS-----------EKT------VQEAQSQDEAARIQANPLVAQELEINLQ---------LSQRLLKATEKLNTltqQN 308
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1622873320 1011 LKISTRLNLLEQelSEKNvqlqtstaeekikISEQVEVLQ 1050
Cdd:PRK11281 309 LRVKNWLDRLTQ--SERN-------------IKEQISVLK 333
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
743-1096 |
3.85e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 51.51 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 743 RILTEAKQKMRELTINIKMKEDLIKELI----KTGNDAKSVSKQYSLKVTKLEHDAEQAKV--------ELTETQKQLQE 810
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKlqelKLKEQAKKALEYYQLKEKLELEEEYLLYLdylklneeRIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 811 LENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENE 890
Cdd:pfam02463 249 EQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEK 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 891 KRKQLDAVIKRDQQKIKELQLKTGQEEGLKPKAEDLDACNLKRR-------KGSFGSIDQLQKLDEQKKWLDEEVEKVLN 963
Cdd:pfam02463 329 ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEeellakkKLESERLSSAAKLKEEELELKSEEEKEAQ 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 964 QRQELEELEEDLKKREAIVSKKEALLQEKShLENKKLRSSQALNTDNLKISTRLNLLEQELSEKNVQLQTSTAEEKIKIS 1043
Cdd:pfam02463 409 LLLELARQLEDLLKEEKKEELEILEEEEES-IELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLE 487
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1622873320 1044 EQVEVLQKEKDqLQKRRNSVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIE 1096
Cdd:pfam02463 488 LLLSRQKLEER-SQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE 539
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
723-938 |
7.35e-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: 49.76 E-value: 7.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 723 KIDYLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELT 802
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 803 ETQKQLQE-----------------LENKDLSDVAMKVKLQKEFrkkmdaAKLRVQVLQKKQQDSKKLASLSIQNEKRAN 865
Cdd:COG4942 101 AQKEELAEllralyrlgrqpplallLSPEDFLDAVRRLQYLKYL------APARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 866 ELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKELQ--------LKTGQEEGLKPKAEDLDACNLKRRKGS 937
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQqeaeeleaLIARLEAEAAAAAERTPAAGFAALKGK 254
|
.
gi 1622873320 938 F 938
Cdd:COG4942 255 L 255
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
742-1201 |
8.04e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 8.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 742 ERILTEAKQKMRELTINIKMKEDliKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELT----------ETQKQLQEL 811
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARETRDeadevleeheERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 812 EnKDLSDVAMKVKlqkEFRKKMDAAKLRVQVLQKKQQD-----SKKLASLSIqNEKRANELEQSVDHMKYQKIQLQRKLR 886
Cdd:PRK02224 257 E-AEIEDLRETIA---ETEREREELAEEVRDLRERLEEleeerDDLLAEAGL-DDADAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 887 EENEKRKQLDAVIKRDQQKIKELQlktGQEEGLKPKAEDLDA----CNLKRRKGSfGSIDQLQK---------------L 947
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLE---ERAEELREEAAELESeleeAREAVEDRR-EEIEELEEeieelrerfgdapvdL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 948 DEQKKWLDEEVEKVLNQRQELEELEEDLKKREAIVSKKEALLQEKSHLE-NKKLRSS---QALNTDNLKISTrlnlLEQE 1023
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPEcGQPVEGSphvETIEEDRERVEE----LEAE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1024 LSEknVQLQTSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYKNESIQ 1103
Cdd:PRK02224 484 LED--LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1104 RRR---NSLRASFHNLSRSEANVLEQIACLSPV-EIRAILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELES 1179
Cdd:PRK02224 562 EAEeeaEEAREEVAELNSKLAELKERIESLERIrTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEA 641
|
490 500
....*....|....*....|..
gi 1622873320 1180 ALDhlklqcDRRLTLQQKEHEQ 1201
Cdd:PRK02224 642 EFD------EARIEEAREDKER 657
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
883-1252 |
1.21e-05 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 49.90 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 883 RKLREENEKRKQLDAVIKRDQQKIKELQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSI---DQLQKLDEQKKWLDEEVE 959
Cdd:PLN02939 38 RRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQKSTSSDDDhnrASMQRDEAIAAIDNEQQT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 960 KVLNQRQELEELEEDL-----KKREAIVSKKEALLQEKSHLEnKKLRSSQALNTdnlkistRLNLLEQELSEKNVQLQTS 1034
Cdd:PLN02939 118 NSKDGEQLSDFQLEDLvgmiqNAEKNILLLNQARLQALEDLE-KILTEKEALQG-------KINILEMRLSETDARIKLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1035 tAEEKIkiseQVEVLQkekDQLQKRRNSVDEK--LKNGRVLSPEEEHVLFQLE-----EGIEALEAAIEYKNES------ 1101
Cdd:PLN02939 190 -AQEKI----HVEILE---EQLEKLRNELLIRgaTEGLCVHSLSKELDVLKEEnmllkDDIQFLKAELIEVAETeervfk 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1102 IQRRRNSLRASFHNLSRSEANVLEQIACLSPVEIRAilfrYFNKVVNLREAERKQQLYNEEMKMkVLERD----NMVREL 1177
Cdd:PLN02939 262 LEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDC----WWEKVENLQDLLDRATNQVEKAAL-VLDQNqdlrDKVDKL 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622873320 1178 ESALDHLKLQ--CDRRLTLQQkeheQKMQLLLHHFKEQDEEgIMETFKTYEDKIQQLEKDLYFYKKTSRdlKKKLKE 1252
Cdd:PLN02939 337 EASLKEANVSkfSSYKVELLQ----QKLKLLEERLQASDHE-IHSYIQLYQESIKEFQDTLSKLKEESK--KRSLEH 406
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
732-1121 |
1.89e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 732 ELNLQKLKNSERILTEAKQKMRELTINIKMKEDL---IKELIKTGNDAKSVSKQYSLKVTKLEHDAE--QAKVELTETQK 806
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELeeeLEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 807 QLQELENkdlsdvamkvKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLR 886
Cdd:COG4717 147 RLEELEE----------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 887 EENEKRKQLDAVIKR---------DQQKIKELQLKTGQE------EGLKPKAEDLDACNLKRRKGSFGSI-DQLQKLDEQ 950
Cdd:COG4717 217 EAQEELEELEEELEQleneleaaaLEERLKEARLLLLIAaallalLGLGGSLLSLILTIAGVLFLVLGLLaLLFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 951 KKWLDEEVEKVLNQRQELEELEEDLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDNLKISTRLNL--LEQELSEKN 1028
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLeeLEQEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1029 VQLQTSTAEEKIKISEQVEvlqkEKDQLQKRRNSVDEKL--KNGRVLSPEEEHVLFQLEEGIEALEAAIEYKNE---SIQ 1103
Cdd:COG4717 377 AEAGVEDEEELRAALEQAE----EYQELKEELEELEEQLeeLLGELEELLEALDEEELEEELEELEEELEELEEeleELR 452
|
410
....*....|....*...
gi 1622873320 1104 RRRNSLRASFHNLSRSEA 1121
Cdd:COG4717 453 EELAELEAELEQLEEDGE 470
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
977-1140 |
2.12e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 977 KREAIVSKKEALLQEKShlENKKLRSSqalntdnlkistrlnlLEQELSEKNVQLQtsTAEEKIKISEqvEVLQKEKDQL 1056
Cdd:PRK12704 48 KKEAEAIKKEALLEAKE--EIHKLRNE----------------FEKELRERRNELQ--KLEKRLLQKE--ENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1057 QKRRNSVDEKLKNgrvlspeeehvLFQLEEGIEALEAAIEYKNESIQRRrnslrasfhnlsrseanvLEQIACLSPVEIR 1136
Cdd:PRK12704 106 EKREEELEKKEKE-----------LEQKQQELEKKEEELEELIEEQLQE------------------LERISGLTAEEAK 156
|
....
gi 1622873320 1137 AILF 1140
Cdd:PRK12704 157 EILL 160
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
851-1128 |
2.77e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 851 KKLASLSIQNEK--RANELEQSVDHMKYQKIQLQRKLREEN--EKRKQLDAVIKRDQQKIKELQLKTGQEEGLKPKAEDL 926
Cdd:COG1196 200 RQLEPLERQAEKaeRYRELKEELKELEAELLLLKLRELEAEleELEAELEELEAELEELEAELAELEAELEELRLELEEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 927 DACNLKRRKGSFGSIDQLQKLDEQKKWLDEEVEKVLNQRQELEELEEDLKKREAIVSKKEALLQEKSHLENKKLRSSQAL 1006
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1007 NTDNLKISTRLNLLEQELSEKNVQLQTSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRVLSPEEEHVLFQLEE 1086
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1622873320 1087 GIEALEAAIEYKNEsIQRRRNSLRASFHNLSRSEANVLEQIA 1128
Cdd:COG1196 440 EEEALEEAAEEEAE-LEEEEEALLELLAELLEEAALLEAALA 480
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
843-1075 |
4.99e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 4.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 843 LQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKELQLKtgqeeglkpk 922
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE---------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 923 aedldacnLKRRKGSFGS-IDQLQKLDEQKKWL-----DEEVEKVLNQRQELEELEEDLKKREAIVSKKEALLQEKSHLE 996
Cdd:COG4942 99 --------LEAQKEELAElLRALYRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622873320 997 NKKlrssQALNTDNLKISTRLNLLEQELSEKNvQLQTSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRVLSP 1075
Cdd:COG4942 171 AER----AELEALLAELEEERAALEALKAERQ-KLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
827-1166 |
6.39e-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: 47.66 E-value: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 827 KEFRKKMDAAKlrvQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKI 906
Cdd:pfam02463 166 RLKRKKKEALK---KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 907 KELQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDQLQKL-DEQKKWLDEEVEKVLNQRQELEELEEDLKKREAIVSKK 985
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLqEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 986 EALLQEKshlenKKLRSSQALNTDNLKISTRLNLLEQELSEKNVQLQTSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDE 1065
Cdd:pfam02463 323 KKKAEKE-----LKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1066 KLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYKNESIQRRRNSLRASFHNLSRSEANVL---EQIACLSPVEIRAILFRY 1142
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQelkLLKDELELKKSEDLLKET 477
|
330 340
....*....|....*....|....
gi 1622873320 1143 FNKVVNLREAERKQQLYNEEMKMK 1166
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQK 501
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
736-966 |
9.50e-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: 46.30 E-value: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 736 QKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELTETQKQLQElenkd 815
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 816 lsdvamkvkLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQN----EKRANELEQSVDHMKYQKIQLQRKLREENEK 891
Cdd:COG4942 95 ---------LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfldaVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622873320 892 RKQLDAVIKRDQQKIKELQLKTGQEEGLKPKAEDLDAcNLKRRKGSFGsiDQLQKLDEQKKWLDEEVEKVLNQRQ 966
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLA-RLEKELAELA--AELAELQQEAEELEALIARLEAEAA 237
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
704-910 |
1.20e-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: 46.59 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 704 ELNDTQDETQKSNLENEDLKIDYLQESQELNLQK--LKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSK 781
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 782 QYSLKVTKLEHDAEQAKVELTETQKQLQELEN--KDLSDVAMKV--KLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLS 857
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAelTLLNEEAANLreRLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622873320 858 IQNEK---RANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKELQ 910
Cdd:TIGR02168 859 AEIEEleeLIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
781-909 |
2.70e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 781 KQYSLKVTKLEHDA----EQAKVELtETQKQLQELENKDLSDvAMKVKLQKEFR-KKMDAAKLRVQVLQKKQQDSKKLAS 855
Cdd:PRK12704 27 KIAEAKIKEAEEEAkrilEEAKKEA-EAIKKEALLEAKEEIH-KLRNEFEKELReRRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622873320 856 LsiqnEKRANELEQsvdhmkyQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEL 909
Cdd:PRK12704 105 L----EKREEELEK-------KEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
723-1121 |
2.84e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.45 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 723 KIDYLQESQELNLQ-KLKNSERILTEAKQKMRELTINIKMKE--DLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKV 799
Cdd:COG5022 770 RIKKIQVIQHGFRLrRLVDYELKWRLFIKLQPLLSLLGSRKEyrSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQ 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 800 ELTET---QKQLQELENKDLSDvamkvklqkEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQsvdhmky 876
Cdd:COG5022 850 KFGRSlkaKKRFSLLKKETIYL---------QSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKK------- 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 877 qkiQLQRKLREENEKRKQLDAVIKRdqqKIKELQLKTGQEEglkpkaedldacnlkrrkgSFGSIDQLQKLDEQKKWLDE 956
Cdd:COG5022 914 ---SLSSDLIENLEFKTELIARLKK---LLNNIDLEEGPSI-------------------EYVKLPELNKLHEVESKLKE 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 957 EVEKVLNQRQELEELEEDLKKREAIVSKKEALLQEKSHlENKKLRSSQALNTDNLKISTRLNLLEQELSE--KNVQLQTS 1034
Cdd:COG5022 969 TSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSK-QYGALQESTKQLKELPVEVAELQSASKIISSesTELSILKP 1047
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1035 TAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRVLspeeehvlfqleEGIEALEAAIEYKNESIQRRRNSLRASFH 1114
Cdd:COG5022 1048 LQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQL------------ESTENLLKTINVKDLEVTNRNLVKPANVL 1115
|
....*..
gi 1622873320 1115 NLSRSEA 1121
Cdd:COG5022 1116 QFIVAQM 1122
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
955-1258 |
3.46e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.06 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 955 DEEVEKVLNQrqeLEELEEDLKKREAIVSKKEALLQEKSHLENKKLRsSQALNTDNLKISTRLNLLEQELSEK---NVQL 1031
Cdd:TIGR02169 169 DRKKEKALEE---LEEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREYEGYELLKEKEALERqkeAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1032 QTSTAEEKI-KISEQVEVLQKEKDQLQKRRNSVDEKLKNgrvlSPEEEHVLFQ-----LEEGIEALEAAIEYKNESIQR- 1104
Cdd:TIGR02169 245 QLASLEEELeKLTEEISELEKRLEEIEQLLEELNKKIKD----LGEEEQLRVKekigeLEAEIASLERSIAEKERELEDa 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1105 ---------RRNSLRASFHNLSRSEANVLEQIACLSPvEIRAILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVR 1175
Cdd:TIGR02169 321 eerlakleaEIDKLLAEIEELEREIEEERKRRDKLTE-EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1176 ELESALDHL--KLQCDRRLTLQQKEHEQKMQLLLHHFKEQDE--EGIMETFKTYEDKIQQLEKDLYFYKKTSRDLKKKLK 1251
Cdd:TIGR02169 400 EINELKRELdrLQEELQRLSEELADLNAAIAGIEAKINELEEekEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479
|
....*..
gi 1622873320 1252 ELIMRLE 1258
Cdd:TIGR02169 480 RVEKELS 486
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
710-996 |
3.60e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 710 DETQKSNLENEDLKIDYLQESQELNLQKLKNSERILTEAKQkmRELtinikmkedlikELIKTGNDAKSVSKQYSLKVTK 789
Cdd:pfam17380 319 EEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERK--REL------------ERIRQEEIAMEISRMRELERLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 790 LEHDAEQAKVEltetqkqlQELEnkdlsdVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQ 869
Cdd:pfam17380 385 MERQQKNERVR--------QELE------AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMER 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 870 SVDHMKYQKIQLQR-KLREENEKRKQLDAVI-KRDQQKIKELQLKTGQEEgLKPKAEDLDACNLKRRKGSfgsidqlQKL 947
Cdd:pfam17380 451 VRLEEQERQQQVERlRQQEEERKRKKLELEKeKRDRKRAEEQRRKILEKE-LEERKQAMIEEERKRKLLE-------KEM 522
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1622873320 948 DEQKKWLDEEVEKvlNQRQELEELEEDLKKREAIVSKKEALLQEKSHLE 996
Cdd:pfam17380 523 EERQKAIYEEERR--REAEEERRKQQEMEERRRIQEQMRKATEERSRLE 569
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
805-1187 |
4.51e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 805 QKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQK--IQLQ 882
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqlLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 883 RKLREENEKRKQLDAVIKRDQQKIKELQLKTGQEEGLKPKAEDL-DACNLKRRKGSFGSIDQLQKLDEQKKWLDEEVEKV 961
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELqEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 962 LNQRQELEELEEDLKKREAIVSKKEALLQEKSHLE--------------------------------------------- 996
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKearlllliaaallallglggsllsliltiagvlflvlgllallfl 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 997 --NKKLRSSQALNTDNLKISTRLNLLEQELSEKNVQLQTSTAEEKIKISEQVEVLQkEKDQLQKRRNSVDEKLKNGRVLS 1074
Cdd:COG4717 292 llAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE-ELQELLREAEELEEELQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1075 PEEEHVLFQLEEGIEALEAAIEYKNE--SIQRRRNSLRASFHNLSRSEANVLEQiacLSPVEIRAilfRYFNKVVNLREA 1152
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEyqELKEELEELEEQLEELLGELEELLEA---LDEEELEE---ELEELEEELEEL 444
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1622873320 1153 ERKQQLYNEEM-----KMKVLERDNMVRELESALDHLKLQ 1187
Cdd:COG4717 445 EEELEELREELaeleaELEQLEEDGELAELLQELEELKAE 484
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
985-1258 |
5.24e-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: 44.67 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 985 KEALLQEKSHLENkklRSSQAlntdnlkiSTRLNLLEQELSEKNVQLQTSTAEEKiKISEQVEVLQKEKDQLQKRRNSVD 1064
Cdd:TIGR02169 690 LSSLQSELRRIEN---RLDEL--------SQELSDASRKIGEIEKEIEQLEQEEE-KLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1065 EKLKNGRVLSPEEEHVLFQLEEGIEALEAaiEYKNESIQRRRNSLRASFHNLSRSEANVLEQIACLSPVEIRAILFRyfN 1144
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE--K 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1145 KVVNL---------REAERKQQLYN-----EEMKMKVLERDNMVRELESALDHLKLQCDRRLT----LQQKEHEQKMQL- 1205
Cdd:TIGR02169 834 EIQELqeqridlkeQIKSIEKEIENlngkkEELEEELEELEAALRDLESRLGDLKKERDELEAqlreLERKIEELEAQIe 913
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622873320 1206 -LLHHFKEQDE--EGIMETFKTYEDKIQQLEKDLYfYKKTSRDLKKKLKELIMRLE 1258
Cdd:TIGR02169 914 kKRKRLSELKAklEALEEELSEIEDPKGEDEEIPE-EELSLEDVQAELQRVEEEIR 968
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
704-1258 |
5.61e-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: 44.29 E-value: 5.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 704 ELNDTQDETQKSNLENEDLkidyLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQY 783
Cdd:TIGR02169 252 ELEKLTEEISELEKRLEEI----EQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 784 SLKVTKLEHDAEQAKVELTETQKQ------------------LQELENKDLSDVAMKVKLqKEFRKKMDAAKLRVQVLQ- 844
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRrdklteeyaelkeeledlRAELEEVDKEFAETRDEL-KDYREKLEKLKREINELKr 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 845 ---KKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKELQLKTGQ-EEGLK 920
Cdd:TIGR02169 407 eldRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRvEKELS 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 921 PKAEDLDACNLKRR--------------------KGSFGSIDQLQKLDEQKKwldEEVEKVLNQRQELEELEEDLKKREA 980
Cdd:TIGR02169 487 KLQRELAEAEAQARaseervrggraveevlkasiQGVHGTVAQLGSVGERYA---TAIEVAAGNRLNNVVVEDDAVAKEA 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 981 IVSKKEALLQEKSHLENKKLRSSQ--------------ALN---------------------------TDNLKISTRLNL 1019
Cdd:TIGR02169 564 IELLKRRKAGRATFLPLNKMRDERrdlsilsedgvigfAVDlvefdpkyepafkyvfgdtlvvedieaARRLMGKYRMVT 643
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1020 LEQELSEKN-------------VQLQTSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRVLSPEEEHVLFQLEE 1086
Cdd:TIGR02169 644 LEGELFEKSgamtggsraprggILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK 723
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1087 GIEALEAAIEYKNESIQRRRNSLRAsfhnLSRSEANVLEQIAclspvEIRAILFRYFNKVVNLREA----------ERKQ 1156
Cdd:TIGR02169 724 EIEQLEQEEEKLKERLEELEEDLSS----LEQEIENVKSELK-----ELEARIEELEEDLHKLEEAlndlearlshSRIP 794
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1157 QLYNE--EMKMKVLERDNMVRELESALDHL------------KLQCDRRLTLQQKEHEQKMQLLLHHFKEQDEEGIMEtf 1222
Cdd:TIGR02169 795 EIQAElsKLEEEVSRIEARLREIEQKLNRLtlekeylekeiqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE-- 872
|
650 660 670
....*....|....*....|....*....|....*.
gi 1622873320 1223 ktYEDKIQQLEKDLYFYKKTSRDLKKKLKELIMRLE 1258
Cdd:TIGR02169 873 --LEAALRDLESRLGDLKKERDELEAQLRELERKIE 906
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
752-1060 |
5.97e-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: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 752 MRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELTETQKQLQELENKDLSDVAMKVKLQKEFRK 831
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 832 KMDAAKLRVQVLQKKQQDSKKLAslsiqneKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIkrdQQKIKELQL 911
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLT-------QRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL---QQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 912 KTGQEEGLKPKAEDLDACNLKRRKgsfgSIDQLQKLDEQKKWLDEEVEKVLNQ-RQELEELEEDLKKREAIVSKKEALLQ 990
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQD----TITTLTQKLTTAHRKEAENEALLEElRSLQERLNASERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622873320 991 EKSH----LENKKLRSSQAlntdNLKIS-TRLNLLEQE--LSEKNVQLQTSTAEEKIKISEQVEVLQKEKDQLQKRR 1060
Cdd:pfam07888 266 QRDRtqaeLHQARLQAAQL----TLQLAdASLALREGRarWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEER 338
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
728-961 |
6.35e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 728 QESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELiktgndaksvsKQYSLKVTKLEHDAEQAKVELTETQKQ 807
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-----------EELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 808 LQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLRE 887
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622873320 888 ENEKRKQldaviKRDQQKIKELQLKTGQEEGLKPKAEDL--DACNLKRRKGSFGS-IDQLQKLDEQKKWLDEEVEKV 961
Cdd:PRK03918 659 EEYEELR-----EEYLELSRELAGLRAELEELEKRREEIkkTLEKLKEELEEREKaKKELEKLEKALERVEELREKV 730
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
943-1216 |
6.47e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 943 QLQKLDEQKKWLDEEVEKVLNQRQEleeLEEDLKKREAivskKEALLQEKSHLENKKLRSSQAlntDNLKISTRLNLLEQ 1022
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEE---LEAELAELEA----ELEELRLELEELELELEEAQA---EEYELLAELARLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1023 ELsEKNVQLQTSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKNgrvLSPEEEHVLFQLEEGIEALEAAIEyKNESI 1102
Cdd:COG1196 303 DI-ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE---AEEELEEAEAELAEAEEALLEAEA-ELAEA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1103 QRRRNSLRASFHNLSRSEANVLEQIAclspveirailfryfnkvvNLREAERKQQLYNEEMKMKVLERDNMVRELESALD 1182
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLE-------------------ELEEAEEALLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270
....*....|....*....|....*....|....
gi 1622873320 1183 HLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDEE 1216
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
736-908 |
7.57e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 736 QKLKNSERILTEAKQKMRELTINIkmkEDLIKELIKTGNDAKsvskQYSLKVTKLEHDAEQAKVELTETQKQLQELENKD 815
Cdd:PRK00409 495 KRLGLPENIIEEAKKLIGEDKEKL---NELIASLEELERELE----QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 816 LSdvamkvKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIqnekRANELEQSvdhmkyqkiqlQRKLREENEKRKQL 895
Cdd:PRK00409 568 LE------EAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASV----KAHELIEA-----------RKRLNKANEKKEKK 626
|
170
....*....|...
gi 1622873320 896 DAVIKRDQQKIKE 908
Cdd:PRK00409 627 KKKQKEKQEELKV 639
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
710-1245 |
7.83e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.94 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 710 DETQKSNLENEDLKIDYLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKtgndaksvsKQYSLkvTK 789
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE---------KKDHL--TK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 790 LEHDAEQAKVELTETQKQLQE---LENKDLSDVAMKVKLQKEFRKKMDAAklRVQVLQKKQQDSKKLASLSIQNEKRane 866
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEdlqIATKTICQLTEEKEAQMEELNKAKAA--HSFVVTEFEATTCSLEELLRTEQQR--- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 867 LEQSVDHMKYQKIQLQRKLREENEKRKqldaVIKRDQQKIKELQLKTGQEEGLkpkaedldacnLKRRKgsfgsidQLQK 946
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTK----FKNNKEVELEELKKILAEDEKL-----------LDEKK-------QFEK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 947 LDEQKKWLDEEVEKVLNQRQeleELEEDLK-KREAIVSKKEALLQE----KSHLENKKLRSSQaLNTDNLKISTRLNLLE 1021
Cdd:pfam05483 430 IAEELKGKEQELIFLLQARE---KEIHDLEiQLTAIKTSEEHYLKEvedlKTELEKEKLKNIE-LTAHCDKLLLENKELT 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1022 QELSEKNVQLQT------STAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRvlsPEEEHVLFQLEEGIEALEAAI 1095
Cdd:pfam05483 506 QEASDMTLELKKhqediiNCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG---DEVKCKLDKSEENARSIEYEV 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1096 ---EYKNESIQRRRNSLRASFHNLSR------SEANVLEQIACLSPVEIRAILFRYFNKVVNLREAERK----QQLYNEE 1162
Cdd:pfam05483 583 lkkEKQMKILENKCNNLKKQIENKNKnieelhQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKfeeiIDNYQKE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1163 MKMKVLERDNMVRELESAldhlKLQCDRRLTLqQKEHEQKMQlllHHFKEQdeEGIMETFKTYEDKI-QQLEKDLYFYKK 1241
Cdd:pfam05483 663 IEDKKISEEKLLEEVEKA----KAIADEAVKL-QKEIDKRCQ---HKIAEM--VALMEKHKHQYDKIiEERDSELGLYKN 732
|
....
gi 1622873320 1242 TSRD 1245
Cdd:pfam05483 733 KEQE 736
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
827-1096 |
8.57e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 8.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 827 KEFRKKMDAAKLRVQVLQKKQQDSKKLAslsiQNEKRANELEQSVDHMKYQkiQLQRKLREENEKRKQLDAVIKRDQQKI 906
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYA----AARERLAELEYLRAALRLW--FAQRRLELLEAELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 907 KELQlktGQEEGLKPKAEDLDAcnlkRRKGSFGsiDQLQKLDEQKKWLDEEVEKVLNQRQELEELEEDLKkreaivskkE 986
Cdd:COG4913 312 ERLE---ARLDALREELDELEA----QIRGNGG--DRLEQLEREIERLERELEERERRRARLEALLAALG---------L 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 987 ALLQEKSHLENKKLRSSQALNTdnlkISTRLNLLEQELSEKNVQLQTSTaeekikisEQVEVLQKEKDQLQKRRNSVDEK 1066
Cdd:COG4913 374 PLPASAEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDLR--------RELRELEAEIASLERRKSNIPAR 441
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1622873320 1067 LKNGR-----VLSPEEEHVLF-----QLEEGIEALEAAIE 1096
Cdd:COG4913 442 LLALRdalaeALGLDEAELPFvgeliEVRPEEERWRGAIE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
704-960 |
9.96e-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: 43.52 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 704 ELNDTQDETQKSNLENEDLKIDYLQESQELNLQKLKNSERILTEAKQKMRELTINI-KMKEDLIKELIKTGNDAKSVSKQ 782
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALnDLEARLSHSRIPEIQAELSKLEE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 783 YSLKVTKLEHDAEQAKVELTETQKQLQElENKDLSDVAMKVKLQK-EFRKKMDAAKLRvqvLQKKQQDSKKLASLSIQNE 861
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEK-EIQELQEQRIDLKEQIkSIEKEIENLNGK---KEELEEELEELEAALRDLE 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 862 KRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEL-----QLKTGQEEGLKPKAEDLDACNLK---- 932
Cdd:TIGR02169 882 SRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALeeelsEIEDPKGEDEEIPEEELSLEDVQaelq 961
|
250 260 270
....*....|....*....|....*....|...
gi 1622873320 933 ---RRKGSFGSIDQL--QKLDEQKKWLDEEVEK 960
Cdd:TIGR02169 962 rveEEIRALEPVNMLaiQEYEEVLKRLDELKEK 994
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
890-1111 |
1.13e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 890 EKRKQLDAVIKRDQQKIKELQLKTGQEEGLKPKAEDLDACNLKRRKgsfgsidQLQKLDEQKKWLDEEVEKVLNQRQELE 969
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR-------RIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 970 EleeDLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDNLKISTRLNLLEQELSEKNVQLQTSTAEekikISEQVEVL 1049
Cdd:COG4942 97 A---ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE----LAALRAEL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622873320 1050 QKEKDQLQKRRNSVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYKNESIQRRRNSLRA 1111
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
759-910 |
1.15e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 759 IKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELTETQKQLQELEnKDLSdvamkvKLQKEFRKKMDAAKL 838
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ-AEIA------EAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 839 RVQVLQKK----------------------------------------QQDSKKLASLSIQNEKRANELEQSVDHMKYQK 878
Cdd:COG3883 91 RARALYRSggsvsyldvllgsesfsdfldrlsalskiadadadlleelKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190
....*....|....*....|....*....|..
gi 1622873320 879 IQLQRKLREENEKRKQLDAVIKRDQQKIKELQ 910
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
704-1242 |
1.19e-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: 43.50 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 704 ELNDTQDETQKSNLE---NEDLKIDYLQESQELNLQKLKNSERILTEAKQKMRELTInikmkEDLIKELIKTGNDAKSVS 780
Cdd:TIGR00606 585 EINQTRDRLAKLNKElasLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDL-----ERLKEEIEKSSKQRAMLA 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 781 KQ---YSLKVTKLEHDAE----------QAKVELTETQKQLQEL----ENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVL 843
Cdd:TIGR00606 660 GAtavYSQFITQLTDENQsccpvcqrvfQTEAELQEFISDLQSKlrlaPDKLKSTESELKKKEKRRDEMLGLAPGRQSII 739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 844 QKKQqdsKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKL-REENEKRKQLD-AVIKRDQQKIKELQLKTGQEEGlKP 921
Cdd:TIGR00606 740 DLKE---KEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMpEEESAKVCLTDvTIMERFQMELKDVERKIAQQAA-KL 815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 922 KAEDLDACNLKRRKGSFGSIDQLQKLDEQKKWLDEEVEKVLNQRQELEELEEDLKKREAIVSKKEALLQEKSHLENKKLR 1001
Cdd:TIGR00606 816 QGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELST 895
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1002 SSQALNTDNLKISTRLNLLEQ---ELSEKNVQLQTSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRvlspeeE 1078
Cdd:TIGR00606 896 EVQSLIREIKDAKEQDSPLETfleKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK------D 969
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1079 HVLFQLEEGIEALEAAI---EYKNESIQRRRNSLRASFHNLSRSEANVLEQIACLSPVEirailfryfnkvvNLREAERK 1155
Cdd:TIGR00606 970 DYLKQKETELNTVNAQLeecEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKREN-------------ELKEVEEE 1036
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1156 QQLYNEEM-KMKVLERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKmqllLHHFKEQDEEGIMETFKTYEDKIQQLE- 1233
Cdd:TIGR00606 1037 LKQHLKEMgQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEI----KHFKKELREPQFRDAEEKYREMMIVMRt 1112
|
570
....*....|....
gi 1622873320 1234 -----KDLYFYKKT 1242
Cdd:TIGR00606 1113 telvnKDLDIYYKT 1126
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
763-960 |
1.28e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 763 EDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELTETQKQLQELENKdlSDVAMK--VKLQKEFRKKMDAAKLRV 840
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE--IDKLQAeiAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 841 QVLQKKQQDSKKLASL----SIQNE-KRANELEQSVDHMKyQKIQLQRKLREENE-KRKQLDAVIKRDQQKIKELQLKTG 914
Cdd:COG3883 93 RALYRSGGSVSYLDVLlgseSFSDFlDRLSALSKIADADA-DLLEELKADKAELEaKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622873320 915 QEEGLKPKAEDLDAcNLKRRKGSFgsIDQLQKLDEQKKWLDEEVEK 960
Cdd:COG3883 172 ELEAQQAEQEALLA-QLSAEEAAA--EAQLAELEAELAAAEAAAAA 214
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
733-910 |
1.55e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 733 LNLQKLKNSeriLTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELTETQKQLQELE 812
Cdd:COG1579 10 LDLQELDSE---LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 813 N-KDLSDvamkvkLQKEfrkkMDAAKLRVQVLQKKQqdskklaslsIQNEKRANELEQSVDHMKYQKIQLQRKLreeNEK 891
Cdd:COG1579 87 NnKEYEA------LQKE----IESLKRRISDLEDEI----------LELMERIEELEEELAELEAELAELEAEL---EEK 143
|
170
....*....|....*....
gi 1622873320 892 RKQLDAVIKRDQQKIKELQ 910
Cdd:COG1579 144 KAELDEELAELEAELEELE 162
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
708-1127 |
1.56e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 708 TQDETQKSNLENEDLKIDYLQESQELN-----LQKL----KNSERILTEAKQKMRELTINIKMKE-------------DL 765
Cdd:PTZ00440 430 IADYALYSNLEIIEIKKKYDEKINELKksinqLKTLisimKSFYDLIISEKDSMDSKEKKESSDSnyqekvdellqiiNS 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 766 IKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELTETQKQLQELENKDLSDVAMKvklqKEFRKKMDAAKLRVQVLQK 845
Cdd:PTZ00440 510 IKEKNNIVNNNFKNIEDYYITIEGLKNEIEGLIELIKYYLQSIETLIKDEKLKRSMK----NDIKNKIKYIEENVDHIKD 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 846 KQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQ------------------QKIK 907
Cdd:PTZ00440 586 IISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYILNKFYKGDLQELLDElshflddhkylyheakskEDLQ 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 908 ELQLKTGQE-EGLKPKAEDLDACNLKRRKGSFGSIDQLQK--LDEQKKWLDEEVEKVLNQrqeLEELEEDLKKR-EAIVS 983
Cdd:PTZ00440 666 TLLNTSKNEyEKLEFMKSDNIDNIIKNLKKELQNLLSLKEniIKKQLNNIEQDISNSLNQ---YTIKYNDLKSSiEEYKE 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 984 KKEALLQEKSHLENKKLRSSQALNTDNLKISTRLNLLEQELSEKNVQLQtstaeEKIKISEQVEVLQKEKDQLQKRRNS- 1062
Cdd:PTZ00440 743 EEEKLEVYKHQIINRKNEFILHLYENDKDLPDGKNTYEEFLQYKDTILN-----KENKISNDINILKENKKNNQDLLNSy 817
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622873320 1063 --VDEKLKNGRVLSPEEEHVLFQleegiealeaaiEYKNESIQRRRNSLRASFHNLSRSEANVLEQI 1127
Cdd:PTZ00440 818 niLIQKLEAHTEKNDEELKQLLQ------------KFPTEDENLNLKELEKEFNENNQIVDNIIKDI 872
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
785-1220 |
1.74e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 785 LKVTKLEHDAEQAKVELTETQKQLQELENKDLSDVAMkvkLQKEFRKKMDAAKLRVQV----LQKKQQ-----DSKKLAS 855
Cdd:pfam12128 258 LRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRT---LDDQWKEKRDELNGELSAadaaVAKDRSelealEDQHGAF 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 856 LSIQNEKRANELEQSVdhmkyqkiQLQRKLREENEKRKQLDAVIKRDQQKIKELQLKTGQEegLKPKAEDLDacnlkrrk 935
Cdd:pfam12128 335 LDADIETAAADQEQLP--------SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ--NNRDIAGIK-------- 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 936 gsfgsiDQLQKLDEQKKWLDEEVEKVLNQRQELEELEEDLKKREAivskKEALLQEKSHLENKKLRSSQALNTDNLKIST 1015
Cdd:pfam12128 397 ------DKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEF----NEEEYRLKSRLGELKLRLNQATATPELLLQL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1016 RLNLL-------EQELSEKNVQ-LQTSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDE---------------------- 1065
Cdd:pfam12128 467 ENFDErierareEQEAANAEVErLQSELRQARKRRDQASEALRQASRRLEERQSALDElelqlfpqagtllhflrkeapd 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1066 -KLKNGRVLSPE-----------------EEHVLFQLEEGIEALEAAiEY--KNESIQRRRNSLRASFHNLSRSEANVLE 1125
Cdd:pfam12128 547 wEQSIGKVISPEllhrtdldpevwdgsvgGELNLYGVKLDLKRIDVP-EWaaSEEELRERLDKAEEALQSAREKQAAAEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1126 QIACLSpVEIRAILFRYFNKVVNLREAERKQQLYNEEMKMkvlERDNMVRELESALDhLKLQCDRRLTLQQKEHEQKMQL 1205
Cdd:pfam12128 626 QLVQAN-GELEKASREETFARTALKNARLDLRRLFDEKQS---EKDKKNKALAERKD-SANERLNSLEAQLKQLDKKHQA 700
|
490
....*....|....*
gi 1622873320 1206 LLHHFKEQDEEGIME 1220
Cdd:pfam12128 701 WLEEQKEQKREARTE 715
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
711-932 |
2.01e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 711 ETQKSNLENE-----------DLKIDYLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSV 779
Cdd:TIGR04523 390 ESQINDLESKiqnqeklnqqkDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 780 SKQYSLKVTKLEHDAEQAKVELTETQKQLQEL--ENKDLSdvamkvKLQKEFRKKMDAAKLRVQVLQK-KQQDSKKLASL 856
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLneEKKELE------EKVKDLTKKISSLKEKIEKLESeKKEKESKISDL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 857 -----SIQNEKRANELEQSVDHM--KYQKIQLQRKLREENEKRKQLDAVIKRDQQK--IKELQLKTGQEEGLKPKAEDLD 927
Cdd:TIGR04523 544 edelnKDDFELKKENLEKEIDEKnkEIEELKQTQKSLKKKQEEKQELIDQKEKEKKdlIKEIEEKEKKISSLEKELEKAK 623
|
....*
gi 1622873320 928 ACNLK 932
Cdd:TIGR04523 624 KENEK 628
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
725-1075 |
2.04e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.73 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 725 DYLQESQELNLQKLKNSERILTEAKQKmrELTINIKMKEDLIKELIKTGNDakSVSKQYSLKVTKLEHDAEQAKVELTET 804
Cdd:PTZ00108 998 EYLLGKLERELARLSNKVRFIKHVING--ELVITNAKKKDLVKELKKLGYV--RFKDIIKKKSEKITAEEEEGAEEDDEA 1073
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 805 QKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQvLQKKQQDSKKLASLSIQNEKRAnELEqsvdhmkyqkiQLQRK 884
Cdd:PTZ00108 1074 DDEDDEEELGAAVSYDYLLSMPIWSLTKEKVEKLNAE-LEKKEKELEKLKNTTPKDMWLE-DLD-----------KFEEA 1140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 885 LREENEKRKQLDAVIKRDQQKIKELQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDQLQKLDEQKKWLDEEVEKVLNq 964
Cdd:PTZ00108 1141 LEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSN- 1219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 965 RQELEELEEDLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDNLKISTRLNLLEQELSEKNVQLQTSTA---EEKIK 1041
Cdd:PTZ00108 1220 SSGSDQEDDEEQKTKPKKSSVKRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRpdgESNGG 1299
|
330 340 350
....*....|....*....|....*....|....
gi 1622873320 1042 ISEQVEVLQKEKDQLQKRRNSVDEKLKNGRVLSP 1075
Cdd:PTZ00108 1300 SKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTAR 1333
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
937-1253 |
2.14e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 937 SFGSIDQLQKLDEQKKWLDEEVEKVLNQRQELEELEedlKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDNLKIST- 1015
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEEKIEELEEKIAELE---KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARl 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1016 ---------RLNLLEQELSEKNVQLQ------TSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRVLSPEEEHV 1080
Cdd:TIGR02168 739 eaeveqleeRIAQLSKELTELEAEIEeleerlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1081 LFQLEEGIEALEAAIEYKNESIQRRRNSLRASFHNLSRSEANVLEQIACLSPVEIRAILFRYFNKVVNLREAERKQQLYN 1160
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1161 EEMKMKVLERDnmVRELESALDHLKLQCDrrltlQQKEHEQKMQLLLHHFKEQ-------DEEGIMETFKTYEDKIQQLE 1233
Cdd:TIGR02168 899 LSEELRELESK--RSELRRELEELREKLA-----QLELRLEGLEVRIDNLQERlseeyslTLEEAEALENKIEDDEEEAR 971
|
330 340
....*....|....*....|
gi 1622873320 1234 KDLyfykktsRDLKKKLKEL 1253
Cdd:TIGR02168 972 RRL-------KRLENKIKEL 984
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
697-1258 |
2.36e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 697 DSVCSLVELNDTQDETQKSNLENEDLKIDYLQES-QELNLQKLKNSERILTEAKQKMRELTINIK--MKEDLIKELIKTG 773
Cdd:TIGR01612 678 NELSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKiQNMETATVELHLSNIENKKNELLDIIVEIKkhIHGEINKDLNKIL 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 774 NDAKSVSKQYSLKVtkleHDAEQAKVELTETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQqdskkl 853
Cdd:TIGR01612 758 EDFKNKEKELSNKI----NDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKE------ 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 854 aslsiqnekraNELEQSVDHMKYQKIQLQRKLRE----ENEKRKQLDAvikrDQQKIKELQLKtgqeegLKPKAEDlDAC 929
Cdd:TIGR01612 828 -----------DEIFKIINEMKFMKDDFLNKVDKfinfENNCKEKIDS----EHEQFAELTNK------IKAEISD-DKL 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 930 NLKRRKGSfgsiDQLQKLDEQKKWLDEEVEKVlnqrqeleeleEDLKKREAIVSKKEALLQEKSHLENKKLRSSQALNtD 1009
Cdd:TIGR01612 886 NDYEKKFN----DSKSLINEINKSIEEEYQNI-----------NTLKKVDEYIKICENTKESIEKFHNKQNILKEILN-K 949
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1010 NLKISTRLNLLEQELSEK--NVQLQTSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKngrvlSPEEEHVLFQLEEG 1087
Cdd:TIGR01612 950 NIDTIKESNLIEKSYKDKfdNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANLG-----KNKENMLYHQFDEK 1024
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1088 IEALEaAIEYKNESIQRRRNSLRASFHNlsrSEANVLEQIACLSPVEIRAIlfryfNKVVnLREAERKQQLYNE-EMKMK 1166
Cdd:TIGR01612 1025 EKATN-DIEQKIEDANKNIPNIEIAIHT---SIYNIIDEIEKEIGKNIELL-----NKEI-LEEAEINITNFNEiKEKLK 1094
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1167 VLERDNMVRE--LESALDHLKLQCDRRLTLQQKEHEQKMqllLHHFKEQDEEGIMETfktyEDKIQQLEK--DLYFYKKT 1242
Cdd:TIGR01612 1095 HYNFDDFGKEenIKYADEINKIKDDIKNLDQKIDHHIKA---LEEIKKKSENYIDEI----KAQINDLEDvaDKAISNDD 1167
|
570
....*....|....*.
gi 1622873320 1243 SRDLKKKLKELIMRLE 1258
Cdd:TIGR01612 1168 PEEIEKKIENIVTKID 1183
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
941-1261 |
2.44e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 941 IDQLQKLDEQKKWLDEEVEKVLNQRQELEELEEDL-KKREAIVSKKEALLQEKSHLENKKLRSSQaLNTDNLKISTRLNL 1019
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELrEELEKLEKEVKELEELKEEIEELEKELES-LEGSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1020 LEQELSEKNVQLqtSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAA----- 1094
Cdd:PRK03918 264 LEERIEELKKEI--EELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKeerle 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1095 -IEYKNESIQRRRNSL--RASFHNLSRSEANVLEQI----ACLSPVEIRAILFRYFNKVVNLREAERKQQLYNEEMKMKV 1167
Cdd:PRK03918 342 eLKKKLKELEKRLEELeeRHELYEEAKAKKEELERLkkrlTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1168 LERDNMVRELESALDHLKLqCDRRLTlqqkeheqkmqlllhhfkEQDEEGIMETfktYEDKIQQLEKDLYFYKKTSRDLK 1247
Cdd:PRK03918 422 KELKKAIEELKKAKGKCPV-CGRELT------------------EEHRKELLEE---YTAELKRIEKELKEIEEKERKLR 479
|
330
....*....|....
gi 1622873320 1248 KKLKELIMRLEMES 1261
Cdd:PRK03918 480 KELRELEKVLKKES 493
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
735-1209 |
2.76e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.03 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 735 LQKLKNSERILTEAKQKMRELTiniKMKEDLIKELIKTG-------NDAKSVSKQYSLKVTKLEHDAEQAKVELTETQKQ 807
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAK---RMYEDKIEELEKQLvlanselTEARTERDQFSQESGNLDDQLQKLLADLHKREKE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 808 L--QELENKDLSDVAMKVKLQ-KEFRKKMDAAKLRVQVL----------------------QKKQQDSKKLASLSIQNEK 862
Cdd:pfam15921 393 LslEKEQNKRLWDRDTGNSITiDHLRRELDDRNMEVQRLeallkamksecqgqmerqmaaiQGKNESLEKVSSLTAQLES 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 863 RANELEQSVDHMKYQKIQLQRKLREEN-------EKRKQLDA-------VIKRDQQKIKELQLKTGQEEGLKPKAEDLDA 928
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLESSERTVSdltaslqEKERAIEAtnaeitkLRSRVDLKLQELQHLKNEGDHLRNVQTECEA 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 929 CNLKRrKGSFGSIDQLQKLDEQKKWL--------------DEEVEKVLNQRQELEELEEDLK-KREAIVSKKEA------ 987
Cdd:pfam15921 553 LKLQM-AEKDKVIEILRQQIENMTQLvgqhgrtagamqveKAQLEKEINDRRLELQEFKILKdKKDAKIRELEArvsdle 631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 988 -------------------LLQEKSHLENKKLRSSQALNTdnlkISTRLNLLEQELSEKNVQLQTSTAEEKIKISEQVEV 1048
Cdd:pfam15921 632 lekvklvnagserlravkdIKQERDQLLNEVKTSRNELNS----LSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSE 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1049 LQKEKDQLQKRRNSVDEKLKNGRVLSPEEEHVLFQleegIEALEAAIEYKNESIQRRRNSlrasfHNLSRSEANVLEQIa 1128
Cdd:pfam15921 708 LEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQ----IDALQSKIQFLEEAMTNANKE-----KHFLKEEKNKLSQE- 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1129 cLSPVEIRAilfryfNKVVNLREAERKQQlynEEMKMKVlerdnmvRELESALDHLKLQCDRRLTLQQKEHEQKMQLLLH 1208
Cdd:pfam15921 778 -LSTVATEK------NKMAGELEVLRSQE---RRLKEKV-------ANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
.
gi 1622873320 1209 H 1209
Cdd:pfam15921 841 H 841
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
704-1184 |
2.92e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 42.35 E-value: 2.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 704 ELNDTQDETQKSNLENEDLKID---YLQESQEL-NLQKLKNSERILTEAKQ---KMRELTINIKMKEDLIKELIKTGNDa 776
Cdd:TIGR01612 1319 DINDIKKELQKNLLDAQKHNSDinlYLNEIANIyNILKLNKIKKIIDEVKEytkEIEENNKNIKDELDKSEKLIKKIKD- 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 777 ksvskQYSLKVTKLEHDAEQAKVELTETQKQLQELENKDLSD---VAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKL 853
Cdd:TIGR01612 1398 -----DINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEesnIDTYFKNADENNENVLLLFKNIEMADNKSQHILKI 1472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 854 ASLSIQNEK--RANELEQSVDHMKYQKIQLQrKLREENEKRKQLdavIKRDQQKIKELqLKTGQEEGLKPKAEdldacnl 931
Cdd:TIGR01612 1473 KKDNATNDHdfNINELKEHIDKSKGCKDEAD-KNAKAIEKNKEL---FEQYKKDVTEL-LNKYSALAIKNKFA------- 1540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 932 KRRKGSFGSIDQLQKLDEQKKWLDEEVEKVLNQRQELEELEEDL-----KKREAIVSKKEALlqekSHLENKKLRSSQAL 1006
Cdd:TIGR01612 1541 KTKKDSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDaakndKSNKAAIDIQLSL----ENFENKFLKISDIK 1616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1007 NTDN----------LKIST-RLNLLEQELSEKNVQLQT------STAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKN 1069
Cdd:TIGR01612 1617 KKINdclketesieKKISSfSIDSQDTELKENGDNLNSlqefleSLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKN 1696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1070 grvlspEEEHVLFQLEEGIEALEAAIEYKNESIQRRRNSLRASFH-----------NLSR--SEANVLEQ---------I 1127
Cdd:TIGR01612 1697 ------YEIGIIEKIKEIAIANKEEIESIKELIEPTIENLISSFNtndlegidpneKLEEynTEIGDIYEefielyniiA 1770
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622873320 1128 ACLSPVEIRAILFRYF--------NKVVNLREAERKQQLYNEEMKMKvlERDNMVRELESALDHL 1184
Cdd:TIGR01612 1771 GCLETVSKEPITYDEIkntrinaqNEFLKIIEIEKKSKSYLDDIEAK--EFDRIINHFKKKLDHV 1833
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
938-1214 |
4.03e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 938 FGSIDQLQKLDEQKKWLDEEVEKVLNQRQELEELEEDLKKREAIVSKKE----------ALLQEKSHLENKKlrssQALN 1007
Cdd:COG4913 606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAeyswdeidvaSAEREIAELEAEL----ERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1008 TDNLKISTrlnlLEQELSEKNVQLQTsTAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLknGRVLSPEEEHVLFQLEEg 1087
Cdd:COG4913 682 ASSDDLAA----LEEQLEELEAELEE-LEEELDELKGEIGRLEKELEQAEEELDELQDRL--EAAEDLARLELRALLEE- 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1088 iealeaaiEYKNESIQRRRNSLRASFHnlsrseanvlEQIAclspvEIRAILFRYFNKVVNLREAerkqqlYNEEMKMKV 1167
Cdd:COG4913 754 --------RFAAALGDAVERELRENLE----------ERID-----ALRARLNRAEEELERAMRA------FNREWPAET 804
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1622873320 1168 LERDNMVRELESALDHLKLQCDRRLtlqqKEHEQKMQLLLHHFKEQD 1214
Cdd:COG4913 805 ADLDADLESLPEYLALLDRLEEDGL----PEYEERFKELLNENSIEF 847
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
878-1009 |
4.25e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 878 KIQLQRKLREENEKRKQLDAVIKRDQQKIKELQLKTGQEEGLKPKAEDLDACNLKRRKgsfgsIDQLQKLDEQKK-WLDE 956
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE-----LQKLEKRLLQKEeNLDR 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1622873320 957 EVEKVLNQRQELEELEEDLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTD 1009
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
703-959 |
4.49e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.58 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 703 VELNDTQDETQKSNLENEDLKIDYLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQ 782
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 783 YSLKVTKLEHDAEQAKVELTETQKQLQELENkdlsdvamkvkLQKEFRKKMDAAKLRVQVLQKKQqdskklaslsiqnek 862
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLN-----------ERASLEEALALLRSELEELSEEL--------------- 903
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 863 raNELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKELQLKTGQEEGLKPKAEDLDACNLKRR-------K 935
Cdd:TIGR02168 904 --RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRlkrlenkI 981
|
250 260
....*....|....*....|....*....
gi 1622873320 936 GSFG-----SIDQLQKLDEQKKWLDEEVE 959
Cdd:TIGR02168 982 KELGpvnlaAIEEYEELKERYDFLTAQKE 1010
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
853-1112 |
4.51e-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: 4.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 853 LASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKELQLKTGQ-EEGLKPKAEDLDAcnL 931
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAlEQELAALEAELAE--L 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 932 KRRkgsfgsIDQLQK-LDEQKkwldEEVEKVLNQRQeleeleedlkkREAIVSKKEALLQEKSHLEnkKLRSSQALNTDN 1010
Cdd:COG4942 89 EKE------IAELRAeLEAQK----EELAELLRALY-----------RLGRQPPLALLLSPEDFLD--AVRRLQYLKYLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1011 LKISTRLNLLEQELSEKNvQLQTSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRVLSPEEEHVLFQLEEGIEA 1090
Cdd:COG4942 146 PARREQAEELRADLAELA-ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
250 260
....*....|....*....|..
gi 1622873320 1091 LEAAIEYKNESIQRRRNSLRAS 1112
Cdd:COG4942 225 LEALIARLEAEAAAAAERTPAA 246
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
752-889 |
4.85e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 40.80 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 752 MRELTINIKMKEDLIKELIKTGNDA-----------KSVSKQYSLKVTKLEHDAEQAKVELTETQKQLQELENKDLSDVA 820
Cdd:smart00435 233 LQEQLKELTAKDGNVAEKILAYNRAnrevailcnhqRTVSKTHEKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRK 312
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622873320 821 MKVKLQKEFRkkmdaaKLRVQVLQKKQQDSKKLASlsiqnEKRANELEQSVdhmkyQKIQLQRKLREEN 889
Cdd:smart00435 313 LKSKFERDNE------KLDAEVKEKKKEKKKEEKK-----KKQIERLEERI-----EKLEVQATDKEEN 365
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
789-1051 |
5.19e-03 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 40.99 E-value: 5.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 789 KLEHDAEQAKVELTETQKQLQELENKDLS----DVAMKVKLQkEFRKKMDAAKLRVQ-VLQKKQQDSKKLASLsiqnEKR 863
Cdd:pfam09726 399 RLEQDIKKLKAELQASRQTEQELRSQISSltslERSLKSELG-QLRQENDLLQTKLHnAVSAKQKDKQTVQQL----EKR 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 864 ANELEQSvdhmkyqKIQLQRKLREENEKRKQLDAVIKRDQQKIKELQLKTGqeEGLKPKAEDLDAcnlkrrkgsfgsidQ 943
Cdd:pfam09726 474 LKAEQEA-------RASAEKQLAEEKKRKKEEEATAARAVALAAASRGECT--ESLKQRKRELES--------------E 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 944 LQKLDEQKKWLDEEVEKVLNQRQELEELEEDLKKREAIVSKKEALLQEKSHLENkklrssqalntdNLKISTRLNL-LEQ 1022
Cdd:pfam09726 531 IKKLTHDIKLKEEQIRELEIKVQELRKYKESEKDTEVLMSALSAMQDKNQHLEN------------SLSAETRIKLdLFS 598
|
250 260
....*....|....*....|....*....
gi 1622873320 1023 ELSEKNVQLQTSTAEEKIKISEQVEVLQK 1051
Cdd:pfam09726 599 ALGDAKRQLEIAQGQIYQKDQEIKDLKQK 627
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
705-1076 |
5.42e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.16 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 705 LNDTQDETQKSNLENEDLKIDYLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQys 784
Cdd:TIGR04523 283 IKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSE-- 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 785 lKVTKLEHDAEQAKVELTETQKQLQELEN--KDLSDVAMKVKLQKEFRKKMDAA-KLRVQVLQKKQQDSKKLASLSIQNE 861
Cdd:TIGR04523 361 -KQRELEEKQNEIEKLKKENQSYKQEIKNleSQINDLESKIQNQEKLNQQKDEQiKKLQQEKELLEKEIERLKETIIKNN 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 862 KRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKI----KELQLKTGQEEGLKPKAEDLDACNLKRRKGS 937
Cdd:TIGR04523 440 SEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLeqkqKELKSKEKELKKLNEEKKELEEKVKDLTKKI 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 938 FGSIDQLQKLDEQKKwldeEVEKVLNQRQELEELEEDLKKREAIVSKKEALLQE--KSHLENKKLRSSQA--------LN 1007
Cdd:TIGR04523 520 SSLKEKIEKLESEKK----EKESKISDLEDELNKDDFELKKENLEKEIDEKNKEieELKQTQKSLKKKQEekqelidqKE 595
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622873320 1008 TDNLKISTRLNLLEQELSEKNVQLQTSTAEEKiKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRVLSPE 1076
Cdd:TIGR04523 596 KEKKDLIKEIEEKEKKISSLEKELEKAKKENE-KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPE 663
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
735-1103 |
5.47e-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: 41.11 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 735 LQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLE------HDAEQAKVELTETQKQL 808
Cdd:TIGR00618 451 AQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCgscihpNPARQDIDNPGPLTRRM 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 809 QELEN--KDLSDVAMKVKLQ--------KEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQK 878
Cdd:TIGR00618 531 QRGEQtyAQLETSEEDVYHQltserkqrASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDML 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 879 IQLQRKLREENEKRKQLDAVIKRDQQKIKELQLK----TGQEEGLKPKAEDLDACNLKRRKGSFGSIDQLQKLDEQKKW- 953
Cdd:TIGR00618 611 ACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKltalHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKe 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 954 ---------------LDEEVEKVLNQRQELEELEEDLKKREAIVSKKEALLQEK------------SHLENKKLRSSQAL 1006
Cdd:TIGR00618 691 qltywkemlaqcqtlLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSlkelmhqartvlKARTEAHFNNNEEV 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1007 NTDnLKISTRLNLLEQELSEKNVQLQTSTAEEKIKISEQVE-------VLQKEKDQLQKRRNSVDEKLKNGRVLSPEEEH 1079
Cdd:TIGR00618 771 TAA-LQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQeipsdedILNLQCETLVQEEEQFLSRLEEKSATLGEITH 849
|
410 420
....*....|....*....|....
gi 1622873320 1080 VLFQLEEGIEALEAAIEYKNESIQ 1103
Cdd:TIGR00618 850 QLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
799-1090 |
5.83e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 799 VELTETQKQLQELENKdLSDVAMKVKLQkefRKKMDAAKLRVQVLQKKQQDSKKLASLSIQneKRANELEQSVDHMKYQK 878
Cdd:PRK04863 837 AELRQLNRRRVELERA-LADHESQEQQQ---RSQLEQAKEGLSALNRLLPRLNLLADETLA--DRVEEIREQLDEAEEAK 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 879 IQLQRKLREENEKRKQLdAVIKRDQQKIKEL-----QLKTGQEEgLKPKAEDLDacNLKRRKGSFGSIDQLQKLDEQkkw 953
Cdd:PRK04863 911 RFVQQHGNALAQLEPIV-SVLQSDPEQFEQLkqdyqQAQQTQRD-AKQQAFALT--EVVQRRAHFSYEDAAEMLAKN--- 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 954 lDEEVEKvLNQRQELEELEEDlKKREAIVSKKEALLQEKSHLEnkKLRSSQALNTDNLKistrlnLLEQELSEKNVQLqT 1033
Cdd:PRK04863 984 -SDLNEK-LRQRLEQAEQERT-RAREQLRQAQAQLAQYNQVLA--SLKSSYDAKRQMLQ------ELKQELQDLGVPA-D 1051
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622873320 1034 STAEEKI-----KISEQVEVLQKEKDQLQKRRNSVDEKLKN--GRVLSPEEEhvLFQLEEGIEA 1090
Cdd:PRK04863 1052 SGAEERArarrdELHARLSANRSRRNQLEKQLTFCEAEMDNltKKLRKLERD--YHEMREQVVN 1113
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
786-1107 |
6.29e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 40.93 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 786 KVTKLEHDAEQAKVELTETQKQLQELENkdlsdvAMKVKLQKEFRKKMDAAKLRVQVLQKKQqdskklaslsiqnekran 865
Cdd:pfam01576 16 KVKERQQKAESELKELEKKHQQLCEEKN------ALQEQLQAETELCAEAEEMRARLAARKQ------------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 866 ELEQSVDHMkyqkiqlQRKLREENEKRKQLDAVIKRDQQKIKELQLKTGQEEGLKPKAE----DLDACNLKRRKGSFGSI 941
Cdd:pfam01576 72 ELEEILHEL-------ESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQlekvTTEAKIKKLEEDILLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 942 DQLQKLDEQKKWLDEEVEKVLNQRQELEELEEDLKKreaIVSKKEALLQEKSHLENKKLRSSQALNtdnlKISTRLNLLE 1021
Cdd:pfam01576 145 DQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSK---LKNKHEAMISDLEERLKKEEKGRQELE----KAKRKLEGES 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1022 QELSEKNVQLQTSTAEEKIKISEQVEVLQKEKDQLQKRRNSVDEKLKNGRVLSPeeehvlfQLEEGIEALEAAIEYKNES 1101
Cdd:pfam01576 218 TDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEA-------QISELQEDLESERAARNKA 290
|
....*.
gi 1622873320 1102 IQRRRN 1107
Cdd:pfam01576 291 EKQRRD 296
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
702-1109 |
9.01e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.31 E-value: 9.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 702 LVELNDTQDETQKSNLENEDLKIDYLQESQELnLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSK 781
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEA-EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 782 QYSLKVTKLEHDAEQAKVELTETQKQLQELENKDLSDVAMKVKLQKEFRKkmdAAKLRVQVLQKKQQDSKKLASLSIQNE 861
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE---AAEEEAELEEEEEALLELLAELLEEAA 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 862 KRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKELQLKTGQEEGLKPKA------------------ 923
Cdd:COG1196 474 LLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAyeaaleaalaaalqnivv 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 924 ---EDLDAC--NLKRRKGSFGSIDQLQK----------------------LDEQKKWLDEEVEKVLNQRQELEELEEDLK 976
Cdd:COG1196 554 eddEVAAAAieYLKAAKAGRATFLPLDKiraraalaaalargaigaavdlVASDLREADARYYVLGDTLLGRTLVAARLE 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 977 KREAIVSKKEALLQEKS---HLENKKLRSSQALNTDNLKISTRLNLLEQELSEKNVQLQTSTAEEKIKISEQVEVLQKEK 1053
Cdd:COG1196 634 AALRRAVTLAGRLREVTlegEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAE 713
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622873320 1054 DQLQKRRNSVDEKLKNGRV--------------LSPEEEHVLFQLEEGIEALEAAIeyknESIQRRRNSL 1109
Cdd:COG1196 714 EERLEEELEEEALEEQLEAereelleelleeeeLLEEEALEELPEPPDLEELEREL----ERLEREIEAL 779
|
|
| |
