|
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: 601.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 4 IPVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 84 GQTGSGKTYTIGGGHIASVVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELET-SMKDLHIRED 161
Cdd:cd01372 81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKDtFEFQLKVSFLEIYNEEIRDLLDPETdKKPTISIRED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEDGSWYSPRHIVSKFH 241
Cdd:cd01372 161 SKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNSTFTSKFH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 242 FVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPS 321
Cdd:cd01372 241 FVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPA 320
|
330 340
....*....|....*....|.
gi 1034670647 322 SSNFDESLNSLKYANRARNIR 342
Cdd:cd01372 321 DSNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
5-348 |
1.86e-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: 445.86 E-value: 1.86e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII-------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTvrspknrQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 78 ATVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISEH-PSIDFNVKVSYIEVYKEDLRDLLEleTSMKDL 156
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLLN--PSSKKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEaaedgswySPRHI 236
Cdd:smart00129 153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSS--------SGSGK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 237 VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRrKSSHIPYRDAKITRLLKDSLGGSAKTVMIT 316
Cdd:smart00129 225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS-KSRHIPYRDSKLTRLLQDSLGGNSKTLMIA 303
|
330 340 350
....*....|....*....|....*....|..
gi 1034670647 317 CVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:smart00129 304 NVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
11-341 |
1.11e-138 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 427.37 E-value: 1.11e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 11 RIRPLLCKEALHNHQVCVRVIPNSQQVII-------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 84 GQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELETSMKD-LHIRED 161
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKErSEFSVKVSYLEIYNEKIRDLLSPSNKNKRkLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEdgswyspRHIVSKFH 241
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEE-------SVKTGKLN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 242 FVDLAGSERVTKTGN-TGERFKESIQINSGLLALGNVISALGDPrrKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSP 320
Cdd:pfam00225 228 LVDLAGSERASKTGAaGGQRLKEAANINKSLSALGNVISALADK--KSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISP 305
|
330 340
....*....|....*....|.
gi 1034670647 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 |
1.78e-129 |
|
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: 402.79 E-value: 1.78e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 5 PVKVAVRIRPLLCKEAlhNHQVCVRVIPNSQQVIIG-------RDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd00106 1 NVRVAVRVRPLNGREA--RSAKSVISVDGGKSVVLDppknrvaPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 78 ATVFAYGQTGSGKTYTIGGGHiasvvEGQKGIIPRAIQEIFQSISEHPSIDFN--VKVSYIEVYKEDLRDLLELETSmKD 155
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKRKETKSSfsVSASYLEIYNEKIYDLLSPVPK-KP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 156 LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNMEAAEDgswyspRH 235
Cdd:cd00106 153 LSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQ--RNREKSGE------SV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 236 IVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKssHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd00106 225 TSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMI 302
|
330 340
....*....|....*....|....
gi 1034670647 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 |
1.36e-111 |
|
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: 355.50 E-value: 1.36e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 6 VKVAVRIRPLLCKEALHNHQVCVRVI----------------------PNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNT 63
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMdnhmlvfdpkdeedgffhggsnNRDRRKRRNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 64 CIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISE-HPSIDFNVKVSYIEVYKED 142
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGT------PQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 143 LRDLLEleTSMKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNM 222
Cdd:cd01370 156 IRDLLN--PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 223 EAAEDgswysprHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLL 302
Cdd:cd01370 234 SINQQ-------VRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLL 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 1034670647 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 |
1.01e-110 |
|
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like subgroup, involved in chromosome movement and/or spindle elongation during mitosis. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276825 [Multi-domain] Cd Length: 321 Bit Score: 352.02 E-value: 1.01e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSqqvIIGRDRV---FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFA 82
Cdd:cd01374 2 ITVTVRVRPLNSREIGINEQVAWEIDNDT---IYLVEPPstsFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 83 YGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISEHPSIDFNVKVSYIEVYKEDLRDLleLETSMKDLHIREDE 162
Cdd:cd01374 79 YGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDL--LSPTSQNLKIRDDV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 163 KGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcQVHKNMEAAEDGSwysprhIVSKFHF 242
Cdd:cd01374 151 EKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITI-ESSERGELEEGTV------RVSTLNL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 243 VDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDpRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSS 322
Cdd:cd01374 224 IDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAE 302
|
330
....*....|....*....
gi 1034670647 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 |
7.26e-109 |
|
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: 347.53 E-value: 7.26e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII--GRD------RVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 78 ATVFAYGQTGSGKTYTIGGghiASVVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELETSmKDL 156
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEG---KREDPELRGIIPNSFAHIFGHIARSQNnQQFLVRVSYLEIYNEEIRDLLGKDQT-KRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhKNMEAAEDGSwyspRHI 236
Cdd:cd01371 159 ELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI----ECSEKGEDGE----NHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 237 -VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPrrKSSHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd01371 231 rVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMC 308
|
330 340
....*....|....*....|....*.
gi 1034670647 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 |
2.20e-107 |
|
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins. Ncd is a spindle motor protein necessary for chromosome segregation in meiosis. KIFC2/KIFC3-like kinesins have been implicated in motility of the Golgi apparatus as well as dentritic and axonal transport in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In this subgroup the motor domain is found at the C-terminus (C-type). C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276817 [Multi-domain] Cd Length: 329 Bit Score: 343.42 E-value: 2.20e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 11 RIRPLLCKEALHNHQVCVRVIPNSQQVII----GRDRVFTFDFVFGKNSTQDEVYNTcIKPLVLSLIEGYNATVFAYGQT 86
Cdd:cd01366 9 RVRPLLPSEENEDTSHITFPDEDGQTIELtsigAKQKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIFAYGQT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 87 GSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISE--HPSIDFNVKVSYIEVYKEDLRDLL-ELETSMKDLHIRED-E 162
Cdd:cd01366 88 GSGKTYTMEG------PPESPGIIPRALQELFNTIKElkEKGWSYTIKASMLEIYNETIRDLLaPGNAPQKKLEIRHDsE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 163 KGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhkNMEAAEDGSwysprHIVSKFHF 242
Cdd:cd01366 162 KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-----SGRNLQTGE-----ISVGKLNL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 243 VDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALgdpRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSS 322
Cdd:cd01366 232 VDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL---RQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAE 308
|
330 340
....*....|....*....|.
gi 1034670647 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 |
1.14e-101 |
|
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: 327.36 E-value: 1.14e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 6 VKVAVRIRPLLCKEALHNHQVCVRvIPNSQQVIIGRD---RVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFA 82
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVK-FDPEDTVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 83 YGQTGSGKTYTIGGGHIAsvvEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLleLETSMKDLHIRED 161
Cdd:cd01369 83 YGQTSSGKTYTMEGKLGD---PESMGIIPRIVQDIFETIYSMDEnLEFHVKVSYFEIYMEKIRDL--LDVSKTNLSVHED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNMeaaEDGSWYSprhivSKFH 241
Cdd:cd01369 158 KNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ--ENV---ETEKKKS-----GKLY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 242 FVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDprRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPS 321
Cdd:cd01369 228 LVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD--GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPS 305
|
330 340
....*....|....*....|
gi 1034670647 322 SSNFDESLNSLKYANRARNI 341
Cdd:cd01369 306 SYNESETLSTLRFGQRAKTI 325
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
6-348 |
2.75e-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: 327.77 E-value: 2.75e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 6 VKVAVRIRPLLCKE---------ALHNHQVCVRVIPNSQQVIIGRDRV---FTFDFVF------GKN-STQDEVYNTCIK 66
Cdd:cd01365 3 VKVAVRVRPFNSREkernskcivQMSGKETTLKNPKQADKNNKATREVpksFSFDYSYwshdseDPNyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 67 PLVLSLIEGYNATVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSI--SEHPSIDFNVKVSYIEVYKEDLR 144
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMG------TQEQPGIIPRLCEDLFSRIadTTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 145 DLLELETSMKD--LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNM 222
Cdd:cd01365 157 DLLNPKPKKNKgnLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQ--KRH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 223 EAAEDGSwyspRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRR-----KSSHIPYRDAK 297
Cdd:cd01365 235 DAETNLT----TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1034670647 298 ITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01365 311 LTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
6-348 |
4.18e-101 |
|
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: 326.98 E-value: 4.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII--------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 78 ATVFAYGQTGSGKTYTIGGGHiaSVVEGQK-------GIIPRAIQEIFQSISEHpSIDFNVKVSYIEVYKEDLRDLLELE 150
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMEGDR--SPNEEYTweldplaGIIPRTLHQLFEKLEDN-GTEYSVKVSYLEIYNEELFDLLSPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 151 TS-MKDLHIRED--EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEd 227
Cdd:cd01364 161 SDvSERLRMFDDprNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 228 gswyspRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDprrKSSHIPYRDAKITRLLKDSLG 307
Cdd:cd01364 240 ------LVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLG 310
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1034670647 308 GSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01364 311 GRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
5-348 |
3.42e-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: 279.39 E-value: 3.42e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVIIG-RDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 84 GQTGSGKTYTIGG--GHIASVVEGQKGIIPRAIQEIFQSISEH-----PSIDFNVKVSYIEVYKEDLRDLleLETSMKDL 156
Cdd:cd01373 82 GQTGSGKTYTMWGpsESDNESPHGLRGVIPRIFEYLFSLIQREkekagEGKSFLCKCSFLEIYNEQIYDL--LDPASRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmEAAEDGSWYSpRHI 236
Cdd:cd01373 160 KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI-------ESWEKKACFV-NIR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 237 VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGD-PRRKSSHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd01373 232 TSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAII 311
|
330 340 350
....*....|....*....|....*....|...
gi 1034670647 316 TCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01373 312 ANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
45-379 |
1.50e-83 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 285.48 E-value: 1.50e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 45 FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISEH 124
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGT------EEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 125 PSI-DFNVKVSYIEVYKEDLRDLLELETsmKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEH 203
Cdd:COG5059 132 SMTkDFAVSISYLEIYNEKIYDLLSPNE--ESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 204 SSRSHAIFTISICQVHKNMeaaedgswysPRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGD 283
Cdd:COG5059 210 SSRSHSIFQIELASKNKVS----------GTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 284 PRrKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVNFSPESDR-IDEMEFE 362
Cdd:COG5059 280 KK-KSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReIEEIKFD 358
|
330
....*....|....*..
gi 1034670647 363 IKLLREALQSQQAGVSQ 379
Cdd:COG5059 359 LSEDRSEIEILVFREQS 375
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
5-337 |
2.05e-83 |
|
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: 276.48 E-value: 2.05e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVI-IGRDRV----------FTFDFVFGKNSTQDEVYNTCIKPLVLSLI 73
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVhEPKLKVdltkyienhtFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 74 EGYNATVFAYGQTGSGKTYTIGGGHiaSVVEGQKGIIPRAIQEIFQSISEHPSID-FNVKVSYIEVYKEDLRDLLEletS 152
Cdd:cd01367 81 EGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKLPYKDnLGVTVSFFEIYGGKVFDLLN---R 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 153 MKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmEAAEDGSwys 232
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-------RDRGTNK--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 233 prhIVSKFHFVDLAGSER-VTKTGNTGERFKESIQINSGLLALGNVISALGDPrrkSSHIPYRDAKITRLLKDSL-GGSA 310
Cdd:cd01367 226 ---LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQN---KAHIPFRGSKLTQVLKDSFiGENS 299
|
330 340
....*....|....*....|....*..
gi 1034670647 311 KTVMITCVSPSSSNFDESLNSLKYANR 337
Cdd:cd01367 300 KTCMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
5-335 |
3.79e-83 |
|
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: 276.58 E-value: 3.79e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 5 PVKVAVRIRPLLCKEALHNHQVCVRVIpNSQQV----------------IIGRDRVFTFDFVFGKNSTQDEVYNTCIKPL 68
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVI-NSTTVvlhppkgsaanksernGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 69 VLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISehpsiDFNVKVSYIEVYKEDLRDLLE 148
Cdd:cd01368 81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGS------PGDGGILPRSLDVIFNSIG-----GYSVFVSYIEIYNEYIYDLLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 149 LETS-----MKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNME 223
Cdd:cd01368 150 PSPSsptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 224 AAEDGSWYSPRhiVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISAL--GDPRRKSSHIPYRDAKITRL 301
Cdd:cd01368 230 GDVDQDKDQIT--VSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLreNQLQGTNKMVPFRDSKLTHL 307
|
330 340 350
....*....|....*....|....*....|....
gi 1034670647 302 LKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYA 335
Cdd:cd01368 308 FQNYFDGEGKASMIVNVNPCASDYDETLHVMKFS 341
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
5-339 |
6.24e-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: 266.29 E-value: 6.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 5 PVKVAVRIRPLLCKEALHNHQVCVRVIpNSQQVIIGRDRV------FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNA 78
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELADPRNhgetlkYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 79 TVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQsISEHPSIDFNVKVSYIEVYKEDLRDLLELETsmKDLHI 158
Cdd:cd01376 80 TVFAYGSTGAGKTFTMLG------SPEQPGLMPLTVMDLLQ-MTRKEAWALSFTMSYLEIYQEKILDLLEPAS--KELVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 159 REDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmeaAEDGSWYSPRHIVS 238
Cdd:cd01376 151 REDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV---------DQRERLAPFRQRTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 239 KFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISAL--GDPRrksshIPYRDAKITRLLKDSLGGSAKTVMIT 316
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALnkNLPR-----IPYRDSKLTRLLQDSLGGGSRCIMVA 296
|
330 340
....*....|....*....|...
gi 1034670647 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 |
2.43e-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: 248.26 E-value: 2.43e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 33 NSQQviigRDRVFTFDFVFgKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGHIASvveGQKGIIPR 112
Cdd:cd01375 42 NNQQ----EDWSFKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENY---KHRGIIPR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 113 AIQEIFQSISEHPSIDFNVKVSYIEVYKEDLRDLL----ELETSMKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEM 188
Cdd:cd01375 114 ALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 189 GNAARHTGTTQMNEHSSRSHAIFTIsicqvHKNMEAAEDGswySPRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQIN 268
Cdd:cd01375 194 GETNRIIASHTMNKNSSRSHCIFTI-----HLEAHSRTLS---SEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYIN 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034670647 269 SGLLALGNVISALGDPRRksSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRAR 339
Cdd:cd01375 266 KSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
6-397 |
1.72e-61 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 231.75 E-value: 1.72e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 6 VKVAVRIRPLLCKEalhNHQVCVRVIPNSQQVIIGRdrVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQ 85
Cdd:PLN03188 100 VKVIVRMKPLNKGE---EGEMIVQKMSNDSLTINGQ--TFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 86 TGSGKTYTIGGGHIASVVEG----QKGIIPRAIQEIFQSISEHP------SIDFNVKVSYIEVYKEDLRDLLEleTSMKD 155
Cdd:PLN03188 175 TGSGKTYTMWGPANGLLEEHlsgdQQGLTPRVFERLFARINEEQikhadrQLKYQCRCSFLEIYNEQITDLLD--PSQKN 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 156 LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTisiCQVHKNMEAAEDG-SWYSpr 234
Cdd:PLN03188 253 LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT---CVVESRCKSVADGlSSFK-- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 235 hiVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRR--KSSHIPYRDAKITRLLKDSLGGSAKT 312
Cdd:PLN03188 328 --TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAKL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 313 VMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVNFSPESDrIDEMEFEIKLLREALQSQQAGVSQTTQINREGSPDTN 392
Cdd:PLN03188 406 AMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDD-VNFLREVIRQLRDELQRVKANGNNPTNPNVAYSTAWN 484
|
....*
gi 1034670647 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 |
1.34e-23 |
|
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: 98.96 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 26 VCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTCiKPLVLSLIEGYN-ATVFAYGQTGSGKTYTIggghiasvve 104
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGESGAGKTETM---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 105 gqKGIIPRAIQEIFqsisehpsidfnvkvSYIEVYKEDLRDLLEletsmkdlhiredekgntvivgakECHVESAGEVMS 184
Cdd:cd01363 70 --KGVIPYLASVAF---------------NGINKGETEGWVYLT------------------------EITVTLEDQILQ 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 185 LLEMGNAARhTGTTQMNEHSSRSHAIFTIsicqvhknmeaaedgswysprhivskfhFVDLAGSERvtktgntgerfkes 264
Cdd:cd01363 109 ANPILEAFG-NAKTTRNENSSRFGKFIEI----------------------------LLDIAGFEI-------------- 145
|
250
....*....|....*.
gi 1034670647 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 |
4.32e-19 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 85.35 E-value: 4.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 6 VKVAVRIRPLLCKEAlhnhQVCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTcIKPLVLSLIEGYNATVFAYGQ 85
Cdd:pfam16796 22 IRVFARVRPELLSEA----QIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQE-ISQLVQSCLDGYNVCIFAYGQ 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034670647 86 TGSGKTytiggghiasvvegqKGIIPRAIQEIFQSISE-HPSIDFNVKVSYIEVYKEDLRDLL 147
Cdd:pfam16796 97 TGSGSN---------------DGMIPRAREQIFRFISSlKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
632-1201 |
2.47e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 78.64 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 632 EEQDKVLHCQFSDNSDDEESEGQEKSGTRCRSRSWIQKPDSVCSLVELSDTQDETQKSDLENEDLKIDCLQESQELNLQK 711
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 712 LKNSERILTEAKQKMREltinIKMKEDLIKELIKTGNDAKSVSKqyslkvtklehdAEQAKVELIETQKQLQELENKD-L 790
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEE----KKKADEAKKKAEEDKKKADELKK------------AAAAKKKADEAKKKAEEKKKADeA 1436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 791 SDVAMKVKLQKEFRKKMDAAKlRVQVLQKKQQDSKKLASLSIQNE--KRANELEQSVDHMKyQKIQLQRKLREENEKRKQ 868
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKKAEEAK-KAEEAKKKAEEAKKADEAKKKAEeaKKADEAKKKAEEAK-KKADEAKKAAEAKKKADE 1514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 869 LdaviKRDQQKIKEIQLKTGQEeglKPKAEDLDACNLKRRKgsfgsiDHLQKLDEQKKwlDEEVEKVLNQRQELEELEAD 948
Cdd:PTZ00121 1515 A----KKAEEAKKADEAKKAEE---AKKADEAKKAEEKKKA------DELKKAEELKK--AEEKKKAEEAKKAEEDKNMA 1579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 949 LKKREAIVSKKEALLQE--KSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKiseqVEVLQKE 1026
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEvmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK----AEELKKA 1655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1027 KDQLQKRRHNVDEKLKngrvlspeeehvlfqlEEGIEALEAAIEYRNESIQNRQKSLRASfhnlsrgEANVLEKLACLSP 1106
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAE----------------EDKKKAEEAKKAEEDEKKAAEALKKEAE-------EAKKAEELKKKEA 1712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1107 VEIRtilfryfnKVVNLREAERKQQLYNEEMKMKVLERDNMVREL------ESALDHLKLQCDRRLTLQQKEHEQKMQll 1180
Cdd:PTZ00121 1713 EEKK--------KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdeeeKKKIAHLKKEEEKKAEEIRKEKEAVIE-- 1782
|
570 580
....*....|....*....|.
gi 1034670647 1181 lHHFKEQDGEGIMETFKTYED 1201
Cdd:PTZ00121 1783 -EELDEEDEKRRMEVDKKIKD 1802
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
721-1286 |
2.73e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 721 EAK--QKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKdlsdvAMKVK 798
Cdd:PTZ00121 1241 EAKkaEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK-----AEEAK 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 799 LQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLS-IQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQ 877
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 878 QKIKEIQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVS 957
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEA 1475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 958 KKEALLQEKSHlENKKLRSSQALNTDSLKISTRLNLLEQEL---SEKNVQLQTSTAEEKTKISEQVEVLQKEK-DQLQK- 1032
Cdd:PTZ00121 1476 KKKAEEAKKAD-EAKKKAEEAKKKADEAKKAAEAKKKADEAkkaEEAKKADEAKKAEEAKKADEAKKAEEKKKaDELKKa 1554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1033 ---RRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIE----YRNESIQNRQKSLRASFHNLSRGEANVLEKLACLS 1105
Cdd:PTZ00121 1555 eelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEevmkLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1106 PVEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDHLKLQCDRrltLQQKEHEQKMQLLLHHFK 1185
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEA---LKKEAEEAKKAEELKKKE 1711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1186 EQDGEGIMETFKTYEDKIQQLEKdlyfYKKTSRDHKKKLKEL-VGEAIRRQLA-PSEYQEAGDGVLKPEGGGMLSEELKW 1263
Cdd:PTZ00121 1712 AEEKKKAEELKKAEEENKIKAEE----AKKEAEEDKKKAEEAkKDEEEKKKIAhLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
570 580
....*....|....*....|...
gi 1034670647 1264 ASRPESMKLSGREREMDSSASSL 1286
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKDIFDNFANI 1810
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
763-1099 |
4.13e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 74.71 E-value: 4.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 763 KLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELE 842
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 843 QSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIqlktgqEEGLKPKAEDLDACNLKRRKGSFGSIDHLQKLD 922
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL------REALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 923 EQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKN 1002
Cdd:TIGR02168 835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1003 VQLQtSTAEEKTKISEQVEVLQKEKDQLQKR---RHNVD----EKLKNGRVLSPEE-EHVLFQLEEGIEAL----EAAI- 1069
Cdd:TIGR02168 915 RELE-ELREKLAQLELRLEGLEVRIDNLQERlseEYSLTleeaEALENKIEDDEEEaRRRLKRLENKIKELgpvnLAAIe 993
|
330 340 350
....*....|....*....|....*....|
gi 1034670647 1070 EYrnESIQNRQKSLRASFHNLSRGEANVLE 1099
Cdd:TIGR02168 994 EY--EELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
678-1093 |
2.38e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 72.10 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 678 ELSDTQDETQKSDLEN---EDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELtiniKMKEDLIK--ELIKTGNDAKS 752
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKkkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEA----KKAEEAKKkaEEAKKADEAKK 1477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 753 VSKQySLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAK---LRVQVLQKKQQDSKKLAS 829
Cdd:PTZ00121 1478 KAEE-AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeAKKAEEKKKADELKKAEE 1556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 830 LSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEglKPKAEDLDACNLKRRK 909
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEA--KIKAEELKKAEEEKKK 1634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 910 gsfgsIDHLQKLDEQKKWLDEEVEKvlnqRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKIST 989
Cdd:PTZ00121 1635 -----VEQLKKKEAEEKKKAEELKK----AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE 1705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 990 RLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAI 1069
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
|
410 420
....*....|....*....|....*...
gi 1034670647 1070 ----EYRNESIQNRQKSLRASFHNLSRG 1093
Cdd:PTZ00121 1786 deedEKRRMEVDKKIKDIFDNFANIIEG 1813
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
721-1092 |
1.36e-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: 69.70 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 721 EAKQKMRELTINIKMKEDLIKELIKtgndaksvskqyslKVTKLEHDAEQAKvELIETQKQLQELEnKDLSdvamkVKLQ 800
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELER--------------QLKSLERQAEKAE-RYKELKAELRELE-LALL-----VLRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 801 KEFRKKMDAAKlrvQVLQKKQQDSKKLASlsiqnekRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKI 880
Cdd:TIGR02168 235 EELREELEELQ---EELKEAEEELEELTA-------ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 881 KEIQLKTGQ-EEGLKPKAEDLDacNLKRRKgsfgsIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKK 959
Cdd:TIGR02168 305 QILRERLANlERQLEELEAQLE--ELESKL-----DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 960 EALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQEL----SEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRH 1035
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRerlqQEIEELLKKLEEAELKELQAELEELEEELEELQEELE 457
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1036 NVDEKLKNGRVLSPEEEHVLFQLEEGIEALEA---AIEYRNESIQNRQKSLRASFHNLSR 1092
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQLQArldSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
711-1227 |
2.58e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.55 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 711 KLKNSERILTEAKQKMRELTINIKMKE---DLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELEn 787
Cdd:PRK03918 194 LIKEKEKELEEVLREINEISSELPELReelEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELK- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 788 KDLSDVAMKVKLQKEFRKKMDA----AKLRVQVLQKKQQDSKKLASLsiqnEKRANELEQSVDHMKYQKIQLQRKLREEN 863
Cdd:PRK03918 273 KEIEELEEKVKELKELKEKAEEyiklSEFYEEYLDELREIEKRLSRL----EEEINGIEERIKELEEKEERLEELKKKLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 864 EKRKQLdAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRRkgsfgsidhLQKLDEQKKWLDEEVEKVLNQRQELE 943
Cdd:PRK03918 349 ELEKRL-EELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKE---------LEELEKAKEEIEEEISKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 944 ELEADLKKreAIVSKKEAL-----------------LQEKSHLENKKLRSSQALNTDSL-KISTRLNLLEQELS-EKNVQ 1004
Cdd:PRK03918 419 KEIKELKK--AIEELKKAKgkcpvcgrelteehrkeLLEEYTAELKRIEKELKEIEEKErKLRKELRELEKVLKkESELI 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1005 LQTSTAEEKTKISEQVEVLQKEKDQLQKRRHnvdEKLKngrvlspeEEhvLFQLEEGIEALEAAIEyRNESIQNRQKSLR 1084
Cdd:PRK03918 497 KLKELAEQLKELEEKLKKYNLEELEKKAEEY---EKLK--------EK--LIKLKGEIKSLKKELE-KLEELKKKLAELE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1085 ASFHNLSRGEANVLEKL-----ACLSPVEIR-TILFRYFNKVVNLREAERKQQLYNEEMKM----------KVLERDNMV 1148
Cdd:PRK03918 563 KKLDELEEELAELLKELeelgfESVEELEERlKELEPFYNEYLELKDAEKELEREEKELKKleeeldkafeELAETEKRL 642
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034670647 1149 RELESALDHLKLQCDrrltlqQKEHEQKMQLLLHhfKEQDGEGIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKEL 1227
Cdd:PRK03918 643 EELRKELEELEKKYS------EEEYEELREEYLE--LSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
763-1085 |
1.95e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 763 KLEHdAEQ--AKVELIETQ--KQLQELENKdlSDVAMKVK-LQKEFR-KKMDAAKLRVQVLQKKQQD-SKKLASLSIQNE 835
Cdd:COG1196 180 KLEA-TEEnlERLEDILGEleRQLEPLERQ--AEKAERYReLKEELKeLEAELLLLKLRELEAELEElEAELEELEAELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 836 KRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDacnlkrrkgsfgsi 915
Cdd:COG1196 257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELE-------------- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 916 dhlQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLE 995
Cdd:COG1196 323 ---EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 996 QELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNES 1075
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
|
330
....*....|
gi 1034670647 1076 IQNRQKSLRA 1085
Cdd:COG1196 480 AELLEELAEA 489
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
705-1227 |
2.81e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 705 QELNLQKL----KNSERILTEAKQKMRELTINIKMKEDlIKELIKTgndaksvskqyslkvtklehdaeqAKVELIETQK 780
Cdd:PRK03918 153 QILGLDDYenayKNLGEVIKEIKRRIERLEKFIKRTEN-IEELIKE------------------------KEKELEEVLR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 781 QLQELEnkdlsdvamkvKLQKEFRKKMDAAKLRVQVLqkkqqdskklaslsiqnEKRANELEQSvdhmKYQKIQLQRKLR 860
Cdd:PRK03918 208 EINEIS-----------SELPELREELEKLEKEVKEL-----------------EELKEEIEEL----EKELESLEGSKR 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 861 EENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRRKgsfgSIDHLQKLDEQKKWLDEEVEKVLNQRQ 940
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE----YLDELREIEKRLSRLEEEINGIEERIK 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 941 ELEELEADLKKreaIVSKKEALLQEKSHLEN--KKLRSSQALNTDSLKISTRLNLLEQELSEKNVQlqtSTAEEKTKISE 1018
Cdd:PRK03918 332 ELEEKEERLEE---LKKKLKELEKRLEELEErhELYEEAKAKKEELERLKKRLTGLTPEKLEKELE---ELEKAKEEIEE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1019 QVEVLQKEKDQLQKRRHNVD---EKLKNGRVLSP------EEEHVLFQLEEGIEALEaAIEYRNESIQNRQKSLRASFHN 1089
Cdd:PRK03918 406 EISKITARIGELKKEIKELKkaiEELKKAKGKCPvcgrelTEEHRKELLEEYTAELK-RIEKELKEIEEKERKLRKELRE 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1090 LsRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREAERKQQLYnEEMKMKVLERDNMVRELESALDHLKLQCDRRLTLQ 1169
Cdd:PRK03918 485 L-EKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY-EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELE 562
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034670647 1170 QKEHEQKMQLL-LHHFKEQDGegiMETFKTYEDKIQQLEKdlyFYKK--TSRDHKKKLKEL 1227
Cdd:PRK03918 563 KKLDELEEELAeLLKELEELG---FESVEELEERLKELEP---FYNEylELKDAEKELERE 617
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
683-1228 |
1.26e-09 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 63.07 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 683 QDETQKSDLENEDLKIDCLQESQELNLQKLKNSERiltEAKQKMRELTINIKMKEDLiKELIKTGNDAKSVSKQyslKVT 762
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE---ELKLLAKEEEELKSELLKL-ERRKVDDEEKLKESEK---EKK 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 763 KLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELE 842
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 843 QSVDhmkyQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKpkaedldacnlkrrkgsfgsiDHLQKLD 922
Cdd:pfam02463 405 KEAQ----LLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEE---------------------LEKQELK 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 923 EQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRssqaLNTDSLKISTRLNLLEQELSEKN 1002
Cdd:pfam02463 460 LLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL----LALIKDGVGGRIISAHGRLGDLG 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1003 VQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKS 1082
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEA 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1083 LRASFHNLSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREAER----------KQQLYNEEMKMKVLERDNMVRELE 1152
Cdd:pfam02463 616 DEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKsevkaslselTKELLEIQELQEKAESELAKEEIL 695
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034670647 1153 SALDHLKLQCDRRLTLQQKEHEQKmQLLLHHFKEQDGEGIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKELV 1228
Cdd:pfam02463 696 RRQLEIKKKEQREKEELKKLKLEA-EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
685-1227 |
2.68e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.96 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 685 ETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKEL----------IKTGNDAKSVS 754
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLnsdlskinseIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 755 KQYSLK------------------VTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEF---RKKMDAAKLR 813
Cdd:TIGR04523 123 EVELNKlekqkkenkknidkflteIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIdkiKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 814 VQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQL----DAVIKRDQQKIKEI------ 883
Cdd:TIGR04523 203 LSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLkdeqNKIKKQLSEKQKELeqnnkk 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 884 ---------QLKTGQEEGLKPKAEDLDacnlKRRKGSFGSIDhlQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREA 954
Cdd:TIGR04523 283 ikelekqlnQLKSEISDLNNQKEQDWN----KELKSELKNQE--KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 955 IVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNvqlqtstaEEKTKISEQVEVLQKEKDQLQKRR 1034
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE--------KLNQQKDEQIKKLQQEKELLEKEI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1035 hnvdEKLKNGRVLSPEE----EHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIR 1110
Cdd:TIGR04523 429 ----ERLKETIIKNNSEikdlTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1111 TILFRYFNKVVNLREAERKQQLynEEMKMKVLERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFK---EQ 1187
Cdd:TIGR04523 505 KKELEEKVKDLTKKISSLKEKI--EKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQTQkslKK 582
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1034670647 1188 DGEGIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKEL 1227
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
696-1210 |
3.19e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 696 LKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVEL 775
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 776 IETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQL 855
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 856 QRKLREENEKRKQLDAVIKRDQQKIkeIQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKV 935
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERL--ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 936 LNQRQELEELEADLKKREAIVSKKEALLQEKSHLE-------NKKLRSSQALNTDSLK------------ISTRLNLLEQ 996
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEgflegvkAALLLAGLRGLAGAVAvligveaayeaaLEAALAAALQ 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 997 ELSEKNVQ-LQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLK-----NGRVLSPEEEHVLFQLEEGIEALEAAIE 1070
Cdd:COG1196 550 NIVVEDDEvAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAigaavDLVASDLREADARYYVLGDTLLGRTLVA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1071 YRNESIQNRQKSLRASFHNLSRG--EANVLEKLACLSPVEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMV 1148
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEgeGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034670647 1149 RELESALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDGEGI-----METFKTYEDKIQQLEKDL 1210
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALeelpePPDLEELERELERLEREI 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
849-1164 |
5.82e-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: 60.84 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 849 KYQKIQLQRKLREENEKRKQLDAVIK--RDQQKIKEIQLKTGQE-EGLKPKAEDLDACNLKRRKGSFgsIDHLQKLDEQK 925
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDILNelERQLKSLERQAEKAERyKELKAELRELELALLVLRLEEL--REELEELQEEL 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 926 KWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLrssQALNTDSLKISTRLNLLEQELSEKNVQL 1005
Cdd:TIGR02168 249 KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI---SRLEQQKQILRERLANLERQLEELEAQL 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1006 QTStAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKngrvlspEEEHVLFQLEEGIEALEAAIEYRN----------ES 1075
Cdd:TIGR02168 326 EEL-ESKLDELAEELAELEEKLEELKEELESLEAELE-------ELEAELEELESRLEELEEQLETLRskvaqlelqiAS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1076 IQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESAL 1155
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
....*....
gi 1034670647 1156 DHLKLQCDR 1164
Cdd:TIGR02168 478 DAAERELAQ 486
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
717-1302 |
1.45e-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: 59.60 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 717 RILTEAKQKMRELTINIKMKEDLIKELIKtgndaksvskqyslkvtKLEHDAEQAKVELIETQKQLQELENKDLSDVAMK 796
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKL-----------------QELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 797 VKLQKEFRKKMDA-AKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKR 875
Cdd:pfam02463 232 LKLNEERIDLLQElLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 876 DQQKIKEIQLKTGQEEGlkpkaedldacNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEE-----LEADLK 950
Cdd:pfam02463 312 DEEKLKESEKEKKKAEK-----------ELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEqleeeLLAKKK 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 951 KREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQL 1030
Cdd:pfam02463 381 LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1031 QKRRHnVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIR 1110
Cdd:pfam02463 461 LKDEL-ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1111 TILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDHLKLQcdrRLTLQQKEHEQKMQLLLHHFKEQDGE 1190
Cdd:pfam02463 540 NYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLP---LKSIAVLEIDPILNLAQLDKATLEAD 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1191 GIMETFKTYEDKIQQLEKDLyfykktSRDHKKKLKELVGEAIRRQLAPSEYQEAGDGVLKPEGGGMLSEELKWASRPESM 1270
Cdd:pfam02463 617 EDDKRAKVVEGILKDTELTK------LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590
....*....|....*....|....*....|..
gi 1034670647 1271 KLSGREREMDSSASSLRTQPNPQKLWEDIPEL 1302
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
684-1046 |
1.66e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 684 DETQKSDlenEDLKIDCLQESQEL----NLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSL 759
Cdd:PTZ00121 1537 DEAKKAE---EKKKADELKKAEELkkaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK 1613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 760 KVTKLEHDAEQAKVELiETQKQLQELENKDlsdvAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLAS-LSIQNEKRA 838
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAE-EEKKKVEQLKKKE----AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEeAKKAEEDEK 1688
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 839 NELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGlKPKAEDLDACNLKRRKGSFGSIDHL 918
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED-KKKAEEAKKDEEEKKKIAHLKKEEE 1767
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 919 QKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREaiVSKKEALLQEKSHLENKKLRSSQALNTDSLK---ISTRLNLLE 995
Cdd:PTZ00121 1768 KKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKD--IFDNFANIIEGGKEGNLVINDSKEMEDSAIKevaDSKNMQLEE 1845
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1034670647 996 QELSEKNVQLQTStaeEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRV 1046
Cdd:PTZ00121 1846 ADAFEKHKFNKNN---ENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKI 1893
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
812-1244 |
4.72e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 812 LRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVikrdQQKIKEIQlktgqee 891
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL----EAELEELR------- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 892 glkpkaEDLDAcnLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEkshlen 971
Cdd:COG4717 116 ------EELEK--LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEE------ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 972 kklrssqALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKtKISEQVEVLQKEKDQL--QKRRHNVDEKLKNGRVL-- 1047
Cdd:COG4717 182 -------LLEQLSLATEEELQDLAEELEELQQRLAELEEELE-EAQEELEELEEELEQLenELEAAALEERLKEARLLll 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1048 -----------------SPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLAC---LSPV 1107
Cdd:COG4717 254 iaaallallglggsllsLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAalgLPPD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1108 EIRTILFRYFNKVVNLREAERKQQLYNEEMKMKVL--ERDNMVREL----ESALDHLKLQCDRRLTLQQKEHEQKMQLLL 1181
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELeqEIAALLAEAgvedEEELRAALEQAEEYQELKEELEELEEQLEE 413
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034670647 1182 hHFKEQDGEGIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKELVGEaIRRQLAPSEYQEA 1244
Cdd:COG4717 414 -LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAE-LEQLEEDGELAEL 474
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
935-1210 |
4.78e-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: 57.76 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 935 VLNQRQELEELEADLKKREAIVSKKEALLQEKSHlenkklrSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKt 1014
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRK-------ELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE- 743
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1015 KISEQVEVLQKEKDQLQKRRHNVDEKLKngrvlspEEEHVLFQLEEGIEALEAAIEYRNESIQN---RQKSLRASFHNLS 1091
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLE-------EAEEELAEAEAEIEELEAQIEQLKEELKAlreALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1092 RGEANVLEKLACLSPvEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDhlklqcdrrltlQQK 1171
Cdd:TIGR02168 817 EEAANLRERLESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN------------ERA 883
|
250 260 270
....*....|....*....|....*....|....*....
gi 1034670647 1172 EHEQKMQLLLHHFKEQdgegiMETFKTYEDKIQQLEKDL 1210
Cdd:TIGR02168 884 SLEEALALLRSELEEL-----SEELRELESKRSELRREL 917
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
936-1244 |
1.67e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.23 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 936 LNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQelseknvqlqtsTAEEKTK 1015
Cdd:TIGR02169 667 LFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ------------LEQEEEK 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1016 ISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAaiEYRNESIQNRQKSLRASFHNLSRGEA 1095
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1096 NVLEKLACLSPVEIRTILFRyfNKVVNL---------REAERKQQLYN-----EEMKMKVLERDNMVRELESALDHLKLQ 1161
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLE--KEIQELqeqridlkeQIKSIEKEIENlngkkEELEEELEELEAALRDLESRLGDLKKE 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1162 CDRRLT----LQQKEHEQKMQL--LLHHFKEQDG--EGIMETFKTYEDKIQQLEKdlYFYKKTSRDHKKKLKELVGEAIR 1233
Cdd:TIGR02169 891 RDELEAqlreLERKIEELEAQIekKRKRLSELKAklEALEEELSEIEDPKGEDEE--IPEEELSLEDVQAELQRVEEEIR 968
|
330
....*....|....*.
gi 1034670647 1234 R-----QLAPSEYQEA 1244
Cdd:TIGR02169 969 AlepvnMLAIQEYEEV 984
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
716-1175 |
9.06e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 9.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 716 ERILTEAKQKMRELTINIKMKEDliKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAK------VELI----ETQKQLQEL 785
Cdd:PRK02224 179 ERVLSDQRGSLDQLKAQIEEKEE--KDLHERLNGLESELAELDEEIERYEEQREQARetrdeaDEVLeeheERREELETL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 786 EnKDLSDVAMKVKlqkEFRKKMDAAKLRVQVLQKKQQD-----SKKLASLSIqNEKRANELEQSVDHMKYQKIQLQRKLR 860
Cdd:PRK02224 257 E-AEIEDLRETIA---ETEREREELAEEVRDLRERLEEleeerDDLLAEAGL-DDADAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 861 EENEKRKQLDAVIKRDQQKIKEIQlktGQEEGLKPKAEDLDA----CNLKRRKGSfGSIDHLQK---------------L 921
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLE---ERAEELREEAAELESeleeAREAVEDRR-EEIEELEEeieelrerfgdapvdL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 922 DEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLE-NKKLRSS---QALNTDSLKISTrlnlLEQE 997
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPEcGQPVEGSphvETIEEDRERVEE----LEAE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 998 LSEknVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQ 1077
Cdd:PRK02224 484 LED--LEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1078 ---NRQKSLRASFHNLSRGEANVLEKLACLSpvEIRTILFR---YFNKVVNLREAERKQQLYNEEMKMKVLERDNMVREL 1151
Cdd:PRK02224 562 eaeEEAEEAREEVAELNSKLAELKERIESLE--RIRTLLAAiadAEDEIERLREKREALAELNDERRERLAEKRERKREL 639
|
490 500
....*....|....*....|....
gi 1034670647 1152 ESALDhlklqcDRRLTLQQKEHEQ 1175
Cdd:PRK02224 640 EAEFD------EARIEEAREDKER 657
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
681-1066 |
1.04e-06 |
|
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: 53.58 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 681 DTQDETQKSDLENedlKIDCLQESQELNLQKLKNSERI----LTEAKQKMRELTINIKMKEDLIKEliktgnDAKSVSKQ 756
Cdd:pfam15921 244 EDQLEALKSESQN---KIELLLQQHQDRIEQLISEHEVeitgLTEKASSARSQANSIQSQLEIIQE------QARNQNSM 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 757 YSLKVTKLEHDAEQAKVELIETQK----QLQELE------NKDLSDVAMKvklQKEFRKKMDAAKLRVQVLQKKQQDSKK 826
Cdd:pfam15921 315 YMRQLSDLESTVSQLRSELREAKRmyedKIEELEkqlvlaNSELTEARTE---RDQFSQESGNLDDQLQKLLADLHKREK 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 827 LASLSIQNEKRANELEQ----SVDHmkyqkiqLQRKLREENEKRKQLDAVIKRDQQKIKeiqlktGQEEGlkpkaedlda 902
Cdd:pfam15921 392 ELSLEKEQNKRLWDRDTgnsiTIDH-------LRRELDDRNMEVQRLEALLKAMKSECQ------GQMER---------- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 903 cNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLnqrQELEELEADLKKREAIVSKKEALLQEKShlenkklRSSQALNT 982
Cdd:pfam15921 449 -QMAAIQGKNESLEKVSSLTAQLESTKEMLRKVV---EELTAKKMTLESSERTVSDLTASLQEKE-------RAIEATNA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 983 DSLKISTRLNLLEQELSE--------KNVQLQTSTAE----EKTKISE----QVE--------------VLQKEKDQLQK 1032
Cdd:pfam15921 518 EITKLRSRVDLKLQELQHlknegdhlRNVQTECEALKlqmaEKDKVIEilrqQIEnmtqlvgqhgrtagAMQVEKAQLEK 597
|
410 420 430
....*....|....*....|....*....|....
gi 1034670647 1033 RRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALE 1066
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
918-1208 |
1.28e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 918 LQKLDEQKkwldEEVEKVLNQRQELEELEADL--KKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTrLNLLE 995
Cdd:TIGR02168 202 LKSLERQA----EKAERYKELKAELRELELALlvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEE-LRLEV 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 996 QELSEKNVQLQTSTAEEKTKISEqvevLQKEKDQLQKRRHNVDEKLKngrVLSPEEEHVLFQLEEGIEALeAAIEYRNES 1075
Cdd:TIGR02168 277 SELEEEIEELQKELYALANEISR----LEQQKQILRERLANLERQLE---ELEAQLEELESKLDELAEEL-AELEEKLEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1076 IQNRQKSLRASFHNLSRGEANVLEKLAclspvEIRTILFRYFNKVVNLREAERKQQLyneemkmkvlerdnmvrELESAL 1155
Cdd:TIGR02168 349 LKEELESLEAELEELEAELEELESRLE-----ELEEQLETLRSKVAQLELQIASLNN-----------------EIERLE 406
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034670647 1156 DHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDG------EGIMETFKTYEDKIQQLEK 1208
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAeleeleEELEELQEELERLEEALEE 465
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
685-1032 |
3.04e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 685 ETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAksvskqySLKVTKL 764
Cdd:pfam05483 446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDM-------TLELKKH 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 765 EHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRvqvLQKKQQDSKKLASLSIQNEKRANELEQS 844
Cdd:pfam05483 519 QEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCK---LDKSEENARSIEYEVLKKEKQMKILENK 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 845 VDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEglkpkaedldaCNLKRRKGSFGSI-DHLQKLDE 923
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLE-----------LELASAKQKFEEIiDNYQKEIE 664
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 924 QKKWLDE----EVEKVLNQRQELEELEADLKKR-EAIVSKKEALLQEKSHLENKKLRSSqalntdslkiSTRLNLL---E 995
Cdd:pfam05483 665 DKKISEEklleEVEKAKAIADEAVKLQKEIDKRcQHKIAEMVALMEKHKHQYDKIIEER----------DSELGLYknkE 734
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1034670647 996 QELSEKNVQLQTSTAE---EKTKISEQVEVLQKEKDQLQK 1032
Cdd:pfam05483 735 QEQSSAKAALEIELSNikaELLSLKKQLEIEKEEKEKLKM 774
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
685-1050 |
3.43e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 685 ETQKSDLENEDLKIDCLQES-QELNlQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTK 763
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIiSQLN-EQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 764 LEHDAEQAK---------VELIETQKQLQELENKDLSDVAMKVKLQ-KEFRKKMDAAKLRVQVL-QKKQQDSKKLASLSI 832
Cdd:TIGR04523 396 LESKIQNQEklnqqkdeqIKKLQQEKELLEKEIERLKETIIKNNSEiKDLTNQDSVKELIIKNLdNTRESLETQLKVLSR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 833 QNEKRANELEQSVDHMKYQKiqlqRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDldacNLKRRKgsf 912
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKE----KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKES----KISDLE--- 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 913 gsiDHLQKLDEQKKWLDEEVEkVLNQRQELEELEADLKKREAIVSKKEALLQEKSHlENKKLRSSQALNTdsLKISTrln 992
Cdd:TIGR04523 545 ---DELNKDDFELKKENLEKE-IDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEK-EKKDLIKEIEEKE--KKISS--- 614
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034670647 993 lLEQELSEKNvqlqtstaEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPE 1050
Cdd:TIGR04523 615 -LEKELEKAK--------KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPE 663
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
744-1231 |
3.44e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 744 IKTGNDAKSVSKQYSLKVTKLEHDAEQAKveLIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAK----LRVQVLQK 819
Cdd:PTZ00121 1178 AEAARKAEEVRKAEELRKAEDARKAEAAR--KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKkaeeERNNEEIR 1255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 820 KQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKqLDAVIKRDQQKIKEIQLKTGQEEG------L 893
Cdd:PTZ00121 1256 KFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKK-ADEAKKKAEEAKKADEAKKKAEEAkkkadaA 1334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 894 KPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLD-----------------EEVEKVLNQRQELEELEA---DLKKRE 953
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkkkeeakkkadaakkkaEEKKKADEAKKKAEEDKKkadELKKAA 1414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 954 AIVSKKEAL---LQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTS-----TAEEKTKISEQVEVLQK 1025
Cdd:PTZ00121 1415 AAKKKADEAkkkAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdeakkKAEEAKKADEAKKKAEE 1494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1026 EKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKlacLS 1105
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA---KK 1571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1106 PVEIRTILFRyfnKVVNLREAERKQ-----QLYNEEMKMKVLERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLL 1180
Cdd:PTZ00121 1572 AEEDKNMALR---KAEEAKKAEEARieevmKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1034670647 1181 LHHFKEQDGEGIM----ETFKTYEDKIQQLEkdlyfYKKTSRDHKKKLKELVGEA 1231
Cdd:PTZ00121 1649 AEELKKAEEENKIkaaeEAKKAEEDKKKAEE-----AKKAEEDEKKAAEALKKEA 1698
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
697-1095 |
3.69e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 51.62 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 697 KIDCLQESQELNLQ-KLKNSERILTEAKQKMRELTINIKMKE--DLIKELIKTGNDAKSVSKQYSLKVTKLEHDAE---Q 770
Cdd:COG5022 770 RIKKIQVIQHGFRLrRLVDYELKWRLFIKLQPLLSLLGSRKEyrSYLACIIKLQKTIKREKKLRETEEVEFSLKAEvliQ 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 771 AKVELIETQKQLQELENKDLSDvamkvklqkEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQsvdhmky 850
Cdd:COG5022 850 KFGRSLKAKKRFSLLKKETIYL---------QSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKK------- 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 851 qkiQLQRKLREENEKRKQLDAVIKRdqqKIKEIQLKTGQEEglkpkaedldacnlkrrkgSFGSIDHLQKLDEQKKWLDE 930
Cdd:COG5022 914 ---SLSSDLIENLEFKTELIARLKK---LLNNIDLEEGPSI-------------------EYVKLPELNKLHEVESKLKE 968
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 931 EVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHlENKKLRSSQALNTDSLKISTRLNLLEQELSEknvqlQTSTA 1010
Cdd:COG5022 969 TSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSK-QYGALQESTKQLKELPVEVAELQSASKIISS-----ESTEL 1042
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1011 EEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEhvlfqLEEGIEALEAAIEYRNESIQNRQKSLRASFHNL 1090
Cdd:COG5022 1043 SILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLY-----QLESTENLLKTINVKDLEVTNRNLVKPANVLQF 1117
|
....*
gi 1034670647 1091 SRGEA 1095
Cdd:COG5022 1118 IVAQM 1122
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
684-1220 |
3.82e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 51.65 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 684 DETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKtgndaksvsKQYSLkvTK 763
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE---------KKDHL--TK 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 764 LEHDAEQAKVELIETQKQLQE---LENKDLSDVAMKVKLQKEFRKKMDAAklRVQVLQKKQQDSKKLASLSIQNEKRane 840
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEdlqIATKTICQLTEEKEAQMEELNKAKAA--HSFVVTEFEATTCSLEELLRTEQQR--- 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 841 LEQSVDHMKYQKIQLQRKLREENEKRKQLDAvikrdqqkiKEIQLktgqEEGLKPKAEDLDACNLKRRkgsfgsidhLQK 920
Cdd:pfam05483 372 LEKNEDQLKIITMELQKKSSELEEMTKFKNN---------KEVEL----EELKKILAEDEKLLDEKKQ---------FEK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 921 LDEQKKWLDEEVEKVLNQRQ-ELEELEADLKkreAIVSKKEALLQE----KSHLENKKLRSSQaLNTDSLKISTRLNLLE 995
Cdd:pfam05483 430 IAEELKGKEQELIFLLQAREkEIHDLEIQLT---AIKTSEEHYLKEvedlKTELEKEKLKNIE-LTAHCDKLLLENKELT 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 996 QELSEKNVQLQT------STAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRvlsPEEEHVLFQLEEGIEALEAAI 1069
Cdd:pfam05483 506 QEASDMTLELKKhqediiNCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKG---DEVKCKLDKSEENARSIEYEV 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1070 ---EYRNESIQNRQKSLRASFHNLSRG------EANVLEKLACLSPVEIRTILFRYFNKVVNLREAERK----QQLYNEE 1136
Cdd:pfam05483 583 lkkEKQMKILENKCNNLKKQIENKNKNieelhqENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKfeeiIDNYQKE 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1137 MKMKVLERDNMVRELESAldhlKLQCDRRLTLqQKEHEQKMQlllHHFKEQdgEGIMETFKTYEDKI-QQLEKDLYFYKK 1215
Cdd:pfam05483 663 IEDKKISEEKLLEEVEKA----KAIADEAVKL-QKEIDKRCQ---HKIAEM--VALMEKHKHQYDKIiEERDSELGLYKN 732
|
....*
gi 1034670647 1216 TSRDH 1220
Cdd:pfam05483 733 KEQEQ 737
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
817-1049 |
4.67e-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: 50.53 E-value: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 817 LQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQ------------ 884
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRaeleaqkeelae 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 885 -LKTGQEEGLKPKAEdldacNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADL-KKREAIVSKKEAL 962
Cdd:COG4942 109 lLRALYRLGRQPPLA-----LLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELeAERAELEALLAEL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 963 LQEKSHLENKKLRSSQALNtdslKISTRLNLLEQELSEKnvqlqtstAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLK 1042
Cdd:COG4942 184 EEERAALEALKAERQKLLA----RLEKELAELAAELAEL--------QQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
....*..
gi 1034670647 1043 NGRVLSP 1049
Cdd:COG4942 252 KGKLPWP 258
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
685-1084 |
4.98e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 685 ETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDlIKELIKTGNDAKSVSKQYSLKVTKL 764
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 765 EHDAEQAKVELIETQKQLQELENKDlSDVAMKVKLQKEFRKKMDAAKLRVQVLQK-------KQQDSKKLASLSIQN--- 834
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKE-ERLEELKKKLKELEKRLEELEERHELYEEakakkeeLERLKKRLTGLTPEKlek 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 835 -----EKRANELEQSVDHMKYQKIQLQRKLREEN----------------------EKRKQLDAVIKRDQQKI-KEIQLK 886
Cdd:PRK03918 392 eleelEKAKEEIEEEISKITARIGELKKEIKELKkaieelkkakgkcpvcgrelteEHRKELLEEYTAELKRIeKELKEI 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 887 TGQEEGLKPKAEDLD---------------ACNLKRRKGSFGSIDhLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKK 951
Cdd:PRK03918 472 EEKERKLRKELRELEkvlkkeseliklkelAEQLKELEEKLKKYN-LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 952 REAIVSKKEALLQEKSHLENKK---LRSSQALNTDSLK-ISTRLNLLEqELSEKNVQLQTSTAE----------EKTKIS 1017
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELaelLKELEELGFESVEeLEERLKELE-PFYNEYLELKDAEKElereekelkkLEEELD 629
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034670647 1018 EQVEVLQKEKDQLQKRRHNVDEKLKNgrvLSPEE----EHVLFQLEEGIEALEAAIEYRNESIQNRQKSLR 1084
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKK---YSEEEyeelREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
710-961 |
6.51e-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: 50.15 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 710 QKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQElenkd 789
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 790 lsdvamkvkLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQN----EKRANELEQSVDHMKYQKIQLQRKLREENEK 865
Cdd:COG4942 95 ---------LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDfldaVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 866 RKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLdacnlkrrkgsfgsidhLQKLDEQKKWLDEEVEKVLNQRQELEEL 945
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKL-----------------LARLEKELAELAAELAELQQEAEELEAL 228
|
250
....*....|....*.
gi 1034670647 946 EADLKKREAIVSKKEA 961
Cdd:COG4942 229 IARLEAEAAAAAERTP 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
706-1095 |
1.12e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 706 ELNLQKLKNSERILTEAKQKMRELTINIKMKEDL---IKELIKTGNDAKSVSKQYSLKVTKLEHDAE--QAKVELIETQK 780
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELeeeLEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 781 QLQELENkdlsdvamkvKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLR 860
Cdd:COG4717 147 RLEELEE----------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 861 EENEKRKQLDAVIKR---------DQQKIKEIQLKTGQE------EGLKPKAEDLDACNLKRRKGSFGSI-DHLQKLDEQ 924
Cdd:COG4717 217 EAQEELEELEEELEQleneleaaaLEERLKEARLLLLIAaallalLGLGGSLLSLILTIAGVLFLVLGLLaLLFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 925 KKWLDEEVEKV--LNQRQELE--ELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKIstRLNLLEQELSE 1000
Cdd:COG4717 297 KASLGKEAEELqaLPALEELEeeELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1001 KNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSpeEEHVLFQLEEGIEALEAAIEYRNE---SIQ 1077
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL--EALDEEELEEELEELEEELEELEEeleELR 452
|
410
....*....|....*...
gi 1034670647 1078 NRQKSLRASFHNLSRGEA 1095
Cdd:COG4717 453 EELAELEAELEQLEEDGE 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
864-1102 |
1.40e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 864 EKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDAcNLKRRKGSfgsidhLQKLDEQKKWLDEEVEKVlnqRQELE 943
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALER-RIAALARR------IRALEQELAALEAELAEL---EKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 944 ELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQtstaEEKTKISEQVEVL 1023
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR----ADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034670647 1024 QKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIeyrnESIQNRQKSLRASFHNLSRGEANVLEKLA 1102
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL----AELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
801-1070 |
1.43e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 801 KEFRKKMDAAKLRVQVLQKKQQDSKKLAslsiQNEKRANELEQSVDHMKYQKIQ-----LQRKLREENEKRKQLDAVIKR 875
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYA----AARERLAELEYLRAALRLWFAQrrlelLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 876 DQQKIKEIQlktgqeeglkpkaEDLDACNLKRRKGSFGSIDHLQKldeQKKWLDEEVEKVLNQRQELEELEADLKkreai 955
Cdd:COG4913 314 LEARLDALR-------------EELDELEAQIRGNGGDRLEQLER---EIERLERELEERERRRARLEALLAALG----- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 956 vskkEALLQEKSHLENKKLRSSQALNTdslkISTRLNLLEQELSEKNVQLQTSTAEEKTkiseqvevLQKEKDQLQKRRH 1035
Cdd:COG4913 373 ----LPLPASAEEFAALRAEAAALLEA----LEEELEALEEALAEAEAALRDLRRELRE--------LEAEIASLERRKS 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034670647 1036 NVDEKLKNGR-----VLSPEEEHVLF-----QLEEGIEALEAAIE 1070
Cdd:COG4913 437 NIPARLLALRdalaeALGLDEAELPFvgeliEVRPEEERWRGAIE 481
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
474-1191 |
1.49e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.73 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 474 TVLQLKRELKKCQCVLAADEVVFNQKELEVKELKNQVQMMVQEnkghavslkeaqkvnrLQNEKIIEQQLLVDQLS--EE 551
Cdd:pfam15921 111 SVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHE----------------LEAAKCLKEDMLEDSNTqiEQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 552 LTKLNLSvtssakencgdgPDARIPERRPYTVPFDTHLGHYIYipsRQDS-RKVHTSPPMYSLDRIFAGFRTRSQMLLGH 630
Cdd:pfam15921 175 LRKMMLS------------HEGVLQEIRSILVDFEEASGKKIY---EHDSmSTMHFRSLGSAISKILRELDTEISYLKGR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 631 I------------EEQDKV--LHCQFSDNSDDEESEGQ-EKSGTRCRSRSWIQKPDSVCSLVELSDTQDETQKSdlened 695
Cdd:pfam15921 240 IfpvedqlealksESQNKIelLLQQHQDRIEQLISEHEvEITGLTEKASSARSQANSIQSQLEIIQEQARNQNS------ 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 696 lkidclqesqeLNLQKLKNSERILTEAKQKMRELTiniKMKEDLIKELIKTG-------NDAKSVSKQYSLKVTKLEHDA 768
Cdd:pfam15921 314 -----------MYMRQLSDLESTVSQLRSELREAK---RMYEDKIEELEKQLvlanselTEARTERDQFSQESGNLDDQL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 769 EQAKVELIETQKQL--QELENKDLSDVAMKVKLQ-KEFRKKMDAAKLRVQVL----------------------QKKQQD 823
Cdd:pfam15921 380 QKLLADLHKREKELslEKEQNKRLWDRDTGNSITiDHLRRELDDRNMEVQRLeallkamksecqgqmerqmaaiQGKNES 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 824 SKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREEN-------EKRKQLDA-------VIKRDQQKIKEIQLKTGQ 889
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdltaslqEKERAIEAtnaeitkLRSRVDLKLQELQHLKNE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 890 EEGLKPKAEDLDACNLKRrKGSFGSIDHLQKLDEQKKWL--------------DEEVEKVLNQRQ-ELEELEADLKKREA 954
Cdd:pfam15921 540 GDHLRNVQTECEALKLQM-AEKDKVIEILRQQIENMTQLvgqhgrtagamqveKAQLEKEINDRRlELQEFKILKDKKDA 618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 955 IVSKKEA-------------------------LLQEKSHLENKKLRSSQALNTdslkISTRLNLLEQELSEKNVQLQTST 1009
Cdd:pfam15921 619 KIRELEArvsdlelekvklvnagserlravkdIKQERDQLLNEVKTSRNELNS----LSEDYEVLKRNFRNKSEEMETTT 694
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1010 aeekTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLrasfHN 1089
Cdd:pfam15921 695 ----NKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEK----HF 766
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1090 LSRGEANVLEKLACLSPVEirtilfryfNKVVNLREAERKQQlynEEMKMKVlerdnmvRELESALDHLKLQCDRRLTLQ 1169
Cdd:pfam15921 767 LKEEKNKLSQELSTVATEK---------NKMAGELEVLRSQE---RRLKEKV-------ANMEVALDKASLQFAECQDII 827
|
810 820
....*....|....*....|....*
gi 1034670647 1170 QKEHEQKMQLLLHH---FKEQDGEG 1191
Cdd:pfam15921 828 QRQEQESVRLKLQHtldVKELQGPG 852
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
678-1158 |
1.57e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 49.66 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 678 ELSDTQDETQKSDLENEDLKIDCLQESQEL----NLQKLKNSERILTEAKQ---KMRELTINIKMKEDLIKELIKTGNDa 750
Cdd:TIGR01612 1319 DINDIKKELQKNLLDAQKHNSDINLYLNEIaniyNILKLNKIKKIIDEVKEytkEIEENNKNIKDELDKSEKLIKKIKD- 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 751 ksvskQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSD---VAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKL 827
Cdd:TIGR01612 1398 -----DINLEECKSKIESTLDDKDIDECIKKIKELKNHILSEesnIDTYFKNADENNENVLLLFKNIEMADNKSQHILKI 1472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 828 ASLSIQNEK--RANELEQSVDHMKYQKIQLQrKLREENEKRKQLDAVIKRD----QQKIKEIQLKTGQEEGLKPKAEDLD 901
Cdd:TIGR01612 1473 KKDNATNDHdfNINELKEHIDKSKGCKDEAD-KNAKAIEKNKELFEQYKKDvtelLNKYSALAIKNKFAKTKKDSEIIIK 1551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 902 ACNLKRRKGSFGSIDHLQKLDEQKK---WLDEEVEK-------VLNQRQELEELEADLKKREAIVSKKEALLQEKSHLEN 971
Cdd:TIGR01612 1552 EIKDAHKKFILEAEKSEQKIKEIKKekfRIEDDAAKndksnkaAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEK 1631
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 972 KKlrSSQALNTDSLKISTRLNLLE--QELSEknvqlqtSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNgrvlsp 1049
Cdd:TIGR01612 1632 KI--SSFSIDSQDTELKENGDNLNslQEFLE-------SLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKN------ 1696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1050 EEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLA----------------------CLSPV 1107
Cdd:TIGR01612 1697 YEIGIIEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNEKLEeynteigdiyeefielyniiagCLETV 1776
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034670647 1108 --------EIRTILFRYFNKVVNLREAERKQQLYNEEMKMKvlERDNMVRELESALDHL 1158
Cdd:TIGR01612 1777 skepitydEIKNTRINAQNEFLKIIEIEKKSKSYLDDIEAK--EFDRIINHFKKKLDHV 1833
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
801-1077 |
2.53e-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: 48.81 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 801 KEFRKKMDAAKlrvQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKI 880
Cdd:pfam02463 166 RLKRKKKEALK---KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 881 KEIQLKTGQEEGLKPKAEDLDACNLKRRKgsfgsidHLQKLDEQKKWLDEEVEKVLNQRQELEELEAD-LKKREAIVSKK 959
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVL-------KENKEEEKEKKLQEEELKLLAKEEEELKSELLkLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 960 EALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQK--RRHNV 1037
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSaaKLKEE 395
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1034670647 1038 DEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQ 1077
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEE 435
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
852-983 |
2.99e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 852 KIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRRKgsfgsIDHLQKLDEQKK-WLDE 930
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNE-----LQKLEKRLLQKEeNLDR 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1034670647 931 EVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTD 983
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAE 153
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
697-912 |
3.23e-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: 47.84 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 697 KIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELI 776
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 777 ETQKQLQE-----------------LENKDLSDVAMKVKLQKEFrkkmdaAKLRVQVLQKKQQDSKKLASLSIQNEKRAN 839
Cdd:COG4942 101 AQKEELAEllralyrlgrqpplallLSPEDFLDAVRRLQYLKYL------APARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 840 ELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQ--------LKTGQEEGLKPKAEDLDACNLKRRKGS 911
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQqeaeeleaLIARLEAEAAAAAERTPAAGFAALKGK 254
|
.
gi 1034670647 912 F 912
Cdd:COG4942 255 L 255
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
680-1030 |
3.23e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 48.66 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 680 SDTQDETQKSDLENEDLKIDCLQESQELN----LQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSK 755
Cdd:pfam10174 434 TDTALTTLEEALSEKERIIERLKEQREREdrerLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGL 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 756 QYSLKVTKLEHDAEQAKVELIETQKQLQELENkdlsdVAMKVKLQKEFrkkmdaaKLRVQVLQKKQQDSKKLASlsiqne 835
Cdd:pfam10174 514 KKDSKLKSLEIAVEQKKEECSKLENQLKKAHN-----AEEAVRTNPEI-------NDRIRLLEQEVARYKEESG------ 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 836 KRANELEQSVDHMKYQKiqlqrklREENEKRKQLDAVIKRDQQKIKE-----IQLKTGQEEGLKPKAEDLDacNLKRRKG 910
Cdd:pfam10174 576 KAQAEVERLLGILREVE-------NEKNDKDKKIAELESLTLRQMKEqnkkvANIKHGQQEMKKKGAQLLE--EARRRED 646
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 911 SFGSIDHLQKLDEqkkwLDEEVEKVlnqRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKIStr 990
Cdd:pfam10174 647 NLADNSQQLQLEE----LMGALEKT---RQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQLEEILEMKQEALLAA-- 717
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1034670647 991 lnlleqeLSEK--NVQLQTSTAEEKTKISEQVEVLQKEKDQL 1030
Cdd:pfam10174 718 -------ISEKdaNIALLELSSSKKKKTQEEVMALKREKDRL 752
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
722-1041 |
3.40e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 722 AKQKMRELTINIKMKEDLIKELIKtgndaksvskqyslKVTKLEHDAEQAkVELIETQKQLQELENKDLsdvamkVKLQK 801
Cdd:TIGR02169 175 ALEELEEVEENIERLDLIIDEKRQ--------------QLERLRREREKA-ERYQALLKEKREYEGYEL------LKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 802 EFRKKMDAAKLRVQVLQKKQQDSKKLASlsiQNEKRANELEQSVDHMKYQ--------KIQLQRKLREENEKRKQLDAVI 873
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEIS---ELEKRLEEIEQLLEELNKKikdlgeeeQLRVKEKIGELEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 874 --KRDQQKIKEIQLKTGQEE--GLKPKAEDLDacnlkrrkgsfGSIDHLQKLDEQKKWLDEEVEKVLNQ-RQELEELEAD 948
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEidKLLAEIEELE-----------REIEEERKRRDKLTEEYAELKEELEDlRAELEEVDKE 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 949 L-----------KKREAIVSKKEALLQEKSHLENKKLRSSQA---LNTDSLKISTRLNLLEQELSEKNVQLQT------S 1008
Cdd:TIGR02169 380 FaetrdelkdyrEKLEKLKREINELKRELDRLQEELQRLSEEladLNAAIAGIEAKINELEEEKEDKALEIKKqewkleQ 459
|
330 340 350
....*....|....*....|....*....|...
gi 1034670647 1009 TAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKL 1041
Cdd:TIGR02169 460 LAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
763-1025 |
3.48e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 48.31 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 763 KLEHDAEQAKVELIETQKQLQELENKDLS----DVAMKVKLQkEFRKKMDAAKLRVQ-VLQKKQQDSKKLASLsiqnEKR 837
Cdd:pfam09726 399 RLEQDIKKLKAELQASRQTEQELRSQISSltslERSLKSELG-QLRQENDLLQTKLHnAVSAKQKDKQTVQQL----EKR 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 838 ANELEQSvdhmkyqKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGqeEGLKPKAEDLDAcnlkrrkgsfgsidH 917
Cdd:pfam09726 474 LKAEQEA-------RASAEKQLAEEKKRKKEEEATAARAVALAAASRGECT--ESLKQRKRELES--------------E 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 918 LQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENkklrssqalntdSLKISTRLNL-LEQ 996
Cdd:pfam09726 531 IKKLTHDIKLKEEQIRELEIKVQELRKYKESEKDTEVLMSALSAMQDKNQHLEN------------SLSAETRIKLdLFS 598
|
250 260
....*....|....*....|....*....
gi 1034670647 997 ELSEKNVQLQTSTAEEKTKISEQVEVLQK 1025
Cdd:pfam09726 599 ALGDAKRQLEIAQGQIYQKDQEIKDLKQK 627
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
679-1024 |
3.82e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 679 LSDTQ---DETQKSDLENEDLKIDCLQESQEL-----NLQKLKNSEriLTEAKQKMRELTInikmkEDLIKELIKTGNDA 750
Cdd:PRK11281 65 LEQTLallDKIDRQKEETEQLKQQLAQAPAKLrqaqaELEALKDDN--DEETRETLSTLSL-----RQLESRLAQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 751 KSVSK---QYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAaklrvqvlqkkqqdskKL 827
Cdd:PRK11281 138 QNAQNdlaEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALRPSQRVLLQA----------------EQ 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 828 ASLSIQNEKRANELEQSVdhmkyqkiQLQRKLreeNEKRKQLDAVIKRDQQKIKEIQlktgqeeglkpkaedlDACNLKR 907
Cdd:PRK11281 202 ALLNAQNDLQRKSLEGNT--------QLQDLL---QKQRDYLTARIQRLEHQLQLLQ----------------EAINSKR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 908 RKGSfgsidhlqkldEQKkwldeeVEKVLNQRQELEELEADLKKREAIVskkeallqekshleNKKLrsSQALntdsLKI 987
Cdd:PRK11281 255 LTLS-----------EKT------VQEAQSQDEAARIQANPLVAQELEI--------------NLQL--SQRL----LKA 297
|
330 340 350
....*....|....*....|....*....|....*...
gi 1034670647 988 STRLN-LLEQELSEKNvQLQTSTAEEKTkISEQVEVLQ 1024
Cdd:PRK11281 298 TEKLNtLTQQNLRVKN-WLDRLTQSERN-IKEQISVLK 333
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
755-883 |
4.91e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 755 KQYSLKVTKLEHDA----EQAKVElIETQKQLQELENKDLSDvAMKVKLQKEFR-KKMDAAKLRVQVLQKKQQDSKKLAS 829
Cdd:PRK12704 27 KIAEAKIKEAEEEAkrilEEAKKE-AEAIKKEALLEAKEEIH-KLRNEFEKELReRRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034670647 830 LsiqnEKRANELEQsvdhmkyQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEI 883
Cdd:PRK12704 105 L----EKREEELEK-------KEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
682-1077 |
5.54e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 5.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 682 TQDETQKSDLENEDLKIDClqesqelNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGND------------ 749
Cdd:TIGR00618 431 KQQELQQRYAELCAAAITC-------TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVvlarllelqeep 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 750 ---AKSVSKQYSLKVTKLEHDAEQAKVE-LIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSK 825
Cdd:TIGR00618 504 cplCGSCIHPNPARQDIDNPGPLTRRMQrGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 826 KLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLK----TGQEEGLKPKAEDLD 901
Cdd:TIGR00618 584 EDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKltalHALQLTLTQERVREH 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 902 ACNLKRRKGSFGSIDHLQKLDEQKKW----------------LDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQE 965
Cdd:TIGR00618 664 ALSIRVLPKELLASRQLALQKMQSEKeqltywkemlaqcqtlLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 966 K------------SHLENKKLRSSQALNTDsLKISTRLNLLEQELSEKNVQLQTST-------AEEKTKISEQVEVLQKE 1026
Cdd:TIGR00618 744 SlkelmhqartvlKARTEAHFNNNEEVTAA-LQTGAELSHLAAEIQFFNRLREEDThllktleAEIGQEIPSDEDILNLQ 822
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1034670647 1027 KDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQ 1077
Cdd:TIGR00618 823 CETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQ 873
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
702-965 |
5.93e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 702 QESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELiktgndaksvsKQYSLKVTKLEHDAEQAKVELIETQKQ 781
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-----------EELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 782 LQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLRE 861
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 862 ENEKRKQLDAVIKRDQQKIKEIQLKtGQEEGLKPKAEDLDacNLKRRKGsfgsidhlqKLDEQKKwldeEVEKVLNQRQE 941
Cdd:PRK03918 659 EEYEELREEYLELSRELAGLRAELE-ELEKRREEIKKTLE--KLKEELE---------EREKAKK----ELEKLEKALER 722
|
250 260
....*....|....*....|....
gi 1034670647 942 LEELEADLKKREAIVskKEALLQE 965
Cdd:PRK03918 723 VEELREKVKKYKALL--KERALSK 744
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
918-1086 |
6.17e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 918 LQKLDEQKKWLDEEVEKVLNQ----RQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQA-----------LNT 982
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEynelQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRsggsvsyldvlLGS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 983 DSL-KISTRLNLLEQeLSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEG 1061
Cdd:COG3883 112 ESFsDFLDRLSALSK-IADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190
|
170 180
....*....|....*....|....*
gi 1034670647 1062 IEALEAAIEYRNESIQNRQKSLRAS 1086
Cdd:COG3883 191 EAAAEAQLAELEAELAAAEAAAAAA 215
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
813-1085 |
6.28e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 813 RVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKyqkiQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEG 892
Cdd:PRK02224 466 HVETIEEDRERVEELEAELEDLEEEVEEVEERLERAE----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 893 LKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENK 972
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAEL 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 973 KLRSSQALNTDSLKISTrlnlLEQELSEKNV---QLQTSTAEE-KTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLS 1048
Cdd:PRK02224 622 NDERRERLAEKRERKRE----LEAEFDEARIeeaREDKERAEEyLEQVEEKLDELREERDDLQAEIGAVENELEELEELR 697
|
250 260 270
....*....|....*....|....*....|....*..
gi 1034670647 1049 PEEEHvlfqLEEGIEALEAAIEyRNESIQNRQKSLRA 1085
Cdd:PRK02224 698 ERREA----LENRVEALEALYD-EAEELESMYGDLRA 729
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
678-883 |
9.92e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.04 E-value: 9.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 678 ELSDTQDETQKSDLE---NEDL--KIDCLQESQELNLQKLKNSERILTE----AKQKMRELTINIKMKEDLIKELIKTGN 748
Cdd:pfam17380 349 ELERIRQEERKRELErirQEEIamEISRMRELERLQMERQQKNERVRQEleaaRKVKILEEERQRKIQQQKVEMEQIRAE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 749 DAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSK--- 825
Cdd:pfam17380 429 QEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqam 508
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034670647 826 ----------------KLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAvIKRDQQKIKEI 883
Cdd:pfam17380 509 ieeerkrkllekemeeRQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEA-MEREREMMRQI 581
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
689-1240 |
1.01e-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: 47.02 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 689 SDLENEDLKIDCLQESQELNLQ----KLKNSERILTEAKQKMREL-----TINIKMKEDLI--KELIKTGNDA------- 750
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKqkenKLQENRKIIEAQRKAIQELqfeneKVSLKLEEEIQenKDLIKENNATrhlcnll 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 751 KSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQEL--------ENKDLSDVAMKVKLQ----------KEFRKKMDAAKL 812
Cdd:pfam05483 161 KETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMilafeelrVQAENARLEMHFKLKedhekiqhleEEYKKEINDKEK 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 813 RVQVL----QKKQQDSKKLASLSIQNEKRANELEQSV--------------DHMKYQ----KIQLQRKLREENEKRKQLD 870
Cdd:pfam05483 241 QVSLLliqiTEKENKMKDLTFLLEESRDKANQLEEKTklqdenlkeliekkDHLTKElediKMSLQRSMSTQKALEEDLQ 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 871 AVIKRDQQKIKEiqlKTGQEEGLKpKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLN-----QRQELEEL 945
Cdd:pfam05483 321 IATKTICQLTEE---KEAQMEELN-KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITmelqkKSSELEEM 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 946 -------EADLKKREAIVSKKEALLQEKSHLEnkklRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKtKISE 1018
Cdd:pfam05483 397 tkfknnkEVELEELKKILAEDEKLLDEKKQFE----KIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEE-HYLK 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1019 QVEVLQKEKDQlqkrrhnvdEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRN--ESIQNRQKS---LRASFHNLSRG 1093
Cdd:pfam05483 472 EVEDLKTELEK---------EKLKNIELTAHCDKLLLENKELTQEASDMTLELKKhqEDIINCKKQeerMLKQIENLEEK 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1094 EANVLEKLACLSPVEIRT---ILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDHLKLQCDRRLTLQQ 1170
Cdd:pfam05483 543 EMNLRDELESVREEFIQKgdeVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1171 KEHEQKMQLLLHHFKEQDGEGIMETFKtyedkiQQLEKDLYFYKKTSRDHKKKLKELVGEAIRRQLAPSE 1240
Cdd:pfam05483 623 KGSAENKQLNAYEIKVNKLELELASAK------QKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
703-976 |
1.50e-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: 46.27 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 703 ESQELNLQKLKNSERILTEAKQkmRELtinikmkedlikELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVElietqkql 782
Cdd:pfam17380 338 EQERMAMERERELERIRQEERK--REL------------ERIRQEEIAMEISRMRELERLQMERQQKNERVR-------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 783 QELEnkdlsdVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQR-KLRE 861
Cdd:pfam17380 396 QELE------AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERlRQQE 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 862 ENEKRKQLDAVI-KRDQQKIKEIQLKTGQEEGLKPKAEDLDACNlkRRKGSFGSIDHLQK--LDEQKKWLDEEVEKVLNQ 938
Cdd:pfam17380 470 EERKRKKLELEKeKRDRKRAEEQRRKILEKELEERKQAMIEEER--KRKLLEKEMEERQKaiYEEERRREAEEERRKQQE 547
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1034670647 939 RQELEELEADLKKREAIVSKKEALLQEKSHL----ENKKLRS 976
Cdd:pfam17380 548 MEERRRIQEQMRKATEERSRLEAMEREREMMrqivESEKARA 589
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
685-951 |
1.53e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 685 ETQKSDLENE-----------DLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSV 753
Cdd:TIGR04523 390 ESQINDLESKiqnqeklnqqkDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 754 SKQYSLKVTKLEHDAEQAKVELIETQKQLQEL--ENKDLSdvamkvKLQKEFRKKMDAAKLRVQVLQK-KQQDSKKLASL 830
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLneEKKELE------EKVKDLTKKISSLKEKIEKLESeKKEKESKISDL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 831 -----SIQNEKRANELEQSVDHM--KYQKIQLQRKLREENEKRKQLDAVIKRDQQK--IKEIQLKTGQEEGLKPKAEDLD 901
Cdd:TIGR04523 544 edelnKDDFELKKENLEKEIDEKnkEIEELKQTQKSLKKKQEEKQELIDQKEKEKKdlIKEIEEKEKKISSLEKELEKAK 623
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1034670647 902 ACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKK 951
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKT 673
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
726-1034 |
1.62e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 726 MRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRK 805
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 806 KMDAAKLRVQVLQKKQQDSKKLAslsiqneKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIkrdQQKIKEIQL 885
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLT-------QRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKL---QQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 886 KTGQEEGLKPKAEDLDACNLKRRKgsfgSIDHLQKLDEQKKWLDEEVEKVLNQRQELEE-LEADLKKREAIVSKKEALLQ 964
Cdd:pfam07888 190 LSKEFQELRNSLAQRDTQVLQLQD----TITTLTQKLTTAHRKEAENEALLEELRSLQErLNASERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034670647 965 EKSH----LENKKLRSSQAlntdSLKIS-TRLNLLEQE--LSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRR 1034
Cdd:pfam07888 266 QRDRtqaeLHQARLQAAQL----TLQLAdASLALREGRarWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEER 338
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
678-973 |
1.75e-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: 46.21 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 678 ELSDTQDETqkSDLENEdlkIDCLQESQELNLQKLKNSERILTEAKQkmrELTINIKMKEDLIKELiktgNDAKSVSKQY 757
Cdd:TIGR02169 710 ELSDASRKI--GEIEKE---IEQLEQEEEKLKERLEELEEDLSSLEQ---EIENVKSELKELEARI----EELEEDLHKL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 758 SLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKV---------------KLQKEFRKKMDAAKLRVQVLQKKQQ 822
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIeqklnrltlekeyleKEIQELQEQRIDLKEQIKSIEKEIE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 823 DSK-KLASLSIQNEKRANELEQ----------SVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEE 891
Cdd:TIGR02169 858 NLNgKKEELEEELEELEAALRDlesrlgdlkkERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 892 GLKPKAEDLDACNLKrrkgsfgsidhLQKLDEQKKWLDEEVEKV--LNQR--QELEELEADL----KKREAIVSKKEALL 963
Cdd:TIGR02169 938 DPKGEDEEIPEEELS-----------LEDVQAELQRVEEEIRALepVNMLaiQEYEEVLKRLdelkEKRAKLEEERKAIL 1006
|
330
....*....|
gi 1034670647 964 QEKSHLENKK 973
Cdd:TIGR02169 1007 ERIEEYEKKK 1016
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
676-1039 |
2.01e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 676 LVELSDTQDETQKSDLENEDlkIDCLQESQeLNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSK 755
Cdd:PTZ00121 1032 LTEYGNNDDVLKEKDIIDED--IDGNHEGK-AEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTET 1108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 756 QYSLKVTKLEHDAEQAK-VELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQvlqKKQQDSKKLASLSIQN 834
Cdd:PTZ00121 1109 GKAEEARKAEEAKKKAEdARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEA---RKAEDAKKAEAARKAE 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 835 E-KRANELEQSVDHMKYQKIQLQRKLREENEKR-----KQLDAVIKRDQQKIKEIQLKTGQEE---GLKPKAEDLDACNL 905
Cdd:PTZ00121 1186 EvRKAEELRKAEDARKAEAARKAEEERKAEEARkaedaKKAEAVKKAEEAKKDAEEAKKAEEErnnEEIRKFEEARMAHF 1265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 906 KRRKGSFGS-----IDHLQKLDEQKKWLD----EEVEKVLNQRQELEEL-EADLKKREAIVSKKEALLQEKSHLENKKLR 975
Cdd:PTZ00121 1266 ARRQAAIKAeearkADELKKAEEKKKADEakkaEEKKKADEAKKKAEEAkKADEAKKKAEEAKKKADAAKKKAEEAKKAA 1345
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034670647 976 SSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDE 1039
Cdd:PTZ00121 1346 EAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE 1409
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
761-1177 |
2.87e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 761 VTKLEHDAEQAKVELIETQKQLQELENKD----------LSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASL 830
Cdd:TIGR00606 697 ISDLQSKLRLAPDKLKSTESELKKKEKRRdemlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGT 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 831 SIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAV--IKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRR 908
Cdd:TIGR00606 777 IMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSdlDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQ 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 909 KgsfgSIDHLQKLDEQKKWLDEEVEKVLNQRQELEEleadlkKREAIVSKKEALLQEKSHLENKKLRSSQALntdslkis 988
Cdd:TIGR00606 857 E----QIQHLKSKTNELKSEKLQIGTNLQRRQQFEE------QLVELSTEVQSLIREIKDAKEQDSPLETFL-------- 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 989 trlnlleQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRvlspeeEHVLFQLEEGIEALEAA 1068
Cdd:TIGR00606 919 -------EKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGK------DDYLKQKETELNTVNAQ 985
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1069 I---EYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEirtilfryfnkvvNLREAERKQQLYNEEM-KMKVLER 1144
Cdd:TIGR00606 986 LeecEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKREN-------------ELKEVEEELKQHLKEMgQMQVLQM 1052
|
410 420 430
....*....|....*....|....*....|...
gi 1034670647 1145 DNMVRELESALDHLKLQCDRRLTLQQKEHEQKM 1177
Cdd:TIGR00606 1053 KQEHQKLEENIDLIKRNHVLALGRQKGYEKEIK 1085
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
710-890 |
3.88e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 710 QKLKNSERILTEAKQKMRELTINIkmkEDLIKELIKTGNDAKsvskQYSLKVTKLEHDAEQAKVELIETQKQLQELENKD 789
Cdd:PRK00409 495 KRLGLPENIIEEAKKLIGEDKEKL---NELIASLEELERELE----QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 790 LSdvamkvKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIqnekRANELEQSvdhmkyqkiqlQRKLREENEKRKQl 869
Cdd:PRK00409 568 LE------EAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASV----KAHELIEA-----------RKRLNKANEKKEK- 625
|
170 180
....*....|....*....|.
gi 1034670647 870 daviKRDQQKIKEIQLKTGQE 890
Cdd:PRK00409 626 ----KKKKQKEKQEELKVGDE 642
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
814-974 |
4.44e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 814 VQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQR--KLREENEKRKQLDAVIKRDQQKikeiqlktgqEE 891
Cdd:PRK12705 22 VVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERnqQRQEARREREELQREEERLVQK----------EE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 892 GLKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQRQE------LEELEADLKKREAIVSKKealLQE 965
Cdd:PRK12705 92 QLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLTPEqarkllLKLLDAELEEEKAQRVKK---IEE 168
|
....*....
gi 1034670647 966 KSHLENKKL 974
Cdd:PRK12705 169 EADLEAERK 177
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
678-1032 |
5.17e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 678 ELSDTQDETQKSDLENEDLKIDCLQESQELNLQK--LKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSK 755
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 756 QYSLKVTKLEHDAEQAKVELIETQKQLQELenkdlsdvamkvklqkefRKKMDAAKLRVQVLQKKQQdskklaslsiQNE 835
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDEL------------------RAELTLLNEEAANLRERLE----------SLE 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 836 KRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQ-LKTGQEEGLKPKAEDLDACNLKRRKGSfgs 914
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLnERASLEEALALLRSELEELSEELRELE--- 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 915 iDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKkrEAIVSKKEALLQEKSHLENKKLrssqalnTDSLKISTRLNLL 994
Cdd:TIGR02168 908 -SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ--ERLSEEYSLTLEEAEALENKIE-------DDEEEARRRLKRL 977
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1034670647 995 EQELSE-KNVQLQT-----STAEEKTKISEQVEVLQKEKDQLQK 1032
Cdd:TIGR02168 978 ENKIKElGPVNLAAieeyeELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
755-1051 |
6.16e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 755 KQYSLKVTKLEHDAEQAKVELIETQKQLQELENKdlsdvamKVKLQKEFRKKMDAAKlrvQVLQKKQQDSKKLASLSiqn 834
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEK-------RDELNAQVKELREEAQ---ELREKRDELNEKVKELK--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 835 EKRaNELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQ---LKTGQEEGLKPKAEDLDAcnlkrrkgs 911
Cdd:COG1340 78 EER-DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQtevLSPEEEKELVEKIKELEK--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 912 fgSIDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKK-REAIVSKKEALLQEKSHLENKKlRSSQALNTDSLKISTR 990
Cdd:COG1340 148 --ELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKElAEEAQELHEEMIELYKEADELR-KEADELHKEIVEAQEK 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034670647 991 LNLLEQELSEKNVQLQtSTAEEKTKISEQVEVLQKEKDQ--LQKRRHNVDEKLKNGRVLSPEE 1051
Cdd:COG1340 225 ADELHEEIIELQKELR-ELRKELKKLRKKQRALKREKEKeeLEEKAEEIFEKLKKGEKLTTEE 286
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
609-1085 |
6.98e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 44.44 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 609 PMYSLDRIFAG-------FRTRSQMLLGHIEEqdkvlhcqfsDNSDDEESEGQeksgtRCRSRSWIQKPDSvcslveLSD 681
Cdd:pfam12128 177 PLRHIDKIAKAmhskegkFRDVKSMIVAILED----------DGVVPPKSRLN-----RQQVEHWIRDIQA------IAG 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 682 TQDETQKSDLENEDLKIdclQESQELNLQKLK--------NSERILTEAKQKMRELTINIKMKEDLIKELIKTGN----- 748
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNT---LESAELRLSHLHfgyksdetLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNgelsa 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 749 -DAKSVSKQYSLKVTKLEH------DAEQAKVEL-----IETQKQLQELENKDLSDVAMKVklQKEFRKKMDAAKLR--- 813
Cdd:pfam12128 313 aDAAVAKDRSELEALEDQHgafldaDIETAAADQeqlpsWQSELENLEERLKALTGKHQDV--TAKYNRRRSKIKEQnnr 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 814 -VQVLQKKQQDSKKLASLSIQNEKRANE-LEQSVDHMKYQKI------QLQRKLREENEKRKQLDAVIKRD---QQKIKE 882
Cdd:pfam12128 391 dIAGIKDKLAKIREARDRQLAVAEDDLQaLESELREQLEAGKlefneeEYRLKSRLGELKLRLNQATATPElllQLENFD 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 883 IQLKTGQEEGLKPKAEDLDACNLKRRKGSfgsidhlqKLDEQKKWLDEEVEKVLNQRQELEELE---------------- 946
Cdd:pfam12128 471 ERIERAREEQEAANAEVERLQSELRQARK--------RRDQASEALRQASRRLEERQSALDELElqlfpqagtllhflrk 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 947 --ADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKIS-TRLNL-----LEQELSEKNVQLQTS--TAEEKTK- 1015
Cdd:pfam12128 543 eaPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDlKRIDVpewaaSEEELRERLDKAEEAlqSAREKQAa 622
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034670647 1016 ISEQVEVLQKEKDQLQKRRHNVDEKLKNGRV----LSPEEEHVLFQLEegiEALEAAIEYRNESIQNRQKSLRA 1085
Cdd:pfam12128 623 AEEQLVQANGELEKASREETFARTALKNARLdlrrLFDEKQSEKDKKN---KALAERKDSANERLNSLEAQLKQ 693
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
857-1220 |
8.66e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 43.74 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 857 RKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRrkGSFGSIDHLQKLDEQKkwlDEEVEKVL 936
Cdd:PLN02939 38 RRRGFSSQQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRTVMELPQ--KSTSSDDDHNRASMQR---DEAIAAID 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 937 NQRQE------------LEELEADLKKREA-IVSKKEALLQEKSHLEnKKLRSSQALNTdslkistRLNLLEQELSEKNV 1003
Cdd:PLN02939 113 NEQQTnskdgeqlsdfqLEDLVGMIQNAEKnILLLNQARLQALEDLE-KILTEKEALQG-------KINILEMRLSETDA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1004 QLQTStAEEKTkiseQVEVLQkekDQLQKRRHNVDEK--LKNGRVLSPEEEHVLFQLE-----EGIEALEAAI------E 1070
Cdd:PLN02939 185 RIKLA-AQEKI----HVEILE---EQLEKLRNELLIRgaTEGLCVHSLSKELDVLKEEnmllkDDIQFLKAELievaetE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1071 YRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIRTilfrYFNKVVNLREAERKQQLYNEEMKMkVLERD----N 1146
Cdd:PLN02939 257 ERVFKLEKERSLLDASLRELESKFIVAQEDVSKLSPLQYDC----WWEKVENLQDLLDRATNQVEKAAL-VLDQNqdlrD 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1147 MVRELESALDHLKLQ--CDRRLTLQQkeheQKMQLLLHHFKEQDGEgIMETFKTYEDKIQQ----LEKDLYFYKKTSRDH 1220
Cdd:PLN02939 332 KVDKLEASLKEANVSkfSSYKVELLQ----QKLKLLEERLQASDHE-IHSYIQLYQESIKEfqdtLSKLKEESKKRSLEH 406
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
706-1049 |
9.81e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.88 E-value: 9.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 706 ELNLQKLKNSERILTEAKQKmrELTINIKMKEDLIKELIKTGNDakSVSKQYSLKVTKLEhdaeqakvelIETQKQLQEL 785
Cdd:PTZ00108 1005 ERELARLSNKVRFIKHVING--ELVITNAKKKDLVKELKKLGYV--RFKDIIKKKSEKIT----------AEEEEGAEED 1070
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 786 ENKDLSDVAMKVKLQKEF----RKKM------DAAKLRVQvLQKKQQDSKKLASLSIQNEKRAnELEqsvdhmkyqkiQL 855
Cdd:PTZ00108 1071 DEADDEDDEEELGAAVSYdyllSMPIwsltkeKVEKLNAE-LEKKEKELEKLKNTTPKDMWLE-DLD-----------KF 1137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 856 QRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKV 935
Cdd:PTZ00108 1138 EEALEEQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKKKEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKK 1217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 936 LNQRQELEELEADLKKREAIVSKKEALLQEKShLENKKLRSSQALNTDSLKISTRLNLLEQELSEKNVQLQTSTA---EE 1012
Cdd:PTZ00108 1218 SNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNN-SSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRpdgES 1296
|
330 340 350
....*....|....*....|....*....|....*..
gi 1034670647 1013 KTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSP 1049
Cdd:PTZ00108 1297 NGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKKTAR 1333
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
726-863 |
1.04e-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: 43.11 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 726 MRELTINIKMKEDLIKELIKTGNDA-----------KSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVA 794
Cdd:smart00435 233 LQEQLKELTAKDGNVAEKILAYNRAnrevailcnhqRTVSKTHEKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRK 312
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034670647 795 MKVKLQKEFRkkmdaaKLRVQVLQKKQQDSKKLASlsiqnEKRANELEQSVdhmkyQKIQLQRKLREEN 863
Cdd:smart00435 313 LKSKFERDNE------KLDAEVKEKKKEKKKEEKK-----KKQIERLEERI-----EKLEVQATDKEEN 365
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
688-1188 |
1.07e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.66 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 688 KSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHD 767
Cdd:pfam10174 218 RNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 768 AEQAKVELIETQKQLQELENKDlSDVAMKVKLQKE-----------FRKKMDAAKLRV----QVLQKKQqdsKKLASLSI 832
Cdd:pfam10174 298 LSKKESELLALQTKLETLTNQN-SDCKQHIEVLKEsltakeqraaiLQTEVDALRLRLeekeSFLNKKT---KQLQDLTE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 833 QNEKRANELEQSVDHM--KYQKIQ-LQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDldACNLKRRK 909
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLdvKERKINvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEE--ALSEKERI 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 910 gsfgsidhLQKLDEQKKWLDEEvekvlnQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKIST 989
Cdd:pfam10174 452 --------IERLKEQREREDRE------RLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDS 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 990 RLNLLEQELSEK------------NVQLQTSTAEEKTKISEQVEVLQKE----KDQLQKRRHNVDEKLKNGRvlspEEEH 1053
Cdd:pfam10174 518 KLKSLEIAVEQKkeecsklenqlkKAHNAEEAVRTNPEINDRIRLLEQEvaryKEESGKAQAEVERLLGILR----EVEN 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1054 VLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIRTILFRYFNKVVNLREaERKQQLy 1133
Cdd:pfam10174 594 EKNDKDKKIAELESLTLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALE-KTRQEL- 671
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1034670647 1134 nEEMKMKVLERDNMVRELESALDhlKLQCDRRLTLQQKeHEQKMQLLLHHFKEQD 1188
Cdd:pfam10174 672 -DATKARLSSTQQSLAEKDGHLT--NLRAERRKQLEEI-LEMKQEALLAAISEKD 722
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
737-979 |
1.32e-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: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 737 EDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKdlSDVAMK--VKLQKEFRKKMDAAKLRV 814
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAE--IDKLQAeiAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 815 QVLQKKQQDSKKLASLSiqnekRANELEQSVDHMKYqkiqlqrklreenekrkqLDAVIKRDQQKIKEIQLKTGQEEGLK 894
Cdd:COG3883 93 RALYRSGGSVSYLDVLL-----GSESFSDFLDRLSA------------------LSKIADADADLLEELKADKAELEAKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 895 PKAEDLdacnlkrrkgsfgsidhLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHLENKKL 974
Cdd:COG3883 150 AELEAK-----------------LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
....*
gi 1034670647 975 RSSQA 979
Cdd:COG3883 213 AAAAA 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
926-1135 |
1.62e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.08 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 926 KWLDEEVEKVlnqRQELEELEADL---KKREAIVS---KKEALLQEKSHLENKKlrssQALNTDSLKISTRLNLLEQELS 999
Cdd:COG3206 178 EFLEEQLPEL---RKELEEAEAALeefRQKNGLVDlseEAKLLLQQLSELESQL----AEARAELAEAEARLAALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1000 EKNVQL-QTSTAEEKTKISEQVEVLQKEKDQLQKR---RH----NVDEKLKNGRVlspeeehvlfQLEEGIEALEAAIEY 1071
Cdd:COG3206 251 SGPDALpELLQSPVIQQLRAQLAELEAELAELSARytpNHpdviALRAQIAALRA----------QLQQEAQRILASLEA 320
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034670647 1072 RNESIQNRQKSLRASFHNLsRGEANVLEKLAclspVEIRTILfryfnkvvnlREAERKQQLYNE 1135
Cdd:COG3206 321 ELEALQAREASLQAQLAQL-EARLAELPELE----AELRRLE----------REVEVARELYES 369
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
759-971 |
1.88e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 759 LKVTKLEHDAEQAKvELIETQKQLQELENKdLSDVamkVKLQKEFRKKMDAAKLRVQVLQKKQQDskkLASLSIQNEKRA 838
Cdd:PRK02224 489 EEVEEVEERLERAE-DLVEAEDRIERLEER-REDL---EELIAERRETIEEKRERAEELRERAAE---LEAEAEEKREAA 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 839 NELEQSVDHMKYQKIQLQRKLREENEKRKQLDAV-------------IKRDQQKIKEIQLKTGQE-EGLKPK-------A 897
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESLERIrtllaaiadaedeIERLREKREALAELNDERrERLAEKrerkrelE 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 898 EDLDACNL---KRRKGSFGSI-----DHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALLQEKSHL 969
Cdd:PRK02224 641 AEFDEARIeeaREDKERAEEYleqveEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEALYDEAEEL 720
|
..
gi 1034670647 970 EN 971
Cdd:PRK02224 721 ES 722
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
829-1179 |
1.90e-03 |
|
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: 43.04 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 829 SLSIQNEKRANELEQ--SVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDACNLK 906
Cdd:pfam02463 146 IIAMMKPERRLEIEEeaAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEY 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 907 RRKgsfgsidhLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIvskkealLQEKSHLENKKLRSSQALNTDSLK 986
Cdd:pfam02463 226 LLY--------LDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEK-------LAQVLKENKEEEKEKKLQEEELKL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 987 ISTRLNLLEQELSEKNVQlqtstaeeKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALE 1066
Cdd:pfam02463 291 LAKEEEELKSELLKLERR--------KVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1067 AAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLSPVEIrtilfryfNKVVNLREAERKQQLYNEEMKMKVLERDN 1146
Cdd:pfam02463 363 KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK--------EAQLLLELARQLEDLLKEEKKEELEILEE 434
|
330 340 350
....*....|....*....|....*....|...
gi 1034670647 1147 MVRELESALDHLKLQCDRRLTLQQKEHEQKMQL 1179
Cdd:pfam02463 435 EEESIELKQGKLTEEKEELEKQELKLLKDELEL 467
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
933-1025 |
2.14e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 933 EKVLNQRQEL----EELEADLKKREAIVSKKEA-LLQEKSHLENKklrsSQALNtdslKISTRLNLLEQELSEKNVQLQT 1007
Cdd:PRK12704 57 EALLEAKEEIhklrNEFEKELRERRNELQKLEKrLLQKEENLDRK----LELLE----KREEELEKKEKELEQKQQELEK 128
|
90
....*....|....*...
gi 1034670647 1008 STAEEKTKISEQVEVLQK 1025
Cdd:PRK12704 129 KEEELEELIEEQLQELER 146
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
773-1133 |
2.43e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.64 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 773 VELIETQKQLQELENKdLSDVAMKVKLQkefRKKMDAAKLRVQVLQKKQQDSKKLASLSIQneKRANELEQSVDHMKYQK 852
Cdd:PRK04863 837 AELRQLNRRRVELERA-LADHESQEQQQ---RSQLEQAKEGLSALNRLLPRLNLLADETLA--DRVEEIREQLDEAEEAK 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 853 IQLQRKLREENEKRKQLdAVIKRDQQKIKEI-----QLKTGQEEgLKPKAEDLDacNLKRRKGSFGSIDHLQKLDEQkkw 927
Cdd:PRK04863 911 RFVQQHGNALAQLEPIV-SVLQSDPEQFEQLkqdyqQAQQTQRD-AKQQAFALT--EVVQRRAHFSYEDAAEMLAKN--- 983
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 928 lDEEVEKVlnqRQELEELEADLkkREAivskKEALLQEKSHLENK-----KLRSSQALNTDSLKistrlnLLEQELSEKN 1002
Cdd:PRK04863 984 -SDLNEKL---RQRLEQAEQER--TRA----REQLRQAQAQLAQYnqvlaSLKSSYDAKRQMLQ------ELKQELQDLG 1047
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1003 VQLqTSTAEEKT-----KISEQVEVLQKEKDQLQKRRHNVDEKLKN--GRVLSPEEEhvLFQLEEGIEALEAAIeyrnes 1075
Cdd:PRK04863 1048 VPA-DSGAEERArarrdELHARLSANRSRRNQLEKQLTFCEAEMDNltKKLRKLERD--YHEMREQVVNAKAGW------ 1118
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1076 iqnrQKSLRASFHN-----LSRGEanvlekLACLSPVEIRTI------LFRY-------FNKVVNLRE----AERKQQLY 1133
Cdd:PRK04863 1119 ----CAVLRLVKDNgverrLHRRE------LAYLSADELRSMsdkalgALRLavadnehLRDVLRLSEdpkrPERKVQFY 1188
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
641-1187 |
2.71e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 641 QFSDNSDDEESEGQEKSGTRCRSRSWIQKPDSVCSLVELSDTQDETQKSDLEnedLKIDCLQE-SQELNLQKLKNSERIL 719
Cdd:TIGR00606 302 QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQ---LQADRHQEhIRARDSLIQSLATRLE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 720 TEAKQKMRELTINIKMKEDLIKEliKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKL 799
Cdd:TIGR00606 379 LDGFERGPFSERQIKNFHTLVIE--RQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEEL 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 800 QKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANE-LEQSVDHMKYQKIQLQRKLREENEKRKQLD-------- 870
Cdd:TIGR00606 457 KFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTEtLKKEVKSLQNEKADLDRKLRKLDQEMEQLNhhtttrtq 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 871 -AVIKRDQ----QKIKEIQLKTGQE----EGLKPKAEDLDACNLKRRKGSFGSIDHL-------QKLDEQKKWLDEEVEK 934
Cdd:TIGR00606 537 mEMLTKDKmdkdEQIRKIKSRHSDEltslLGYFPNKKQLEDWLHSKSKEINQTRDRLaklnkelASLEQNKNHINNELES 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 935 VLNQRQELEE----------LEADL---KKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSLKISTRLNLLEQELSEK 1001
Cdd:TIGR00606 617 KEEQLSSYEDklfdvcgsqdEESDLerlKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEF 696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1002 NVQLQTSTAEEKTKISEqvevLQKEKDQLQKRRhnvDEKLkngrVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQK 1081
Cdd:TIGR00606 697 ISDLQSKLRLAPDKLKS----TESELKKKEKRR---DEML----GLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKN 765
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1082 SLRASFHNLsrGEANVLEKLA--CLSPVEIRTILFRYFnKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDHL- 1158
Cdd:TIGR00606 766 DIEEQETLL--GTIMPEEESAkvCLTDVTIMERFQMEL-KDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVv 842
|
570 580 590
....*....|....*....|....*....|
gi 1034670647 1159 -KLQCDRRLTLQQKEHEQKMQLLLHHFKEQ 1187
Cdd:TIGR00606 843 sKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
743-1066 |
2.95e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 42.04 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 743 LIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELEnKDLSDVAMK-VKLQKEFRKKMDAAKLRVQ----VL 817
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQ-KRIRLLEKReAEAEEALREQAELNRLKKKyleaLN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 818 QKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKA 897
Cdd:pfam05557 90 KKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 898 EDL------------DACNLKRRKGSFGSIDHLQK----LDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEA 961
Cdd:pfam05557 170 QRIkelefeiqsqeqDSEIVKNSKSELARIPELEKelerLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAAT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 962 LLQEKSHLEnKKLRSSQALNTDslkisTRLNLLEQE-LSEKNVQLQtstaEEKTKISEQVEVLQKEKDQLQKRRHNVDEK 1040
Cdd:pfam05557 250 LELEKEKLE-QELQSWVKLAQD-----TGLNLRSPEdLSRRIEQLQ----QREIVLKEENSSLTSSARQLEKARRELEQE 319
|
330 340
....*....|....*....|....*.
gi 1034670647 1041 LKNGRVLSPEEEHVLFQLEEGIEALE 1066
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRHKALVRRLQ 345
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
689-884 |
2.97e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 689 SDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKtgndaksvskqyslKVTKLEHDA 768
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA--------------EIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 769 EQAKVELIETQKQLQE-----------LENKDLSDVAMKVKLQKEFrkkMDAAKlrvQVLQKKQQDSKKLASLSIQNEKR 837
Cdd:COG3883 82 EERREELGERARALYRsggsvsyldvlLGSESFSDFLDRLSALSKI---ADADA---DLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034670647 838 ANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQ 884
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELE 202
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
933-1076 |
3.17e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.69 E-value: 3.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 933 EKVLNQRQELEELEADL----KKREAIVSKKEALLQEKShlENKKLRSSqalntdslkistrlnlLEQELSEKNVQLQTs 1008
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRileeAKKEAEAIKKEALLEAKE--EIHKLRNE----------------FEKELRERRNELQK- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034670647 1009 tAEEKTK-----ISEQVEVLQKEKDQLQKRRHNVDEKLKNgrvlspeeehvLFQLEEGIEALEAAIEYRNESI 1076
Cdd:PRK12704 87 -LEKRLLqkeenLDRKLELLEKREEELEKKEKELEQKQQE-----------LEKKEEELEELIEEQLQELERI 147
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
772-1031 |
3.39e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.84 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 772 KVELI-------ETQKQLQEL---ENKDLSDVAMKVKLQKEFRKKMDAAKLrvqvLQKKQQDSKKLASL-SIQNEKRANE 840
Cdd:PRK05771 8 KVLIVtlksykdEVLEALHELgvvHIEDLKEELSNERLRKLRSLLTKLSEA----LDKLRSYLPKLNPLrEEKKKVSVKS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 841 LEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEiqlktgqeegLKP-KAEDLDACNLKRRKGS---FGSID 916
Cdd:PRK05771 84 LEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIER----------LEPwGNFDLDLSLLLGFKYVsvfVGTVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 917 HlQKLDEQKKWLDEEVEKVLNQRQELEELEA-DLKKREAIVSK--KEALLQEKSHLENKKLrsSQALNtdslKISTRLNL 993
Cdd:PRK05771 154 E-DKLEELKLESDVENVEYISTDKGYVYVVVvVLKELSDEVEEelKKLGFERLELEEEGTP--SELIR----EIKEELEE 226
|
250 260 270
....*....|....*....|....*....|....*...
gi 1034670647 994 LEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQ 1031
Cdd:PRK05771 227 IEKERESLLEELKELAKKYLEELLALYEYLEIELERAE 264
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
862-1178 |
3.40e-03 |
|
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: 42.03 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 862 ENEKRKQLDAVIKRdQQKIKEIQ----LKTGQEEGLKPKAEDLDACNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLN 937
Cdd:pfam17380 267 ENEFLNQLLHIVQH-QKAVSERQqqekFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 938 QRQELEELEADLKKREaivskKEALLQEKSHLENKKLRssqalntdslkistRLNLLEQELSEKNvqlqtstaeekTKIS 1017
Cdd:pfam17380 346 RERELERIRQEERKRE-----LERIRQEEIAMEISRMR--------------ELERLQMERQQKN-----------ERVR 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1018 EQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVlfqLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANV 1097
Cdd:pfam17380 396 QELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEA---RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1098 LEKLACLSPVEIRTILFRYFNKVVNLRE-AERKQQLYNEEMKMKVLErdnmvRELESALDHLKLQCDRRLTLQQKEHEQK 1176
Cdd:pfam17380 473 KRKKLELEKEKRDRKRAEEQRRKILEKElEERKQAMIEEERKRKLLE-----KEMEERQKAIYEEERRREAEEERRKQQE 547
|
..
gi 1034670647 1177 MQ 1178
Cdd:pfam17380 548 ME 549
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
678-1057 |
3.49e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 41.65 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 678 ELSDTQDETQKSDLE--NEDLKIDCLQESQELNLQKLKNSERI----------LTEAKQKMRELTINIKMKEDLIKELIK 745
Cdd:pfam05557 112 ELSELRRQIQRAELElqSTNSELEELQERLDLLKAKASEAEQLrqnlekqqssLAEAEQRIKELEFEIQSQEQDSEIVKN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 746 TGNDAKSVSKQYSLKVTKLEH---------DAEQAKVELIETQKQLQELENKDLSDVAMKVKLQK--------------- 801
Cdd:pfam05557 192 SKSELARIPELEKELERLREHnkhlnenieNKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKleqelqswvklaqdt 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 802 --EFRKKMDAAKLRVQVLQKKQQDSKKLASLsiqnEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQK 879
Cdd:pfam05557 272 glNLRSPEDLSRRIEQLQQREIVLKEENSSL----TSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRR 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 880 I----KEIQlktGQEEGLKPKAEDLDACN-----LKRRKGSFGSIDHLQ-KLDEQKKWLDEEVEKVLNQRQELEELEADL 949
Cdd:pfam05557 348 VllltKERD---GYRAILESYDKELTMSNyspqlLERIEEAEDMTQKMQaHNEEMEAQLSVAEEELGGYKQQAQTLEREL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 950 KKREAIVSKKEA---------LLQEKSHL--ENKKLRSSqalntdslKISTRLNLLEQEL-------SEKNVQLQ---TS 1008
Cdd:pfam05557 425 QALRQQESLADPsyskeevdsLRRKLETLelERQRLREQ--------KNELEMELERRCLqgdydpkKTKVLHLSmnpAA 496
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1034670647 1009 TAEEKTKisEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQ 1057
Cdd:pfam05557 497 EAYQQRK--NQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFK 543
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
723-951 |
3.95e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 723 KQKMRELTINIK---MKEDLIKELIKTGND----AKSVSKQ----YSLKVTKLEHDAEQAKVELIETQKQLQEL--ENKD 789
Cdd:PHA02562 173 KDKIRELNQQIQtldMKIDHIQQQIKTYNKnieeQRKKNGEniarKQNKYDELVEEAKTIKAEIEELTDELLNLvmDIED 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 790 LSDVAMKVKlQKEFRKKMDAAKL-RVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQ 868
Cdd:PHA02562 253 PSAALNKLN-TAAAKIKSKIEQFqKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 869 LDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDLDAcnlkrrkgsfgsidHLQKLDEQKKWLDEEVEKVLNQRQELEELEAD 948
Cdd:PHA02562 332 FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKA--------------AIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
...
gi 1034670647 949 LKK 951
Cdd:PHA02562 398 LVK 400
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
812-965 |
4.55e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 812 LRVQVLQKKQQDSKKLASLSIQN-EKRANEL-EQSVDHMKYQKIQLQRKL-REENEKRKQLDAVIKRDQQKikeiqlktg 888
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEaKKEAEAIkKEALLEAKEEIHKLRNEFeKELRERRNELQKLEKRLLQK--------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 889 qEEGLKPKAEDLDacnlKRRK---GSFGSIDHLQK-LDEQKKWLDEEVEKvlnQRQELEELeADLKKREAivskKEALLQ 964
Cdd:PRK12704 95 -EENLDRKLELLE----KREEeleKKEKELEQKQQeLEKKEEELEELIEE---QLQELERI-SGLTAEEA----KEILLE 161
|
.
gi 1034670647 965 E 965
Cdd:PRK12704 162 K 162
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
673-1059 |
5.51e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.19 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 673 VCSLVELSDTQDETQKSDLENEDLKIDCLQESQELNLQKL-KNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAK 751
Cdd:TIGR00606 682 VCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKeKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQ 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 752 SVSKQYSLKVTKLEH-DAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASL 830
Cdd:TIGR00606 762 RLKNDIEEQETLLGTiMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTV 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 831 SIQNE----------KRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLKTGQEEGLKPKAEDL 900
Cdd:TIGR00606 842 VSKIElnrkliqdqqEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKD 921
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 901 dacnLKRRKGSFGSIDHLQKLDEQK-KWLDEEVEKVLNQRQELEELEAD-----LKKREAIVSKKEALLQE-KSHLE--N 971
Cdd:TIGR00606 922 ----QQEKEELISSKETSNKKAQDKvNDIKEKVKNIHGYMKDIENKIQDgkddyLKQKETELNTVNAQLEEcEKHQEkiN 997
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 972 KKLRSSQAlNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISE--QVEVLQkEKDQLQKRRHNVD-----EKLKNG 1044
Cdd:TIGR00606 998 EDMRLMRQ-DIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEmgQMQVLQ-MKQEHQKLEENIDlikrnHVLALG 1075
|
410
....*....|....*
gi 1034670647 1045 RVLSPEEEHVLFQLE 1059
Cdd:TIGR00606 1076 RQKGYEKEIKHFKKE 1090
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
707-884 |
5.98e-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: 39.91 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 707 LNLQKLKNSeriLTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELE 786
Cdd:COG1579 10 LDLQELDSE---LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 787 N-KDLSDvamkvkLQKEfrkkMDAAKLRVQVLQKKQqdskklaslsIQNEKRANELEQSVDHMKYQKIQLQRKLreeNEK 865
Cdd:COG1579 87 NnKEYEA------LQKE----IESLKRRISDLEDEI----------LELMERIEELEEELAELEAELAELEAEL---EEK 143
|
170
....*....|....*....
gi 1034670647 866 RKQLDAVIKRDQQKIKEIQ 884
Cdd:COG1579 144 KAELDEELAELEAELEELE 162
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
678-1208 |
6.50e-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: 41.19 E-value: 6.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 678 ELSDTQDETQ----KSDLENEDLKIDCLQ-ESQELNLQKLKNSerilteaKQKMRELTINIK--MKEDLIKELIKTGNDA 750
Cdd:TIGR01612 688 AIDNTEDKAKlddlKSKIDKEYDKIQNMEtATVELHLSNIENK-------KNELLDIIVEIKkhIHGEINKDLNKILEDF 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 751 KSVSKQYSLKVtkleHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASl 830
Cdd:TIGR01612 761 KNKEKELSNKI----NDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIIN- 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 831 SIQNEKraNELEQSVDhmKYqkIQLQRKLREE-NEKRKQLDAVIKRDQQKIKEIQLKtgqeeglkpkaedldacnlkrrk 909
Cdd:TIGR01612 836 EMKFMK--DDFLNKVD--KF--INFENNCKEKiDSEHEQFAELTNKIKAEISDDKLN----------------------- 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 910 gsfgsiDHLQKLDEQKKWLDEEVEKVLNQRQELEELEADLKKREAIVSKKEALlqEKSHLENKKLRSSQALNTDSLKISt 989
Cdd:TIGR01612 887 ------DYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKICENTKESI--EKFHNKQNILKEILNKNIDTIKES- 957
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 990 rlNLLEQELSEK--NVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKngrvlSPEEEHVLFQLEEGIEA--- 1064
Cdd:TIGR01612 958 --NLIEKSYKDKfdNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANLG-----KNKENMLYHQFDEKEKAtnd 1030
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 1065 LEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEK-LACLSpveiRTILFRYFNKVVNLREAERKQQLYN--EEMKMKV 1141
Cdd:TIGR01612 1031 IEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKnIELLN----KEILEEAEINITNFNEIKEKLKHYNfdDFGKEEN 1106
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034670647 1142 LERDNMVRELESALDHLKLQCDRRLTlQQKEHEQKMQLLLHHFKEQ--DGEGIMETfKTYEDKIQQLEK 1208
Cdd:TIGR01612 1107 IKYADEINKIKDDIKNLDQKIDHHIK-ALEEIKKKSENYIDEIKAQinDLEDVADK-AISNDDPEEIEK 1173
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
790-1086 |
6.83e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.77 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 790 LSDVAMKVKLQKEFRKKMDAAKLRVQVLQK----KQQDSKKLASLSIQNE------KRANELEQSvdhmkYQKIQLQRKL 859
Cdd:COG3206 96 LERVVDKLNLDEDPLGEEASREAAIERLRKnltvEPVKGSNVIEISYTSPdpelaaAVANALAEA-----YLEQNLELRR 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 860 REENEKRKQLDAVIKRDQQKIKEIQLKtgqeegLKpkaedldacNLKRRKGSFGSIDHLQKLDEQKKWLDEEVEKVLNQR 939
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELEEAEAA------LE---------EFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 940 QELEELEADLKKREAIVSKKEALLQEKSHLENKKLRSSQaLNTDSLKISTRLN-------LLEQELSEKNVQLQTSTAEE 1012
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAE-LEAELAELSARYTpnhpdviALRAQIAALRAQLQQEAQRI 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034670647 1013 KTKISEQVEVLQKEKDQLQKRRHNVDEKLKNgrvlSPEEEHVLFQLEEGIEALEAAieYrnESIQNRQKSLRAS 1086
Cdd:COG3206 315 LASLEAELEALQAREASLQAQLAQLEARLAE----LPELEAELRRLEREVEVAREL--Y--ESLLQRLEEARLA 380
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
688-1104 |
9.74e-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: 40.59 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 688 KSDLENEDLKIDCLQESQELNLQKLKNSERIlteakQKMRE-LTINIKMKEDLIKELIKtgndAKSVSKQYSLKVTKLEH 766
Cdd:pfam12128 443 KSRLGELKLRLNQATATPELLLQLENFDERI-----ERAREeQEAANAEVERLQSELRQ----ARKRRDQASEALRQASR 513
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 767 DAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQ------VLQKKQQDSKKLASLSIQNEK-RAN 839
Cdd:pfam12128 514 RLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRtdldpeVWDGSVGGELNLYGVKLDLKRiDVP 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 840 ELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKEIQLK-TGQEEGLKPKAEDL-----------DACN--L 905
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREeTFARTALKNARLDLrrlfdekqsekDKKNkaL 673
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 906 KRRKGSFGsiDHLQKLDEQKKWLDEEVEKVLNQRQEleeleadlKKREAIVSKKEALLQEKSHLENKKLRSSQALNTDSL 985
Cdd:pfam12128 674 AERKDSAN--ERLNSLEAQLKQLDKKHQAWLEEQKE--------QKREARTEKQAYWQVVEGALDAQLALLKAAIAARRS 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034670647 986 KISTRLNLLEQ----ELSEKNVQLQTStaeekTKISEQVEVLQKEKDQLQKRRHNVDE----------KLKNGRVLSPEE 1051
Cdd:pfam12128 744 GAKAELKALETwykrDLASLGVDPDVI-----AKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwlQRRPRLATQLSN 818
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034670647 1052 -EHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLS---RGEANVLEKLACL 1104
Cdd:pfam12128 819 iERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSenlRGLRCEMSKLATL 875
|
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