|
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: 600.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 4 IPVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:cd01372 1 SSVRVAVRVRPLLPKEIIEGCRICVSFVPGEPQVTVGTDKSFTFDYVFDPSTEQEEVYNTCVAPLVDGLFEGYNATVLAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 84 GQTGSGKTYTIGGGHIASVVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELET-SMKDLHIRED 161
Cdd:cd01372 81 GQTGSGKTYTMGTAYTAEEDEEQVGIIPRAIQHIFKKIEKKKDtFEFQLKVSFLEIYNEEIRDLLDPETdKKPTISIRED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEDGSWYSPRHIVSKFH 241
Cdd:cd01372 161 SKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQTKKNGPIAPMSADDKNSTFTSKFH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 242 FVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPS 321
Cdd:cd01372 241 FVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISALGDESKKGAHVPYRDSKLTRLLQDSLGGNSHTLMIACVSPA 320
|
330 340
....*....|....*....|.
gi 429535824 322 SSNFDESLNSLKYANRARNIR 342
Cdd:cd01372 321 DSNFEETLNTLKYANRARNIK 341
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
5-348 |
4.19e-146 |
|
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: 445.48 E-value: 4.19e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII-------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:smart00129 1 NIRVVVRVRPLNKREKSRKSPSVVPFPDKVGKTLTvrspknrQGEKKFTFDKVFDATASQEDVFEETAAPLVDSVLEGYN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 78 ATVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISEH-PSIDFNVKVSYIEVYKEDLRDLLEleTSMKDL 156
Cdd:smart00129 81 ATIFAYGQTGSGKTYTMIG------TPDSPGIIPRALKDLFEKIDKReEGWQFSVKVSYLEIYNEKIRDLLN--PSSKKL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEaaedgswySPRHI 236
Cdd:smart00129 153 EIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSS--------SGSGK 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 237 VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRrKSSHIPYRDAKITRLLKDSLGGSAKTVMIT 316
Cdd:smart00129 225 ASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHS-KSRHIPYRDSKLTRLLQDSLGGNSKTLMIA 303
|
330 340 350
....*....|....*....|....*....|..
gi 429535824 317 CVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:smart00129 304 NVSPSSSNLEETLSTLRFASRAKEIKNKPIVN 335
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
11-341 |
2.67e-139 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 427.37 E-value: 2.67e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 11 RIRPLLCKEALHNHQVCVRVIPNSQQVII-------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDSETVEsshltnkNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEGYNVTIFAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 84 GQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELETSMKD-LHIRED 161
Cdd:pfam00225 81 GQTGSGKTYTMEG------SDEQPGIIPRALEDLFDRIQKTKErSEFSVKVSYLEIYNEKIRDLLSPSNKNKRkLRIRED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEdgswyspRHIVSKFH 241
Cdd:pfam00225 155 PKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQRNRSTGGEE-------SVKTGKLN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 242 FVDLAGSERVTKTGN-TGERFKESIQINSGLLALGNVISALGDPrrKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSP 320
Cdd:pfam00225 228 LVDLAGSERASKTGAaGGQRLKEAANINKSLSALGNVISALADK--KSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISP 305
|
330 340
....*....|....*....|.
gi 429535824 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 |
5.39e-130 |
|
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276812 [Multi-domain] Cd Length: 326 Bit Score: 402.79 E-value: 5.39e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 5 PVKVAVRIRPLLCKEAlhNHQVCVRVIPNSQQVIIG-------RDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd00106 1 NVRVAVRVRPLNGREA--RSAKSVISVDGGKSVVLDppknrvaPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDSALEGYN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 78 ATVFAYGQTGSGKTYTIGGGHiasvvEGQKGIIPRAIQEIFQSISEHPSIDFN--VKVSYIEVYKEDLRDLLELETSmKD 155
Cdd:cd00106 79 GTIFAYGQTGSGKTYTMLGPD-----PEQRGIIPRALEDIFERIDKRKETKSSfsVSASYLEIYNEKIYDLLSPVPK-KP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 156 LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNMEAAEDgswyspRH 235
Cdd:cd00106 153 LSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQ--RNREKSGE------SV 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 236 IVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKssHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd00106 225 TSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQNK--HIPYRDSKLTRLLQDSLGGNSKTIMI 302
|
330 340
....*....|....*....|....
gi 429535824 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 |
4.62e-112 |
|
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: 4.62e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 6 VKVAVRIRPLLCKEALHNHQVCVRVI----------------------PNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNT 63
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMdnhmlvfdpkdeedgffhggsnNRDRRKRRNKELKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 64 CIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISE-HPSIDFNVKVSYIEVYKED 142
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGT------PQEPGLMVLTMKELFKRIESlKDEKEFEVSMSYLEIYNET 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 143 LRDLLEleTSMKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNM 222
Cdd:cd01370 156 IRDLLN--PSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDKTA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 223 EAAEDgswysprHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRRKSSHIPYRDAKITRLL 302
Cdd:cd01370 234 SINQQ-------VRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINALADPGKKNKHIPYRDSKLTRLL 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 429535824 303 KDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNI 341
Cdd:cd01370 307 KDSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
6-341 |
4.35e-111 |
|
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: 351.63 E-value: 4.35e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSqqvIIGRDRV---FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFA 82
Cdd:cd01374 2 ITVTVRVRPLNSREIGINEQVAWEIDNDT---IYLVEPPstsFTFDHVFGGDSTNREVYELIAKPVVKSALEGYNGTIFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 83 YGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISEHPSIDFNVKVSYIEVYKEDLRDLleLETSMKDLHIREDE 162
Cdd:cd01374 79 YGQTSSGKTFTMSGD------EDEPGIIPLAIRDIFSKIQDTPDREFLLRVSYLEIYNEKINDL--LSPTSQNLKIRDDV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 163 KGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcQVHKNMEAAEDGSwysprhIVSKFHF 242
Cdd:cd01374 151 EKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITI-ESSERGELEEGTV------RVSTLNL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 243 VDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDpRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSS 322
Cdd:cd01374 224 IDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE-GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITPAE 302
|
330
....*....|....*....
gi 429535824 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 |
2.40e-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: 2.40e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII--GRD------RVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd01371 3 VKVVVRCRPLNGKEKAAGALQIVDVDEKRGQVSVrnPKAtaneppKTFTFDAVFDPNSKQLDVYDETARPLVDSVLEGYN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 78 ATVFAYGQTGSGKTYTIGGghiASVVEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLLELETSmKDL 156
Cdd:cd01371 83 GTIFAYGQTGTGKTYTMEG---KREDPELRGIIPNSFAHIFGHIARSQNnQQFLVRVSYLEIYNEEIRDLLGKDQT-KRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhKNMEAAEDGSwyspRHI 236
Cdd:cd01371 159 ELKERPDTGVYVKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI----ECSEKGEDGE----NHI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 237 -VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPrrKSSHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd01371 231 rVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG--KSTHIPYRDSKLTRLLQDSLGGNSKTVMC 308
|
330 340
....*....|....*....|....*.
gi 429535824 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 |
9.41e-108 |
|
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: 343.04 E-value: 9.41e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 11 RIRPLLCKEALHNHQVCVRVIPNSQQVII----GRDRVFTFDFVFGKNSTQDEVYNTcIKPLVLSLIEGYNATVFAYGQT 86
Cdd:cd01366 9 RVRPLLPSEENEDTSHITFPDEDGQTIELtsigAKQKEFSFDKVFDPEASQEDVFEE-VSPLVQSALDGYNVCIFAYGQT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 87 GSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSISE--HPSIDFNVKVSYIEVYKEDLRDLL-ELETSMKDLHIRED-E 162
Cdd:cd01366 88 GSGKTYTMEG------PPESPGIIPRALQELFNTIKElkEKGWSYTIKASMLEIYNETIRDLLaPGNAPQKKLEIRHDsE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 163 KGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhkNMEAAEDGSwysprHIVSKFHF 242
Cdd:cd01366 162 KGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-----SGRNLQTGE-----ISVGKLNL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 243 VDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALgdpRRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSS 322
Cdd:cd01366 232 VDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISAL---RQKQSHIPYRNSKLTYLLQDSLGGNSKTLMFVNISPAE 308
|
330 340
....*....|....*....|.
gi 429535824 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 |
4.55e-102 |
|
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: 4.55e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 6 VKVAVRIRPLLCKEALHNHQVCVRvIPNSQQVIIGRD---RVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFA 82
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVK-FDPEDTVVIATSetgKTFSFDRVFDPNTTQEDVYNFAAKPIVDDVLNGYNGTIFA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 83 YGQTGSGKTYTIGGGHIAsvvEGQKGIIPRAIQEIFQSISEHPS-IDFNVKVSYIEVYKEDLRDLleLETSMKDLHIRED 161
Cdd:cd01369 83 YGQTSSGKTYTMEGKLGD---PESMGIIPRIVQDIFETIYSMDEnLEFHVKVSYFEIYMEKIRDL--LDVSKTNLSVHED 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 162 EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNMeaaEDGSWYSprhivSKFH 241
Cdd:cd01369 158 KNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ--ENV---ETEKKKS-----GKLY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 242 FVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDprRKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPS 321
Cdd:cd01369 228 LVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTD--GKKTHIPYRDSKLTRILQDSLGGNSRTTLIICCSPS 305
|
330 340
....*....|....*....|
gi 429535824 322 SSNFDESLNSLKYANRARNI 341
Cdd:cd01369 306 SYNESETLSTLRFGQRAKTI 325
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
6-348 |
1.01e-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: 327.75 E-value: 1.01e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 6 VKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVII--------GRDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYN 77
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVRKEVSVrtggladkSSTKTYTFDMVFGPEAKQIDVYRSVVCPILDEVLMGYN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 78 ATVFAYGQTGSGKTYTIGGGHiaSVVEGQK-------GIIPRAIQEIFQSISEHpSIDFNVKVSYIEVYKEDLRDLLELE 150
Cdd:cd01364 84 CTIFAYGQTGTGKTYTMEGDR--SPNEEYTweldplaGIIPRTLHQLFEKLEDN-GTEYSVKVSYLEIYNEELFDLLSPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 151 TS-MKDLHIRED--EKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNMEAAEd 227
Cdd:cd01364 161 SDvSERLRMFDDprNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKETTIDGEE- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 228 gswyspRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDprrKSSHIPYRDAKITRLLKDSLG 307
Cdd:cd01364 240 ------LVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITALVE---RAPHVPYRESKLTRLLQDSLG 310
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 429535824 308 GSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01364 311 GRTKTSIIATISPASVNLEETLSTLEYAHRAKNIKNKPEVN 351
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
6-348 |
1.14e-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: 1.14e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 6 VKVAVRIRPLLCKE---------ALHNHQVCVRVIPNSQQVIIGRDRV---FTFDFVF------GKN-STQDEVYNTCIK 66
Cdd:cd01365 3 VKVAVRVRPFNSREkernskcivQMSGKETTLKNPKQADKNNKATREVpksFSFDYSYwshdseDPNyASQEQVYEDLGE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 67 PLVLSLIEGYNATVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQSI--SEHPSIDFNVKVSYIEVYKEDLR 144
Cdd:cd01365 83 ELLQHAFEGYNVCLFAYGQTGSGKSYTMMG------TQEQPGIIPRLCEDLFSRIadTTNQNMSYSVEVSYMEIYNEKVR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 145 DLLELETSMKD--LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQvhKNM 222
Cdd:cd01365 157 DLLNPKPKKNKgnLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQ--KRH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 223 EAAEDGSwyspRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRR-----KSSHIPYRDAK 297
Cdd:cd01365 235 DAETNLT----TEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALADMSSgkskkKSSFIPYRDSV 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 429535824 298 ITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01365 311 LTWLLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKIVNRAVVN 361
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
45-379 |
1.16e-84 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 288.18 E-value: 1.16e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 45 FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISEH 124
Cdd:COG5059 58 YAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGT------EEEPGIIPLSLKELFSKLEDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 125 PSI-DFNVKVSYIEVYKEDLRDLLELETsmKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEH 203
Cdd:COG5059 132 SMTkDFAVSISYLEIYNEKIYDLLSPNE--ESLNIREDSLLGVKVAGLTEKHVSSKEEILDLLRKGEKNRTTASTEINDE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 204 SSRSHAIFTISICQVHKNMeaaedgswysPRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGD 283
Cdd:COG5059 210 SSRSHSIFQIELASKNKVS----------GTSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGD 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 284 PRrKSSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVNFSPESDR-IDEMEFE 362
Cdd:COG5059 280 KK-KSGHIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSIKNKIQVNSSSDSSReIEEIKFD 358
|
330
....*....|....*..
gi 429535824 363 IKLLREALQSQQAGVSQ 379
Cdd:COG5059 359 LSEDRSEIEILVFREQS 375
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
5-348 |
1.84e-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: 279.78 E-value: 1.84e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVIIG-RDRVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAY 83
Cdd:cd01373 2 AVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVLHSkPPKTFTFDHVADSNTNQESVFQSVGKPIVESCLSGYNGTIFAY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 84 GQTGSGKTYTIGG--GHIASVVEGQKGIIPRAIQEIFQSISEH-----PSIDFNVKVSYIEVYKEDLRDLleLETSMKDL 156
Cdd:cd01373 82 GQTGSGKTYTMWGpsESDNESPHGLRGVIPRIFEYLFSLIQREkekagEGKSFLCKCSFLEIYNEQIYDL--LDPASRNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 157 HIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmEAAEDGSWYSpRHI 236
Cdd:cd01373 160 KLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTI-------ESWEKKACFV-NIR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 237 VSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGD-PRRKSSHIPYRDAKITRLLKDSLGGSAKTVMI 315
Cdd:cd01373 232 TSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDvAHGKQRHVCYRDSKLTFLLRDSLGGNAKTAII 311
|
330 340 350
....*....|....*....|....*....|...
gi 429535824 316 TCVSPSSSNFDESLNSLKYANRARNIRNKPTVN 348
Cdd:cd01373 312 ANVHPSSKCFGETLSTLRFAQRAKLIKNKAVVN 344
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
5-337 |
1.32e-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: 1.32e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 5 PVKVAVRIRPLLCKEALHNHQVCVRVIPNSQQVI-IGRDRV----------FTFDFVFGKNSTQDEVYNTCIKPLVLSLI 73
Cdd:cd01367 1 KIKVCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVhEPKLKVdltkyienhtFRFDYVFDESSSNETVYRSTVKPLVPHIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 74 EGYNATVFAYGQTGSGKTYTIGGGHiaSVVEGQKGIIPRAIQEIFQSISEHPSID-FNVKVSYIEVYKEDLRDLLEletS 152
Cdd:cd01367 81 EGGKATCFAYGQTGSGKTYTMGGDF--SGQEESKGIYALAARDVFRLLNKLPYKDnLGVTVSFFEIYGGKVFDLLN---R 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 153 MKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmEAAEDGSwys 232
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIIL-------RDRGTNK--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 233 prhIVSKFHFVDLAGSER-VTKTGNTGERFKESIQINSGLLALGNVISALGDPrrkSSHIPYRDAKITRLLKDSL-GGSA 310
Cdd:cd01367 226 ---LHGKLSFVDLAGSERgADTSSADRQTRMEGAEINKSLLALKECIRALGQN---KAHIPFRGSKLTQVLKDSFiGENS 299
|
330 340
....*....|....*....|....*..
gi 429535824 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 |
2.36e-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: 2.36e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 5 PVKVAVRIRPLLCKEALHNHQVCVRVIpNSQQV----------------IIGRDRVFTFDFVFGKNSTQDEVYNTCIKPL 68
Cdd:cd01368 2 PVKVYLRVRPLSKDELESEDEGCIEVI-NSTTVvlhppkgsaanksernGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 69 VLSLIEGYNATVFAYGQTGSGKTYTIGGGhiasvvEGQKGIIPRAIQEIFQSISehpsiDFNVKVSYIEVYKEDLRDLLE 148
Cdd:cd01368 81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGS------PGDGGILPRSLDVIFNSIG-----GYSVFVSYIEIYNEYIYDLLE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 149 LETS-----MKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISICQVHKNME 223
Cdd:cd01368 150 PSPSsptkkRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 224 AAEDGSWYSPRhiVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISAL--GDPRRKSSHIPYRDAKITRL 301
Cdd:cd01368 230 GDVDQDKDQIT--VSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLreNQLQGTNKMVPFRDSKLTHL 307
|
330 340 350
....*....|....*....|....*....|....
gi 429535824 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 |
5.39e-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: 265.91 E-value: 5.39e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 5 PVKVAVRIRPLLCKEALHNHQVCVRVIpNSQQVIIGRDRV------FTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNA 78
Cdd:cd01376 1 NVRVAVRVRPFVDGTAGASDPSCVSGI-DSCSVELADPRNhgetlkYQFDAFYGEESTQEDIYAREVQPIVPHLLEGQNA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 79 TVFAYGQTGSGKTYTIGGghiasvVEGQKGIIPRAIQEIFQsISEHPSIDFNVKVSYIEVYKEDLRDLLELETsmKDLHI 158
Cdd:cd01376 80 TVFAYGSTGAGKTFTMLG------SPEQPGLMPLTVMDLLQ-MTRKEAWALSFTMSYLEIYQEKILDLLEPAS--KELVI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 159 REDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTISIcqvhknmeaAEDGSWYSPRHIVS 238
Cdd:cd01376 151 REDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKV---------DQRERLAPFRQRTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 239 KFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISAL--GDPRrksshIPYRDAKITRLLKDSLGGSAKTVMIT 316
Cdd:cd01376 222 KLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALnkNLPR-----IPYRDSKLTRLLQDSLGGGSRCIMVA 296
|
330 340
....*....|....*....|...
gi 429535824 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 |
1.97e-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: 1.97e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 33 NSQQviigRDRVFTFDFVFgKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQTGSGKTYTIGGGHIASvveGQKGIIPR 112
Cdd:cd01375 42 NNQQ----EDWSFKFDGVL-HNASQELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENY---KHRGIIPR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 113 AIQEIFQSISEHPSIDFNVKVSYIEVYKEDLRDLL----ELETSMKDLHIREDEKGNTVIVGAKECHVESAGEVMSLLEM 188
Cdd:cd01375 114 ALQQVFRMIEERPTKAYTVHVSYLEIYNEQLYDLLstlpYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 189 GNAARHTGTTQMNEHSSRSHAIFTIsicqvHKNMEAAEDGswySPRHIVSKFHFVDLAGSERVTKTGNTGERFKESIQIN 268
Cdd:cd01375 194 GETNRIIASHTMNKNSSRSHCIFTI-----HLEAHSRTLS---SEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYIN 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429535824 269 SGLLALGNVISALGDPRRksSHIPYRDAKITRLLKDSLGGSAKTVMITCVSPSSSNFDESLNSLKYANRAR 339
Cdd:cd01375 266 KSLSFLEQAIIALSDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFASRVK 334
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
6-397 |
3.88e-62 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 233.29 E-value: 3.88e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 6 VKVAVRIRPLLCKEalhNHQVCVRVIPNSQQVIIGRdrVFTFDFVFGKNSTQDEVYNTCIKPLVLSLIEGYNATVFAYGQ 85
Cdd:PLN03188 100 VKVIVRMKPLNKGE---EGEMIVQKMSNDSLTINGQ--TFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQ 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 86 TGSGKTYTIGGGHIASVVEG----QKGIIPRAIQEIFQSISEHP------SIDFNVKVSYIEVYKEDLRDLLEleTSMKD 155
Cdd:PLN03188 175 TGSGKTYTMWGPANGLLEEHlsgdQQGLTPRVFERLFARINEEQikhadrQLKYQCRCSFLEIYNEQITDLLD--PSQKN 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 156 LHIREDEKGNTVIVGAKECHVESAGEVMSLLEMGNAARHTGTTQMNEHSSRSHAIFTisiCQVHKNMEAAEDG-SWYSpr 234
Cdd:PLN03188 253 LQIREDVKSGVYVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFT---CVVESRCKSVADGlSSFK-- 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 235 hiVSKFHFVDLAGSERVTKTGNTGERFKESIQINSGLLALGNVISALGDPRR--KSSHIPYRDAKITRLLKDSLGGSAKT 312
Cdd:PLN03188 328 --TSRINLVDLAGSERQKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQtgKQRHIPYRDSRLTFLLQESLGGNAKL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 313 VMITCVSPSSSNFDESLNSLKYANRARNIRNKPTVNFSPESDrIDEMEFEIKLLREALQSQQAGVSQTTQINREGSPDTN 392
Cdd:PLN03188 406 AMVCAISPSQSCKSETFSTLRFAQRAKAIKNKAVVNEVMQDD-VNFLREVIRQLRDELQRVKANGNNPTNPNVAYSTAWN 484
|
....*
gi 429535824 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 |
1.99e-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: 98.57 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 26 VCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTCiKPLVLSLIEGYN-ATVFAYGQTGSGKTYTIggghiasvve 104
Cdd:cd01363 1 VLVRVNPFKELPIYRDSKIIVFYRGFRRSESQPHVFAIA-DPAYQSMLDGYNnQSIFAYGESGAGKTETM---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 105 gqKGIIPRAIQEIFqsisehpsidfnvkvSYIEVYKEDLRDLLEletsmkdlhiredekgntvivgakECHVESAGEVMS 184
Cdd:cd01363 70 --KGVIPYLASVAF---------------NGINKGETEGWVYLT------------------------EITVTLEDQILQ 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 185 LLEMGNAARhTGTTQMNEHSSRSHAIFTIsicqvhknmeaaedgswysprhivskfhFVDLAGSERvtktgntgerfkes 264
Cdd:cd01363 109 ANPILEAFG-NAKTTRNENSSRFGKFIEI----------------------------LLDIAGFEI-------------- 145
|
250
....*....|....*.
gi 429535824 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 |
3.66e-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: 3.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 6 VKVAVRIRPLLCKEAlhnhQVCVRVIPNSQQVIIGRDRVFTFDFVFGKNSTQDEVYNTcIKPLVLSLIEGYNATVFAYGQ 85
Cdd:pfam16796 22 IRVFARVRPELLSEA----QIDYPDETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQE-ISQLVQSCLDGYNVCIFAYGQ 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 429535824 86 TGSGKTytiggghiasvvegqKGIIPRAIQEIFQSISE-HPSIDFNVKVSYIEVYKEDLRDLL 147
Cdd:pfam16796 97 TGSGSN---------------DGMIPRAREQIFRFISSlKKGWKYTIELQFVEIYNESSQDLL 144
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
763-1067 |
1.42e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.23 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 763 KLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELE 842
Cdd:TIGR02168 681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 843 QSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALNTDSLKISTRLNLLEQELSEKNVQLQTSTAeEKTKISEQ 922
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER-RIAATERR 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 923 VEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLE 1002
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429535824 1003 KLACLSPVEIRTILFRyfNKVVNLREAER-KQQLYNEEMKMKVLERDNMVRELESALDHLKLQCDR 1067
Cdd:TIGR02168 920 LREKLAQLELRLEGLE--VRIDNLQERLSeEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
696-937 |
2.19e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.26 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 696 LKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVEL 775
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 776 IETQKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQL 855
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 856 QRKLREENEKRKQLDAVIKRDQQKIKALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQK 935
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
..
gi 429535824 936 RR 937
Cdd:COG1196 472 AA 473
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
685-1137 |
2.80e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 61.62 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 685 ETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDlIKELIKTGNDAKSVSKQYSLKVTKL 764
Cdd:PRK03918 234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREI 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 765 EHDAEQAKVELIETQKQLQELENKDlSDVAMKVKLQKEFRKKMDAAKLRVQVLQK-------KQQDSKKLASLSIQnekr 837
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKE-ERLEELKKKLKELEKRLEELEERHELYEEakakkeeLERLKKRLTGLTPE---- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 838 anELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALNTDSLKISTRLNLLEQElsEKNVQLQTSTAEEKt 917
Cdd:PRK03918 388 --KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE--HRKELLEEYTAELK- 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 918 KISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEhVLFQLEE--------GIEALEAAI-EYRN------------ 976
Cdd:PRK03918 463 RIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE-LAEQLKEleeklkkyNLEELEKKAeEYEKlkekliklkgei 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 977 ----------ESIQNRQKSLRASFHNLSRGEANVLEKL-----ACLSPVEIR-TILFRYFNKVVNLREAERKQQLYNEEM 1040
Cdd:PRK03918 542 kslkkeleklEELKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERlKELEPFYNEYLELKDAEKELEREEKEL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1041 KM----------KVLERDNMVRELESALDHLKLQCDrrltlqQKEHEQKMQLLLHhfKEQDGEGIMETFKTYEDKIQQLE 1110
Cdd:PRK03918 622 KKleeeldkafeELAETEKRLEELRKELEELEKKYS------EEEYEELREEYLE--LSRELAGLRAELEELEKRREEIK 693
|
490 500
....*....|....*....|....*....
gi 429535824 1111 KDLYFYK--KTSRDHKKKLKELVGEAIRR 1137
Cdd:PRK03918 694 KTLEKLKeeLEEREKAKKELEKLEKALER 722
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
678-996 |
6.33e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 60.93 E-value: 6.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 678 ELSDTQDETQKSdlENEDLKIDCLQESQElnlqKLKNSERILTEAKQKMRELTiniKMKEDLIKELIKTGNDAKSVSKQY 757
Cdd:PTZ00121 1494 EAKKKADEAKKA--AEAKKKADEAKKAEE----AKKADEAKKAEEAKKADEAK---KAEEKKKADELKKAEELKKAEEKK 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 758 SLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQK-EFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNE- 835
Cdd:PTZ00121 1565 KAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAe 1644
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 836 --KRANELEQSVDHMKYQKIQLQRKL-----------REENEKRKQLDAVIKRDQQKIKA-----LNTDSLKISTRLNLL 897
Cdd:PTZ00121 1645 ekKKAEELKKAEEENKIKAAEEAKKAeedkkkaeeakKAEEDEKKAAEALKKEAEEAKKAeelkkKEAEEKKKAEELKKA 1724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 898 EQELSEKNVQLQTSTAEEKTKISEqvevLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVlfqLEEGIEALEaaiEYRNE 977
Cdd:PTZ00121 1725 EEENKIKAEEAKKEAEEDKKKAEE----AKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAV---IEEELDEED---EKRRM 1794
|
330
....*....|....*....
gi 429535824 978 SIQNRQKSLRASFHNLSRG 996
Cdd:PTZ00121 1795 EVDKKIKDIFDNFANIIEG 1813
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
685-953 |
8.43e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.03 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 685 ETQKSDLENE-----------DLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSV 753
Cdd:TIGR04523 390 ESQINDLESKiqnqeklnqqkDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 754 SKQYSLKVTKLEHDAEQAKVELIETQKQLQEL--ENKDLSdvamkvKLQKEFRKKMDAAKLRVQVLQK-KQQDSKKLASL 830
Cdd:TIGR04523 470 LKVLSRSINKIKQNLEQKQKELKSKEKELKKLneEKKELE------EKVKDLTKKISSLKEKIEKLESeKKEKESKISDL 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 831 -----SIQNEKRANELEQSVDHmKYQKIQlqrKLREENE----KRKQLDAVIKRDQQKIKALNTDSLKISTRLNLLEQEL 901
Cdd:TIGR04523 544 edelnKDDFELKKENLEKEIDE-KNKEIE---ELKQTQKslkkKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKEL 619
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 429535824 902 SEKNvqlqtstaEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPE 953
Cdd:TIGR04523 620 EKAK--------KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPE 663
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
717-1114 |
9.63e-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: 59.99 E-value: 9.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 717 RILTEAKQKMRELTINIKMKEDLIKELIKtgndaksvskqyslkvtKLEHDAEQAKVELIETQKQLQELENKDLSDVAMK 796
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEELKL-----------------QELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 797 VKLQKEFRKKMDA-AKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKR 875
Cdd:pfam02463 232 LKLNEERIDLLQElLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 876 DQQKIKALNTDSLKISTRLNLLEQELSEKNVQLQTStaeEKTKISEQVEVLQKEKDQLQkrrhnvDEKLKNGRVLSPEEE 955
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEELEKELKEL---EIKREAEEEEEEELEKLQEK------LEQLEEELLAKKKLE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 956 HVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKLAcLSPVEIRTILFRYFNKVVNLREAERKQQL 1035
Cdd:pfam02463 383 SERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL-EEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1036 YNEEMKMKV---LERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDGEGIMETFKTYEDKIQQLEKD 1112
Cdd:pfam02463 462 KDELELKKSedlLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENY 541
|
..
gi 429535824 1113 LY 1114
Cdd:pfam02463 542 KV 543
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
632-1104 |
1.50e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.77 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 632 EEQDKVLHCQFSDNSDDEESEGQEKSGTRCRSRSWIQKPDSVCSLVELSDTQDETQKSDLENEDLKIDCLQESQELNLQK 711
Cdd:PTZ00121 1293 DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 712 LKNSERILTEAKQKMREL---------TINIKMKEDLIKELIKTGNDAKSVSKQYS--LKVTKLEHDAEQAK-----VEL 775
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKkkadeakkkAEEDKKKADELKKAAAAKKKADEAKKKAEekKKADEAKKKAEEAKkadeaKKK 1452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 776 IETQKQLQELENK--------DLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKR---------- 837
Cdd:PTZ00121 1453 AEEAKKAEEAKKKaeeakkadEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKkadeakkaee 1532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 838 ---ANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALNTDSLK------ISTRLNLLEQELSEKNVQL 908
Cdd:PTZ00121 1533 akkADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKkaeearIEEVMKLYEEEKKMKAEEA 1612
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 909 QtsTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEgiEALEAAIEYRN-ESIQNRQKSLR 987
Cdd:PTZ00121 1613 K--KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE--EAKKAEEDKKKaEEAKKAEEDEK 1688
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 988 ASFHNLSRG--EANVLEKLACLSPVEIRtilfryfnKVVNLREAERKQQLYNEEMKMKVLERDNMVREL------ESALD 1059
Cdd:PTZ00121 1689 KAAEALKKEaeEAKKAEELKKKEAEEKK--------KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAkkdeeeKKKIA 1760
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 429535824 1060 HLKLQCDRRLTLQQKEHEQKMQlllHHFKEQDGEGIMETFKTYED 1104
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIE---EELDEEDEKRRMEVDKKIKD 1802
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
825-1171 |
1.84e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 825 KKLASLSIQNEK--RANELEQSVDhmKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALNTDSLKISTRLNLLEQELS 902
Cdd:COG1196 200 RQLEPLERQAEKaeRYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 903 EKNVQLQTSTAEEkTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNR 982
Cdd:COG1196 278 ELELELEEAQAEE-YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 983 QKSLRASFHNLSRGEANVLEKLAclspvEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDHLK 1062
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEE-----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1063 LQCDRRLTLQQKEHEQKMQLLlhhfkEQDGEGIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKELVGEAIRRQLA-- 1140
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEA-----ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEgf 506
|
330 340 350
....*....|....*....|....*....|.
gi 429535824 1141 PSEYQEAGDGVLKPEGGGMLSEELKWASRPE 1171
Cdd:COG1196 507 LEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
678-1002 |
2.44e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 678 ELSDTQDETQKSDLENEDLKIDCLQESQELNLQK--LKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSK 755
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQISALRkdLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 756 QYSLKVTKLEHDAEQAKVELIETQKQLQELEN--KDLSDVAMKV--KLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLS 831
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAelTLLNEEAANLreRLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 832 IQNEK---RANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALNTDSLKISTRLNLLEQELSEKNVQL 908
Cdd:TIGR02168 859 AEIEEleeLIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 909 QtstaEEKTKISEQVEVLQKEkdqlqkrrhnvDEKLKNGRVLSPEE-EHVLFQLEEGIEAL----EAAI-EYrnESIQNR 982
Cdd:TIGR02168 939 D----NLQERLSEEYSLTLEE-----------AEALENKIEDDEEEaRRRLKRLENKIKELgpvnLAAIeEY--EELKER 1001
|
330 340
....*....|....*....|
gi 429535824 983 QKSLRASFHNLSRGEANVLE 1002
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAKETLEE 1021
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
685-987 |
2.55e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 685 ETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKEL----------IKTGNDAKSVS 754
Cdd:TIGR04523 43 KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLnsdlskinseIKNDKEQKNKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 755 KQY--SLKVTKLEHDAEQAKV--ELIETQKQLQELENKDLSDVAMKVKLQKEFRK-KMDAAKLRVQVLQKKQQDSKKLAS 829
Cdd:TIGR04523 123 EVElnKLEKQKKENKKNIDKFltEIKKKEKELEKLNNKYNDLKKQKEELENELNLlEKEKLNIQKNIDKIKNKLLKLELL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 830 LSIQNEK--RANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALNTDSLKISTRLNLLEQELSEKNVQ 907
Cdd:TIGR04523 203 LSNLKKKiqKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKK 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 908 LQTSTAEEKtKISEQVEVLQKEKDQ-----LQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNR 982
Cdd:TIGR04523 283 IKELEKQLN-QLKSEISDLNNQKEQdwnkeLKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEK 361
|
....*
gi 429535824 983 QKSLR 987
Cdd:TIGR04523 362 QRELE 366
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
681-1156 |
5.08e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.82 E-value: 5.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 681 DTQDETQKSDLENedlKIDCLQESQELNLQKLKNSERI----LTEAKQKMRELTINIKMKEDLIKEliktgnDAKSVSKQ 756
Cdd:pfam15921 244 EDQLEALKSESQN---KIELLLQQHQDRIEQLISEHEVeitgLTEKASSARSQANSIQSQLEIIQE------QARNQNSM 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 757 YSLKVTKLEHDAEQAKVELIETQK----QLQELE------NKDLSDVAMKV--------KLQKEFRKKMDAAKLRVQVLQ 818
Cdd:pfam15921 315 YMRQLSDLESTVSQLRSELREAKRmyedKIEELEkqlvlaNSELTEARTERdqfsqesgNLDDQLQKLLADLHKREKELS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 819 KKQQDSKKLASLSIQNEKRANELEQSVD--HMKYQKIQ-LQRKLREE--NEKRKQLDAVIKRDQ--QKIKALNTDSLKIS 891
Cdd:pfam15921 395 LEKEQNKRLWDRDTGNSITIDHLRRELDdrNMEVQRLEaLLKAMKSEcqGQMERQMAAIQGKNEslEKVSSLTAQLESTK 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 892 TRLNLLEQELSEKNVQLQTS---TAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHvLFQLEEGIEAL 968
Cdd:pfam15921 475 EMLRKVVEELTAKKMTLESSertVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDH-LRNVQTECEAL 553
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 969 EAAIEYRNESIQnrqkSLRASFHNLSR--GEANvleKLACLSPVEIRTIlfryfNKVVNLREAERKqqlyneEMKMKVLE 1046
Cdd:pfam15921 554 KLQMAEKDKVIE----ILRQQIENMTQlvGQHG---RTAGAMQVEKAQL-----EKEINDRRLELQ------EFKILKDK 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1047 RDNMVRELESALDHLKLQcdrRLTLQQKEHEQkmqllLHHFKE--QDGEGIMETFKTYEDKIQQLEKDLYFYKKTSRDHK 1124
Cdd:pfam15921 616 KDAKIRELEARVSDLELE---KVKLVNAGSER-----LRAVKDikQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKS 687
|
490 500 510
....*....|....*....|....*....|....
gi 429535824 1125 KKLkELVGEAIRRQL--APSEYQEAGDGVLKPEG 1156
Cdd:pfam15921 688 EEM-ETTTNKLKMQLksAQSELEQTRNTLKSMEG 720
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
647-1134 |
5.12e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 647 DDEESEGQEKSGTRCRSRSWIQKPDSVCSLVELSDTQDETQKSD---LENEDLKIDCLQESQEL----NLQKLKNSERIL 719
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADelkKAEEKKKADEAKKAEEKkkadEAKKKAEEAKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 720 TEAKQKMREltinIKMKEDLIKEliktgndaKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKL 799
Cdd:PTZ00121 1318 DEAKKKAEE----AKKKADAAKK--------KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKK 1385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 800 QKEFRKKMDAAKLRVQVLQKKQQDSKKLAslsiQNEKRANELEQsvdhmKYQKIQLQRKLREENEKRKQLDAVIKRDQQK 879
Cdd:PTZ00121 1386 KAEEKKKADEAKKKAEEDKKKADELKKAA----AAKKKADEAKK-----KAEEKKKADEAKKKAEEAKKADEAKKKAEEA 1456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 880 IKAlntdslkistrLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLF 959
Cdd:PTZ00121 1457 KKA-----------EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD 1525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 960 QLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLEKlacLSPVEIRTILFRyfnKVVNLREAERKQ-----Q 1034
Cdd:PTZ00121 1526 EAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEA---KKAEEDKNMALR---KAEEAKKAEEARieevmK 1599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1035 LYNEEMKMKVLERDNMVRELESALDHLKLQCDRRLTLQQKEHEQKMQLLLHHFKEQDGEGIM----ETFKTYEDKIQQLE 1110
Cdd:PTZ00121 1600 LYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIkaaeEAKKAEEDKKKAEE 1679
|
490 500
....*....|....*....|....
gi 429535824 1111 kdlyfYKKTSRDHKKKLKELVGEA 1134
Cdd:PTZ00121 1680 -----AKKAEEDEKKAAEALKKEA 1698
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
721-990 |
9.95e-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: 56.60 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 721 EAKQKMRELTINIKMKEDLIKELIKTGN----DAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMK 796
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLKslerQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 797 VKLQKEFRK---KMDAAKLRVQVLQKKQQDSKKlASLSIQNEKraNELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVI 873
Cdd:TIGR02168 256 EELTAELQEleeKLEELRLEVSELEEEIEELQK-ELYALANEI--SRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 874 KRDQQKIKALNTDSLKISTRLNLLEQELSEKNVQLQTSTA--------------------EEKTKISEQVEVLQKEKDQL 933
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESrleeleeqletlrskvaqleLQIASLNNEIERLEARLERL 412
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 429535824 934 QKRRHNVDEKLK--NGRVLSPEEEHVLFQLEEGIEALEAAIEyRNESIQNRQKSLRASF 990
Cdd:TIGR02168 413 EDRRERLQQEIEelLKKLEEAELKELQAELEELEEELEELQE-ELERLEEALEELREEL 470
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
779-1111 |
1.08e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.31 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 779 QKQLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQK------ 852
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllply 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 853 ---IQLQRKLREENEKRKQLDA---VIKRDQQKIKALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVL 926
Cdd:COG4717 132 qelEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 927 QKEKDQLQKRRHNVDEKLKNgrvlsPEEEHVLFQLEEGIEALEAAIeyrneSIQNRQKSLRASFHNLSRGEANVLEKLAC 1006
Cdd:COG4717 212 EEELEEAQEELEELEEELEQ-----LENELEAAALEERLKEARLLL-----LIAAALLALLGLGGSLLSLILTIAGVLFL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1007 LSPVEIRTILFRYFNKVVNLREAERKQQL-----YNEEMKMKVLER--------DNMVRELESALDHLKLQCDR----RL 1069
Cdd:COG4717 282 VLGLLALLFLLLAREKASLGKEAEELQALpaleeLEEEELEELLAAlglppdlsPEELLELLDRIEELQELLREaeelEE 361
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 429535824 1070 TLQQKEHEQKMQLLLHHFKEQDGEGIMETFKTYEDKIQQLEK 1111
Cdd:COG4717 362 ELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEE 403
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
688-1111 |
1.61e-07 |
|
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: 55.98 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 688 KSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHD 767
Cdd:pfam10174 218 RNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 768 AEQAKVELIETQKQLQELENKDlSDVAMKVKLQKE-----------FRKKMDAAKLRV----QVLQKKQqdsKKLASLSI 832
Cdd:pfam10174 298 LSKKESELLALQTKLETLTNQN-SDCKQHIEVLKEsltakeqraaiLQTEVDALRLRLeekeSFLNKKT---KQLQDLTE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 833 QNEKRANELEQSVDHM--KYQKIQ-LQRKLREENEKRKQLDAVIKRDQQKIKALNTDSLKISTRLNLLEQELSEKN---V 906
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLdvKERKINvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKEriiE 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 907 QLQTSTAEEKTKISEQVEVLQKE-KDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEG------IEALEAAIEYRNESI 979
Cdd:pfam10174 454 RLKEQREREDRERLEELESLKKEnKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGlkkdskLKSLEIAVEQKKEEC 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 980 QNRQKSLRASfHNL---SRGEANVLEKLACLSpveirtilfryfNKVVNLREAERKQQLYNE-------EMKMKVLERDN 1049
Cdd:pfam10174 534 SKLENQLKKA-HNAeeaVRTNPEINDRIRLLE------------QEVARYKEESGKAQAEVErllgilrEVENEKNDKDK 600
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429535824 1050 MVRELES-ALDHLKLQCDRRLTLQQKEHEQK---MQLLLHHFKEQDGEGIMETFKTYEDKIQQLEK 1111
Cdd:pfam10174 601 KIAELESlTLRQMKEQNKKVANIKHGQQEMKkkgAQLLEEARRREDNLADNSQQLQLEELMGALEK 666
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
719-935 |
1.61e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 719 LTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKdlsdvamKVK 798
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE-------IAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 799 LQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQ 878
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 429535824 879 KIKALNTdslKISTRLNLLEQELSEKNvQLQTSTAEEKTKISEQVEVLQKEKDQLQK 935
Cdd:COG4942 175 ELEALLA---ELEEERAALEALKAERQ-KLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
683-1205 |
1.61e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.13 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 683 QDETQKSDLENEDLKIDCLQESQELNLQKLKNSERiltEAKQKMRELTINIKMKEDLiKELIKTGNDAKSVSKQyslKVT 762
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEE---ELKLLAKEEEELKSELLKL-ERRKVDDEEKLKESEK---EKK 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 763 KLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRKKmdaaklrvQVLQKKQQDSKKLASLSIQNEKRANELE 842
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL--------EQLEEELLAKKKLESERLSSAAKLKEEE 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 843 QSVDHMKYQKIQLQRKLREENEKrkqldavIKRDQQKIKALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQ 922
Cdd:pfam02463 397 LELKSEEEKEAQLLLELARQLED-------LLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 923 VEVLQKEKDQLQKRRHNVDEKLKngrvlspeeehvlfQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVLE 1002
Cdd:pfam02463 470 SEDLLKETQLVKLQEQLELLLSR--------------QKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLG 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1003 KLACLSPVEIRTILFRYFNKVVNLREAERKQQLYneemkmkVLERDNMVRELESALDHLKLQcdrRLTLQQKEHEQKMQL 1082
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRA-------LTELPLGARKLRLLIPKLKLP---LKSIAVLEIDPILNL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1083 LLHHFKEQDGEGIMETFKTYEDKIQQLEKDLyfykktSRDHKKKLKELVGEAIRRQLAPSEYQEAGDGVLKPEGGGMLSE 1162
Cdd:pfam02463 606 AQLDKATLEADEDDKRAKVVEGILKDTELTK------LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ 679
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 429535824 1163 ELKWASRPESMKLSGREREMDSSASSLRTQPNPQKLWEDIPEL 1205
Cdd:pfam02463 680 ELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEEL 722
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
679-927 |
2.51e-07 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 55.30 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 679 LSDTQ---DETQKSDLENEDLKIDCLQESQEL-----NLQKLKNSEriLTEAKQKMRELTInikmkEDLIKELIKTGNDA 750
Cdd:PRK11281 65 LEQTLallDKIDRQKEETEQLKQQLAQAPAKLrqaqaELEALKDDN--DEETRETLSTLSL-----RQLESRLAQTLDQL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 751 KSVSK---QYSLKVTKLEHDAEQAKVELIETQKQLQELEN---------KDLSDvAMKVKLQKE---------FRKKMDA 809
Cdd:PRK11281 138 QNAQNdlaEYNSQLVSLQTQPERAQAALYANSQRLQQIRNllkggkvggKALRP-SQRVLLQAEqallnaqndLQRKSLE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 810 AKLRVQVLQKKQQDskkLASLSIQ-------------NEKRANELEQSVDhmkyqkiQLQRKlreENEKRKQLDAVIKRD 876
Cdd:PRK11281 217 GNTQLQDLLQKQRD---YLTARIQrlehqlqllqeaiNSKRLTLSEKTVQ-------EAQSQ---DEAARIQANPLVAQE 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 429535824 877 QQKIKALNTDSLKISTRLN-LLEQELSEKNvQLQTSTAEEKTkISEQVEVLQ 927
Cdd:PRK11281 284 LEINLQLSQRLLKATEKLNtLTQQNLRVKN-WLDRLTQSERN-IKEQISVLK 333
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
733-936 |
6.75e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 6.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 733 IKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELEnKDLSdvamkvKLQKEFRKKMDAAKL 812
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ-AEIA------EAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 813 RVQVLQKKQQDSKKLASL----SIQNE-KRANELEQSVDHMKyQKIQLQRKLREENE-KRKQLDAVIKRDQQKIKALNTd 886
Cdd:COG3883 91 RARALYRSGGSVSYLDVLlgseSFSDFlDRLSALSKIADADA-DLLEELKADKAELEaKKAELEAKLAELEALKAELEA- 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 429535824 887 slkistRLNLLEQELSEKNVQLQTSTAEEKTKIsEQVEVLQKEKDQLQKR 936
Cdd:COG3883 169 ------AKAELEAQQAEQEALLAQLSAEEAAAE-AQLAELEAELAAAEAA 211
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
849-1147 |
1.70e-06 |
|
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: 52.76 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 849 KYQKIQLQRkLREENEKRKQLDAVIKRDQQKIKALnTDSLKIstRLNLLEQELSEKNVQLQtSTAEEKTKISEQVEVLQK 928
Cdd:TIGR02169 670 RSEPAELQR-LRERLEGLKRELSSLQSELRRIENR-LDELSQ--ELSDASRKIGEIEKEIE-QLEQEEEKLKERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 929 EKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAaiEYRNESIQNRQKSLRASFHNLSRGEANVLEKLACLS 1008
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEA--RLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLN 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1009 PVEIRTILFRyfNKVVNL---------REAERKQQLYN-----EEMKMKVLERDNMVRELESALDHLKLQCDRRLT---- 1070
Cdd:TIGR02169 823 RLTLEKEYLE--KEIQELqeqridlkeQIKSIEKEIENlngkkEELEEELEELEAALRDLESRLGDLKKERDELEAqlre 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1071 LQQKEHEQKMQL--LLHHFKEQDG--EGIMETFKTYEDKIQQLEKdlYFYKKTSRDHKKKLKELVGEAIRR-----QLAP 1141
Cdd:TIGR02169 901 LERKIEELEAQIekKRKRLSELKAklEALEEELSEIEDPKGEDEE--IPEEELSLEDVQAELQRVEEEIRAlepvnMLAI 978
|
....*.
gi 429535824 1142 SEYQEA 1147
Cdd:TIGR02169 979 QEYEEV 984
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
697-904 |
2.03e-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: 51.69 E-value: 2.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 697 KIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELI 776
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 777 ETQKQLQE-----------------LENKDLSDVAMKVKLQKEFrkkmdaAKLRVQVLQKKQQDSKKLASLSIQNEKRAN 839
Cdd:COG4942 101 AQKEELAEllralyrlgrqpplallLSPEDFLDAVRRLQYLKYL------APARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 429535824 840 ELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALNTDSLKISTRLNLLEQELSEK 904
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
706-1140 |
2.52e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 706 ELNLQKLKNSERILTEAKQKMRELTINIKMKEDL---IKELIKTGNDAKSVSKQYSLKVTKLEHDAE--QAKVELIETQK 780
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELeeeLEELEAELEELREELEKLEKLLQLLPLYQEleALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 781 QLQELENkdlsdvamkvKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLR 860
Cdd:COG4717 147 RLEELEE----------RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 861 EENEKRKQLDAVIKR---------DQQKIKALNTDSLKISTRLNLLEQELSEKN-------------------VQLQTST 912
Cdd:COG4717 217 EAQEELEELEEELEQleneleaaaLEERLKEARLLLLIAAALLALLGLGGSLLSliltiagvlflvlgllallFLLLARE 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 913 AEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQnrQKSLRASFHN 992
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ--LEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 993 LsrgeanvLEKLACLSPVEIRTILFRYfNKVVNLRE--AERKQQLYNEEMKMKVLERDNMVRELESALDHLKlQCDRRLT 1070
Cdd:COG4717 375 L-------LAEAGVEDEEELRAALEQA-EEYQELKEelEELEEQLEELLGELEELLEALDEEELEEELEELE-EELEELE 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1071 LQQKEHEQKMQLLLHHFKEqdgegiMETFKTYEDKIQQLEkdlyfykktsrDHKKKLKELVGEAIRRQLA 1140
Cdd:COG4717 446 EELEELREELAELEAELEQ------LEEDGELAELLQELE-----------ELKAELRELAEEWAALKLA 498
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
678-953 |
4.61e-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: 51.26 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 678 ELSDTQDETQKSDLENEDLKiDCLQESQELnLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQY 757
Cdd:pfam05483 392 ELEEMTKFKNNKEVELEELK-KILAEDEKL-LDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHY 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 758 SLKVTKLEHDAEQAKVELIE--TQKQLQELENKDL----SDVAMKVKLQKE----FRKKMDAAKLRVQVLQKKQQDSK-K 826
Cdd:pfam05483 470 LKEVEDLKTELEKEKLKNIEltAHCDKLLLENKELtqeaSDMTLELKKHQEdiinCKKQEERMLKQIENLEEKEMNLRdE 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 827 LASLSIQNEKRANEL-------EQSVDHMKYQKIQLQRKLREENEK----RKQLD---AVIKRDQQKIKALNTDSLKIST 892
Cdd:pfam05483 550 LESVREEFIQKGDEVkckldksEENARSIEYEVLKKEKQMKILENKcnnlKKQIEnknKNIEELHQENKALKKKGSAENK 629
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429535824 893 RLNLLEQELSEKNVQLQTStaeeKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPE 953
Cdd:pfam05483 630 QLNAYEIKVNKLELELASA----KQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
767-1005 |
6.26e-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: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 767 DAEQAKVELIETQKQLQELEnkdlsdvamkvKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASlsiQNEKRANELEQSVD 846
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELE-----------KELAALKKEEKALLKQLAALERRIAALARRIR---ALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 847 HMKYQKIQLQRKLREENEK-RKQLDAVIKRDQQKIKAL---NTDSLKISTRLNLLEQeLSEKNVQLQTSTAEEKTKISEQ 922
Cdd:COG4942 87 ELEKEIAELRAELEAQKEElAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKY-LAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 923 VEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIeyrnESIQNRQKSLRASFHNLSRGEANVLE 1002
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL----AELQQEAEELEALIARLEAEAAAAAE 241
|
...
gi 429535824 1003 KLA 1005
Cdd:COG4942 242 RTP 244
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
828-1113 |
1.39e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 828 ASLSIQNEKRA-NELEQSVDHMKYQKIQLQRKLreeNEKRKQLDAVikrdQQKIKALNTDSLKISTRLNLLEQELSEKNV 906
Cdd:TIGR02168 668 TNSSILERRREiEELEEKIEELEEKIAELEKAL---AELRKELEEL----EEELEQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 907 QLQTsTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIeyrnESIQNRQKSL 986
Cdd:TIGR02168 741 EVEQ-LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL----DELRAELTLL 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 987 RASFHNLSRGEANVLEKLACLSpVEIRTILFRyfnkvvnLREAERKQQLYNEEMKMKVLERDNMVRELESALDhlklqcd 1066
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATE-RRLEDLEEQ-------IEELSEDIESLAAEIEELEELIEELESELEALLN------- 880
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 429535824 1067 rrltlQQKEHEQKMQLLLHHFKEQdgegiMETFKTYEDKIQQLEKDL 1113
Cdd:TIGR02168 881 -----ERASLEEALALLRSELEEL-----SEELRELESKRSELRREL 917
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
703-945 |
1.41e-05 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 49.35 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 703 ESQELNLQKLKNSERILTEAKQkmRELtinikmkedlikELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVElietqkql 782
Cdd:pfam17380 338 EQERMAMERERELERIRQEERK--REL------------ERIRQEEIAMEISRMRELERLQMERQQKNERVR-------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 783 QELEnkdlsdVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRkLREE 862
Cdd:pfam17380 396 QELE------AARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVER-LRQQ 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 863 NEKRKQLDAVIKRDQQKIKALNTDSLKIstrlnlLEQELSEKnvqlQTSTAEEKTK---ISEQVEVLQKEKDQLQKRRHN 939
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKI------LEKELEER----KQAMIEEERKrklLEKEMEERQKAIYEEERRREA 538
|
....*.
gi 429535824 940 VDEKLK 945
Cdd:pfam17380 539 EEERRK 544
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
703-1245 |
2.13e-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: 49.20 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 703 ESQELNLQKLKNSERILTE-AKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEhDAEQAKVELIETQKQ 781
Cdd:TIGR00618 190 KSLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQE-EQLKKQQLLKQLRAR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 782 LQELEN--KDLSDVAMKVKLQkefRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMK------YQKI 853
Cdd:TIGR00618 269 IEELRAqeAVLEETQERINRA---RKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKqqssieEQRR 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 854 QLQRKLREENEKRKQLDAVIKRDQQKIKALntdslkistrlnlleqELSEKNVQLQtstaEEKTKISEQVEVLQKEKDQL 933
Cdd:TIGR00618 346 LLQTLHSQEIHIRDAHEVATSIREISCQQH----------------TLTQHIHTLQ----QQKTTLTQKLQSLCKELDIL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 934 QKRRHNVDEKLKNGRVLS-----PEEEHVLFQLEEGIEALEAAIEYRNESIQNR-QKSLRASFHNLSRGEANVleKLACL 1007
Cdd:TIGR00618 406 QREQATIDTRTSAFRDLQgqlahAKKQQELQQRYAELCAAAITCTAQCEKLEKIhLQESAQSLKEREQQLQTK--EQIHL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1008 SPVEIRTILFRYFNKVVNLR----------EAERKQQLYNEEMKMKVLERDNMVRELESALDHLKLQCDrRLTLQQKEHE 1077
Cdd:TIGR00618 484 QETRKKAVVLARLLELQEEPcplcgscihpNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLT-SERKQRASLK 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1078 QKMQLLLHHFkeQDGEGIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKelvgEAIRRQLAPSEYQEAGDGVLKPEGG 1157
Cdd:TIGR00618 563 EQMQEIQQSF--SILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLA----CEQHALLRKLQPEQDLQDVRLHLQQ 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1158 GMLSEELKWASRPESMKLSGREREMDSSASS--------LRTQPNPQKLWEDIPELPPIHSSLAPPSGHMLGNENKTETD 1229
Cdd:TIGR00618 637 CSQELALKLTALHALQLTLTQERVREHALSIrvlpkellASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEY 716
|
570
....*....|....*.
gi 429535824 1230 DNQFTKSHSRLSSQIQ 1245
Cdd:TIGR00618 717 DREFNEIENASSSLGS 732
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
702-963 |
3.57e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 702 QESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELiktgndaksvsKQYSLKVTKLEHDAEQAKVELIETQKQ 781
Cdd:PRK03918 510 EKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKL-----------EELKKKLAELEKKLDELEEELAELLKE 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 782 LQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLRE 861
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 862 ENEKRK-----QLDAVIKRDQQKIKALNTDSLKISTRLNLLEQELseknvqlqtstaEEKTKISEQVEVLQKEKDQLQKR 936
Cdd:PRK03918 659 EEYEELreeylELSRELAGLRAELEELEKRREEIKKTLEKLKEEL------------EEREKAKKELEKLEKALERVEEL 726
|
250 260
....*....|....*....|....*..
gi 429535824 937 RhnvdEKLKNGRVLspEEEHVLFQLEE 963
Cdd:PRK03918 727 R----EKVKKYKAL--LKERALSKVGE 747
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
849-1140 |
3.58e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 849 KYQKIQLQRKLREENEKRKQLDAV---IKRDQQKIK--------------ALNTDSLKIST-RLNLLEQELSEKNVQLqT 910
Cdd:TIGR02168 171 KERRKETERKLERTRENLDRLEDIlneLERQLKSLErqaekaerykelkaELRELELALLVlRLEELREELEELQEEL-K 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 911 STAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKngrvlspEEEHVLFQLEEGIEALEAAIeyrnESIQNRQKSLRASF 990
Cdd:TIGR02168 250 EAEEELEELTAELQELEEKLEELRLEVSELEEEIE-------ELQKELYALANEISRLEQQK----QILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 991 HNLSRGEANVLEKLACLSpveirtilfryfnkvVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDHLKLQCDRRLT 1070
Cdd:TIGR02168 319 EELEAQLEELESKLDELA---------------EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1071 LQQKEHEQKMQLLLhhfkeqdgegIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKELVGEAIRRQLA 1140
Cdd:TIGR02168 384 LRSKVAQLELQIAS----------LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE 443
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
695-963 |
4.39e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 4.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 695 DLKidcLQEsqelnLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVE 774
Cdd:pfam15921 527 DLK---LQE-----LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 775 LIETQKQLQEL----ENKD---------LSDVAM-KVKL----QKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNE- 835
Cdd:pfam15921 599 INDRRLELQEFkilkDKKDakirelearVSDLELeKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEv 678
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 836 ------KRANELEQSVDHMKYQKIQLQRKLREENE-------------------------KRKQLDAVikrdQQKIKALN 884
Cdd:pfam15921 679 lkrnfrNKSEEMETTTNKLKMQLKSAQSELEQTRNtlksmegsdghamkvamgmqkqitaKRGQIDAL----QSKIQFLE 754
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429535824 885 TDSLKISTRLNLLEQELSEKNVQLQTsTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEE 963
Cdd:pfam15921 755 EAMTNANKEKHFLKEEKNKLSQELST-VATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQ 832
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
726-938 |
5.42e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.20 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 726 MRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVAMKVKLQKEFRK 805
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 806 KMDAAKLRVQVLQKKQQDSKKLAslsiqneKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALNT 885
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLT-------QRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSK 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 429535824 886 DSLKISTRLNLLE---QELSEKNVQLQTSTAEEKTKISEQvEVLQKEKDQLQKRRH 938
Cdd:pfam07888 193 EFQELRNSLAQRDtqvLQLQDTITTLTQKLTTAHRKEAEN-EALLEELRSLQERLN 247
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
759-988 |
7.65e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.34 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 759 LKVTKLEHDAEQAKvELIETQKQLQELENKdLSDVamkVKLQKEFRKKMDAAKLRVQVLQKKQQDskkLASLSIQNEKRA 838
Cdd:PRK02224 489 EEVEEVEERLERAE-DLVEAEDRIERLEER-REDL---EELIAERRETIEEKRERAEELRERAAE---LEAEAEEKREAA 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 839 NELEQSVDHMKYQKIQLQRKLREENEKRKQLDAV-------------IKRDQQKIKALNT------DSLK-ISTRLNLLE 898
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNSKLAELKERIESLERIrtllaaiadaedeIERLREKREALAElnderrERLAeKRERKRELE 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 899 QELSEKNV---QLQTSTAEE-KTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHvlfqLEEGIEALEAAIEy 974
Cdd:PRK02224 641 AEFDEARIeeaREDKERAEEyLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREA----LENRVEALEALYD- 715
|
250
....*....|....
gi 429535824 975 RNESIQNRQKSLRA 988
Cdd:PRK02224 716 EAEELESMYGDLRA 729
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
766-1038 |
1.20e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 766 HDAEQAKV---ELIET-QKQLQELENKDLSDVAMKVKLQ-KEFRKKMDAAKLRVQVLQKKQQdskklaslSIQNEKRANE 840
Cdd:COG3206 145 PDPELAAAvanALAEAyLEQNLELRREEARKALEFLEEQlPELRKELEEAEAALEEFRQKNG--------LVDLSEEAKL 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 841 LEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALNTDSL--KISTRLNLLEQELSEknvQLQTSTAEektk 918
Cdd:COG3206 217 LLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAE---LSARYTPN---- 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 919 iSEQVEVLQKEKDQLQKRrhnvdeklkngrvLSPEEEHVLFQLEEGIEALEAaieyRNESIQNRQKSLRASFHNLSRGEA 998
Cdd:COG3206 290 -HPDVIALRAQIAALRAQ-------------LQQEAQRILASLEAELEALQA----REASLQAQLAQLEARLAELPELEA 351
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 429535824 999 --NVLEklaclspveirtilfryfnkvvnlREAERKQQLYNE 1038
Cdd:COG3206 352 elRRLE------------------------REVEVARELYES 369
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
678-946 |
1.51e-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: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 678 ELSDTQDETqkSDLENEdlkIDCLQESQELNLQKLKNSERILTEAKQkmrELTINIKMKEDLIKELiktgNDAKSVSKQY 757
Cdd:TIGR02169 710 ELSDASRKI--GEIEKE---IEQLEQEEEKLKERLEELEEDLSSLEQ---EIENVKSELKELEARI----EELEEDLHKL 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 758 SLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDV--AMKVKLQKEFRKK-------------MDAAKLRVQVLQKKQQ 822
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARlrEIEQKLNRLTLEKeylekeiqelqeqRIDLKEQIKSIEKEIE 857
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 823 DSK-KLASLSIQNEKRANELEQ----------SVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALN------- 884
Cdd:TIGR02169 858 NLNgKKEELEEELEELEAALRDlesrlgdlkkERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEeelseie 937
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 885 -------------TDSLKISTRLNLLEQELSE------KNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLK 945
Cdd:TIGR02169 938 dpkgedeeipeeeLSLEDVQAELQRVEEEIRAlepvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKR 1017
|
.
gi 429535824 946 N 946
Cdd:TIGR02169 1018 E 1018
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
703-981 |
1.85e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.22 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 703 ESQELNLQKLKNSERILTEAKQKMRELtinikMKEDLIKELIKTGNDaksvSKQYSLKVTKLEHDAEQAKVELIETQKQL 782
Cdd:COG5022 816 LACIIKLQKTIKREKKLRETEEVEFSL-----KAEVLIQKFGRSLKA----KKRFSLLKKETIYLQSAQRVELAERQLQE 886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 783 QELENKDLSDVAMK-VKLQKE-FRKKMDAAKLRVQVLQKKQQDSKKLASLsiqNEKRANELEQSvdhMKYQKIQLQRKLR 860
Cdd:COG5022 887 LKIDVKSISSLKLVnLELESEiIELKKSLSSDLIENLEFKTELIARLKKL---LNNIDLEEGPS---IEYVKLPELNKLH 960
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 861 EENEKrkqldavIKRDQQKIKALNTDSLKISTRLNLLEQELSEKNvqlqtstaEEKTKISEQVEVLQKEKDQLQKRRHNV 940
Cdd:COG5022 961 EVESK-------LKETSEEYEDLLKKSTILVREGNKANSELKNFK--------KELAELSKQYGALQESTKQLKELPVEV 1025
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 429535824 941 DEKLKNGRVLS--PEEEHVLFQLEEGIEALEAAIEYRNESIQN 981
Cdd:COG5022 1026 AELQSASKIISseSTELSILKPLQKLKGLLLLENNQLQARYKA 1068
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
710-949 |
1.96e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 710 QKLKNSERILTEAKQKMRELTINIkmkEDLIKELIKTGNDAKsvskQYSLKVTKLEHDAEQAKVELIETQKQLQELENKD 789
Cdd:PRK00409 495 KRLGLPENIIEEAKKLIGEDKEKL---NELIASLEELERELE----QKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 790 LSdvamkvKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIqnekRANELEQSvdhmkyqkiqlQRKLREENEKRKQL 869
Cdd:PRK00409 568 LE------EAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASV----KAHELIEA-----------RKRLNKANEKKEKK 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 870 DAVIKRDQQKIKAlnTDSLKISTrLN----LLEQeLSEKNVQLQTSTAEEKTKISEqVEVLQKEKDQLQKRRHNVDEKLK 945
Cdd:PRK00409 627 KKKQKEKQEELKV--GDEVKYLS-LGqkgeVLSI-PDDKEAIVQAGIMKMKVPLSD-LEKIQKPKKKKKKKPKTVKPKPR 701
|
....
gi 429535824 946 NGRV 949
Cdd:PRK00409 702 TVSL 705
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
686-933 |
2.23e-04 |
|
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: 45.58 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 686 TQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDL---IKELIKTGNDAKSVSKQYSLKVT 762
Cdd:pfam10174 503 EHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEIndrIRLLEQEVARYKEESGKAQAEVE 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 763 KLEHDAEQAKVELIETQKQLQELEN------KDLSDVAMKVKLQKEFRKKMDAAKLrvqVLQKKQQDSKKLASLSIQNEK 836
Cdd:pfam10174 583 RLLGILREVENEKNDKDKKIAELESltlrqmKEQNKKVANIKHGQQEMKKKGAQLL---EEARRREDNLADNSQQLQLEE 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 837 RANELE---QSVDHMKYQKIQLQRKLREEN--------EKRKQLDAVIKRDQQKIKAlntdslkistrlnlleqELSEK- 904
Cdd:pfam10174 660 LMGALEktrQELDATKARLSSTQQSLAEKDghltnlraERRKQLEEILEMKQEALLA-----------------AISEKd 722
|
250 260 270
....*....|....*....|....*....|
gi 429535824 905 -NVQLQTSTAEEKTKISEQVEVLQKEKDQL 933
Cdd:pfam10174 723 aNIALLELSSSKKKKTQEEVMALKREKDRL 752
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
705-1094 |
2.97e-04 |
|
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: 45.49 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 705 QELNLQK--LKNSERILTEakqkmreLTINIKMKEDLIKeliKTGNDAKSVSKQYSLKVTKLEH-------------DAE 769
Cdd:pfam15921 482 EELTAKKmtLESSERTVSD-------LTASLQEKERAIE---ATNAEITKLRSRVDLKLQELQHlknegdhlrnvqtECE 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 770 QAKVELIETQKQLQELENKdlsdVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDS----KKLASLSIQNEKRANELEQSV 845
Cdd:pfam15921 552 ALKLQMAEKDKVIEILRQQ----IENMTQLVGQHGRTAGAMQVEKAQLEKEINDRrlelQEFKILKDKKDAKIRELEARV 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 846 DHMKYQKIQL-------QRKLREENEKRKQLDAVIKRDQQKIKALNTDslkistrLNLLEQELSEKNVQLQTSTaeekTK 918
Cdd:pfam15921 628 SDLELEKVKLvnagserLRAVKDIKQERDQLLNEVKTSRNELNSLSED-------YEVLKRNFRNKSEEMETTT----NK 696
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 919 ISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLrasfHNLSRGEA 998
Cdd:pfam15921 697 LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEK----HFLKEEKN 772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 999 NVLEKLACLSPVEirtilfryfNKVVNLREAERKQQlynEEMKMKVlerdnmvRELESALDHLKLQCDRRLTLQQKEHEQ 1078
Cdd:pfam15921 773 KLSQELSTVATEK---------NKMAGELEVLRSQE---RRLKEKV-------ANMEVALDKASLQFAECQDIIQRQEQE 833
|
410
....*....|....*....
gi 429535824 1079 KMQLLLHH---FKEQDGEG 1094
Cdd:pfam15921 834 SVRLKLQHtldVKELQGPG 852
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
707-894 |
5.09e-04 |
|
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: 42.99 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 707 LNLQKLKNSeriLTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELE 786
Cdd:COG1579 10 LDLQELDSE---LDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 787 N-KDLSDvamkvkLQKEfrkkMDAAKLRVQVLQKKQqdskklaslsIQNEKRANELEQSVDHMKYQKIQLQRKLreeNEK 865
Cdd:COG1579 87 NnKEYEA------LQKE----IESLKRRISDLEDEI----------LELMERIEELEEELAELEAELAELEAEL---EEK 143
|
170 180
....*....|....*....|....*....
gi 429535824 866 RKQLDAVIKRDQQKIKALNTDSLKISTRL 894
Cdd:COG1579 144 KAELDEELAELEAELEELEAEREELAAKI 172
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
827-1083 |
5.18e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 5.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 827 LASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALNTDSLKISTRLNLLEQELSEknv 906
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 907 qLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLkngrVLSPEEehvLFQLEEGIEALEAAIEYRNESIQnrqkSL 986
Cdd:COG4942 88 -LEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL----LLSPED---FLDAVRRLQYLKYLAPARREQAE----EL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 987 RASFHNLSRGEANVLEKLAclspveirtilfryfNKVVNLREAERKQQLYNEEMKmkvlERDNMVRELESALDHLKlqcd 1066
Cdd:COG4942 156 RADLAELAALRAELEAERA---------------ELEALLAELEEERAALEALKA----ERQKLLARLEKELAELA---- 212
|
250
....*....|....*..
gi 429535824 1067 RRLTLQQKEHEQKMQLL 1083
Cdd:COG4942 213 AELAELQQEAEELEALI 229
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
708-973 |
5.27e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 708 NLQKLKNSERILTEAKQKMRELTiNIKMKEDLIKELIKTGNDAKSVSKQysLKVTKLEHDAEQAKVELIETQKQLQELEN 787
Cdd:COG4913 233 HFDDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAA--LRLWFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 788 KdlsdvamkvklQKEFRKKMDAAKLRVQVL--QKKQQDSKKLASLsiqnekrANELEQsvdhmkyqkiqLQRKLREENEK 865
Cdd:COG4913 310 E-----------LERLEARLDALREELDELeaQIRGNGGDRLEQL-------EREIER-----------LERELEERERR 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 866 RKQLDAVIKRDQQKI----KALNTDSLKISTRLNLLEQELsEKNVQLQTSTAEEKTKISEQVEVLQKEKDQLQKRRHNVD 941
Cdd:COG4913 361 RARLEALLAALGLPLpasaEEFAALRAEAAALLEALEEEL-EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 429535824 942 EKLKNGR-----VLSPEEEHVLF-----QLEEGIEALEAAIE 973
Cdd:COG4913 440 ARLLALRdalaeALGLDEAELPFvgeliEVRPEEERWRGAIE 481
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
689-922 |
6.29e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 689 SDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKtgndaksvskqyslKVTKLEHDA 768
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA--------------EIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 769 EQAKVELIETQKQLQE-----------LENKDLSDVAMKVKLQKEFrkkMDAAKlrvQVLQKKQQDSKKLASLSIQNEKR 837
Cdd:COG3883 82 EERREELGERARALYRsggsvsyldvlLGSESFSDFLDRLSALSKI---ADADA---DLLEELKADKAELEAKKAELEAK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 838 ANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKT 917
Cdd:COG3883 156 LAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
|
....*
gi 429535824 918 KISEQ 922
Cdd:COG3883 236 AAAAA 240
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
726-863 |
6.37e-04 |
|
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: 43.88 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 726 MRELTINIKMKEDLIKELIKTGNDA-----------KSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENKDLSDVA 794
Cdd:smart00435 233 LQEQLKELTAKDGNVAEKILAYNRAnrevailcnhqRTVSKTHEKSMEKLQEKIKALKYQLKRLKKMILLFEMISDLKRK 312
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 429535824 795 MKVKLQKEFRkkmdaaKLRVQVLQKKQQDSKKLASlsiqnEKRANELEQSVdhmkyQKIQLQRKLREEN 863
Cdd:smart00435 313 LKSKFERDNE------KLDAEVKEKKKEKKKEEKK-----KKQIERLEERI-----EKLEVQATDKEEN 365
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
759-937 |
6.74e-04 |
|
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: 42.99 E-value: 6.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 759 LKVTKLEHDAEQAKVELIETQKQLQELEnKDLSDVAMKVKlqkEFRKKMDAAKLRVQVLQKKQQDSKKLaSLSIQNEKRA 838
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALE-ARLEAAKTELE---DLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 839 NELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALntdslkistrlnllEQELseknvqlqtstAEEKTK 918
Cdd:COG1579 92 EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAEL--------------EAEL-----------EEKKAE 146
|
170
....*....|....*....
gi 429535824 919 ISEQVEVLQKEKDQLQKRR 937
Cdd:COG1579 147 LDEELAELEAELEELEAER 165
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
705-1133 |
6.88e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 705 QELNLQKL----KNSERILTEAKQKMRELTINIKMKEDlIKELIKTgndaksvskqyslkvtklehdaeqAKVELIETQK 780
Cdd:PRK03918 153 QILGLDDYenayKNLGEVIKEIKRRIERLEKFIKRTEN-IEELIKE------------------------KEKELEEVLR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 781 QLQELEnkdlsdvamkvKLQKEFRKKMDAAKLRVQVLQKKQQdskKLASLSIQNEKraneLEQSVDHMKYQKIQLQRKLR 860
Cdd:PRK03918 208 EINEIS-----------SELPELREELEKLEKEVKELEELKE---EIEELEKELES----LEGSKRKLEEKIRELEERIE 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 861 EENEKRKQLDAVIKRDQQ---------KIKALNTDSLKISTRLNLLEQELSE--KNVQLQTSTAEEKT----KISEQVEV 925
Cdd:PRK03918 270 ELKKEIEELEEKVKELKElkekaeeyiKLSEFYEEYLDELREIEKRLSRLEEeiNGIEERIKELEEKEerleELKKKLKE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 926 LQKEKDQLQKRRHNVDE-KLKNGRVLSPEEEHVLFQLEEGIEALEAAiEYRNESIQNRQKSLRASFHNLSRGEA------ 998
Cdd:PRK03918 350 LEKRLEELEERHELYEEaKAKKEELERLKKRLTGLTPEKLEKELEEL-EKAKEEIEEEISKITARIGELKKEIKelkkai 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 999 NVLEKLACLSPV--------EIRTILFRYFNKVVNLRE-----AERKQQLYNEEMKM-KVLERDNMVRELESALDHLKLQ 1064
Cdd:PRK03918 429 EELKKAKGKCPVcgrelteeHRKELLEEYTAELKRIEKelkeiEEKERKLRKELRELeKVLKKESELIKLKELAEQLKEL 508
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1065 CDRRLTLQQKEHEQKMQLLLHHFKEQDG-EGIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKELVGE 1133
Cdd:PRK03918 509 EEKLKKYNLEELEKKAEEYEKLKEKLIKlKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKE 578
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
680-944 |
7.65e-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: 43.86 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 680 SDTQDETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNdaksvskqysl 759
Cdd:TIGR04523 354 SESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKE----------- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 760 kvtKLEHDAEQAKVELIETQKQLQELENKDlsdvAMKVKLQKEFRKKMDAAKLRVQVLQKK----QQDSKKLASLSIQNE 835
Cdd:TIGR04523 423 ---LLEKEIERLKETIIKNNSEIKDLTNQD----SVKELIIKNLDNTRESLETQLKVLSRSinkiKQNLEQKQKELKSKE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 836 KRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALNTDSLKISTRLN--LLEQELSEKNVQLQTSTA 913
Cdd:TIGR04523 496 KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkeNLEKEIDEKNKEIEELKQ 575
|
250 260 270
....*....|....*....|....*....|.
gi 429535824 914 EEKTKISEQVEvLQKEKDQLQKRRHNVDEKL 944
Cdd:TIGR04523 576 TQKSLKKKQEE-KQELIDQKEKEKKDLIKEI 605
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
688-1130 |
8.67e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.74 E-value: 8.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 688 KSDLENEDLKIDCLQESqelnLQKLKNSERIlTEAKQKMRELTINIKMKE-DLIKELIKTGNDAKSVSKQYSLKVTKLEH 766
Cdd:PRK01156 189 EEKLKSSNLELENIKKQ----IADDEKSHSI-TLKEIERLSIEYNNAMDDyNNLKSALNELSSLEDMKNRYESEIKTAES 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 767 D---AEQAKVELIETQKQLQELEN--------------KDLSDVAMKVKLQKEFR---KKMDAAKLRVQVLQKKQQDSKK 826
Cdd:PRK01156 264 DlsmELEKNNYYKELEERHMKIINdpvyknrnyindyfKYKNDIENKKQILSNIDaeiNKYHAIIKKLSVLQKDYNDYIK 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 827 LASLSIQNEKRANELEQsvDHMKYQKI-----QLQRKLREENEKRKQLDAVIKRD------------------------- 876
Cdd:PRK01156 344 KKSRYDDLNNQILELEG--YEMDYNSYlksieSLKKKIEEYSKNIERMSAFISEIlkiqeidpdaikkelneinvklqdi 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 877 -------QQKIKALNTDSLKISTRLNLLEQEL----------SEKNVQLQTSTAEEKTKISEQVEVLQKE-KDQLQKRRH 938
Cdd:PRK01156 422 sskvsslNQRIRALRENLDELSRNMEMLNGQSvcpvcgttlgEEKSNHIINHYNEKKSRLEEKIREIEIEvKDIDEKIVD 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 939 --NVDEKLKNGRVLSPEEEHVLFQLEEG----IEALEAAIEYRN---ESIQNRQKSLRasFHNLSRGEANVLEKLACLSP 1009
Cdd:PRK01156 502 lkKRKEYLESEEINKSINEYNKIESARAdledIKIKINELKDKHdkyEEIKNRYKSLK--LEDLDSKRTSWLNALAVISL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1010 VEIRTILFRYFNKVVNLREAERKQQLYNEEMKMKVLERDNMVRELESALDHLKLQcdRRLTLQQKEHEQKMQLLLHHFKE 1089
Cdd:PRK01156 580 IDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNK--YNEIQENKILIEKLRGKIDNYKK 657
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 429535824 1090 QDGE--GIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKEL 1130
Cdd:PRK01156 658 QIAEidSIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARL 700
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
853-1003 |
9.09e-04 |
|
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: 42.22 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 853 IQLQR---KLREENEKRKQLDAVIKRDQQKIKALNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKT--------KISE 921
Cdd:COG1579 10 LDLQEldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqlgnvRNNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 922 QVEVLQKEKDQLQKRRHNVDEKLKngrvlspEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRGEANVL 1001
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEIL-------ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
..
gi 429535824 1002 EK 1003
Cdd:COG1579 163 AE 164
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
709-1131 |
9.89e-04 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 43.67 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 709 LQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAK--------SVSKQYSLKVTKLEHDAEQAKVeLIETQK 780
Cdd:PTZ00440 392 IETLLDSEYFISKYTNIISLSEHTLKAAEDVLKENSQKIADYAlysnleiiEIKKKYDEKINELKKSINQLKT-LISIMK 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 781 ---QLQELENKDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQ----QDSKKLASLSIQNEKRANELEQSVDHMKYQKi 853
Cdd:PTZ00440 471 sfyDLIISEKDSMDSKEKKESSDSNYQEKVDELLQIINSIKEKNnivnNNFKNIEDYYITIEGLKNEIEGLIELIKYYL- 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 854 QLQRKLREENEKRKQLDAVIKRDQQKIKAlNTDSLKISTRLNLLEQELSEKNVQLQTSTAEEKTKISEQVEVLQKEKDQL 933
Cdd:PTZ00440 550 QSIETLIKDEKLKRSMKNDIKNKIKYIEE-NVDHIKDIISLNDEIDNIIQQIEELINEALFNKEKFINEKNDLQEKVKYI 628
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 934 QKRRHNVDEKLKNGRVLSPEEEHVLFQleegiealeaaieYRNESIQNRQkslraSFHNLSRGEANVLEKLACLSPVEIR 1013
Cdd:PTZ00440 629 LNKFYKGDLQELLDELSHFLDDHKYLY-------------HEAKSKEDLQ-----TLLNTSKNEYEKLEFMKSDNIDNII 690
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1014 TILFRYFNKVVNLREAERKQQLYNEEMKM-KVLER-DNMVRELESALDHLKLQcDRRLTLQQKEHEQKMQLLLHHFKEQD 1091
Cdd:PTZ00440 691 KNLKKELQNLLSLKENIIKKQLNNIEQDIsNSLNQyTIKYNDLKSSIEEYKEE-EEKLEVYKHQIINRKNEFILHLYEND 769
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 429535824 1092 -----GEGIMETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLKELV 1131
Cdd:PTZ00440 770 kdlpdGKNTYEEFLQYKDTILNKENKISNDINILKENKKNNQDLL 814
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
833-988 |
1.39e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 833 QNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALNTDSLKISTRLNlleqelseknvqlQTST 912
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG-------------NVRN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 429535824 913 AEEKTKISEQVEVLQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRA 988
Cdd:COG1579 88 NKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEA 163
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
678-882 |
1.97e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 678 ELSDTQDETQK--SDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTgndAKSVSK 755
Cdd:COG4942 42 ELAALKKEEKAllKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA---LYRLGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 756 QYSLKVTKLEHDAEQAKVELI-------ETQKQLQELEnKDLSDVAMKVKLQKEFRKKMDAAklrvqvLQKKQQDSKKLA 828
Cdd:COG4942 119 QPPLALLLSPEDFLDAVRRLQylkylapARREQAEELR-ADLAELAALRAELEAERAELEAL------LAELEEERAALE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 429535824 829 SLSIQNEKRANELEQsvdhmkyQKIQLQRKLREENEKRKQLDAVIKRDQQKIKA 882
Cdd:COG4942 192 ALKAERQKLLARLEK-------ELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
709-937 |
2.25e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 709 LQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELENK 788
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 789 DlsdvAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKI-----QLQRKLREEN 863
Cdd:COG4717 370 Q----EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELeeeleELEEELEELE 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 429535824 864 EKRKQLDAVIKRDQQKIKALNTDslkisTRLNLLEQELSEKNVQLQtSTAEEKTKISEQVEVLQKEKDQLQKRR 937
Cdd:COG4717 446 EELEELREELAELEAELEQLEED-----GELAELLQELEELKAELR-ELAEEWAALKLALELLEEAREEYREER 513
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
743-1092 |
2.33e-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: 42.42 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 743 LIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQELEnKDLSDVAMK-VKLQKEFRKKMDAAKLRVQ----VL 817
Cdd:pfam05557 11 LSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQ-KRIRLLEKReAEAEEALREQAELNRLKKKyleaLN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 818 QKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQ---QKIKALNTdSLKISTRL 894
Cdd:pfam05557 90 KKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASeaeQLRQNLEK-QQSSLAEA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 895 NLLEQELSEKNVQLQTSTAEEKTKISEQVEV--LQKEKDQLQKRRHNVDEKLKNGRVLSPEEEHVLFQLE--EGIEALEA 970
Cdd:pfam05557 169 EQRIKELEFEIQSQEQDSEIVKNSKSELARIpeLEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEreEKYREEAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 971 AIEYRNESIQnrqkslrasfhnlsrGEANVLEKLACLSPVEIRT-ILFRYFNKVVNLREAERKQQLYNEEMKMKVLE--R 1047
Cdd:pfam05557 249 TLELEKEKLE---------------QELQSWVKLAQDTGLNLRSpEDLSRRIEQLQQREIVLKEENSSLTSSARQLEkaR 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 429535824 1048 DNMVRELESALDH-LKLQCDRRLTLQQKEHEQKMQLLLHhfKEQDG 1092
Cdd:pfam05557 314 RELEQELAQYLKKiEDLNKKLKRHKALVRRLQRRVLLLT--KERDG 357
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
677-935 |
2.88e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.97 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 677 VELSDTQDETQKSDLENEDLKIDCLQESQELNLQKLKNSERILTEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQ 756
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 757 YSLKVTKLEHDAEQAKVELIETQKQLQELEN-KDLSDVAMkvklqKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSiqnE 835
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNeRASLEEAL-----ALLRSELEELSEELRELESKRSELRRELEEL---R 921
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 836 KRANELEQSVDHMKYQKIQLQRKLREE---------------NEKRKQLDAVIKRDQQKIKALNtdslkistRLNLL-EQ 899
Cdd:TIGR02168 922 EKLAQLELRLEGLEVRIDNLQERLSEEysltleeaealenkiEDDEEEARRRLKRLENKIKELG--------PVNLAaIE 993
|
250 260 270
....*....|....*....|....*....|....*.
gi 429535824 900 ELSEKNvqlqtstaEEKTKISEQVEVLQKEKDQLQK 935
Cdd:TIGR02168 994 EYEELK--------ERYDFLTAQKEDLTEAKETLEE 1021
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
763-903 |
5.03e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 38.82 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 763 KLEHDAEQAKVELIETQKQLQELENKDLSDVAmkvklqKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELE 842
Cdd:pfam12718 6 KLEAENAQERAEELEEKVKELEQENLEKEQEI------KSLTHKNQQLEEEVEKLEEQLKEAKEKAEESEKLKTNNENLT 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 429535824 843 QSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQKIKALNTDSLKISTRLNLLEQELSE 903
Cdd:pfam12718 80 RKIQLLEEELEESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEELEEKYKE 140
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
689-1128 |
5.73e-03 |
|
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: 41.25 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 689 SDLENEDLKIDCLQESQELNLQ----KLKNSERILTEAKQKMRELT-----INIKMKEDLI--KELIKTGNDA------- 750
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKqkenKLQENRKIIEAQRKAIQELQfenekVSLKLEEEIQenKDLIKENNATrhlcnll 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 751 KSVSKQYSLKVTKLEHDAEQAKVELIETQKQLQEL-----------ENKDLsDVAMKVK--------LQKEFRKKMDAAK 811
Cdd:pfam05483 161 KETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMilafeelrvqaENARL-EMHFKLKedhekiqhLEEEYKKEINDKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 812 LRVQVL----QKKQQDSKKLASLSIQNEKRANELEQSVdhmKYQKIQLQRKLREENEKRKQLDAV---IKRDQQKIKALN 884
Cdd:pfam05483 240 KQVSLLliqiTEKENKMKDLTFLLEESRDKANQLEEKT---KLQDENLKELIEKKDHLTKELEDIkmsLQRSMSTQKALE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 885 TDsLKISTR-----LNLLEQELSEKN----------VQLQTSTAEEKTKISEQVEVLQKEKDQ-------LQKRRHNVDE 942
Cdd:pfam05483 317 ED-LQIATKticqlTEEKEAQMEELNkakaahsfvvTEFEATTCSLEELLRTEQQRLEKNEDQlkiitmeLQKKSSELEE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 943 --KLKNGRVLSPEEEHVLFQLEEGIEALEAAIEYRNESIQNRQKSLRASFHNLSRgEANVLEklacLSPVEIRTILFRYF 1020
Cdd:pfam05483 396 mtKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREK-EIHDLE----IQLTAIKTSEEHYL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 1021 NKVVNLREAERKQQLYNEEM----KMKVLERDNMVRELESaldhlklqcdrrLTLQQKEHEQKmqllLHHFKEQDgEGIM 1096
Cdd:pfam05483 471 KEVEDLKTELEKEKLKNIELtahcDKLLLENKELTQEASD------------MTLELKKHQED----IINCKKQE-ERML 533
|
490 500 510
....*....|....*....|....*....|..
gi 429535824 1097 ETFKTYEDKIQQLEKDLYFYKKTSRDHKKKLK 1128
Cdd:pfam05483 534 KQIENLEEKEMNLRDELESVREEFIQKGDEVK 565
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
708-954 |
6.24e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 6.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 708 NLQKLKNSERiltEAKQKMRELTINIKMKEDLIKELIKTGNDAKSVSKQYSlkvtKLEhDAEQAKVELIETQKQLqelen 787
Cdd:COG1340 72 KVKELKEERD---ELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIE----RLE-WRQQTEVLSPEEEKEL----- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 788 kdlsdvamkVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNE---KRANELEQSVDHMKYQKIQLQRKLREENE 864
Cdd:COG1340 139 ---------VEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEeihKKIKELAEEAQELHEEMIELYKEADELRK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 865 KRKQLDAVIKRDQQKIKALNTDSLKISTRLNLLEQELSEKnvqlqtstaeektKISEQVEVLQKEKDQLQKRRHNVDEKL 944
Cdd:COG1340 210 EADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKL-------------RKKQRALKREKEKEELEEKAEEIFEKL 276
|
250
....*....|
gi 429535824 945 KNGRVLSPEE 954
Cdd:COG1340 277 KKGEKLTTEE 286
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
705-884 |
7.85e-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: 40.81 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 705 QELNLQKLKNSERILT---EAKQKMRELTINIKMKEDLIK---ELIKTGNDAKSVSKQYSLKVTKLEHDAEQAKVELIET 778
Cdd:TIGR01612 1069 ELLNKEILEEAEINITnfnEIKEKLKHYNFDDFGKEENIKyadEINKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEI 1148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 779 QKQLQELEnkDLSDVAMKVKLQKEFRKKMDAAKLRVQVLQKKQQDSKKLASLSIQNEKRANELEQSVD-HMKYQKIQLQR 857
Cdd:TIGR01612 1149 KAQINDLE--DVADKAISNDDPEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEVKGiNLSYGKNLGKL 1226
|
170 180
....*....|....*....|....*..
gi 429535824 858 KLREENEKRKQLDAVIKRDQQKIKALN 884
Cdd:TIGR01612 1227 FLEKIDEEKKKSEHMIKAMEAYIEDLD 1253
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
773-1032 |
8.00e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 773 VELIETQKQLQELENKdLSDVAMKVKLQkefRKKMDAAKLRVQVLQKKQQDSKKLASLSIQneKRANELEQSVDHMKYQK 852
Cdd:PRK04863 837 AELRQLNRRRVELERA-LADHESQEQQQ---RSQLEQAKEGLSALNRLLPRLNLLADETLA--DRVEEIREQLDEAEEAK 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 853 IQLQR-------------KLREENEKRKQL-------DAVIKRDQQKIKAL---------------------NTD-SLKI 890
Cdd:PRK04863 911 RFVQQhgnalaqlepivsVLQSDPEQFEQLkqdyqqaQQTQRDAKQQAFALtevvqrrahfsyedaaemlakNSDlNEKL 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 891 STRLNLLEQELSEKNVQLQTSTAEektkISEQVEVLQKEKDQLQKRRHNVDEklkngrvLSPEEEHVLFQLEEGIEALEA 970
Cdd:PRK04863 991 RQRLEQAEQERTRAREQLRQAQAQ----LAQYNQVLASLKSSYDAKRQMLQE-------LKQELQDLGVPADSGAEERAR 1059
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 429535824 971 AieyRNESIQNRqksLRAsfhnlSRGEANVLEKLACLSPVEIRTILFRyfnkvvnLREAERK 1032
Cdd:PRK04863 1060 A---RRDELHAR---LSA-----NRSRRNQLEKQLTFCEAEMDNLTKK-------LRKLERD 1103
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
814-999 |
8.33e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 814 VQVLQKKQQDSKKLASLSIQNEKRANELEQSVDHMKYQKIQLQR--KLREENEKRKQLDAVIKRDQQKIKALNTDSLKis 891
Cdd:PRK12705 22 VVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERnqQRQEARREREELQREEERLVQKEEQLDARAEK-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 892 trLNLLEQELSEKNVQLQTSTAEektkiseqvevlqkekdqLQKRRHNVDEKLKNGRVLSPEEehvlfQLEEGIEALEAA 971
Cdd:PRK12705 100 --LDNLENQLEEREKALSARELE------------------LEELEKQLDNELYRVAGLTPEQ-----ARKLLLKLLDAE 154
|
170 180
....*....|....*....|....*...
gi 429535824 972 IEyrnESIQNRQKSLRASFHNLSRGEAN 999
Cdd:PRK12705 155 LE---EEKAQRVKKIEEEADLEAERKAQ 179
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
800-895 |
8.96e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 37.55 E-value: 8.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 429535824 800 QKEFRKKMDAAKLRVQVLQKKQQdskklaslsiQNEKRANELEQSVDHMKYQKIQLQRKLREENEKRKQLDAVIKRDQQK 879
Cdd:pfam13863 19 REEIERLEELLKQREEELEKKEQ----------ELKEDLIKFDKFLKENDAKRRRALKKAEEETKLKKEKEKEIKKLTAQ 88
|
90
....*....|....*.
gi 429535824 880 IKALNTDSLKISTRLN 895
Cdd:pfam13863 89 IEELKSEISKLEEKLE 104
|
|
| |
