|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
57-406 |
8.64e-162 |
|
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: 496.15 E-value: 8.64e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 57 DYLQVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQCILGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQP 136
Cdd:cd01368 1 DPVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 137 VKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLYTKMNLKPHRSREYLRLsseqekEEIASK 216
Cdd:cd01368 81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGGYSVFVSYIEIYNEYIYDLL------EPSPSS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 217 SAllrqiKERKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSE- 295
Cdd:cd01368 155 PT-----KKRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSd 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 296 -----MSRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSKFQQHVPFRESKLTHYFQ 370
Cdd:cd01368 230 gdvdqDKDQITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQ 309
|
330 340 350
....*....|....*....|....*....|....*.
gi 1841445197 371 SFFNGKGKICMIVNISQCYLAYDETLNVLKFSAIAQ 406
Cdd:cd01368 310 NYFDGEGKASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
60-408 |
2.93e-85 |
|
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: 282.92 E-value: 2.93e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 60 QVCLRIRPFTQSEKELESEGCVHILDSQTVVLkepqcilgRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:smart00129 3 RVVVRVRPLNKREKSRKSPSVVPFPDKVGKTL--------TVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 140 LLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytKMNLKPHRSREYLRLSSEQEKEeiasksaL 219
Cdd:smart00129 75 VLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKR---EEGWQFSVKVSYLEIYNEKIRD-------L 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 220 LrqIKERKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSRV 299
Cdd:smart00129 145 L--NPSSKKLEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 300 IRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKskfQQHVPFRESKLTHYFQSFFNGKGKI 379
Cdd:smart00129 223 GKASKLNLVDLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSK---SRHIPYRDSKLTRLLQDSLGGNSKT 299
|
330 340
....*....|....*....|....*....
gi 1841445197 380 CMIVNISQCYLAYDETLNVLKFSAIAQKV 408
Cdd:smart00129 300 LMIANVSPSSSNLEETLSTLRFASRAKEI 328
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
64-408 |
3.52e-85 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 282.15 E-value: 3.52e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 64 RIRPFTQSEKELESEGCVHILDSQTvvlkepqcILGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLLKG 143
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDS--------ETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 144 QSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmnlkPHRSREYLRLSS-EQEKEEIaskSALL-- 220
Cdd:pfam00225 73 YNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKT--------KERSEFSVKVSYlEIYNEKI---RDLLsp 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 221 RQIKERKmLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQ-IEDSEMSRV 299
Cdd:pfam00225 142 SNKNKRK-LRIREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQrNRSTGGEES 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 300 IRVSELSLCDLAGSERTMKTQN-EGERLRETGNINTSLLTLGKCINVLKnsekSKFQQHVPFRESKLTHYFQSFFNGKGK 378
Cdd:pfam00225 221 VKTGKLNLVDLAGSERASKTGAaGGQRLKEAANINKSLSALGNVISALA----DKKSKHIPYRDSKLTRLLQDSLGGNSK 296
|
330 340 350
....*....|....*....|....*....|
gi 1841445197 379 ICMIVNISQCYLAYDETLNVLKFSAIAQKV 408
Cdd:pfam00225 297 TLMIANISPSSSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
60-406 |
1.79e-81 |
|
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: 271.44 E-value: 1.79e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 60 QVCLRIRPFTQSEKELESEgCVHILDSQTVVLKEPqcilgrlseKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:cd00106 3 RVAVRVRPLNGREARSAKS-VISVDGGKSVVLDPP---------KNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 140 LLKGQSRLIFTYGLTNSGKTYTFQGT-EENIGILPRTLNVLFDSLQERLYTKMNLKPHRSreYLRLSSEQEKEeiasksa 218
Cdd:cd00106 73 ALEGYNGTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKRKETKSSFSVSAS--YLEIYNEKIYD------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 219 LLRqIKERKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSR 298
Cdd:cd00106 144 LLS-PVPKKPLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 299 VIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKskfqQHVPFRESKLTHYFQSFFNGKGK 378
Cdd:cd00106 223 SVTSSKLNLVDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN----KHIPYRDSKLTRLLQDSLGGNSK 298
|
330 340
....*....|....*....|....*...
gi 1841445197 379 ICMIVNISQCYLAYDETLNVLKFSAIAQ 406
Cdd:cd00106 299 TIMIACISPSSENFEETLSTLRFASRAK 326
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
64-408 |
3.54e-63 |
|
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: 219.00 E-value: 3.54e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 64 RIRPFTQSEkelESEGCVHIL----DSQTVVLKepqcilgrlseksSGQMAQK-FSFSKVFGPATTQKEFFQGcIMQPVK 138
Cdd:cd01366 9 RVRPLLPSE---ENEDTSHITfpdeDGQTIELT-------------SIGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlyTKMNLKPHRSREYLRLSSEQEKEEIASKSA 218
Cdd:cd01366 72 SALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKEL--KEKGWSYTIKASMLEIYNETIRDLLAPGNA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 219 llrqikERKMLRLSQD-VKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKIlQIEDsEMS 297
Cdd:cd01366 150 ------PQKKLEIRHDsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-SGRN-LQT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 298 RVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSekskfQQHVPFRESKLTHYFQSFFNGKG 377
Cdd:cd01366 222 GEISVGKLNLVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQK-----QSHIPYRNSKLTYLLQDSLGGNS 296
|
330 340 350
....*....|....*....|....*....|.
gi 1841445197 378 KICMIVNISQCYLAYDETLNVLKFsaiAQKV 408
Cdd:cd01366 297 KTLMFVNISPAESNLNETLNSLRF---ASKV 324
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
60-408 |
9.54e-62 |
|
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: 215.27 E-value: 9.54e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 60 QVCLRIRPFTQSEKeleSEGCvhiLDSQTVVLKEPQCILGRlsekssgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:cd01372 4 RVAVRVRPLLPKEI---IEGC---RICVSFVPGEPQVTVGT---------DKSFTFDYVFDPSTEQEEVYNTCVAPLVDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 140 LLKGQSRLIFTYGLTNSGKTYTFQGT------EENIGILPRTLNVLFDSLQErlytkmnlKPHRSREYLRLSS-EQEKEE 212
Cdd:cd01372 69 LFEGYNATVLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEK--------KKDTFEFQLKVSFlEIYNEE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 213 IasKSALLRQIKERKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQ-- 290
Cdd:cd01372 141 I--RDLLDPETDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQtk 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 291 --IEDSEMSRVIR----VSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKFQQHVPFRESK 364
Cdd:cd01372 219 knGPIAPMSADDKnstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISAL--GDESKKGAHVPYRDSK 296
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1841445197 365 LTHYFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFSAIAQKV 408
Cdd:cd01372 297 LTRLLQDSLGGNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
59-408 |
1.21e-60 |
|
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: 212.20 E-value: 1.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 59 LQVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQCILGRLSEKSSGQMAQ-------KFSFSKVFGPATTQKEFFQG 131
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGFFHGGSNNRDRRkrrnkelKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 132 CIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlyTKMNLKPHRSREYLRLSSEQEKE 211
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIES---LKDEKEFEVSMSYLEIYNETIRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 212 eiasksaLLrqIKERKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQI 291
Cdd:cd01370 159 -------LL--NPSSGPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 292 E-DSEMSRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKFQQHVPFRESKLTHYFQ 370
Cdd:cd01370 230 DkTASINQQVRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINAL--ADPGKKNKHIPYRDSKLTRLLK 307
|
330 340 350
....*....|....*....|....*....|....*...
gi 1841445197 371 SFFNGKGKICMIVNISQCYLAYDETLNVLKFSAIAQKV 408
Cdd:cd01370 308 DSLGGNCRTVMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
59-405 |
5.38e-60 |
|
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: 210.64 E-value: 5.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 59 LQVCLRIRPFTQSEKELESEGCVHILDSQtvvlKEPQCILGRLSEKSSgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVK 138
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVR----KEVSVRTGGLADKSS---TKTYTFDMVFGPEAKQIDVYRSVVCPILD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTE-----------ENIGILPRTLNVLFDSLqERLYTKMNLKPhrsrEYLRLSSE 207
Cdd:cd01364 77 EVLMGYNCTIFAYGQTGTGKTYTMEGDRspneeytweldPLAGIIPRTLHQLFEKL-EDNGTEYSVKV----SYLEIYNE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 208 QEKEEIASKSALlrqikeRKMLRLSQDV--KGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFT 285
Cdd:cd01364 152 ELFDLLSPSSDV------SERLRMFDDPrnKRGVIIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 286 VKILQIE-DSEMSRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKfqqHVPFRESK 364
Cdd:cd01364 226 ITIHIKEtTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL--VERAP---HVPYRESK 300
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1841445197 365 LTHYFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFSAIA 405
Cdd:cd01364 301 LTRLLQDSLGGRTKTSIIATISPASVNLEETLSTLEYAHRA 341
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
60-408 |
1.67e-59 |
|
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: 207.96 E-value: 1.67e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 60 QVCLRIRPFTQSEKELEsEGCVHILDSQTVVLKEPQcilgrlsekssgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:cd01374 3 TVTVRVRPLNSREIGIN-EQVAWEIDNDTIYLVEPP--------------STSFTFDHVFGGDSTNREVYELIAKPVVKS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 140 LLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmnlkpHRSREYL-RLSS-EQEKEEIASks 217
Cdd:cd01374 68 ALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD----------TPDREFLlRVSYlEIYNEKIND-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 218 aLLRqiKERKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMS 297
Cdd:cd01374 136 -LLS--PTSQNLKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELE 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 298 RV-IRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNsekSKFQQHVPFRESKLTHYFQSFFNGK 376
Cdd:cd01374 213 EGtVRVSTLNLIDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE---GKVGGHIPYRDSKLTRILQPSLGGN 289
|
330 340 350
....*....|....*....|....*....|..
gi 1841445197 377 GKICMIVNISQCYLAYDETLNVLKFSAIAQKV 408
Cdd:cd01374 290 SRTAIICTITPAESHVEETLNTLKFASRAKKI 321
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
57-408 |
7.69e-54 |
|
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: 192.29 E-value: 7.69e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 57 DYLQVCLRIRPFTQSEKeleSEGCVHILD----SQTVVLKEPqcilgrlsEKSSGQMAQKFSFSKVFGPATTQKEFFQGC 132
Cdd:cd01371 1 ENVKVVVRCRPLNGKEK---AAGALQIVDvdekRGQVSVRNP--------KATANEPPKTFTFDAVFDPNSKQLDVYDET 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 133 IMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSLQerlytkmnlKPHRSREYLRLSSEQE 209
Cdd:cd01371 70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKredPELRGIIPNSFAHIFGHIA---------RSQNNQQFLVRVSYLE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 210 --KEEIasKSALLRQIKERKMLRLSQDVKGYsfIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVK 287
Cdd:cd01371 141 iyNEEI--RDLLGKDQTKRLELKERPDTGVY--VKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTIT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 288 IlqiEDSEM----SRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSeKSkfqQHVPFRES 363
Cdd:cd01371 217 I---ECSEKgedgENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG-KS---THIPYRDS 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1841445197 364 KLTHYFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFSAIAQKV 408
Cdd:cd01371 290 KLTRLLQDSLGGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
59-401 |
2.21e-52 |
|
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: 187.54 E-value: 2.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 59 LQVCLRIRPFTQSEKELESEGCVHILDSQTVVLkepqcilgRLSEKSSgqmaqKFSFSKVFGPATTQKEFFQGCIMQPVK 138
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVI--------ATSETGK-----TFSFDRVFDPNTTQEDVYNFAAKPIVD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 139 DLLKGQSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSLQerlytKM--NLKPHRSREYLRLSSEQEKEEI 213
Cdd:cd01369 71 DVLNGYNGTIFAYGQTSSGKTYTMEGKlgdPESMGIIPRIVQDIFETIY-----SMdeNLEFHVKVSYFEIYMEKIRDLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 214 A-SKSALlrQIKERKmlrlSQDVkgysFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQiE 292
Cdd:cd01369 146 DvSKTNL--SVHEDK----NRGP----YVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-E 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 293 DSEmSRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSkfqqHVPFRESKLTHYFQSF 372
Cdd:cd01369 215 NVE-TEKKKSGKLYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKT----HIPYRDSKLTRILQDS 289
|
330 340
....*....|....*....|....*....
gi 1841445197 373 FNGKGKICMIVNISQCYLAYDETLNVLKF 401
Cdd:cd01369 290 LGGNSRTTLIICCSPSSYNESETLSTLRF 318
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
60-408 |
1.76e-51 |
|
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: 186.40 E-value: 1.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 60 QVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQcilGRLSEKSSGQMAQKFSFSKVF------GPA-TTQKEFFQGC 132
Cdd:cd01365 4 KVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQ---ADKNNKATREVPKSFSFDYSYwshdseDPNyASQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 133 IMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLYTKMNLKPHRSreYLRLSSEQEKEE 212
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLFSRIADTTNQNMSYSVEVS--YMEIYNEKVRDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 213 IASKSAllrqiKERKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQI- 291
Cdd:cd01365 159 LNPKPK-----KNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKr 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 292 -EDSEMSRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVL---KNSEKSKFQQHVPFRESKLTH 367
Cdd:cd01365 234 hDAETNLTTEKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmSSGKSKKKSSFIPYRDSVLTW 313
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1841445197 368 YFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFSAIAQKV 408
Cdd:cd01365 314 LLKENLGGNSKTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
59-403 |
7.64e-49 |
|
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: 177.31 E-value: 7.64e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 59 LQVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQcilgrlseksSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVK 138
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPR----------NHGETLKYQFDAFYGEESTQEDIYAREVQPIVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFdslqeRLYTKMNLKPHRSREYLRLSSEQEKEEIASKSa 218
Cdd:cd01376 72 HLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTVMDLL-----QMTRKEAWALSFTMSYLEIYQEKILDLLEPAS- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 219 llrqikerKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSR 298
Cdd:cd01376 146 --------KELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFR 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 299 VIRvSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKskfqqHVPFRESKLTHYFQSFFNGKGK 378
Cdd:cd01376 218 QRT-GKLNLIDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLP-----RIPYRDSKLTRLLQDSLGGGSR 291
|
330 340
....*....|....*....|....*
gi 1841445197 379 ICMIVNISQCYLAYDETLNVLKFSA 403
Cdd:cd01376 292 CIMVANIAPERTFYQDTLSTLNFAA 316
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
57-401 |
8.13e-48 |
|
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: 175.39 E-value: 8.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 57 DYLQVCLRIRPFTQSEKELESEGCVHILDSQTVVLkepqcilgrlseksSGQMAQKFSFSKVFGPATTQKEFFQGCIMQP 136
Cdd:cd01373 1 DAVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVL--------------HSKPPKTFTFDHVADSNTNQESVFQSVGKPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 137 VKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENI--------GILPRTLNVLFDSLQ-ERLYTKMNLKPHRSREYLRLSSE 207
Cdd:cd01373 67 VESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQrEKEKAGEGKSFLCKCSFLEIYNE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 208 QEKEEIASKSAllrqikerkMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVK 287
Cdd:cd01373 147 QIYDLLDPASR---------NLKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 288 ILQIEDSEMSRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSKfQQHVPFRESKLTH 367
Cdd:cd01373 218 IESWEKKACFVNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGK-QRHVCYRDSKLTF 296
|
330 340 350
....*....|....*....|....*....|....
gi 1841445197 368 YFQSFFNGKGKICMIVNISQCYLAYDETLNVLKF 401
Cdd:cd01373 297 LLRDSLGGNAKTAIIANVHPSSKCFGETLSTLRF 330
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
105-527 |
2.12e-46 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 177.24 E-value: 2.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 105 SSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQ 184
Cdd:COG5059 50 LEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 185 ERlytKMNLKPHRSREYLrlssEQEKEEIASksaLLRQIKERKMLRLsqDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIK 264
Cdd:COG5059 130 DL---SMTKDFAVSISYL----EIYNEKIYD---LLSPNEESLNIRE--DSLLGVKVAGLTEKHVSSKEEILDLLRKGEK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 265 HQSVAFTKLNNASSRSHSIFTVKiLQIEDSEMSrVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCIN 344
Cdd:COG5059 198 NRTTASTEINDESSRSHSIFQIE-LASKNKVSG-TSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVIN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 345 VLKNSEKSKfqqHVPFRESKLTHYFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFSAIAQK------VCVPDTLNSSQ 418
Cdd:COG5059 276 ALGDKKKSG---HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASRAKSiknkiqVNSSSDSSREI 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 419 EKLFGPVKSSQDVSLDSNSNSKILNVKRATISWENSLEDLMEDEDLVEELENAEETQNV----ETKLLDEDLDKTLEENK 494
Cdd:COG5059 353 EEIKFDLSEDRSEIEILVFREQSQLSQSSLSGIFAYMQSLKKETETLKSRIDLIMKSIIsgtfERKKLLKEEGWKYKSTL 432
|
410 420 430
....*....|....*....|....*....|....
gi 1841445197 495 AFISHEEKRKLLDLIEDLKKKLINE-KKEKLTLE 527
Cdd:COG5059 433 QFLRIEIDRLLLLREEELSKKKTKIhKLNKLRHD 466
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
61-404 |
4.27e-40 |
|
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: 152.06 E-value: 4.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 61 VCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQCILgRLSEKSSgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVKDL 140
Cdd:cd01367 4 VCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKV-DLTKYIE---NHTFRFDYVFDESSSNETVYRSTVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 141 LKGQSRLIFTYGLTNSGKTYT----FQGTEENIGI-------LPRTLNVLFDSLQERLYTKMNlkphrsreylrlsseqe 209
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTmggdFSGQEESKGIyalaardVFRLLNKLPYKDNLGVTVSFF----------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 210 keEIASKSA--LLrqiKERKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVK 287
Cdd:cd01367 143 --EIYGGKVfdLL---NRKKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQII 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 288 ILQIEDSEMSrvirvSELSLCDLAGSERTMKT-QNEGERLRETGNINTSLLTLGKCINVLKNSekskfQQHVPFRESKLT 366
Cdd:cd01367 218 LRDRGTNKLH-----GKLSFVDLAGSERGADTsSADRQTRMEGAEINKSLLALKECIRALGQN-----KAHIPFRGSKLT 287
|
330 340 350
....*....|....*....|....*....|....*....
gi 1841445197 367 HYFQ-SFFNGKGKICMIVNISQCYLAYDETLNVLKFSAI 404
Cdd:cd01367 288 QVLKdSFIGENSKTCMIATISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
59-403 |
6.94e-40 |
|
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: 151.96 E-value: 6.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 59 LQVCLRIRPFTQSEKELESEGcvhiLDSQTVVLKEPQCIlgRLSEKSSGQMAQKFSFSKVFGPATtQKEFFQGCIMQPVK 138
Cdd:cd01375 2 VQAFVRVRPTDDFAHEMIKYG----EDGKSISIHLKKDL--RRGVVNNQQEDWSFKFDGVLHNAS-QELVYETVAKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTEENI---GILPRTLNVLFDSLQERlYTKMnLKPHRSreYLRLSSEQEKEEIAS 215
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENYkhrGIIPRALQQVFRMIEER-PTKA-YTVHVS--YLEIYNEQLYDLLST 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 216 KSALLRQIKERKMLrlsQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSE 295
Cdd:cd01375 151 LPYVGPSVTPMTIL---EDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 296 MSRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKfqQHVPFRESKLTHYFQSFFNG 375
Cdd:cd01375 228 SSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIAL--SDKDR--THVPFRQSKLTHVLRDSLGG 303
|
330 340
....*....|....*....|....*...
gi 1841445197 376 KGKICMIVNISQCYLAYDETLNVLKFSA 403
Cdd:cd01375 304 NCNTVMVANIYGEAAQLEETLSTLRFAS 331
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
92-408 |
3.30e-32 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 137.37 E-value: 3.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 92 KEPQCILGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQG-----TE 166
Cdd:PLN03188 113 EEGEMIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglLE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 167 ENI-----GILPRTLNVLFDSLQERL--YTKMNLKPHRSREYLRLSSEQEKEeiasksaLLRQIKERKMLRlsQDVKGYS 239
Cdd:PLN03188 193 EHLsgdqqGLTPRVFERLFARINEEQikHADRQLKYQCRCSFLEIYNEQITD-------LLDPSQKNLQIR--EDVKSGV 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 240 FIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTV----KILQIEDSEMSrvIRVSELSLCDLAGSER 315
Cdd:PLN03188 264 YVENLTEEYVKTMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCvvesRCKSVADGLSS--FKTSRINLVDLAGSER 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 316 TMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSKFQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQCYLAYDET 395
Cdd:PLN03188 342 QKLTGAAGDRLKEAGNINRSLSQLGNLINILAEISQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSET 421
|
330
....*....|...
gi 1841445197 396 LNVLKFSAIAQKV 408
Cdd:PLN03188 422 FSTLRFAQRAKAI 434
|
|
| RBD_KIF20B |
cd21786 |
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ... |
529-583 |
1.89e-19 |
|
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B (also called cancer/testis antigen 90 (CT90), kinesin family member 20B, kinesin-related motor interacting with PIN1, or M-phase phosphoprotein 1 (MPP1)) is a plus-end-directed motor enzyme that is required for completion of cytokinesis. It is required for proper midbody organization and abscission in polarized cortical stem cells. KIF20B plays a role in the regulation of neuronal polarization by mediating the transport of specific cargos. It participates in the mobilization of SHTN1 (shootin 1) and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, KIF20B cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. KIF20B acts as an oncogene for promoting bladder cancer cell proliferation, apoptosis inhibition, and carcinogenic progression. This model corresponds to a conserved region in KIF20B that shows some sequence similarity to the RAB6 binding domain (RBD) of KIF20A. KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.
Pssm-ID: 409644 [Multi-domain] Cd Length: 56 Bit Score: 83.30 E-value: 1.89e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1841445197 529 KIREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREE 583
Cdd:cd21786 1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNKTAKEEE 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1006-1280 |
8.85e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.02 E-value: 8.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1006 QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLkEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGV 1085
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1086 TCYKAKIKELETILETQKVEcshSAKLEQDILEKESIILKLERNLKEFQEHLQDsvkntkdLNVKELKLKEEITQLTNNL 1165
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAE---IEELEAQIEQLKEELKALREALDELRAELTL-------LNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1166 QDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLL 1245
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270
....*....|....*....|....*....|....*
gi 1841445197 1246 RIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQ 1280
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
558-1387 |
2.50e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.48 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 558 EILEENAERRLAIFKDLVG--KCDTR-EEAAKDIcatkVETEEthNYVGFEDIIDSLQDNVADIKKQAEIAHLYI---AS 631
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAGisKYKERrKETERKL----ERTRE--NLDRLEDILNELERQLKSLERQAEKAERYKelkAE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 632 LPDPQEATACLELK-FNQIKAELAKTKGELIKTKEELKKRENESDSLIQELETS----NKKIITQNQRIKELINIIDQKE 706
Cdd:TIGR02168 222 LRELELALLVLRLEeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEvselEEEIEELQKELYALANEISRLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 707 DTINEFQNLKSHMENTFKcndKADTSSLIINNKLICNETVEvpKDSKSKICSERKRVNENELQQDEPPAKKGSIHvsSAI 786
Cdd:TIGR02168 302 QQKQILRERLANLERQLE---ELEAQLEELESKLDELAEEL--AELEEKLEELKEELESLEAELEELEAELEELE--SRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 787 TEDQKKSEEVRPNIAEIEdirvLQENneglrafLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLsKEVQQIQ 866
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLE----LQIA-------SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL-KELQAEL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 867 SNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKlmhTKIDELRTLdsvsqisnidLLNLRDLSNGse 946
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ---ARLDSLERL----------QENLEGFSEG-- 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 947 EDNLPNTQLDLLGNDYLVSKQVK---EY----------RIQEP--NRENSFHSSIEAIWEECKEIVK---ASSKKSHQIE 1008
Cdd:TIGR02168 508 VKALLKNQSGLSGILGVLSELISvdeGYeaaieaalggRLQAVvvENLNAAKKAIAFLKQNELGRVTflpLDSIKGTEIQ 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1009 ELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLL------KEKETLIQQLKE-ELQEKNVTLD---VQIQHVVEGKRAl 1078
Cdd:TIGR02168 588 GNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvvDDLDNALELAKKlRPGYRIVTLDgdlVRPGGVITGGSA- 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1079 sELTQGVTCYKAKIKELETILEtqkvecshsaKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEI 1158
Cdd:TIGR02168 667 -KTNSSILERRREIEELEEKIE----------ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1159 TQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVM 1238
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1239 RDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQV 1318
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI--ESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1319 EQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNL-QDELQESEQKYNAD 1387
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKI 963
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
669-1279 |
1.67e-12 |
|
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: 72.75 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 669 KRENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNlkshMENTFKCNDKADTSSLIINNKLICNETVEV 748
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNN----KIKILEQQIKDLNDKLKKNKDKINKLNSDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 749 PK-DSKSKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVRPNIAEIEDIRVLQENnegLRAFLLTIENEL 827
Cdd:TIGR04523 106 SKiNSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE---LENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 828 KNEKEEKAELNKQIVHFQQELSLSEKKN----------LTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEI 897
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIqknkslesqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 898 ETATRSITNNVSQIKLMHTKIDELRtlDSVSQISNidllNLRDLSNGSEEDNLPNTQLDLLGNDylvsKQVKEYRIQEPN 977
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELE--KQLNQLKS----EISDLNNQKEQDWNKELKSELKNQE----KKLEEIQNQISQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 978 RE---NSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLK------EKEHKNQDDLLKEKET 1048
Cdd:TIGR04523 333 NNkiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLEsqindlESKIQNQEKLNQQKDE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1049 LIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVECS-----------HSAKLEQDIL 1117
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqNLEQKQKELK 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1118 EKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLL---------QLKEEEEETNRQETEK 1188
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEE 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1189 LKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQR 1268
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
650
....*....|.
gi 1841445197 1269 TIQQLKEQLNN 1279
Cdd:TIGR04523 653 TIKEIRNKWPE 663
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1007-1292 |
3.12e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1007 IEELEQQIEKL--QAEV----KGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQH----VVEGKR 1076
Cdd:COG1196 195 LGELERQLEPLerQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEleaeLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1077 ALSELTQGVTCYKAKIKELETILETQKVECSHSAKLEQDILEKesiILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKE 1156
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER---LEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1157 EITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVS 1236
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1841445197 1237 VMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERA 1292
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
|
| RBD_KIF20A-like |
cd21744 |
RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; ... |
529-583 |
6.49e-12 |
|
RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; This family includes kinesin-like proteins KIF20A and KIF20B. KIF20A (also called GG10_2, mitotic kinesin-like protein 2 (MKlp2), Rab6-interacting kinesin-like protein, or rabkinesin-6) is a mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1 (polo-like kinase 1), it is involved in recruitment of PLK1 to the central spindle. KIF20A interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. It may act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. KIF20A has a microtubule plus-end-directed motility. KIF20B (also called cancer/testis antigen 90 (CT90), kinesin family member 20B, kinesin-related motor interacting with PIN1, or M-phase phosphoprotein 1 (MPP1)) is a plus-end-directed motor enzyme that is required for completion of cytokinesis. It is required for proper midbody organization and abscission in polarized cortical stem cells. KIF20B plays a role in the regulation of neuronal polarization by mediating the transport of specific cargoes. It participates in the mobilization of SHTN1 and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, KIF20B cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. This model corresponds to a conserved domain in the KIF20A subfamily, that shows RAB6 binding ability and has been called the RAB6 binding domain (RBD). KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.
Pssm-ID: 409643 [Multi-domain] Cd Length: 56 Bit Score: 62.09 E-value: 6.49e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1841445197 529 KIREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREE 583
Cdd:cd21744 1 RIREEVSEEFEEQFALMEEDYEERLENEKEILEERYEKRLEIRKELIKKLSAALE 55
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1005-1290 |
7.39e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.74 E-value: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1005 HQIEELEQQIEKLQAEVKGYKDENNRLKEKehknqddlLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQG 1084
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAE--------LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1085 VTCYKAKIKELETILETQKVECshsAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNN 1164
Cdd:COG1196 304 IARLEERRRELEERLEELEEEL---AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1165 LQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKL 1244
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1841445197 1245 LRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKveEAIQQYE 1290
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLL--EAEADYE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
982-1340 |
4.40e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.17 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 982 FHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEkn 1061
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQ-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1062 vtLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVEcsHSAKLEQDILEKESIILKLERNLKEFQEHLQDSV 1141
Cdd:TIGR02169 246 --LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE--EQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1142 KNTKDLNVKELKLKEEITQLTNNLQDMKhllqlkeeeeetnrQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKL 1221
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEER--------------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1222 TDAKKQIKQVQKEvsvmrdedkllrikINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKEK 1301
Cdd:TIGR02169 388 KDYREKLEKLKRE--------------INELKRELDRLQEELQRLSEELADLNAAI--AGIEAKINELEEEKEDKALEIK 451
|
330 340 350
....*....|....*....|....*....|....*....
gi 1841445197 1302 IIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEK 1340
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1209-1512 |
8.76e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 8.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1209 RKEEDYADLKEKLTDAKKQIKQVQKEVsvMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN--NQKVEEAI 1286
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRE--LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEelELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1287 QQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHEnntdv 1366
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE----- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1367 lgkltnLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEmkkyAEDRERFFKQQNEMEILTAQLTEKDSDLQK 1446
Cdd:COG1196 363 ------AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL----EELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1841445197 1447 WREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPKRISSADPDKLQTE 1512
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1002-1431 |
3.29e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1002 KKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDdlLKEKETLIQQLKEELqeKNVTLDVQIQHVVEGKRALSEL 1081
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE--AKAKKEELERLKKRL--TGLTPEKLEKELEELEKAKEEI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1082 TQGVTCYKAKIKELETILETQK--VECSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEIT 1159
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKkaIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1160 QLTNNLQDMKHLLQLKEEEEETNRqetekLKEELSASSARtqnlkaDLQRKEEDYADLKEKLTDAKKQIKQVQKEVSvmr 1239
Cdd:PRK03918 484 ELEKVLKKESELIKLKELAEQLKE-----LEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELE--- 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1240 dedkllriKINELEKKKNQCSQELDMKQRTIQQLKEQLNN------QKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQ 1313
Cdd:PRK03918 550 --------KLEELKKKLAELEKKLDELEEELAELLKELEElgfesvEELEERLKELEPFYNEYLELKDAEKELEREEKEL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1314 EQTQVEqdqvLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGK----LTNLQDELQESEQKYNADRK 1389
Cdd:PRK03918 622 KKLEEE----LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRelagLRAELEELEKRREEIKKTLE 697
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1841445197 1390 KWLEEKMMLITQAKEAENIrNKEMKKYAEDRERFFKQQNEME 1431
Cdd:PRK03918 698 KLKEELEEREKAKKELEKL-EKALERVEELREKVKKYKALLK 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
953-1497 |
3.29e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 953 TQLDLLGNDYLVSKQVKEYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLK 1032
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1033 ----------------EKEHKNQDDLLKEKETLIQQLKEELQ--EKNVTLDVQIQHVVEGKRALSELTQGvtcYKAKIKE 1094
Cdd:PRK03918 235 elkeeieelekeleslEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEE---YLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1095 LETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQ---EHLQDSVKNTKDLNVKELKLKEEITQLTN-NLQDMKH 1170
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTGlTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1171 LLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQR---------------KEEDYADLKEKLTdakKQIKQVQKEV 1235
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEYT---AELKRIEKEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1236 SVMRDEDKLLRIKINELEKKKNQCSQELDMKQrTIQQLKE------QLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMT 1309
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIKLKE-LAEQLKEleeklkKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1310 LEEQEQTQVEQDqVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRK 1389
Cdd:PRK03918 548 LEKLEELKKKLA-ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1390 KWLEEKMMLITQAKEAENIRNK-EMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEiQLKALISS 1468
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKElEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE-KLKEELEE 705
|
570 580
....*....|....*....|....*....
gi 1841445197 1469 NVQKDNEIEQLKRIISETSKIETQIMDIK 1497
Cdd:PRK03918 706 REKAKKELEKLEKALERVEELREKVKKYK 734
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
558-1440 |
3.43e-10 |
|
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: 65.38 E-value: 3.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 558 EILEENAERRLAIFKDLVGKCDTREEAAKdicATKVETEETHNYVGFEDIIDSLQDNVADIKKQAEIAhlyiasLPDPQE 637
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSRLKRKKKE---ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKA------LEYYQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 638 ATACLELKFNQIKAELAKTKGELIKTKEELKKRENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNLKs 717
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 718 hmentfkCNDKADTSSLIINNKLICNETVEVPKDSKSKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVR 797
Cdd:pfam02463 295 -------EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 798 PNIAEIEDIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQSnyDIAIAELH 877
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE--SIELKQGK 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 878 VQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRTLDSVsqisniDLLNLRDLSNGSEEDNLPNTQLDL 957
Cdd:pfam02463 446 LTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL------EERSQKESKARSGLKVLLALIKDG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 958 LGNDyLVSKQVKEYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHK 1037
Cdd:pfam02463 520 VGGR-IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1038 NQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKI-------KELETILETQKVECSHSA 1110
Cdd:pfam02463 599 IDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSleeglaeKSEVKASLSELTKELLEI 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1111 KLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLK 1190
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1191 EELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTI 1270
Cdd:pfam02463 759 KEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1271 QQLKEQLNNQKvEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLET 1350
Cdd:pfam02463 839 ALELKEEQKLE-KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1351 KNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEM 1430
Cdd:pfam02463 918 EIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEK 997
|
890
....*....|
gi 1841445197 1431 EILTAQLTEK 1440
Cdd:pfam02463 998 ERLEEEKKKL 1007
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
838-1498 |
8.01e-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: 64.31 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 838 NKQIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTK 917
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 918 IDEL-RTLDSVSQISNIDLLNLRDLSNGSEEDNlpnTQLDLLgndylvSKQVKEYRIQEPNRENSFHSSIEAIWEECKEI 996
Cdd:TIGR02168 318 LEELeAQLEELESKLDELAEELAELEEKLEELK---EELESL------EAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 997 VKASSKK---SHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLK----EKETLIQQLKEELQEKNVTLDVQIQ 1069
Cdd:TIGR02168 389 AQLELQIaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQaeleELEEELEELQEELERLEEALEELRE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1070 HVVEGKRALSELTQGVTCYKAKIKELETILETQK---------------------------------------------- 1103
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvkallknqsglsgilgvlselisvdegyeaaieaalggrlq 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1104 ---VECSHSAKLEQDILEKESIIL------------KLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQL------T 1162
Cdd:TIGR02168 549 avvVENLNAAKKAIAFLKQNELGRvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1163 NNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSAR------TQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVS 1236
Cdd:TIGR02168 629 DDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSaktnssILERRREIEELEEKIEELEEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1237 VMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVE-----EAIQQYERACKDLNVKEKIIEDMRMTLE 1311
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKElteleAEIEELEERLEEAEEELAEAEAEIEELE 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1312 EQEQTQVEQDQVLEAKL----EEVERLATELEKWKEKCNDLE------TKNNQRSNKEHENNTDVLGKLTNLQDELQESE 1381
Cdd:TIGR02168 789 AQIEQLKEELKALREALdelrAELTLLNEEAANLRERLESLErriaatERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1382 QKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAAL--- 1458
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsee 948
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1841445197 1459 -EIQLKALISSNVQKDNEIEQLKRiisETSKIETQIMDIKP 1498
Cdd:TIGR02168 949 ySLTLEEAEALENKIEDDEEEARR---RLKRLENKIKELGP 986
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1215-1480 |
1.99e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1215 ADLKEKLTDAKKQIKQVQKEVSVMRDEDklLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN-----NQKVEEAIQQY 1289
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQELEEKLEelrleVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1290 ERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVER----LATELEKWKEKCNDLEtknnqrsnkehENNTD 1365
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldeLAEELAELEEKLEELK-----------EELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1366 VLGKLTNLQDELQESEQKYNADRKKWLEEKmmlitqakeaenirnkemKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQ 1445
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLR------------------SKVAQLELQIASLNNEIERLEARLERLEDRRE 417
|
250 260 270
....*....|....*....|....*....|....*.
gi 1841445197 1446 KWREERDQLVAAL-EIQLKALISSNVQKDNEIEQLK 1480
Cdd:TIGR02168 418 RLQQEIEELLKKLeEAELKELQAELEELEEELEELQ 453
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
983-1301 |
5.96e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 5.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 983 HSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKehknqddlLKEKETLIQQLKEELQEKNV 1062
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR--------IEELEEDLHKLEEALNDLEA 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1063 TLDVQIQHVVEGKraLSELTQGVTCYKAKIKELETILETQKVEcshSAKLEQDILEKESIILKLERNLKEFQEHLQDSVK 1142
Cdd:TIGR02169 787 RLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLE---KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1143 NTKDLNVKELKLKEEITQLTNNLQDMKhllqlkeeeeetnrQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLT 1222
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLK--------------KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1223 DAKKQIKQVQKEVSVMrdedkllrIKINELEKKKNQCSQELDMKQRTIQQLkEQLNNQkveeAIQQYERACKDLN-VKEK 1301
Cdd:TIGR02169 928 ALEEELSEIEDPKGED--------EEIPEEELSLEDVQAELQRVEEEIRAL-EPVNML----AIQEYEEVLKRLDeLKEK 994
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1084-1481 |
6.74e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1084 GVTCYKAKIKE-LETILETQkvecshsAKLE--QDIL-EKESIILKLER---------NLKEFQEHLQDS--VKNTKDLN 1148
Cdd:COG1196 166 GISKYKERKEEaERKLEATE-------ENLErlEDILgELERQLEPLERqaekaeryrELKEELKELEAEllLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1149 VKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQI 1228
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1229 KQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNN--QKVEEAIQQYERACKDLNVKEKIIEDM 1306
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEaeAELAEAEEELEELAEELLEALRAAAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1307 RMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNA 1386
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1387 DRKKwleekmmlitQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALI 1466
Cdd:COG1196 479 LAEL----------LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
410 420
....*....|....*....|
gi 1841445197 1467 SSNVQKDNE-----IEQLKR 1481
Cdd:COG1196 549 QNIVVEDDEvaaaaIEYLKA 568
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
961-1275 |
7.12e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.85 E-value: 7.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 961 DYLVSKQVKEYRIQEPNRENsFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGY-KDENNRLKEKEHKNQ 1039
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEA-IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1040 DDL--LKEKETLIQQLKEELQEKNVTLDVQIQHvvegkralseltqgvtcYKAKIKELETILETQKVEcshSAKLEQDIL 1117
Cdd:TIGR02169 301 AEIasLERSIAEKERELEDAEERLAKLEAEIDK-----------------LLAEIEELEREIEEERKR---RDKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1118 EKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLqdmkhllqlkeeeeetnrqetEKLKEELSASS 1197
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL---------------------DRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1198 ARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRD-----EDKLLRIK--INELEKKKNQCSQELDMKQRTI 1270
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAdlskyEQELYDLKeeYDRVEKELSKLQRELAEAEAQA 499
|
....*
gi 1841445197 1271 QQLKE 1275
Cdd:TIGR02169 500 RASEE 504
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1007-1415 |
8.30e-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: 60.42 E-value: 8.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1007 IEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDL------LKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSE 1080
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEInektteISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1081 LTQGVTCYKAKI------------KELETILETQKVECSHS-----------AKLEQDILEKESIILKLERNLKEFQEHL 1137
Cdd:TIGR04523 286 LEKQLNQLKSEIsdlnnqkeqdwnKELKSELKNQEKKLEEIqnqisqnnkiiSQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1138 QDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADL 1217
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1218 KEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQlnNQKVEEAIQQYERACKDLN 1297
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE--KKELEEKVKDLTKKISSLK 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1298 VKEKIiedmrmtLEEQEQTQVEQDQVLEAKLEEVerlatELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDEL 1377
Cdd:TIGR04523 524 EKIEK-------LESEKKEKESKISDLEDELNKD-----DFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
410 420 430
....*....|....*....|....*....|....*...
gi 1841445197 1378 QESEQKYNADRKKwLEEKMMLITQAKEAENIRNKEMKK 1415
Cdd:TIGR04523 592 DQKEKEKKDLIKE-IEEKEKKISSLEKELEKAKKENEK 628
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1006-1350 |
2.08e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1006 QIEELEQQIEKLQAEVKGYKDENNRLkEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGV 1085
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRI-ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1086 TCYKAKIKELETILEtQKVECSHSAKLEQDILEKE---SIILKLERNLKEFQEHLQDSVKNTKDLNVKELKL---KEEIT 1159
Cdd:TIGR02169 754 ENVKSELKELEARIE-ELEEDLHKLEEALNDLEARlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLtleKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1160 QLTNNLQDMKHLLQLKEEEeetnrqetekLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSvmr 1239
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKS----------IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR--- 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1240 dedkllrikinELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEA-IQQYERACKDLNVKEKIIEDMRMTLEEQEQTQV 1318
Cdd:TIGR02169 900 -----------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSeIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
330 340 350
....*....|....*....|....*....|..
gi 1841445197 1319 EQDQVLEAKLEEVERLATELEKWKEKCNDLET 1350
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
466-1292 |
4.31e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 58.44 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 466 EELENAEETQNVETKLLDED-------LDKTLEENKAFISHEEKRKLLDLIEDLKKKLINEKKEKLTLEFKIREEVTQEF 538
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLeelklqeLKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 539 TQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREEAAKDICATKVETEETHNYVGF--------EDIIDS 610
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKEsekekkkaEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 611 LQDNVADIKKQAEIAHLYIASLPDPQEATACLELKFNQIKAELAKTKGELIKTKEELKKRENESDSLIQELETSNKKII- 689
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLe 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 690 ---TQNQRIKELINIIDQKEDTINEFQNLKSHMENtfKCNDKADTSSLIINNKLICNETVEVPKDSKSKICSERKRVNEN 766
Cdd:pfam02463 413 larQLEDLLKEEKKEELEILEEEEESIELKQGKLT--EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 767 ELQQDEPPAKKGSIHVSSAITEDQKKSEEVRPNIAEIEDIRVLQENNEGlrAFLLTIENELKNEKEEKAELNKQIVHFQQ 846
Cdd:pfam02463 491 SRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE--NYKVAISTAVIVEVSATADEVEERQKLVR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 847 ELSLSEKKNLTLSKEVQQIQSNyDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRTLDS 926
Cdd:pfam02463 569 ALTELPLGARKLRLLIPKLKLP-LKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESG 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 927 VSQISNIDLLNLRDLSNGSEEDNLPNTQLDllgndylvskqvkeyrIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQ 1006
Cdd:pfam02463 648 LRKGVSLEEGLAEKSEVKASLSELTKELLE----------------IQELQEKAESELAKEEILRRQLEIKKKEQREKEE 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1007 IEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVT 1086
Cdd:pfam02463 712 LKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1087 CY---KAKIKELETILETQKVECSHSAKLEQDILEKESI-ILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLT 1162
Cdd:pfam02463 792 KEeklKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIkEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1163 NNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDED 1242
Cdd:pfam02463 872 LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKE 951
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1243 KLLrIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERA 1292
Cdd:pfam02463 952 ENN-KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERL 1000
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1006-1465 |
4.84e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1006 QIEELEQQIEKLQAEVKGYKDENNRLKEkEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGV 1085
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1086 TCYKAKIKELETILETQKVEcshSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNL 1165
Cdd:COG1196 396 AELAAQLEELEEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1166 QDMKHLLQLKEEEEETNRQETEKLKE-----ELSASSARTQNLKADLQRKEEDYADL--KEKLTDAKKQIKQVQKEVSVM 1238
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEaeadyEGFLEGVKAALLLAGLRGLAGAVAVLigVEAAYEAALEAALAAALQNIV 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1239 RDEDKLLRIKINELEKKKNQCSQELDM-KQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIED---MRMTLEEQE 1314
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLdKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllGRTLVAARL 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1315 QTQVEQDQVLEAKLEEVERLATELEKWKEKcndLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEE 1394
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSL---TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841445197 1395 KMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLvAALEIQLKAL 1465
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL-ERLEREIEAL 779
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
115-344 |
2.69e-07 |
|
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: 52.35 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 115 FSKVFGPATTQKEFFQGC--IMQPVKDLLKGQSrlIFTYGLTNSGKTYTFQgteeniGILPRTLNVLFDSlqerlytkmn 192
Cdd:cd01363 22 FYRGFRRSESQPHVFAIAdpAYQSMLDGYNNQS--IFAYGESGAGKTETMK------GVIPYLASVAFNG---------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 193 lkphrsreylrlsseqekeeIASKSALLRQIKERKMLRLSQDVkgysfikdlqwIQVSDSKEAYRllklgikhqsVAFTK 272
Cdd:cd01363 84 --------------------INKGETEGWVYLTEITVTLEDQI-----------LQANPILEAFG----------NAKTT 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841445197 273 LNNASSRSHSIFTVkilqiedsemsrvirvselsLCDLAGSERtmktqnegerlretgnINTSLLTLGKCIN 344
Cdd:cd01363 123 RNENSSRFGKFIEI--------------------LLDIAGFEI----------------INESLNTLMNVLR 158
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
970-1527 |
3.30e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 970 EYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDllkeKETL 1049
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDA----KRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1050 IQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKA----------------------KIKELETILETQKVECS 1107
Cdd:PTZ00121 1156 IARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAedarkaeaarkaeeerkaeearKAEDAKKAEAVKKAEEA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1108 HSAKLEQDILEKE---SIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQL--TNNLQDMKHLLQLKEEEEETN 1182
Cdd:PTZ00121 1236 KKDAEEAKKAEEErnnEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1183 RQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKltDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQE 1262
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE--AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1263 LDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWK 1342
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1343 E-KCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEkmmlitqAKEAENIRNKEMKKYAEDRE 1421
Cdd:PTZ00121 1474 EaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE-------AKKAEEAKKADEAKKAEEKK 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1422 RFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQiMDIKPKRI 1501
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEEL 1625
|
570 580
....*....|....*....|....*.
gi 1841445197 1502 SSADPDKLQTEPLSTSFEISRNKIED 1527
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
777-1095 |
3.81e-07 |
|
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: 55.45 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 777 KGSIHVSSAITEDQKKSEEVRPNIAEIE-DIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKN 855
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEeKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 856 LTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRtldsvsqiSNIDL 935
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR--------AELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 936 LNLRDLSNGSEEDNLPNTQLDLLGNDYLVSKQVKEYR--IQEPNRE-NSFHSSIEAIWEECKEIVKASSKKSHQIEELEQ 1012
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSedIESLAAEiEELEELIEELESELEALLNERASLEEALALLRS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1013 QIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETL------IQQLKEELQEK-NVTLDVQIQHVVEGKRALSELTQGV 1085
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLeglevrIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRL 974
|
330
....*....|
gi 1841445197 1086 TCYKAKIKEL 1095
Cdd:TIGR02168 975 KRLENKIKEL 984
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1215-1499 |
7.54e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1215 ADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRtIQQLKEQLNNQKVEEAIQQYERACK 1294
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE-KREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1295 DLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLAT-ELEKWKEKCNDLETKNNQRSNKEHENNTDvlgkltnl 1373
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1374 QDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRErffkqqnEMEILTAQLTEKDSDLQKWREERDQ 1453
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE-------ELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1841445197 1454 LVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPK 1499
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
852-1291 |
7.56e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 7.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 852 EKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRTLDSVSQIs 931
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 932 nidllnLRDLSNGSEEDNLPNTQLDLLGNDYlvsKQVKEYRIQEPNRENSFHSSIEAIWEECKEIvkaSSKKSHQIEELE 1011
Cdd:COG4717 131 ------YQELEALEAELAELPERLEELEERL---EELRELEEELEELEAELAELQEELEELLEQL---SLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1012 QQIEKLQAEVKGYKDENNRLK-EKEHKNQDDLLKEKETLIQQLKEELQEKNVTL------------DVQIQHVVEGKRAL 1078
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQeELEELEEELEQLENELEAAALEERLKEARLLLliaaallallglGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1079 SELTQGVTCYKAKIKELETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQE-----HLQDSVKNTKDLNVKELK 1153
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeellELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1154 LKEEItQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEE---------DYADLKEKLTDA 1224
Cdd:COG4717 359 LEEEL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGeleellealDEEELEEELEEL 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841445197 1225 KKQIKQVQKEVSVMRDEDKLLRIKINELEKkknqcSQELDMKQRTIQQLKEQLNN------------QKVEEAIQQYER 1291
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRElaeewaalklalELLEEAREEYRE 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
856-1459 |
1.01e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 856 LTLSKEVQQIQSNYdiAIAELHVQKSKNQEQEEKIMKLSNEIETATRsitnnvsQIKLMHTKIDELRTldsvsqisniDL 935
Cdd:COG1196 216 RELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEA-------ELAELEAELEELRL----------EL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 936 LNLRDLSNgseednlpntqldllgndylvSKQVKEYRIQepnrensfhSSIEAIWEECKEIVKASSKKSHQIEELEQQIE 1015
Cdd:COG1196 277 EELELELE---------------------EAQAEEYELL---------AELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1016 KLQAEVKGYKDENNRLKEkEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKEL 1095
Cdd:COG1196 327 ELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1096 ETILETQKVEcshSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLK 1175
Cdd:COG1196 406 EEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1176 EEEEETNRQETEKLKE-----ELSASSARTQNLKADLQRKEEDYADL--KEKLTDAKKQIKQVQKEVSVMRDEDKLLRIK 1248
Cdd:COG1196 483 LEELAEAAARLLLLLEaeadyEGFLEGVKAALLLAGLRGLAGAVAVLigVEAAYEAALEAALAAALQNIVVEDDEVAAAA 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1249 INELEKKKNQCSQELDM-KQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIED---MRMTLEEQEQTQVEQDQVL 1324
Cdd:COG1196 563 IEYLKAAKAGRATFLPLdKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllGRTLVAARLEAALRRAVTL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1325 EAKLEEVERLATELEKWKEKcndLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKE 1404
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSL---TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1841445197 1405 AENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDS---DLQKWREERDQLVAALE 1459
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppDLEELERELERLEREIE 777
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1188-1390 |
1.04e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1188 KLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQ 1267
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1268 RTIQQLKEQ------LNNQKVEEAIQQYERACKDLNVKEKIIEDMRMT---LEEQEQTQVEQDQVLEAKLEEVERLATEL 1338
Cdd:COG4942 111 RALYRLGRQpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADlaeLAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1841445197 1339 EKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKK 1390
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1006-1228 |
1.05e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.48 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1006 QIEELEQQIEKLQAEVKGYKDENNRLKEK------EHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEgkrALS 1079
Cdd:PHA02562 182 QIQTLDMKIDHIQQQIKTYNKNIEEQRKKngeniaRKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSA---ALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1080 ELTQGVTCYKAKIKELETILE--TQKVECSHSAkleQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKElklkEE 1157
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCT---QQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIM----DE 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841445197 1158 ITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQI 1228
Cdd:PHA02562 332 FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1006-1480 |
1.19e-06 |
|
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: 53.82 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1006 QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDllKEKETLIQQLKEELQEKNVTLDVQIQHVvEGKRALSELTQGV 1085
Cdd:TIGR00618 450 TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE--TRKKAVVLARLLELQEEPCPLCGSCIHP-NPARQDIDNPGPL 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1086 TCykakikELETILETQKvecshsaKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNL 1165
Cdd:TIGR00618 527 TR------RMQRGEQTYA-------QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1166 QDMKHLLQLKEEEEETNRQETEKLKEELsassartqNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLL 1245
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKL--------QPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1246 RIKINELEKkknqcSQELDMKQRTIQQLKEQLNNQKveEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLE 1325
Cdd:TIGR00618 666 SIRVLPKEL-----LASRQLALQKMQSEKEQLTYWK--EMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARE 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1326 AKLEEVERLATELEKWKEKCNDLEtknNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEA 1405
Cdd:TIGR00618 739 DALNQSLKELMHQARTVLKARTEA---HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD 815
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1841445197 1406 ENIRNKEMKKYAEDRERFfkqQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKalISSNVQKDNEIEQLK 1480
Cdd:TIGR00618 816 EDILNLQCETLVQEEEQF---LSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK--IIQLSDKLNGINQIK 885
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1203-1507 |
1.38e-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: 53.53 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1203 LKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKV 1282
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL--SSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1283 EEAIQQYERACKDLnvkEKIIEDMRMTLEEqeqtqveqdqvLEAKLEEVERLATElEKWKEKCNDLETKNNQRSNKEhen 1362
Cdd:TIGR02169 750 EQEIENVKSELKEL---EARIEELEEDLHK-----------LEEALNDLEARLSH-SRIPEIQAELSKLEEEVSRIE--- 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1363 ntdvlGKLTNLQDELQESEQK--YNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKqqnEMEILTAQLTEK 1440
Cdd:TIGR02169 812 -----ARLREIEQKLNRLTLEkeYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE---ELEAALRDLESR 883
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841445197 1441 DSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPKRISSADPD 1507
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
791-1338 |
2.29e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 791 KKSEEVRPNIAEIEDIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLsKEVQQIQSNYD 870
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 871 IAIAELHVQKSKNQEQEEKIMKLSNEIETATRSI---TNNVSQIKLMHTKIDELRtldsvsqisnidllnlRDLSNGSEE 947
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkelEEKEERLEELKKKLKELE----------------KRLEELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 948 DNLPNTQLDLLGNDYLVSKQVKEYRIQEPNREnsfhssIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQA---EVKGY 1024
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGLTPEKLEKE------LEELEKAKEEIEEEISKITARIGELKKEIKELKKaieELKKA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1025 K------------DENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKnvtldVQIQHVVEGKRALSELTQGVTcykaKI 1092
Cdd:PRK03918 435 KgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL-----RELEKVLKKESELIKLKELAE----QL 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1093 KELETILETQKVECSHSAKLEQDILEKESIILKLErnlkefQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLL 1172
Cdd:PRK03918 506 KELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1173 QLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINE- 1251
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEe 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1252 ----LEKKKNQCSQELDMKQRTIQQLKEQL-----NNQKVEEAIQQYERACKDLNVKEKIIEDMRmtlEEQEQTQVEQDQ 1322
Cdd:PRK03918 660 eyeeLREEYLELSRELAGLRAELEELEKRReeikkTLEKLKEELEEREKAKKELEKLEKALERVE---ELREKVKKYKAL 736
|
570
....*....|....*.
gi 1841445197 1323 VLEAKLEEVERLATEL 1338
Cdd:PRK03918 737 LKERALSKVGEIASEI 752
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1193-1422 |
2.47e-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: 2.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1193 LSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQ 1272
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1273 LKEQLNNQKveEAIQQYERACKDLNVKEKI-----------IEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKW 1341
Cdd:COG4942 95 LRAELEAQK--EELAELLRALYRLGRQPPLalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1342 KEKCNDLETKNNQRSNkehenntdvlgKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRE 1421
Cdd:COG4942 173 RAELEALLAELEEERA-----------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
.
gi 1841445197 1422 R 1422
Cdd:COG4942 242 R 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
636-1301 |
2.81e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.53 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 636 QEATACLELKFNQIKAEL----AKTKGELIKTKEELKKRENESDSLiqeletSNKKIITQNQRIKELINIIDQKEDTINE 711
Cdd:pfam12128 282 QETSAELNQLLRTLDDQWkekrDELNGELSAADAAVAKDRSELEAL------EDQHGAFLDADIETAAADQEQLPSWQSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 712 FQNL-KSHMENTFKCND-KADTSSLIINNKLICNETVEVPKDSKSKICSERKR---VNENELQQDEPPAKkgsihvssai 786
Cdd:pfam12128 356 LENLeERLKALTGKHQDvTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRqlaVAEDDLQALESELR---------- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 787 tedqkksEEVRPNIAEIEDIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQ 866
Cdd:pfam12128 426 -------EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 867 SNYDIA-----IAELHVQKSKNQEQEEKIMkLSNEIETATRSITNNVSQIKlmhtkiDELRTLDSVSQISNIDLLNLRDL 941
Cdd:pfam12128 499 KRRDQAsealrQASRRLEERQSALDELELQ-LFPQAGTLLHFLRKEAPDWE------QSIGKVISPELLHRTDLDPEVWD 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 942 SNGSEEDNLPNTQLDLLG---NDYLVSKQVKEYRIqepnreNSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQ 1018
Cdd:pfam12128 572 GSVGGELNLYGVKLDLKRidvPEWAASEEELRERL------DKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1019 AEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQeknvTLDVQIQHVVEGKRALSELTQGvTCYKAKIKELETI 1098
Cdd:pfam12128 646 TALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLN----SLEAQLKQLDKKHQAWLEEQKE-QKREARTEKQAYW 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1099 LEtqkVECSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNL----QDMKHLLQL 1174
Cdd:pfam12128 721 QV---VEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIeriaVRRQEVLRY 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1175 KEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEdyadlkekltDAKKQIKQVQKEvsvmRDEDKLLRIKINELEK 1254
Cdd:pfam12128 798 FDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIA----------DTKLRRAKLEME----RKASEKQQVRLSENLR 863
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1841445197 1255 KknqcsqeLDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEK 1301
Cdd:pfam12128 864 G-------LRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRD 903
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
991-1497 |
3.55e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.96 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 991 EECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEK--EHKNQ--------DDLLKEKE------TLIQQLK 1054
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEvrDLRERleeleeerDDLLAEAGlddadaEAVEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1055 EELQEKnvtlDVQIQHVVEGKR-ALSELTQGVTCYKAKIKELETILETQKVEcshSAKLEQDILEKESIILKLERNLKEF 1133
Cdd:PRK02224 317 EELEDR----DEELRDRLEECRvAAQAHNEEAESLREDADDLEERAEELREE---AAELESELEEAREAVEDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1134 QEHLQDsvkntkdlnvkelkLKEEITQLTNNLQDMKHLLQLkeeeeetnrqetekLKEELSASSARTQNLKADLQRKEED 1213
Cdd:PRK02224 390 EEEIEE--------------LRERFGDAPVDLGNAEDFLEE--------------LREERDELREREAELEATLRTARER 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1214 YADlKEKLTDAKK---------------QIKQVQKEVSVMRDEDKLLRIKINELEKKKNQcSQELDMKQRTIQQLKEQLN 1278
Cdd:PRK02224 442 VEE-AEALLEAGKcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERRE 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1279 NqkVEEAIQQyerackdlnvKEKIIEDMRMTLEEQEQTQVEqdqvLEAKLEEVERLATELEKWKEKCNDlETKNNQRSNK 1358
Cdd:PRK02224 520 D--LEELIAE----------RRETIEEKRERAEELRERAAE----LEAEAEEKREAAAEAEEEAEEARE-EVAELNSKLA 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1359 EHENNTDVLGKLTNLQDELQESEQKYNADRKKwLEEKMMLITQAKEAENIRNKEMKKYAE--DRERFFKQQNEMEILTAQ 1436
Cdd:PRK02224 583 ELKERIESLERIRTLLAAIADAEDEIERLREK-REALAELNDERRERLAEKRERKRELEAefDEARIEEAREDKERAEEY 661
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841445197 1437 LTEKDSDLQKWREERDQLVAAL-----EIQ-LKALISSNVQKDNEIEQLKRIISETSKIETQIMDIK 1497
Cdd:PRK02224 662 LEQVEEKLDELREERDDLQAEIgavenELEeLEELRERREALENRVEALEALYDEAEELESMYGDLR 728
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
966-1480 |
6.88e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 966 KQVKEYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKShQIEELEQQIEKLQ--AEVKGYKDENNRLKEKEHKNQDDLL 1043
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK-KAEEAKKKADAAKkkAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1044 KEKETLIQQLKEELQEKNVTLDVQiqhvVEGKRALSELTQGVTCYKAKIKELETILETQKVECSHSAKLEQ----DILEK 1119
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKK----AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkkkaDEAKK 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1120 ESIILKLERNLKEFQEHLQDSVKNTKDLNVK----ELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSA 1195
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkadEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1196 SSARtqnlKADLQRKEEDYADLKE-KLTDAKKQIKQVQKEVSVMRDEDKllrikiNELEKKKNQcSQELDMKQRTIQQLK 1274
Cdd:PTZ00121 1519 EEAK----KADEAKKAEEAKKADEaKKAEEKKKADELKKAEELKKAEEK------KKAEEAKKA-EEDKNMALRKAEEAK 1587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1275 eQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQV--LEAKLEEVERLATELEKWKEkcnDLETKN 1352
Cdd:PTZ00121 1588 -KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVeqLKKKEAEEKKKAEELKKAEE---ENKIKA 1663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1353 NQRSNKEHENNTdvlgKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERF----FKQQN 1428
Cdd:PTZ00121 1664 AEEAKKAEEDKK----KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIkaeeAKKEA 1739
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1841445197 1429 EMEILTAQLTEKDSD----LQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLK 1480
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEekkkIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1088-1417 |
8.59e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1088 YKAKIKELETILETQKVECSHS--AKLEQDILEKESIILKLERNLKEFQEHLQDsvkntkdLNVKELKLKEEITQLTNNL 1165
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREelEELQEELKEAEEELEELTAELQELEEKLEE-------LRLEVSELEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1166 QDMKHLLQlkeeeeetnrqeteKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKevsvmrdedkll 1245
Cdd:TIGR02168 291 YALANEIS--------------RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE------------ 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1246 riKINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKEKIIEdmrmtleeqeqtqveqdqvle 1325
Cdd:TIGR02168 345 --KLEELKEELESLEAELEELEAELEELESRL--EELEEQLETLRSKVAQLELQIASLN--------------------- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1326 aklEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEA 1405
Cdd:TIGR02168 400 ---NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330
....*....|..
gi 1841445197 1406 ENIRNKEMKKYA 1417
Cdd:TIGR02168 477 LDAAERELAQLQ 488
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1188-1439 |
1.30e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1188 KLKEELSASSARTQNLKADL------QRKEEDYAD-LKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCS 1260
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELsslqseLRRIENRLDeLSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1261 QELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKE-----KIIEDMRMTLEEQEQTQVEQDQVLEAKLEEV---- 1331
Cdd:TIGR02169 751 QEIENVKSELKELEARI--EELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLtlek 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1332 ERLATELEKWKEKCNDLETKNNQRSNKEHENNTDvLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNK 1411
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK-KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
250 260
....*....|....*....|....*...
gi 1841445197 1412 EMKKYAEDRERFFKQQNEMEILTAQLTE 1439
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1004-1255 |
1.38e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1004 SHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLlKEKETLIQQLKEELQEKNVTLDVQiqhvvegKRALSELTQ 1083
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-AALERRIAALARRIRALEQELAAL-------EAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1084 gvtcykaKIKELETILETQKVECSHSAKLEQDILEKESIILKLErnlkefQEHLQDSVKNTKDLNVKELKLKEEITQLTN 1163
Cdd:COG4942 91 -------EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLS------PEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1164 NLQDMKhllqlkeeeeetnrqeteKLKEELSASSARTQNLKADLQRKEEDYADLKEK----LTDAKKQIKQVQKEVSVMR 1239
Cdd:COG4942 158 DLAELA------------------ALRAELEAERAELEALLAELEEERAALEALKAErqklLARLEKELAELAAELAELQ 219
|
250
....*....|....*.
gi 1841445197 1240 DEDKLLRIKINELEKK 1255
Cdd:COG4942 220 QEAEELEALIARLEAE 235
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1007-1497 |
1.62e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.82 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1007 IEELEQQIEKLQAE-VKGYKDENNRLKEKE-HKNQDDLLKEKetlIQQLKEELQEKNV----------TLDVQI----QH 1070
Cdd:pfam10174 249 IRDLEDEVQMLKTNgLLHTEDREEEIKQMEvYKSHSKFMKNK---IDQLKQELSKKESellalqtkleTLTNQNsdckQH 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1071 VVEGKRALSELTQGVTCYKAKIKELETILEtqkvecshsakleqdilEKESIilklernLKEFQEHLQDsvkntkdlnvk 1150
Cdd:pfam10174 326 IEVLKESLTAKEQRAAILQTEVDALRLRLE-----------------EKESF-------LNKKTKQLQD----------- 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1151 elkLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEED-------YADLKEKLTD 1223
Cdd:pfam10174 371 ---LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtaLTTLEEALSE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1224 AKKQIKQVQKEVS----VMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQ------------KVEEAIQ 1287
Cdd:pfam10174 448 KERIIERLKEQREredrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLassglkkdsklkSLEIAVE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1288 QYERACKDLNVKEKIIEDMRMTlEEQEQTQVEQDQVLEA----KLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENN 1363
Cdd:pfam10174 528 QKKEECSKLENQLKKAHNAEEA-VRTNPEINDRIRLLEQevarYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELE 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1364 TDVLGKLTNLQDELQESEQKYNADRKKWLEEkmMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLT----- 1438
Cdd:pfam10174 607 SLTLRQMKEQNKKVANIKHGQQEMKKKGAQL--LEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSstqqs 684
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841445197 1439 --EKDSDLQKWR-EERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIK 1497
Cdd:pfam10174 685 laEKDGHLTNLRaERRKQLEEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALK 746
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1042-1538 |
1.89e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.44 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1042 LLKEKETLIQQLKEELQEKNVTLD-----VQIQHVVEGKRA-LSELTQGvtcykakIKELETILETQKvecsHSAKLEQD 1115
Cdd:pfam10174 200 LLDQKEKENIHLREELHRRNQLQPdpaktKALQTVIEMKDTkISSLERN-------IRDLEDEVQMLK----TNGLLHTE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1116 ILEKESIILKLERNLKEFQEHLQDSVKntKDLNVKE---LKLKEEITQLTNNLQDMKHLLQLkeeeeetnrqetekLKEE 1192
Cdd:pfam10174 269 DREEEIKQMEVYKSHSKFMKNKIDQLK--QELSKKEselLALQTKLETLTNQNSDCKQHIEV--------------LKES 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1193 LSASSARTQNLKAD-------LQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDM 1265
Cdd:pfam10174 333 LTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRD 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1266 KQRTIQQLKE-----QLNNQKVEEAIQQYERACKDlnvKEKIIEDMRMTLEEQEqtqveqdqvlEAKLEEVERLATELEK 1340
Cdd:pfam10174 413 KDKQLAGLKErvkslQTDSSNTDTALTTLEEALSE---KERIIERLKEQRERED----------RERLEELESLKKENKD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1341 WKEKCNDLETKNNQRSN-----KEHENNTDVLG-----KLTNLQDELQESEQ---KYNADRKKWLEEKMMLITQAKEAEN 1407
Cdd:pfam10174 480 LKEKVSALQPELTEKESslidlKEHASSLASSGlkkdsKLKSLEIAVEQKKEecsKLENQLKKAHNAEEAVRTNPEINDR 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1408 IRN--KEMKKYAEDRErffKQQNEMEILTAQLTEKDSDlqkwREERDQLVAALEIQLKALISSNVQKdneIEQLKRIISE 1485
Cdd:pfam10174 560 IRLleQEVARYKEESG---KAQAEVERLLGILREVENE----KNDKDKKIAELESLTLRQMKEQNKK---VANIKHGQQE 629
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1841445197 1486 TSKIETQIMD--IKPKRISSADPDKLQTEPLSTSFEISRNKIEDGSVVLDSCEVS 1538
Cdd:pfam10174 630 MKKKGAQLLEeaRRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQS 684
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1001-1490 |
4.47e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.50 E-value: 4.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1001 SKKSHQIEELEQQIEklqaevkgykdennrlkEKEHKNQDDLLKEKETLIQQLKEELQEKNVtldvQIQHVVEGKRALSE 1080
Cdd:PRK02224 183 SDQRGSLDQLKAQIE-----------------EKEEKDLHERLNGLESELAELDEEIERYEE----QREQARETRDEADE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1081 LtqgVTCYKAKIKELETiletqkvecshsakLEQDILEKESIILKLERNLKEFQEHLQDsvkntkdlnvkelkLKEEITQ 1160
Cdd:PRK02224 242 V---LEEHEERREELET--------------LEAEIEDLRETIAETEREREELAEEVRD--------------LRERLEE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1161 LTNNLQDMKHLLQLKEEeeetnrqeteklkeELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRD 1240
Cdd:PRK02224 291 LEEERDDLLAEAGLDDA--------------DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1241 EDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLnnqkvEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEq 1320
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEI-----EELRERFGDAPVDLGNAEDFLEELREERDELREREAE- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1321 dqvLEAKLEEVERLATELEKWKE--KC----NDLETKNNQRSNKEHEnntdvlGKLTNLQDELQESEQKyNADRKKWLEE 1394
Cdd:PRK02224 431 ---LEATLRTARERVEEAEALLEagKCpecgQPVEGSPHVETIEEDR------ERVEELEAELEDLEEE-VEEVEERLER 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1395 KMMLITQAKEAENIRNKE---MKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREE----RDQLVAALEiQLKALIS 1467
Cdd:PRK02224 501 AEDLVEAEDRIERLEERRedlEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAaaeaEEEAEEARE-EVAELNS 579
|
490 500
....*....|....*....|...
gi 1841445197 1468 SNVQKDNEIEQLKRIISETSKIE 1490
Cdd:PRK02224 580 KLAELKERIESLERIRTLLAAIA 602
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1156-1340 |
5.15e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 5.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1156 EEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEV 1235
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1236 SVMRDEdklLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN-----NQKVEEAIQQYERACKDLNVKEKIIEDMRMTL 1310
Cdd:COG4942 100 EAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|
gi 1841445197 1311 EEQEQTQVEQDQVLEAKLEEVERLATELEK 1340
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEK 206
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1188-1310 |
5.61e-05 |
|
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: 46.46 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1188 KLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQV--QKEVSVMRDEDKLLRIKINELEKKKNQCSQELDM 1265
Cdd:COG1579 42 ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEE 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1841445197 1266 KQRTIQQLKEQLNNQK--VEEAIQQYERACKDLNVKEKIIEDMRMTL 1310
Cdd:COG1579 122 LEEELAELEAELAELEaeLEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1324-1512 |
5.89e-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: 48.13 E-value: 5.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1324 LEAKLEEVERLATELEKWKEKCNDLETKNNQRSnkehenntdvlGKLTNLQDELQESEQKYNADRKKWLE--------EK 1395
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELE-----------EKLEELRLEVSELEEEIEELQKELYAlaneisrlEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1396 MMLITQAKEAENIRNKEMkkYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISSNVQKDNE 1475
Cdd:TIGR02168 303 QKQILRERLANLERQLEE--LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190
....*....|....*....|....*....|....*..
gi 1841445197 1476 IEQLKRIISETSKIETQIMdikpKRISSADPDKLQTE 1512
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLN----NEIERLEARLERLE 413
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1006-1237 |
6.77e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1006 QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLlKEKETLIQQLKEELQEKNVTLDVQIQHVveGKRALSELTQGV 1085
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-EALQAEIDKLQAEIAEAEAEIEERREEL--GERARALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1086 TcykakIKELETILETQKVecshsakleQDILEKESIILKL-ERNLKEFQEHLQDsvknTKDLNVKELKLKEEITQLTNN 1164
Cdd:COG3883 101 S-----VSYLDVLLGSESF---------SDFLDRLSALSKIaDADADLLEELKAD----KAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841445197 1165 LQDMKhllqlkeeeeetnrqeteKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSV 1237
Cdd:COG3883 163 KAELE------------------AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
853-1500 |
7.02e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.97 E-value: 7.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 853 KKNLTLSKEVQQIQSNYDI---AIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELrtlDSVSQ 929
Cdd:PRK01156 152 KKILDEILEINSLERNYDKlkdVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERL---SIEYN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 930 ISNIDLLNLRdlsngsEEDNLPNTQLDLLgNDYLVSKQVKEYRIQEPNRENSFHSSIEaiwEECKEIVKASSKKSH---- 1005
Cdd:PRK01156 229 NAMDDYNNLK------SALNELSSLEDMK-NRYESEIKTAESDLSMELEKNNYYKELE---ERHMKIINDPVYKNRnyin 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1006 -------QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKEtliqqlKEELqeknvtldvqiqhvvegKRAL 1078
Cdd:PRK01156 299 dyfkyknDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSR------YDDL-----------------NNQI 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1079 SELTQGVTCYKAKIKELETI---LETQKVECSHSAKLEQDILEKESI---ILKLERNlkEFQEHLQDSVKNTKDLNVKEL 1152
Cdd:PRK01156 356 LELEGYEMDYNSYLKSIESLkkkIEEYSKNIERMSAFISEILKIQEIdpdAIKKELN--EINVKLQDISSKVSSLNQRIR 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1153 KLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARtqnLKADLQRKEEDYADLKEKLTDAKKQIKQVQ 1232
Cdd:PRK01156 434 ALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSR---LEEKIREIEIEVKDIDEKIVDLKKRKEYLE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1233 -KEVSVMRDEDKLLRIKINELEKKKNQCSqELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIiedmrmtle 1311
Cdd:PRK01156 511 sEEINKSINEYNKIESARADLEDIKIKIN-ELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLI--------- 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1312 eqeqtqveqdqvleakleEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNAdrkkw 1391
Cdd:PRK01156 581 ------------------DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNE----- 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1392 LEEKMMLITQAKEaeniRNKEMKKYAEDRERFFKQQNEmeiLTAQLTEKDSDLQKWREERDQLVAALEiQLKALISSNVQ 1471
Cdd:PRK01156 638 IQENKILIEKLRG----KIDNYKKQIAEIDSIIPDLKE---ITSRINDIEDNLKKSRKALDDAKANRA-RLESTIEILRT 709
|
650 660 670
....*....|....*....|....*....|...
gi 1841445197 1472 KDNEIEQ----LKRIISETSKIETQIMDIKPKR 1500
Cdd:PRK01156 710 RINELSDrindINETLESMKKIKKAIGDLKRLR 742
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
994-1463 |
7.79e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 47.86 E-value: 7.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 994 KEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENN---RLKEKEHKNQDDL------LKEKETLIQQLKEELQEKNVTL 1064
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEmraRLAARKQELEEILhelesrLEEEEERSQQLQNEKKKMQQHI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1065 DVQIQHVVEGKRALSELTQGVTCYKAKIKELET---ILETQKVECSHSAKLeqdilekesiilkLERNLKEFQEHLQDSV 1141
Cdd:pfam01576 106 QDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEdilLLEDQNSKLSKERKL-------------LEERISEFTSNLAEEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1142 KNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKL 1221
Cdd:pfam01576 173 EKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1222 TD-------AKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELdmkqrtiQQLKEQLNNQKVEEAIQQYERAck 1294
Cdd:pfam01576 253 EEetaqknnALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL-------EALKTELEDTLDTTAAQQELRS-- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1295 dlnVKEKIIEDMRMTLEEQEQTQVEQDQVLEAK-LEEVERLATELEKWKEKCNDLEtKNNQRSNKEhenNTDVLGKLTNL 1373
Cdd:pfam01576 324 ---KREQEVTELKKALEEETRSHEAQLQEMRQKhTQALEELTEQLEQAKRNKANLE-KAKQALESE---NAELQAELRTL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1374 QDELQESEQKynadRKKWLEEKMMLITQAKEAENIRNkemkkyaEDRERFFKQQNEMEILTAQLTEKDSDLQKWREErdq 1453
Cdd:pfam01576 397 QQAKQDSEHK----RKKLEGQLQELQARLSESERQRA-------ELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD--- 462
|
490
....*....|
gi 1841445197 1454 lVAALEIQLK 1463
Cdd:pfam01576 463 -VSSLESQLQ 471
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1076-1525 |
1.05e-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: 47.42 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1076 RALSELTQGVTCYKAKIKELETILETQKVECS---------HSAKLEQDILEKESIILKLER----------NLKEFQEH 1136
Cdd:pfam15921 224 KILRELDTEISYLKGRIFPVEDQLEALKSESQnkielllqqHQDRIEQLISEHEVEITGLTEkassarsqanSIQSQLEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1137 LQDSVKNTKDLNVKEL-KLKEEITQLTNNLQDMKHLLQLKEEeeetnrqeteKLKEELSASSARTQNLKADLQRKEEDYA 1215
Cdd:pfam15921 304 IQEQARNQNSMYMRQLsDLESTVSQLRSELREAKRMYEDKIE----------ELEKQLVLANSELTEARTERDQFSQESG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1216 DLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKvEEAIQQYERACKD 1295
Cdd:pfam15921 374 NLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMK-SECQGQMERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1296 LNVKEKiiedmrmtleeqeqtqveqdqvleaKLEEVERLATELEKWKEKCNDL-ETKNNQRSNKEHENNTdvlgkLTNLQ 1374
Cdd:pfam15921 453 IQGKNE-------------------------SLEKVSSLTAQLESTKEMLRKVvEELTAKKMTLESSERT-----VSDLT 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1375 DELQESEQKYNADRKKwleekmmlITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERD-- 1452
Cdd:pfam15921 503 ASLQEKERAIEATNAE--------ITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnm 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1453 -QLV--------------AALE-------IQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPKRISSADPDKLQ 1510
Cdd:pfam15921 575 tQLVgqhgrtagamqvekAQLEkeindrrLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQE 654
|
490
....*....|....*
gi 1841445197 1511 TEPLSTSFEISRNKI 1525
Cdd:pfam15921 655 RDQLLNEVKTSRNEL 669
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1324-1497 |
2.06e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1324 LEAKLEEVERlatELEKWKEKCNDLETknNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKwLEEKMMLITQAK 1403
Cdd:COG3206 187 LRKELEEAEA---ALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ-LGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1404 EAENIRNKemkkyaedRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQL-----------VAALEIQLKALISSNVQK 1472
Cdd:COG3206 261 QSPVIQQL--------RAQLAELEAELAELSARYTPNHPDVIALRAQIAALraqlqqeaqriLASLEAELEALQAREASL 332
|
170 180
....*....|....*....|....*
gi 1841445197 1473 DNEIEQLKRIISETSKIETQIMDIK 1497
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELRRLE 357
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
994-1478 |
2.96e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 994 KEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLiQQLKEELQEKNVTLDvqiqhvve 1073
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQL-KIITMELQKKSSELE-------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1074 gkralsELTQGVTCYKAKIKELETILETQKvecshsaKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELK 1153
Cdd:pfam05483 395 ------EMTKFKNNKEVELEELKKILAEDE-------KLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTA 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1154 LKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQK 1233
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1234 EVSVMRDEDKLLRikiNELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNV----KEKIIEDMRMT 1309
Cdd:pfam05483 542 KEMNLRDELESVR---EEFIQKGDEVKCKLDKSEENARSIEYEV--LKKEKQMKILENKCNNLKKqienKNKNIEELHQE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1310 LEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLeTKNNQRSNKEHENNTDvlgkltNLQDELQESeqKYNADRK 1389
Cdd:pfam05483 617 NKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEI-IDNYQKEIEDKKISEE------KLLEEVEKA--KAIADEA 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1390 KWLEEKMMLITQAKEAENIRNKEMKKYAEDRerffkqqnemeiltaQLTEKDSDLQKWR---EERDQLVAALEIQLKALI 1466
Cdd:pfam05483 688 VKLQKEIDKRCQHKIAEMVALMEKHKHQYDK---------------IIEERDSELGLYKnkeQEQSSAKAALEIELSNIK 752
|
490
....*....|....
gi 1841445197 1467 SS--NVQKDNEIEQ 1478
Cdd:pfam05483 753 AEllSLKKQLEIEK 766
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1430-1716 |
3.18e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 45.81 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1430 MEILTAQLTEKDSDLQK---------WREERDQLVAALEiqlkaliSSNVQKDNEIEQLKRIISETSKIETQIMDIKPKR 1500
Cdd:PTZ00108 1104 VEKLNAELEKKEKELEKlknttpkdmWLEDLDKFEEALE-------EQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKK 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1501 ISSADPDKLQTEPLSTSFEISRNKIEDGSVVLDSCEVSTENDQSTRFPKPELEIQFTplqpnKMAVKHPGCTTPVTVKIP 1580
Cdd:PTZ00108 1177 KEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKT-----KPKKSSVKRLKSKKNNSS 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1581 KARKRKSNEMEEDLVKCENKKNATPRTNLKFPISDDRNSSVKKEQKVAIRPSS--KKTYSLRSQASIIGVNLATKKKEGT 1658
Cdd:PTZ00108 1252 KSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSptKKKVKKRLEGSLAALKKKKKSEKKT 1331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1841445197 1659 LQKfgdflqhspsilqskakkiietmSSSKLSNVEASKENVSQPKRAKRKLYTSEISS 1716
Cdd:PTZ00108 1332 ARK-----------------------KKSKTRVKQASASQSSRLLRRPRKKKSDSSSE 1366
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1207-1358 |
3.33e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1207 LQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKIN--ELEKKKNQCSQELDMKQRTIQQLKEQLNN----- 1279
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEElrele 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1280 ---QKVEEAIQQYERACKDL-----NVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETK 1351
Cdd:COG4717 163 eelEELEAELAELQEELEELleqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
....*..
gi 1841445197 1352 NNQRSNK 1358
Cdd:COG4717 243 ERLKEAR 249
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
988-1292 |
3.55e-04 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 45.71 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 988 AIWEECKEIVKASSKKSHQIEELEQQIEKLQaeVKGYKDENnRLKEKEHKNQDDLLKeKETLIQQLKE------------ 1055
Cdd:pfam15818 75 ALEEEKGKYQLATEIKEKEIEGLKETLKALQ--VSKYSLQK-KVSEMEQKLQLHLLA-KEDHHKQLNEiekyyatitgqf 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1056 -ELQEKNVTLDVQIQHVVEGKRALSELTQG----VTCYKAKIKELETILETQKVECSHSakleqdiLEKESIILKL-ERN 1129
Cdd:pfam15818 151 gLVKENHGKLEQNVQEAIQLNKRLSALNKKqeseICSLKKELKKVTSDLIKSKVTCQYK-------MGEENINLTIkEQK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1130 LKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQlkeeeeeTNRQETEKLKEELSASSARTQNLKAD--L 1207
Cdd:pfam15818 224 FQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQ-------QQTQANTEMEAELKALKENNQTLERDneL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1208 QRK-----EEDYADLKEKLTDA----KKQIKQVQKEVSVMRDEDKLLRIKINELEKKKN-QCSQELDMKQRTIQQLKEqL 1277
Cdd:pfam15818 297 QREkvkenEEKFLNLQNEHEKAlgtwKKHVEELNGEINEIKNELSSLKETHIKLQEHYNkLCNQKKFEEDKKFQNVPE-V 375
|
330
....*....|....*
gi 1841445197 1278 NNQKVEEAIQQYERA 1292
Cdd:pfam15818 376 NNENSEMSTEKSENL 390
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1153-1291 |
3.56e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 43.74 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1153 KLKEEITQLTNNLQDMKHLLQlkeeeeeTNRQETEKLKEELsassARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQ 1232
Cdd:pfam13851 30 SLKEEIAELKKKEERNEKLMS-------EIQQENKRLTEPL----QKAQEEVEELRKQLENYEKDKQSLKNLKARLKVLE 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841445197 1233 KEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQ---LKEQLNNQKVEEAIQQYER 1291
Cdd:pfam13851 99 KELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktgLKNLLLEKKLQALGETLEK 160
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
884-1280 |
3.73e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 884 QEQEEKIMKLSNEIETATRSITNNVSQIklmhtkiDELRTLDSVSQISNIDLLNLRDLSNGSEE--DNLPNTQLDLLG-N 960
Cdd:PRK11281 76 DRQKEETEQLKQQLAQAPAKLRQAQAEL-------EALKDDNDEETRETLSTLSLRQLESRLAQtlDQLQNAQNDLAEyN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 961 DYLVSKQVKEYRIQEPNRENSFHS-SIEAI---WEECKEIVKASSKKSHQIEE--LEQQIEKLQAEVKGykdeNNRLKEK 1034
Cdd:PRK11281 149 SQLVSLQTQPERAQAALYANSQRLqQIRNLlkgGKVGGKALRPSQRVLLQAEQalLNAQNDLQRKSLEG----NTQLQDL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1035 EHKnQDDLLKEKetlIQQLKEELQEknvtldvqIQHVVEGKR-ALSELTqgvtcykakIKELETILETQKV--------E 1105
Cdd:PRK11281 225 LQK-QRDYLTAR---IQRLEHQLQL--------LQEAINSKRlTLSEKT---------VQEAQSQDEAARIqanplvaqE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1106 CSHSAKLEQDILEKEsiilklERNLKEFQEHLQdsVKNTKD-LNVKELKLKEEITQLTNNLQDMKHLLQLKeeeeetnrq 1184
Cdd:PRK11281 284 LEINLQLSQRLLKAT------EKLNTLTQQNLR--VKNWLDrLTQSERNIKEQISVLKGSLLLSRILYQQQ--------- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1185 eteklkeelsassartQNLKADlqrkeedyaDLKEKLTDAKKQIKQVQKEVSVMRDE--------DKLLRIKINELEKK- 1255
Cdd:PRK11281 347 ----------------QALPSA---------DLIEGLADRIADLRLEQFEINQQRDAlfqpdayiDKLEAGHKSEVTDEv 401
|
410 420
....*....|....*....|....*
gi 1841445197 1256 KNQCSQELDMKQRTIQQLKEQLNNQ 1280
Cdd:PRK11281 402 RDALLQLLDERRELLDQLNKQLNNQ 426
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1093-1297 |
4.66e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.75 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1093 KELETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLL 1172
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1173 QlKEEEEETNRQETEKLKEELSASSA-RTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEdklLRIKINE 1251
Cdd:COG4942 107 A-ELLRALYRLGRQPPLALLLSPEDFlDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE---LEALLAE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1841445197 1252 LEKKKNQCSQELDMKQRTIQQLKEQLNNQkvEEAIQQYERACKDLN 1297
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAEL--AAELAELQQEAEELE 226
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
453-811 |
5.57e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.03 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 453 NSLEDLMEDEDLVEELENAEETQNVETKlldEDLDKTLEEnkafisHEEKRKLLDLIEdlkkKLINEKKEKLTLEFKIRE 532
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETR---DEADEVLEE------HEERREELETLE----AEIEDLRETIAETERERE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 533 evtqeftqywaqreaDFKETLLQEREILEENAERRlaifKDLVGKCDtREEAAKDICATKVETeethnyvgFEDIIDSLQ 612
Cdd:PRK02224 276 ---------------ELAEEVRDLRERLEELEEER----DDLLAEAG-LDDADAEAVEARREE--------LEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 613 DNVADIKKQAEIAHLYIASLpdpQEATACLELKFNQIKAELAKTKGELIKTKEELKKRENESDSLIQELETSNKKIitqn 692
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESL---REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF---- 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 693 qrikeliniidqkEDTINEFQNLKSHMEntfkcndkadtssLIINNKlicNETVEVPKDSKSKICSERKRVNENELQQDE 772
Cdd:PRK02224 401 -------------GDAPVDLGNAEDFLE-------------ELREER---DELREREAELEATLRTARERVEEAEALLEA 451
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1841445197 773 PPAK------KGSIHVsSAITEDQKKSEEVRpniAEIEDIRVLQE 811
Cdd:PRK02224 452 GKCPecgqpvEGSPHV-ETIEEDRERVEELE---AELEDLEEEVE 492
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
986-1384 |
5.69e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 986 IEAIWEECKEIVKASSKKS----HQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKnqddlLKEKETLIQQLKEELQEKN 1061
Cdd:COG4717 48 LERLEKEADELFKPQGRKPelnlKELKELEEELKEAEEKEEEYAELQEELEELEEE-----LEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1062 VTLDVQ--IQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVECSHSAKLEQDI--------LEKESIILKLERNLK 1131
Cdd:COG4717 123 KLLQLLplYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELeelleqlsLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1132 EFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEE------------------------------- 1180
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflv 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1181 -----TNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKL-----------TDAKKQIKQVQKEVSVMRDEDKL 1244
Cdd:COG4717 283 lgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspeelLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1245 LRIKINELEKK----KNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKII--EDMRMTLEEQEQTQV 1318
Cdd:COG4717 363 LQLEELEQEIAallaEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELE 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1841445197 1319 EQDQVLEAKLEEVERLATELEKWKEKCN------DLETKNNQRSNKEHENNTDVLGkLTNLQDELQESEQKY 1384
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEDGElaellqELEELKAELRELAEEWAALKLA-LELLEEAREEYREER 513
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
65-190 |
5.79e-04 |
|
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding site.
Pssm-ID: 465274 [Multi-domain] Cd Length: 144 Bit Score: 41.82 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 65 IRPFTQSEKELESEGCVHILDsqtvvlkepqcilGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQ--GCIMQPVkdlLK 142
Cdd:pfam16796 22 IRVFARVRPELLSEAQIDYPD-------------ETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQeiSQLVQSC---LD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1841445197 143 GQSRLIFTYGLTNSGktytfqgteENIGILPRTLNVLFDSLQERLYTK 190
Cdd:pfam16796 86 GYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGW 124
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1188-1340 |
5.91e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1188 KLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINEL---EKKKNQCSQELD 1264
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraLYRSGGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1265 M------------KQRTIQQLKEQLNnqkveEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVE 1332
Cdd:COG3883 107 VllgsesfsdfldRLSALSKIADADA-----DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
....*...
gi 1841445197 1333 RLATELEK 1340
Cdd:COG3883 182 ALLAQLSA 189
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1006-1225 |
6.89e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 6.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1006 QIEELEQQIEKLQAEVKGYKDENNRLK-EKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQ- 1083
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGLVDlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQs 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1084 -GVTCYKAKIKELETILetqkvecshsAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELK-LKEEITQL 1161
Cdd:COG3206 263 pVIQQLRAQLAELEAEL----------AELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEaLQAREASL 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1841445197 1162 TNNLQDMKHLLQlkeeeeetnrqeteklkeELSASSARTQNLKADLQRKEEDYADLKEKLTDAK 1225
Cdd:COG3206 333 QAQLAQLEARLA------------------ELPELEAELRRLEREVEVARELYESLLQRLEEAR 378
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1154-1289 |
7.64e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 7.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1154 LKEEIT-------QLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSA---RTQNLKADLQRK----EEDYADLKE 1219
Cdd:PRK09039 44 LSREISgkdsaldRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAersRLQALLAELAGAgaaaEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841445197 1220 KLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN---NQKVEEaIQQY 1289
Cdd:PRK09039 124 ELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNvalAQRVQE-LNRY 195
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1110-1450 |
1.10e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1110 AKLEqdILEKEsiILKLERNLKEFQEHLQDsVKNTKDLNVKELKLKEEITQLTNNLQDM----KHLLQLKEEeeetnrqe 1185
Cdd:COG4913 610 AKLA--ALEAE--LAELEEELAEAEERLEA-LEAELDALQERREALQRLAEYSWDEIDVasaeREIAELEAE-------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1186 teklKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQcSQELDM 1265
Cdd:COG4913 677 ----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL-ELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1266 KQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATEL------- 1338
Cdd:COG4913 752 EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLeedglpe 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1339 --EKWKEKCNDLETKN----NQRSNKEHENNTDVLGKLtNlqDELQESEqkYNADRKKWLEEKMMLITQAKE----AENI 1408
Cdd:COG4913 832 yeERFKELLNENSIEFvadlLSKLRRAIREIKERIDPL-N--DSLKRIP--FGPGRYLRLEARPRPDPEVREfrqeLRAV 906
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1841445197 1409 RNKEMKKYAEDRERFFKQQNE-MEILTAQLTEKDsdlQKWREE 1450
Cdd:COG4913 907 TSGASLFDEELSEARFAALKRlIERLRSEEEESD---RRWRAR 946
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1134-1385 |
1.79e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1134 QEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEED 1213
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1214 YADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERAC 1293
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1294 KDLNVKEKIIEDMRMTLEEQEQ-TQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTN 1372
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESlPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250
....*....|...
gi 1841445197 1373 LQDELQESEQKYN 1385
Cdd:COG4372 270 EKDTEEEELEIAA 282
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1202-1340 |
1.83e-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: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1202 NLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCS--QELDMKQRTIQQLKEQLN- 1278
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEIESLKRRISd 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1841445197 1279 -NQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEK 1340
Cdd:COG1579 108 lEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
991-1395 |
2.18e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.11 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 991 EECKEIVKASSKKSHQIEELEQQIEKLQAEVKgykdennrLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQH 1070
Cdd:TIGR00606 709 DKLKSTESELKKKEKRRDEMLGLAPGRQSIID--------LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1071 VVEGKRALSELTQgVTCYKAKIKELETILETQKVECSHS------AKLEQDILEKESIILKLERNLKEFQEHLQDSVKNT 1144
Cdd:TIGR00606 781 EESAKVCLTDVTI-MERFQMELKDVERKIAQQAAKLQGSdldrtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1145 KDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDA 1224
Cdd:TIGR00606 860 QHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKA 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1225 KKQIKQVQKEVSVMRDEDKLLRIKINElEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIE 1304
Cdd:TIGR00606 940 QDKVNDIKEKVKNIHGYMKDIENKIQD-GKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQ 1018
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1305 DmrmtleeqeqtqVEQDQVLEAKLEEVERlatELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKY 1384
Cdd:TIGR00606 1019 D------------NLTLRKRENELKEVEE---ELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKE 1083
|
410
....*....|.
gi 1841445197 1385 NADRKKWLEEK 1395
Cdd:TIGR00606 1084 IKHFKKELREP 1094
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1215-1355 |
2.29e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1215 ADLKEKLTDAKKQIKQVQKEVSVMRDEdKLLRIKiNELEKKKNQCSQELDMKQRTIQQLKEQLNnQKVEeaiqQYERACK 1294
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKE-ALLEAK-EEIHKLRNEFEKELRERRNELQKLEKRLL-QKEE----NLDRKLE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1841445197 1295 DLNVKEKIiedmrmtleeqeqtqveqdqvLEAKLEEVERLATELEKWKEKCNDLETKNNQR 1355
Cdd:PRK12704 104 LLEKREEE---------------------LEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1001-1310 |
2.38e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.80 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1001 SKKSHQIEELEQQIEKLQAEVKGYKDENN-RLKEKEH-KNQDDLLKEKETLIQQLKEELQEKNVTLDV---QIQHVVE-- 1073
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVDlKLQELQHlKNEGDHLRNVQTECEALKLQMAEKDKVIEIlrqQIENMTQlv 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1074 ---GKRALSELTQGVTCYK--------------------AKIKELE---TILETQKVECSHSA----------KLEQDIL 1117
Cdd:pfam15921 579 gqhGRTAGAMQVEKAQLEKeindrrlelqefkilkdkkdAKIRELEarvSDLELEKVKLVNAGserlravkdiKQERDQL 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1118 EKESIILKLERN-LKEFQEHLQDSVKN-TKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSA 1195
Cdd:pfam15921 659 LNEVKTSRNELNsLSEDYEVLKRNFRNkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITA 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1196 SSARTQNLKADLQRkeedyadLKEKLTDAkkqikqvQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKE 1275
Cdd:pfam15921 739 KRGQIDALQSKIQF-------LEEAMTNA-------NKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
330 340 350
....*....|....*....|....*....|....*..
gi 1841445197 1276 QLNNQKV--EEAIQQYERaCKDLnVKEKIIEDMRMTL 1310
Cdd:pfam15921 805 KVANMEValDKASLQFAE-CQDI-IQRQEQESVRLKL 839
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1002-1291 |
2.69e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.52 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1002 KKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKEtLIQQLKEELQEKNVT-------LDVQIQH---- 1070
Cdd:PRK04778 102 KAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKD-LYRELRKSLLANRFSfgpaldeLEKQLENleee 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1071 ------------VVEGKRALSELTQGVTCYKAKIKELETILETQKVEC-SHSAKLE---QDILEKESII--LKLERNLKE 1132
Cdd:PRK04778 181 fsqfveltesgdYVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKagyRELVEEGYHLdhLDIEKEIQD 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1133 FQEHLQDSVKNTKDLNVKElkLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEE 1212
Cdd:PRK04778 261 LKEQIDENLALLEELDLDE--AEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQ 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1213 DY---ADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNN-----QKVEE 1284
Cdd:PRK04778 339 SYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGlrkdeLEARE 418
|
....*..
gi 1841445197 1285 AIQQYER 1291
Cdd:PRK04778 419 KLERYRN 425
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1110-1306 |
2.70e-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: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1110 AKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQlkeEEEETNRQETEKL 1189
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1190 KEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRT 1269
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1841445197 1270 IQQLKEQLNNQ-----KVEEAIQQYERACKDLNVKEKIIEDM 1306
Cdd:COG4942 187 RAALEALKAERqkllaRLEKELAELAAELAELQQEAEELEAL 228
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
984-1248 |
3.13e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.43 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 984 SSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDE----NNRLKE-----KEHKNQDDLLKEKetlIQQLK 1054
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKrdelNAQVKElreeaQELREKRDELNEK---VKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1055 EELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKA---KIKELETILETQKVECSHSAKLEQDILEKESIILKLERnLK 1131
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGGSIDKlrkEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKK-AL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1132 EFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKE 1211
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 1841445197 1212 EDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIK 1248
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1043-1356 |
3.38e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1043 LKEKETLIQQLKEELQEKNVTLDVQIQHVvegkralselTQGVTCYKAKIKELEtiletqkvecshsAKLEQDILEKESI 1122
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHI----------QQQIKTYNKNIEEQR-------------KKNGENIARKQNK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1123 I---LKLERNLKEFQEHLQDSVKNtkdlnvkelkLKEEITQLTNNLQDMKHlLQLKEEEEETNRQETEKLKEELSASSAR 1199
Cdd:PHA02562 222 YdelVEEAKTIKAEIEELTDELLN----------LVMDIEDPSAALNKLNT-AAAKIKSKIEQFQKVIKMYEKGGVCPTC 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1200 TQNLKadlqrkeedyaDLKEKLTDAKKQIKQVQKEVsvmrdedKLLRIKINELEKKKNqcsqELDMKQRTIQQLKEQLNN 1279
Cdd:PHA02562 291 TQQIS-----------EGPDRITKIKDKLKELQHSL-------EKLDTAIDELEEIMD----EFNEQSKKLLELKNKIST 348
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841445197 1280 QKveEAIQQYERACKDLnvkEKIIEDMRMTLEEQEqtqveqdqvleaklEEVERLATELEKWKEKCNDLETKNNQRS 1356
Cdd:PHA02562 349 NK--QSLITLVDKAKKV---KAAIEELQAEFVDNA--------------EELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
978-1132 |
3.39e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 978 RENSFHSSIEAIWEECKEIVKASSKKshqIEELEQQIEkLQAevkgyKDENNRLK---EKEHKNQDDLLKEKETLIQQLK 1054
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKE---AEAIKKEAL-LEA-----KEEIHKLRnefEKELRERRNELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1841445197 1055 EELQEKNVTLDVQIQHVVEGKRALSELTQGVtcyKAKIKELETILETQKVECSHSAKLEQDilE-KESIILKLERNLKE 1132
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQEL---EKKEEELEELIEEQLQELERISGLTAE--EaKEILLEKVEEEARH 169
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1002-1291 |
3.60e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.15 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1002 KKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKEtLIQQLKEELQEKNVT-------LDVQIQHV--- 1071
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKD-KYRELRKTLLANRFSygpaideLEKQLAEIeee 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1072 -------------VEGKRALSELTQGVTCYKAKIKELETILETQKVEcshsakLEQDILEKESII------------LKL 1126
Cdd:pfam06160 162 fsqfeeltesgdyLEAREVLEKLEEETDALEELMEDIPPLYEELKTE------LPDQLEELKEGYremeeegyalehLNV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1127 ERNLKEFQEHLQDSVKNTKDLNVKElkLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKAD 1206
Cdd:pfam06160 236 DKEIQQLEEQLEENLALLENLELDE--AEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1207 LQRKEEDY---ADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNN---- 1279
Cdd:pfam06160 314 LERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSlrkd 393
|
330
....*....|...
gi 1841445197 1280 -QKVEEAIQQYER 1291
Cdd:pfam06160 394 eLEAREKLDEFKL 406
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1199-1489 |
4.39e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.03 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1199 RTQNLKADLQRKEEDYADLKEKLTDAKKQIKQ-----VQKEVSVMRDEDKLLRIKINELEKKKNQCSQ-ELDMKQRTIQQ 1272
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaiyAEQERMAMERERELERIRQEERKRELERIRQeEIAMEISRMRE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1273 LKE-QLNNQKVEEAIQQYERACKDLNVKEKiiEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETK 1351
Cdd:pfam17380 380 LERlQMERQQKNERVRQELEAARKVKILEE--ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1352 NNQRSNKEHENNTDVLGKLTNLQDElQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMe 1431
Cdd:pfam17380 458 RQQQVERLRQQEEERKRKKLELEKE-KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR- 535
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1841445197 1432 iltaqltekdsdlQKWREERdqlvaaleiqlkalissnvQKDNEIEQLKRIISETSKI 1489
Cdd:pfam17380 536 -------------REAEEER-------------------RKQQEMEERRRIQEQMRKA 561
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1125-1505 |
4.42e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1125 KLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLK 1204
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1205 ADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKIN-------ELEKKKNQCSQELDMKQRTIQQLKEQL 1277
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNdlkkqkeELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1278 NNQK-----VEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKN 1352
Cdd:TIGR04523 197 LKLElllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1353 NQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQ----QN 1428
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEltnsES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1429 EMEILTAQLTEKDSDLQKWREERDQL----------VAALEIQLKALISSNVQKDNEIEQLKriiSETSKIETQIMDIKP 1498
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYkqeiknlesqINDLESKIQNQEKLNQQKDEQIKKLQ---QEKELLEKEIERLKE 433
|
....*..
gi 1841445197 1499 KRISSAD 1505
Cdd:TIGR04523 434 TIIKNNS 440
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1206-1351 |
4.67e-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: 40.68 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1206 DLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEA 1285
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841445197 1286 IQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVE-RLATELEKWKEKCNDLETK 1351
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEaELEEKKAELDEELAELEAE 157
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
648-724 |
4.91e-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: 41.29 E-value: 4.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1841445197 648 QIKAELAKTKGELIKTKEELKKRENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNLKSHMENTFK 724
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1219-1485 |
5.49e-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: 41.29 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1219 EKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN--NQKVEEAIQQYERACKDL 1296
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAalEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1297 NVKEKIIEDMRMTLEeqeqtqveqdqvleaKLEEVERLATELekwkekcndletknNQRSNKEHENNTDVLGKLTnlqDE 1376
Cdd:COG4942 100 EAQKEELAELLRALY---------------RLGRQPPLALLL--------------SPEDFLDAVRRLQYLKYLA---PA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1377 LQESEQKYNADRKKwleekmmLITQAKEAEnirnkemkkyaedrerffKQQNEMEILTAQLTEKDSDLQKWREERDQLVA 1456
Cdd:COG4942 148 RREQAEELRADLAE-------LAALRAELE------------------AERAELEALLAELEEERAALEALKAERQKLLA 202
|
250 260
....*....|....*....|....*....
gi 1841445197 1457 ALEIQLKALISSNVQKDNEIEQLKRIISE 1485
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1223-1497 |
5.81e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1223 DAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKI 1302
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1303 IEdmrmtleeqeqtqveqdqVLEAKLEEVERLATELEKWKEKCNDLETKNNQRsnkehenNTDVLGKLTNLQDELQESEQ 1382
Cdd:COG4913 687 LA------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAAED 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1383 KYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEME-----------ILTAQLTEKDSDLQKWREER 1451
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELEramrafnrewpAETADLDADLESLPEYLALL 821
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1452 DQLVA----ALEIQLKALIssNVQKDNEIEQLKriisetSKIETQIMDIK 1497
Cdd:COG4913 822 DRLEEdglpEYEERFKELL--NENSIEFVADLL------SKLRRAIREIK 863
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1049-1488 |
6.10e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 6.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1049 LIQQLKEELQE----KNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETiLETQKVEcshsakLEQDILEKESIIL 1124
Cdd:COG4717 47 LLERLEKEADElfkpQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEE------LEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1125 KLERnLKEFQEHLQDSVKNTKDLNvkelKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNlk 1204
Cdd:COG4717 120 KLEK-LLQLLPLYQELEALEAELA----ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1205 aDLQRKEEDYADLKEKLTDAKKQIKQVQKEVsvmrdedKLLRIKINELEKKknqcsQELDMKQRTIQQLKEQLN------ 1278
Cdd:COG4717 193 -ELQDLAEELEELQQRLAELEEELEEAQEEL-------EELEEELEQLENE-----LEAAALEERLKEARLLLLiaaall 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1279 ---------------------------------NQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVeqdqvlE 1325
Cdd:COG4717 260 allglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPP------D 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1326 AKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDE-----LQESEQKYNADRKKWLEEKMMLIT 1400
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelraALEQAEEYQELKEELEELEEQLEE 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1401 QAKEAENIRNKEMKKYAEDrerffkqqnEMEILTAQLTEKDSDLQKWREERdqlvAALEIQLKALISSN--VQKDNEIEQ 1478
Cdd:COG4717 414 LLGELEELLEALDEEELEE---------ELEELEEELEELEEELEELREEL----AELEAELEQLEEDGelAELLQELEE 480
|
490
....*....|
gi 1841445197 1479 LKRIISETSK 1488
Cdd:COG4717 481 LKAELRELAE 490
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
986-1168 |
8.68e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.52 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 986 IEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLlKEKETLIQQLKEELQEKNVTLD 1065
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI-AELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1066 VQIQH--------------VVEGKRALSELTQG----VTCYKAKIKELETILETQKVEcshSAKLEQDILEKESIILKLE 1127
Cdd:COG4942 115 RLGRQpplalllspedfldAVRRLQYLKYLAPArreqAEELRADLAELAALRAELEAE---RAELEALLAELEEERAALE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1841445197 1128 RNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDM 1168
Cdd:COG4942 192 ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1010-1148 |
8.76e-03 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 40.80 E-value: 8.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1841445197 1010 LEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDL--LKEK-ETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVT 1086
Cdd:pfam10168 566 LKLQKEQQLQELQSLEEERKSLSERAEKLAEKYeeIKDKqEKLMRRCKKVLQRLNSQLPVLSDAEREMKKELETINEQLK 645
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1841445197 1087 CYKAKIKELETILETQKvecSHSAKlEQDILEKESIILKLER------NLKEFQEHLQDSVKNTKDLN 1148
Cdd:pfam10168 646 HLANAIKQAKKKMNYQR---YQIAK-SQSIRKKSSLSLSEKQrktikeILKQLGSEIDELIKQVKDIN 709
|
|
| |
