|
Name |
Accession |
Description |
Interval |
E-value |
| KISc_KIF23_like |
cd01368 |
Kinesin motor domain, KIF23-like subgroup; Kinesin motor domain, KIF23-like subgroup. Members ... |
57-477 |
1.56e-172 |
|
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: 525.42 E-value: 1.56e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 57 DYLQVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQCILGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQP 136
Cdd:cd01368 1 DPVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 137 VKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmnlkphrsreylrlsseqekeeiask 216
Cdd:cd01368 81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 217 sallrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmansikFSVWVSFFEIYNEYIYDLFVPV-SSKFQ 295
Cdd:cd01368 130 ----------------------------------------------------YSVFVSYIEIYNEYIYDLLEPSpSSPTK 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 296 KRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSE------MSR 369
Cdd:cd01368 158 KRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSdgdvdqDKD 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 370 VIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSKFQQHVPFRESKLTHYFQSFFNGKGK 449
Cdd:cd01368 238 QITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGK 317
|
410 420
....*....|....*....|....*...
gi 5911999 450 ICMIVNISQCYLAYDETLNVLKFSAIAQ 477
Cdd:cd01368 318 ASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
64-479 |
6.05e-92 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 301.80 E-value: 6.05e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 64 RIRPFTQSEKELESEGCVHILDSQTvvlkepqcILGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLLKG 143
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDS--------ETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 144 QSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLytkmnlkphrsreylrlsseqekeeiasksallrqi 223
Cdd:pfam00225 73 YNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK------------------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 224 kevtvhndsddtlygsltnslnisefeesikdyeqanlnmaNSIKFSVWVSFFEIYNEYIYDLFVPVSSKFQKrkmLRLS 303
Cdd:pfam00225 117 -----------------------------------------ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRK---LRIR 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 304 QDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQ-IEDSEMSRVIRVSELSLCDLA 382
Cdd:pfam00225 153 EDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQrNRSTGGEESVKTGKLNLVDLA 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 383 GSERTMKTQN-EGERLRETGNINTSLLTLGKCINVLKnsekSKFQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQCYL 461
Cdd:pfam00225 233 GSERASKTGAaGGQRLKEAANINKSLSALGNVISALA----DKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSS 308
|
410
....*....|....*...
gi 5911999 462 AYDETLNVLKFSAIAQKV 479
Cdd:pfam00225 309 NYEETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
60-479 |
2.73e-90 |
|
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: 297.18 E-value: 2.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 60 QVCLRIRPFTQSEKELESEGCVHILDSQTVVLkepqcilgRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:smart00129 3 RVVVRVRPLNKREKSRKSPSVVPFPDKVGKTL--------TVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 140 LLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLYTKmnlkphrsreylrlsseqekeeiasksal 219
Cdd:smart00129 75 VLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGW----------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 220 lrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmansiKFSVWVSFFEIYNEYIYDLFVPVSSKfqkrkm 299
Cdd:smart00129 126 ------------------------------------------------QFSVKVSYLEIYNEKIRDLLNPSSKK------ 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 300 LRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSRVIRVSELSLC 379
Cdd:smart00129 152 LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNLV 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 380 DLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKskfQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQC 459
Cdd:smart00129 232 DLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSK---SRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPS 308
|
410 420
....*....|....*....|
gi 5911999 460 YLAYDETLNVLKFSAIAQKV 479
Cdd:smart00129 309 SSNLEETLSTLRFASRAKEI 328
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
60-477 |
1.24e-86 |
|
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: 286.46 E-value: 1.24e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 60 QVCLRIRPFTQSEKELESEgCVHILDSQTVVLKEPqcilgrlseKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:cd00106 3 RVAVRVRPLNGREARSAKS-VISVDGGKSVVLDPP---------KNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 140 LLKGQSRLIFTYGLTNSGKTYTFQGT-EENIGILPRTLNVLFDSLQERLYTKMNlkphrsreylrlsseqekeeiasksa 218
Cdd:cd00106 73 ALEGYNGTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKRKETKSS-------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 219 llrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmansikFSVWVSFFEIYNEYIYDLFVPVsskfqKRK 298
Cdd:cd00106 127 --------------------------------------------------FSVSASYLEIYNEKIYDLLSPV-----PKK 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 299 MLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSRVIRVSELSL 378
Cdd:cd00106 152 PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVTSSKLNL 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 379 CDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKskfqQHVPFRESKLTHYFQSFFNGKGKICMIVNISQ 458
Cdd:cd00106 232 VDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN----KHIPYRDSKLTRLLQDSLGGNSKTIMIACISP 307
|
410
....*....|....*....
gi 5911999 459 CYLAYDETLNVLKFSAIAQ 477
Cdd:cd00106 308 SSENFEETLSTLRFASRAK 326
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
64-479 |
3.63e-64 |
|
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: 221.70 E-value: 3.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 64 RIRPFTQSEkelESEGCVHIL----DSQTVVLKepqcilgrlseksSGQMAQK-FSFSKVFGPATTQKEFFQGcIMQPVK 138
Cdd:cd01366 9 RVRPLLPSE---ENEDTSHITfpdeDGQTIELT-------------SIGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmnlkphrsreylrlsSEQekeeiasksa 218
Cdd:cd01366 72 SALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKEL-------------------KEK---------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 219 llrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmanSIKFSVWVSFFEIYNEYIYDLfvpVSSKFQKRK 298
Cdd:cd01366 123 -----------------------------------------------GWSYTIKASMLEIYNETIRDL---LAPGNAPQK 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 299 MLRLSQD-VKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKIlQIEDsEMSRVIRVSELS 377
Cdd:cd01366 153 KLEIRHDsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-SGRN-LQTGEISVGKLN 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 378 LCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSekskfQQHVPFRESKLTHYFQSFFNGKGKICMIVNIS 457
Cdd:cd01366 231 LVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQK-----QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNIS 305
|
410 420
....*....|....*....|..
gi 5911999 458 QCYLAYDETLNVLKFsaiAQKV 479
Cdd:cd01366 306 PAESNLNETLNSLRF---ASKV 324
|
|
| KISc_KIF4 |
cd01372 |
Kinesin motor domain, KIF4-like subfamily; Kinesin motor domain, KIF4-like subfamily. Members ... |
60-479 |
3.48e-63 |
|
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: 219.51 E-value: 3.48e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 60 QVCLRIRPFTQSEKeleSEGCvhiLDSQTVVLKEPQCILGRlsekssgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:cd01372 4 RVAVRVRPLLPKEI---IEGC---RICVSFVPGEPQVTVGT---------DKSFTFDYVFDPSTEQEEVYNTCVAPLVDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 140 LLKGQSRLIFTYGLTNSGKTYTFQGT------EENIGILPRTLNVLFDSLQErlytkmnlkphrsreylrlsseqekeei 213
Cdd:cd01372 69 LFEGYNATVLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEK---------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 214 asksallrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnMANSIKFSVWVSFFEIYNEYIYDLFvpvSSK 293
Cdd:cd01372 121 -------------------------------------------------KKDTFEFQLKVSFLEIYNEEIRDLL---DPE 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 294 FQKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQ----IEDSEMSR 369
Cdd:cd01372 149 TDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQtkknGPIAPMSA 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 370 VIR----VSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKFQQHVPFRESKLTHYFQSFFN 445
Cdd:cd01372 229 DDKnstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISAL--GDESKKGAHVPYRDSKLTRLLQDSLG 306
|
410 420 430
....*....|....*....|....*....|....
gi 5911999 446 GKGKICMIVNISQCYLAYDETLNVLKFSAIAQKV 479
Cdd:cd01372 307 GNSHTLMIACVSPADSNFEETLNTLKYANRARNI 340
|
|
| KISc_KIP3_like |
cd01370 |
Kinesin motor domain, KIP3-like subgroup; Kinesin motor domain, KIP3-like subgroup. The yeast ... |
59-479 |
8.95e-61 |
|
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: 212.59 E-value: 8.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 59 LQVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQCILGRLSEKSSGQMAQ-------KFSFSKVFGPATTQKEFFQG 131
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGFFHGGSNNRDRRkrrnkelKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 132 CIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmnlkphrsreylrlsseqeke 211
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIES-------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 212 eiasksallrqikevtvhnDSDDTlygsltnslnisefeesikdyeqanlnmansiKFSVWVSFFEIYNEYIYDLFVPVS 291
Cdd:cd01370 136 -------------------LKDEK--------------------------------EFEVSMSYLEIYNETIRDLLNPSS 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 292 skfqkrKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIE-DSEMSRV 370
Cdd:cd01370 165 ------GPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDkTASINQQ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 371 IRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKFQQHVPFRESKLTHYFQSFFNGKGKI 450
Cdd:cd01370 239 VRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINAL--ADPGKKNKHIPYRDSKLTRLLKDSLGGNCRT 316
|
410 420
....*....|....*....|....*....
gi 5911999 451 CMIVNISQCYLAYDETLNVLKFSAIAQKV 479
Cdd:cd01370 317 VMIANISPSSSSYEETHNTLKYANRAKNI 345
|
|
| KISc_BimC_Eg5 |
cd01364 |
Kinesin motor domain, BimC/Eg5 spindle pole proteins; Kinesin motor domain, BimC/Eg5 spindle ... |
59-476 |
2.91e-59 |
|
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: 208.72 E-value: 2.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 59 LQVCLRIRPFTQSEKELESEGCVHILDSQtvvlKEPQCILGRLSEKSSgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVK 138
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVR----KEVSVRTGGLADKSS---TKTYTFDMVFGPEAKQIDVYRSVVCPILD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTE-----------ENIGILPRTLNVLFDSLqerlytkmnlkphrsreylrlsSE 207
Cdd:cd01364 77 EVLMGYNCTIFAYGQTGTGKTYTMEGDRspneeytweldPLAGIIPRTLHQLFEKL----------------------ED 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 208 QEKEeiasksallrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmansikFSVWVSFFEIYNEYIYDLF 287
Cdd:cd01364 135 NGTE---------------------------------------------------------YSVKVSYLEIYNEELFDLL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 288 VPVSSKFQKRKMLRLSQDVKGYsFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIE-DSE 366
Cdd:cd01364 158 SPSSDVSERLRMFDDPRNKRGV-IIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKEtTID 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 367 MSRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKfqqHVPFRESKLTHYFQSFFNG 446
Cdd:cd01364 237 GEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL--VERAP---HVPYRESKLTRLLQDSLGG 311
|
410 420 430
....*....|....*....|....*....|
gi 5911999 447 KGKICMIVNISQCYLAYDETLNVLKFSAIA 476
Cdd:cd01364 312 RTKTSIIATISPASVNLEETLSTLEYAHRA 341
|
|
| KISc_CENP_E |
cd01374 |
Kinesin motor domain, CENP-E/KIP2-like subgroup; Kinesin motor domain, CENP-E/KIP2-like ... |
60-479 |
3.54e-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: 207.19 E-value: 3.54e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 60 QVCLRIRPFTQSEKELEsEGCVHILDSQTVVLKEPQcilgrlsekssgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:cd01374 3 TVTVRVRPLNSREIGIN-EQVAWEIDNDTIYLVEPP--------------STSFTFDHVFGGDSTNREVYELIAKPVVKS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 140 LLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmnlkpHRSREYLrlsseqekeeiasksal 219
Cdd:cd01374 68 ALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD----------TPDREFL----------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 220 lrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmansikfsVWVSFFEIYNEYIYDLFVPVSskfqkrKM 299
Cdd:cd01374 121 ---------------------------------------------------LRVSYLEIYNEKINDLLSPTS------QN 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 300 LRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSRV-IRVSELSL 378
Cdd:cd01374 144 LKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGtVRVSTLNL 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 379 CDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNsekSKFQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQ 458
Cdd:cd01374 224 IDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE---GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITP 300
|
410 420
....*....|....*....|.
gi 5911999 459 CYLAYDETLNVLKFSAIAQKV 479
Cdd:cd01374 301 AESHVEETLNTLKFASRAKKI 321
|
|
| KISc_KHC_KIF5 |
cd01369 |
Kinesin motor domain, kinesin heavy chain (KHC) or KIF5-like subgroup; Kinesin motor domain, ... |
59-472 |
4.42e-55 |
|
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: 195.63 E-value: 4.42e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 59 LQVCLRIRPFTQSEKELESEGCVHILDSQTVVLkepqcilgRLSEKSSgqmaqKFSFSKVFGPATTQKEFFQGCIMQPVK 138
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVI--------ATSETGK-----TFSFDRVFDPNTTQEDVYNFAAKPIVD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 139 DLLKGQSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSLqerlytkmnlkphrsreylrlsseqekeeias 215
Cdd:cd01369 71 DVLNGYNGTIFAYGQTSSGKTYTMEGKlgdPESMGIIPRIVQDIFETI-------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 216 ksallrqikevtvhndsddtlygsltnslnisefeesikdyeqanLNMANSIKFSVWVSFFEIYNEYIYDLFVPvsskfq 295
Cdd:cd01369 119 ---------------------------------------------YSMDENLEFHVKVSYFEIYMEKIRDLLDV------ 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 296 KRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQiEDSEmSRVIRVSE 375
Cdd:cd01369 148 SKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-ENVE-TEKKKSGK 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 376 LSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSkfqqHVPFRESKLTHYFQSFFNGKGKICMIVN 455
Cdd:cd01369 226 LYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKT----HIPYRDSKLTRILQDSLGGNSRTTLIIC 301
|
410
....*....|....*..
gi 5911999 456 ISQCYLAYDETLNVLKF 472
Cdd:cd01369 302 CSPSSYNESETLSTLRF 318
|
|
| KISc_KIF1A_KIF1B |
cd01365 |
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A ... |
60-479 |
1.18e-53 |
|
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: 192.57 E-value: 1.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 60 QVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQcilGRLSEKSSGQMAQKFSFSKVF------GPA-TTQKEFFQGC 132
Cdd:cd01365 4 KVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQ---ADKNNKATREVPKSFSFDYSYwshdseDPNyASQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 133 IMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFdslqerlytkmnlkphrsreylrlsseqekEE 212
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLF------------------------------SR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 213 IASKSAllrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmaNSIKFSVWVSFFEIYNEYIYDLFVPvsS 292
Cdd:cd01365 131 IADTTN----------------------------------------------QNMSYSVEVSYMEIYNEKVRDLLNP--K 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 293 KFQKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQI--EDSEMSRV 370
Cdd:cd01365 163 PKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKrhDAETNLTT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 371 IRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVL---KNSEKSKFQQHVPFRESKLTHYFQSFFNGK 447
Cdd:cd01365 243 EKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmSSGKSKKKSSFIPYRDSVLTWLLKENLGGN 322
|
410 420 430
....*....|....*....|....*....|..
gi 5911999 448 GKICMIVNISQCYLAYDETLNVLKFSAIAQKV 479
Cdd:cd01365 323 SKTAMIAAISPADINYEETLSTLRYADRAKKI 354
|
|
| KISc_KIF3 |
cd01371 |
Kinesin motor domain, kinesins II or KIF3_like proteins; Kinesin motor domain, kinesins II or ... |
57-479 |
1.21e-52 |
|
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: 188.82 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 57 DYLQVCLRIRPFTQSEKeleSEGCVHILD----SQTVVLKEPqcilgrlsEKSSGQMAQKFSFSKVFGPATTQKEFFQGC 132
Cdd:cd01371 1 ENVKVVVRCRPLNGKEK---AAGALQIVDvdekRGQVSVRNP--------KATANEPPKTFTFDAVFDPNSKQLDVYDET 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 133 IMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSlqerlytkmnlkphrsreylrlsseqe 209
Cdd:cd01371 70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKredPELRGIIPNSFAHIFGH--------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 210 keeIASKSallrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmaNSIKFSVWVSFFEIYNEYIYDLFvp 289
Cdd:cd01371 123 ---IARSQ-----------------------------------------------NNQQFLVRVSYLEIYNEEIRDLL-- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 290 vsSKFQKRKM-LRLSQDVKGYsfIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKIlqiEDSEM- 367
Cdd:cd01371 151 --GKDQTKRLeLKERPDTGVY--VKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI---ECSEKg 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 368 ---SRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSeKSkfqQHVPFRESKLTHYFQSFF 444
Cdd:cd01371 224 edgENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG-KS---THIPYRDSKLTRLLQDSL 299
|
410 420 430
....*....|....*....|....*....|....*
gi 5911999 445 NGKGKICMIVNISQCYLAYDETLNVLKFSAIAQKV 479
Cdd:cd01371 300 GGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
59-474 |
1.60e-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: 179.24 E-value: 1.60e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 59 LQVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQcilgrlseksSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVK 138
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPR----------NHGETLKYQFDAFYGEESTQEDIYAREVQPIVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLnvlfdslqerlytkmnlkphrsREYLRLSSEQekeeiasksa 218
Cdd:cd01376 72 HLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTV----------------------MDLLQMTRKE---------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 219 llrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmanSIKFSVWVSFFEIYNEYIYDLFVPvsskfqKRK 298
Cdd:cd01376 120 -----------------------------------------------AWALSFTMSYLEIYQEKILDLLEP------ASK 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 299 MLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSRVIRvSELSL 378
Cdd:cd01376 147 ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRT-GKLNL 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 379 CDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKskfqqHVPFRESKLTHYFQSFFNGKGKICMIVNISQ 458
Cdd:cd01376 226 IDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLP-----RIPYRDSKLTRLLQDSLGGGSRCIMVANIAP 300
|
410
....*....|....*.
gi 5911999 459 CYLAYDETLNVLKFSA 474
Cdd:cd01376 301 ERTFYQDTLSTLNFAA 316
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
57-472 |
5.83e-49 |
|
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: 178.47 E-value: 5.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 57 DYLQVCLRIRPFTQSEKELESEGCVHILDSQTVVLkepqcilgrlseksSGQMAQKFSFSKVFGPATTQKEFFQGCIMQP 136
Cdd:cd01373 1 DAVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVL--------------HSKPPKTFTFDHVADSNTNQESVFQSVGKPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 137 VKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENI--------GILPRTLNVLFDSLQErlytkmnlkphrsreylrlssEQ 208
Cdd:cd01373 67 VESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQR---------------------EK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 209 EKEEiasksallrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmaNSIKFSVWVSFFEIYNEYIYDLFV 288
Cdd:cd01373 126 EKAG----------------------------------------------------EGKSFLCKCSFLEIYNEQIYDLLD 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 289 PVSSKfqkrkmLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMS 368
Cdd:cd01373 154 PASRN------LKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACF 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 369 RVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSKfQQHVPFRESKLTHYFQSFFNGKG 448
Cdd:cd01373 228 VNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGK-QRHVCYRDSKLTFLLRDSLGGNA 306
|
410 420
....*....|....*....|....
gi 5911999 449 KICMIVNISQCYLAYDETLNVLKF 472
Cdd:cd01373 307 KTAIIANVHPSSKCFGETLSTLRF 330
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
105-598 |
3.50e-43 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 167.61 E-value: 3.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 105 SSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQ 184
Cdd:COG5059 50 LEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 185 ERLYTKmnlkphrsreylrlsseqekeeiasksallrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnma 264
Cdd:COG5059 130 DLSMTK-------------------------------------------------------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 265 nsiKFSVWVSFFEIYNEYIYDLFVPvsSKFQKRKMLRLSQDVKgysfIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKL 344
Cdd:COG5059 136 ---DFAVSISYLEIYNEKIYDLLSP--NEESLNIREDSLLGVK----VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 345 NNASSRSHSIFTVKiLQIEDSEMSrVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSK 424
Cdd:COG5059 207 NDESSRSHSIFQIE-LASKNKVSG-TSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 425 fqqHVPFRESKLTHYFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFSA----IAQKVCVP-------------DTLNS 487
Cdd:COG5059 285 ---HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASraksIKNKIQVNsssdssreieeikFDLSE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 488 SQDKLFGPVKSSQDVSLDSNSN---SKILNVKRATISWENSLEDLMededlveeLENAEETQNVETKLLDEDLDKTLEEN 564
Cdd:COG5059 362 DRSEIEILVFREQSQLSQSSLSgifAYMQSLKKETETLKSRIDLIM--------KSIISGTFERKKLLKEEGWKYKSTLQ 433
|
490 500 510
....*....|....*....|....*....|....*
gi 5911999 565 KAFIshEEKRKLLDLIEDLKKKLINE-KKEKLTLE 598
Cdd:COG5059 434 FLRI--EIDRLLLLREEELSKKKTKIhKLNKLRHD 466
|
|
| KISc_KIF2_like |
cd01367 |
Kinesin motor domain, KIF2-like group; Kinesin motor domain, KIF2-like group. KIF2 is a ... |
61-475 |
5.07e-43 |
|
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: 160.54 E-value: 5.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 61 VCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQCILgRLSEKSSgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVKDL 140
Cdd:cd01367 4 VCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKV-DLTKYIE---NHTFRFDYVFDESSSNETVYRSTVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 141 LKGQSRLIFTYGLTNSGKTYT----FQGTEENIGILprtlnvlfdslqerlytkmnlkphrsreylrlsseqekeEIASK 216
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTmggdFSGQEESKGIY---------------------------------------ALAAR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 217 SaLLRQIKEVTVHNDsddtlygsltnslnisefeesikdyeqanlnmansikFSVWVSFFEIYNEYIYDLFvpvsskfQK 296
Cdd:cd01367 121 D-VFRLLNKLPYKDN-------------------------------------LGVTVSFFEIYGGKVFDLL-------NR 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 297 RKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSrvirvSEL 376
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTNKLH-----GKL 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 377 SLCDLAGSERTMKT-QNEGERLRETGNINTSLLTLGKCINVLKNSekskfQQHVPFRESKLTHYFQ-SFFNGKGKICMIV 454
Cdd:cd01367 231 SFVDLAGSERGADTsSADRQTRMEGAEINKSLLALKECIRALGQN-----KAHIPFRGSKLTQVLKdSFIGENSKTCMIA 305
|
410 420
....*....|....*....|.
gi 5911999 455 NISQCYLAYDETLNVLKFSAI 475
Cdd:cd01367 306 TISPGASSCEHTLNTLRYADR 326
|
|
| KISc_KIF9_like |
cd01375 |
Kinesin motor domain, KIF9-like subgroup; Kinesin motor domain, KIF9-like subgroup; might play ... |
59-474 |
8.03e-39 |
|
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: 148.88 E-value: 8.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 59 LQVCLRIRPFTQSEKELESEGcvhiLDSQTVVLKEPQCIlgRLSEKSSGQMAQKFSFSKVFGPATtQKEFFQGCIMQPVK 138
Cdd:cd01375 2 VQAFVRVRPTDDFAHEMIKYG----EDGKSISIHLKKDL--RRGVVNNQQEDWSFKFDGVLHNAS-QELVYETVAKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTEENI---GILPRTLNVLFDSLQERlYTKMnlkphrsreylrlsseqekeeias 215
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENYkhrGIIPRALQQVFRMIEER-PTKA------------------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 216 ksallrqikeVTVHndsddtlygsltnslnisefeesikdyeqanlnmansikfsvwVSFFEIYNEYIYDLFVPVSSKFQ 295
Cdd:cd01375 130 ----------YTVH-------------------------------------------VSYLEIYNEQLYDLLSTLPYVGP 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 296 KRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSRVIRVSE 375
Cdd:cd01375 157 SVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLSSEKYITSK 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 376 LSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKfqQHVPFRESKLTHYFQSFFNGKGKICMIVN 455
Cdd:cd01375 237 LNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIAL--SDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVAN 312
|
410
....*....|....*....
gi 5911999 456 ISQCYLAYDETLNVLKFSA 474
Cdd:cd01375 313 IYGEAAQLEETLSTLRFAS 331
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
92-501 |
4.88e-32 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 136.99 E-value: 4.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 92 KEPQCILGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQG-----TE 166
Cdd:PLN03188 113 EEGEMIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglLE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 167 ENI-----GILPRTLNVLFDslqerlytkmnlkphrsreylRLSSEQEKeeiasksallrqikevtvHNDsddtlygslt 241
Cdd:PLN03188 193 EHLsgdqqGLTPRVFERLFA---------------------RINEEQIK------------------HAD---------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 242 nslnisefeesikdyeqanlnmaNSIKFSVWVSFFEIYNEYIYDLFVPVsskfQKRKMLRlsQDVKGYSFIKDLQWIQVS 321
Cdd:PLN03188 224 -----------------------RQLKYQCRCSFLEIYNEQITDLLDPS----QKNLQIR--EDVKSGVYVENLTEEYVK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 322 DSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTV----KILQIEDSEMSrvIRVSELSLCDLAGSERTMKTQNEGERL 397
Cdd:PLN03188 275 TMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCvvesRCKSVADGLSS--FKTSRINLVDLAGSERQKLTGAAGDRL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 398 RETGNINTSLLTLGKCINVLKNSEKSKFQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFS---- 473
Cdd:PLN03188 353 KEAGNINRSLSQLGNLINILAEISQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAqrak 432
|
410 420
....*....|....*....|....*...
gi 5911999 474 AIAQKVCVPDTLNSSQDKLFGPVKSSQD 501
Cdd:PLN03188 433 AIKNKAVVNEVMQDDVNFLREVIRQLRD 460
|
|
| RBD_KIF20B |
cd21786 |
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ... |
600-654 |
1.63e-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: 83.68 E-value: 1.63e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 5911999 600 KIREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREE 654
Cdd:cd21786 1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNKTAKEEE 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1037-1311 |
3.09e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 78.56 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1037 QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLkEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGV 1116
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1117 TCYKAKIKELETILETQKVERshsAKLEQDILEKESIILKLERNLKEFQEHLQDsvkntkdLNVKELKLKEEITQLTNNL 1196
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEI---EELEAQIEQLKEELKALREALDELRAELTL-------LNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1197 QDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLL 1276
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270
....*....|....*....|....*....|....*
gi 5911999 1277 RIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQ 1311
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEE 948
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
700-1310 |
4.72e-13 |
|
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: 74.29 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 700 KRENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNlkshMENTFKCNDKADTSSLIINNKLICNETVEV 779
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNN----KIKILEQQIKDLNDKLKKNKDKINKLNSDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 780 PK-DSKSKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVRPNIAEIEDIRVLQENnegLRAFLLTIENEL 858
Cdd:TIGR04523 106 SKiNSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE---LENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 859 KNEKEEKAELNKQIVHFQQELSLSEKKN----------LTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEI 928
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIqknkslesqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 929 ETATRSITNNVSQIKLMHTKIDELRtlDSVSQISNidllNLRDLSNGSEEDNLPNTQLDLLGNDylvsKQVKEYRIQEPN 1008
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELE--KQLNQLKS----EISDLNNQKEQDWNKELKSELKNQE----KKLEEIQNQISQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1009 RE---NSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLK------EKEHKNQDDLLKEKET 1079
Cdd:TIGR04523 333 NNkiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLEsqindlESKIQNQEKLNQQKDE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1080 LIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQ-----------KVERSHSAKLEQDIL 1148
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLetqlkvlsrsiNKIKQNLEQKQKELK 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1149 EKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLL---------QLKEEEEETNRQETEK 1219
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEE 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1220 LKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQR 1299
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
650
....*....|.
gi 5911999 1300 TIQQLKEQLNN 1310
Cdd:TIGR04523 653 TIKEIRNKWPE 663
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1036-1321 |
1.69e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.66 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1036 HQIEELEQQIEKLQAEVKGYKDENNRLKEKehknqddlLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQG 1115
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAE--------LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1116 VTCYKAKIKELETILETQKVERshsAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNN 1195
Cdd:COG1196 304 IARLEERRRELEERLEELEEEL---AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1196 LQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKL 1275
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 5911999 1276 LRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQkvEEAIQQYE 1321
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLL--LEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
679-1418 |
2.01e-12 |
|
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: 72.78 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 679 QIKAELAKTKGELIKTKEELKKR--ENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNLKSHMENTFkc 756
Cdd:TIGR02168 206 ERQAEKAERYKELKAELRELELAllVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI-- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 757 nDKADTSSLIINNKL-ICNETVEVPKDSKSKICSERKRVNEnELQQDEppakKGSIHVSSAITEDQKKSEEVRPNIAEIE 835
Cdd:TIGR02168 284 -EELQKELYALANEIsRLEQQKQILRERLANLERQLEELEA-QLEELE----SKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 836 D--------IRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIA-IAE 906
Cdd:TIGR02168 358 AeleeleaeLEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAeLKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 907 LHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKL-MHTKIDELRTLDSVSQISNIDLLNLRDLSNGseEDNLPNTQ 985
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQaLDAAERELAQLQARLDSLERLQENLEGFSEG--VKALLKNQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 986 LDLLGNDYLVSKQVK---EY----------RIQEP--NRENSFHSSIEAIWEECKEIVK---ASSKKSHQIEELEQQIEK 1047
Cdd:TIGR02168 516 SGLSGILGVLSELISvdeGYeaaieaalggRLQAVvvENLNAAKKAIAFLKQNELGRVTflpLDSIKGTEIQGNDREILK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1048 LQAEVKGYKDENNRLKEKEHKNQDDLL------KEKETLIQQLKE-ELQEKNVTLD---VQIQHVVEGKRAlsELTQGVT 1117
Cdd:TIGR02168 596 NIEGFLGVAKDLVKFDPKLRKALSYLLggvlvvDDLDNALELAKKlRPGYRIVTLDgdlVRPGGVITGGSA--KTNSSIL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1118 CYKAKIKELETILEtqkvershsaKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQ 1197
Cdd:TIGR02168 674 ERRREIEELEEKIE----------ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1198 DMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLR 1277
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLR 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1278 IKINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEA 1357
Cdd:TIGR02168 824 ERLESLERRIAATERRLEDLEEQIEELSEDI--ESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5911999 1358 KLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNL-QDELQESEQKYNAD 1418
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKI 963
|
|
| RBD_KIF20A-like |
cd21744 |
RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; ... |
600-654 |
5.65e-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: 5.65e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 5911999 600 KIREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREE 654
Cdd:cd21744 1 RIREEVSEEFEEQFALMEEDYEERLENEKEILEERYEKRLEIRKELIKKLSAALE 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1038-1415 |
1.42e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.09 E-value: 1.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1038 IEELEQQIEKLQAEVKG---YKDENNRLKEKEHknqdDLLKekeTLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTq 1114
Cdd:TIGR02168 195 LNELERQLKSLERQAEKaerYKELKAELRELEL----ALLV---LRLEELREELEELQEELKEAEEELEELTAELQELE- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1115 gvtcykAKIKELEtiLETQKVERShSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTN 1194
Cdd:TIGR02168 267 ------EKLEELR--LEVSELEEE-IEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1195 NLQDMKHLLQLkeeeeetnrqetekLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDK 1274
Cdd:TIGR02168 338 ELAELEEKLEE--------------LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1275 LLRIKINELEKKKNQCSQEldmkqrtIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQV 1354
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQE-------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5911999 1355 LEAKLEEVERLATELEKWKEKCNDLEtkNNQRSNKEHENNTDVLGKLTNLQDELQESEQKY 1415
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLE--GFSEGVKALLKNQSGLSGILGVLSELISVDEGY 535
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1013-1371 |
1.50e-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: 69.71 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1013 FHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEkn 1092
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQ-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1093 vtLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVERShsAKLEQDILEKESIILKLERNLKEFQEHLQDSV 1172
Cdd:TIGR02169 246 --LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ--LRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1173 KNTKDLNVKELKLKEEITQLTNNLQDMKhllqlkeeeeetnrQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKL 1252
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEER--------------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1253 TDAKKQIKQVQKEvsvmrdedkllrikINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKEK 1332
Cdd:TIGR02169 388 KDYREKLEKLKRE--------------INELKRELDRLQEELQRLSEELADLNAAI--AGIEAKINELEEEKEDKALEIK 451
|
330 340 350
....*....|....*....|....*....|....*....
gi 5911999 1333 IIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEK 1371
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1033-1462 |
6.21e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1033 KKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDdlLKEKETLIQQLKEELqeKNVTLDVQIQHVVEGKRALSEL 1112
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE--AKAKKEELERLKKRL--TGLTPEKLEKELEELEKAKEEI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1113 TQGVTCYKAKIKELETILETQK--VERSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEIT 1190
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKkaIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1191 QLTNNLQDMKHLLQLKEEEEETNRqetekLKEELSASSARtqnlkaDLQRKEEDYADLKEKLTDAKKQIKQVQKEVSvmr 1270
Cdd:PRK03918 484 ELEKVLKKESELIKLKELAEQLKE-----LEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELE--- 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1271 dedkllriKINELEKKKNQCSQELDMKQRTIQQLKEQLNN------QKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQ 1344
Cdd:PRK03918 550 --------KLEELKKKLAELEKKLDELEEELAELLKELEElgfesvEELEERLKELEPFYNEYLELKDAEKELEREEKEL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1345 EQTQVEqdqvLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGK----LTNLQDELQESEQKYNADRK 1420
Cdd:PRK03918 622 KKLEEE----LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRelagLRAELEELEKRREEIKKTLE 697
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 5911999 1421 KWLEEKMMLITQAKEAENIrNKEMKKYAEDRERFFKQQNEME 1462
Cdd:PRK03918 698 KLKEELEEREKAKKELEKL-EKALERVEELREKVKKYKALLK 738
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1240-1543 |
6.43e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.65 E-value: 6.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1240 RKEEDYADLKEKLTDAKKQIKQVQKEvsVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN--NQKVEEAI 1317
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLR--ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEelELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1318 QQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHEnntdv 1397
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE----- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1398 lgkltnLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEmkkyAEDRERFFKQQNEMEILTAQLTEKDSDLQK 1477
Cdd:COG1196 363 ------AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL----EELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5911999 1478 WREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPKRISSADPDKLQTE 1543
Cdd:COG1196 433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
617-1471 |
8.41e-11 |
|
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: 67.30 E-value: 8.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 617 EADFKETLLQEREILEENAERRLAIFKDLVGKCDTREEAAKDICATKVETEEATACLELKFNQIKAELAKTKGELIKTKE 696
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 697 ELKKRENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNLKshmentfkCNDKADTSSLIINNKLICNET 776
Cdd:pfam02463 244 ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE--------EEELKSELLKLERRKVDDEEK 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 777 VEVPKDSKSKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVRPNIAEIEDIRVLQENNEGLRAFLLTIEN 856
Cdd:pfam02463 316 LKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 857 ELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQSnyDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSIT 936
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE--SIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 937 NNVSQIKLMHTKIDELRTLDSVsqisniDLLNLRDLSNGSEEDNLPNTQLDLLGNDyLVSKQVKEYRIQEPNRENSFHSS 1016
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKL------EERSQKESKARSGLKVLLALIKDGVGGR-IISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1017 IEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLD 1096
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1097 VQIQHVVEGKRALSELTQGVTCYKAKI-------KELETILETQKVERSHSAKLEQDILEKESIILKLERNLKEFQEHLQ 1169
Cdd:pfam02463 627 GILKDTELTKLKESAKAKESGLRKGVSleeglaeKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQ 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1170 DSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLK 1249
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKL 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1250 EKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKvEEAIQQYERACKDLNV 1329
Cdd:pfam02463 787 KVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLE-KLAEEELERLEEEITK 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1330 KEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQ 1409
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA 945
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5911999 1410 ESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEK 1471
Cdd:pfam02463 946 DEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKL 1007
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
984-1528 |
9.65e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 9.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 984 TQLDLLGNDYLVSKQVKEYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLK 1063
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1064 ----------------EKEHKNQDDLLKEKETLIQQLKEELQ--EKNVTLDVQIQHVVEGKRALSELTQGvtcYKAKIKE 1125
Cdd:PRK03918 235 elkeeieelekeleslEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEE---YLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1126 LETILETQKVERSHSAKLEQDILEKESIILKLERNLKEFQ---EHLQDSVKNTKDLNVKELKLKEEITQLTN-NLQDMKH 1201
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTGlTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1202 LLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQR---------------KEEDYADLKEKLTdakKQIKQVQKEV 1266
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEYT---AELKRIEKEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1267 SVMRDEDKLLRIKINELEKKKNQCSQELDMKQrTIQQLKE------QLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMT 1340
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIKLKE-LAEQLKEleeklkKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1341 LEEQEQTQVEQDqVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRK 1420
Cdd:PRK03918 548 LEKLEELKKKLA-ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1421 KWLEEKMMLITQAKEAENIRNK-EMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEiQLKALISS 1499
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKElEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE-KLKEELEE 705
|
570 580
....*....|....*....|....*....
gi 5911999 1500 NVQKDNEIEQLKRIISETSKIETQIMDIK 1528
Cdd:PRK03918 706 REKAKKELEKLEKALERVEELREKVKKYK 734
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
869-1529 |
1.36e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 869 NKQIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTK 948
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 949 IDEL-RTLDSVSQISNIDLLNLRDLSNGSEEDNlpnTQLDLLgndylvSKQVKEYRIQEPNRENSFHSSIEAIWEECKEI 1027
Cdd:TIGR02168 318 LEELeAQLEELESKLDELAEELAELEEKLEELK---EELESL------EAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1028 VKASSKK---SHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLK----EKETLIQQLKEELQEKNVTLDVQIQ 1100
Cdd:TIGR02168 389 AQLELQIaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQaeleELEEELEELQEELERLEEALEELRE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1101 HVVEGKRALSELTQGVTCYKAKIKELETILETQK---------------------------------------------- 1134
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvkallknqsglsgilgvlselisvdegyeaaieaalggrlq 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1135 ---VERSHSAKLEQDILEKESIIL------------KLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQL------T 1193
Cdd:TIGR02168 549 avvVENLNAAKKAIAFLKQNELGRvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1194 NNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSAR------TQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVS 1267
Cdd:TIGR02168 629 DDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSaktnssILERRREIEELEEKIEELEEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1268 VMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVE-----EAIQQYERACKDLNVKEKIIEDMRMTLE 1342
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKElteleAEIEELEERLEEAEEELAEAEAEIEELE 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1343 EQEQTQVEQDQVLEAKL----EEVERLATELEKWKEKCNDLE------TKNNQRSNKEHENNTDVLGKLTNLQDELQESE 1412
Cdd:TIGR02168 789 AQIEQLKEELKALREALdelrAELTLLNEEAANLRERLESLErriaatERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1413 QKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAAL--- 1489
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsee 948
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 5911999 1490 -EIQLKALISSNVQKDNEIEQLKRiisETSKIETQIMDIKP 1529
Cdd:TIGR02168 949 ySLTLEEAEALENKIEDDEEEARR---RLKRLENKIKELGP 986
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1038-1375 |
4.95e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1038 IEELEQQIEKL--QAEV----KGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALse 1111
Cdd:COG1196 195 LGELERQLEPLerQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-- 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1112 ltqgvtcyKAKIKELE-TILETQKVERSHSAKLEQdiLEKESIILKLERnlkefqehlqdsvkntKDLNVKELKLKEEIT 1190
Cdd:COG1196 273 --------RLELEELElELEEAQAEEYELLAELAR--LEQDIARLEERR----------------RELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1191 QLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMR 1270
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1271 DEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEA--IQQYERACKDLNVKEKIIEDMRMTLEEQEQTQ 1348
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAelEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340
....*....|....*....|....*..
gi 5911999 1349 VEQDQVLEAKLEEVERLATELEKWKEK 1375
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAA 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
992-1306 |
8.57e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 63.93 E-value: 8.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 992 DYLVSKQVKEYRIQEPNRENsFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGY-KDENNRLKEKEHKNQ 1070
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEA-IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1071 DDL--LKEKETLIQQLKEELQEKNVTLDVQIQHvvegkralseltqgvtcYKAKIKELETILETQKVERshsAKLEQDIL 1148
Cdd:TIGR02169 301 AEIasLERSIAEKERELEDAEERLAKLEAEIDK-----------------LLAEIEELEREIEEERKRR---DKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1149 EKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLqdmkhllqlkeeeeetnrqetEKLKEELSASS 1228
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL---------------------DRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1229 ARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRD-----EDKLLRIK--INELEKKKNQCSQELDMKQRTI 1301
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAdlskyEQELYDLKeeYDRVEKELSKLQRELAEAEAQA 499
|
....*
gi 5911999 1302 QQLKE 1306
Cdd:TIGR02169 500 RASEE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1246-1511 |
1.49e-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: 63.15 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1246 ADLKEKLTDAKKQIKQVQKEVSVMRDEDklLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN-----NQKVEEAIQQY 1320
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQELEEKLEelrleVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1321 ERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVER----LATELEKWKEKCNDLEtknnqrsnkehENNTD 1396
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldeLAEELAELEEKLEELK-----------EELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1397 VLGKLTNLQDELQESEQKYNADRKKWLEEKmmlitqakeaenirnkemKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQ 1476
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLR------------------SKVAQLELQIASLNNEIERLEARLERLEDRRE 417
|
250 260 270
....*....|....*....|....*....|....*.
gi 5911999 1477 KWREERDQLVAAL-EIQLKALISSNVQKDNEIEQLK 1511
Cdd:TIGR02168 418 RLQQEIEELLKKLeEAELKELQAELEELEEELEELQ 453
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1014-1332 |
1.91e-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: 62.78 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1014 HSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKehknqddlLKEKETLIQQLKEELQEKNV 1093
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR--------IEELEEDLHKLEEALNDLEA 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1094 TLDVQIQHVVEGKraLSELTQGVTCYKAKIKELETILETQKVERshsAKLEQDILEKESIILKLERNLKEFQEHLQDSVK 1173
Cdd:TIGR02169 787 RLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLEK---EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1174 NTKDLNVKELKLKEEITQLTNNLQDMKhllqlkeeeeetnrQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLT 1253
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLK--------------KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1254 DAKKQIKQVQKEVSVMrdedkllrIKINELEKKKNQCSQELDMKQRTIQQLkEQLNNQkveeAIQQYERACKDLN-VKEK 1332
Cdd:TIGR02169 928 ALEEELSEIEDPKGED--------EEIPEEELSLEDVQAELQRVEEEIRAL-EPVNML----AIQEYEEVLKRLDeLKEK 994
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1038-1446 |
4.71e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1038 IEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDL------LKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSE 1111
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEInektteISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1112 LTQGVTCYKAKI------------KELETILETQKVERSHS-----------AKLEQDILEKESIILKLERNLKEFQEHL 1168
Cdd:TIGR04523 286 LEKQLNQLKSEIsdlnnqkeqdwnKELKSELKNQEKKLEEIqnqisqnnkiiSQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1169 QDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADL 1248
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1249 KEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQlnNQKVEEAIQQYERACKDLN 1328
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE--KKELEEKVKDLTKKISSLK 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1329 VKEKIiedmrmtLEEQEQTQVEQDQVLEAKLEEVerlatELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDEL 1408
Cdd:TIGR04523 524 EKIEK-------LESEKKEKESKISDLEDELNKD-----DFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
410 420 430
....*....|....*....|....*....|....*...
gi 5911999 1409 QESEQKYNADRKKwLEEKMMLITQAKEAENIRNKEMKK 1446
Cdd:TIGR04523 592 DQKEKEKKDLIKE-IEEKEKKISSLEKELEKAKKENEK 628
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1037-1381 |
9.60e-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: 60.47 E-value: 9.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1037 QIEELEQQIEKLQAEVKGYKDENNRLkEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGV 1116
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRI-ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1117 TCYKAKIKELETILEtQKVERSHSAKLEQDILEKE---SIILKLERNLKEFQEHLQDSVKNTKDLNVKELKL---KEEIT 1190
Cdd:TIGR02169 754 ENVKSELKELEARIE-ELEEDLHKLEEALNDLEARlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLtleKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1191 QLTNNLQDMKHLLQLKEEEeetnrqetekLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSvmr 1270
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKS----------IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR--- 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1271 dedkllrikinELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEA-IQQYERACKDLNVKEKIIEDMRMTLEEQEQTQV 1349
Cdd:TIGR02169 900 -----------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSeIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
330 340 350
....*....|....*....|....*....|..
gi 5911999 1350 EQDQVLEAKLEEVERLATELEKWKEKCNDLET 1381
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1037-1496 |
1.03e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1037 QIEELEQQIEKLQAEVKGYKDENNRLKEkEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGV 1116
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1117 TCYKAKIKELETILETQKVERshsAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNL 1196
Cdd:COG1196 396 AELAAQLEELEEAEEALLERL---ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1197 QDMKHLLQLKEEEEETNRQETEKLKE-----ELSASSARTQNLKADLQRKEEDYADL--KEKLTDAKKQIKQVQKEVSVM 1269
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEaeadyEGFLEGVKAALLLAGLRGLAGAVAVLigVEAAYEAALEAALAAALQNIV 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1270 RDEDKLLRIKINELEKKKNQCSQELDM-KQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIED---MRMTLEEQE 1345
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLdKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllGRTLVAARL 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1346 QTQVEQDQVLEAKLEEVERLATELEKWKEKcndLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEE 1425
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSL---TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5911999 1426 KMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLvAALEIQLKAL 1496
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL-ERLEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
778-1471 |
2.81e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 778 EVPKDSKSKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVRpniaEIEDIRVLQEnneglraflltienE 857
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELK----KAEEKKKADE--------------A 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 858 LKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITN 937
Cdd:PTZ00121 1296 KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 938 NVSQIKLMHTKIDELRTLDSVSQISNIDLLNLRDLSNGSEE----DNLPNTQLDLLGNDYLVSKQVKEYRIQEPNRENSF 1013
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAkkkaDEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1014 HSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKEtliQQLKEELQEKNV 1093
Cdd:PTZ00121 1456 AKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE---AKKADEAKKAEE 1532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1094 TLDVQIQHVVEGKRALSELTqgvtcykaKIKELETILETQKVERSHSAKLEQDILEKESIILKL--ERNLKEFQEHLQDS 1171
Cdd:PTZ00121 1533 AKKADEAKKAEEKKKADELK--------KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKaeEARIEEVMKLYEEE 1604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1172 VKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKeeeeeTNRQETEKLKEELSASSARTQNLKADLQRKEED----YAD 1247
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK-----KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEdkkkAEE 1679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1248 LKEKLTDAKKQIKQVQKEVSVMRDEDKlLRIKINELEKKKNQCSQELDMKQRTIQQLKeqlnnQKVEEAIQQYERACKDL 1327
Cdd:PTZ00121 1680 AKKAEEDEKKAAEALKKEAEEAKKAEE-LKKKEAEEKKKAEELKKAEEENKIKAEEAK-----KEAEEDKKKAEEAKKDE 1753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1328 NVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEhenNTDVLgkltNLQDE 1407
Cdd:PTZ00121 1754 EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKE---GNLVI----NDSKE 1826
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5911999 1408 LQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAED--RERFFKQQNEMEILTAQLTEK 1471
Cdd:PTZ00121 1827 MEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADfnKEKDLKEDDEEEIEEADEIEK 1892
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1001-1558 |
8.26e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.84 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1001 EYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDllkeKETL 1080
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDA----KRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1081 IQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKA----------------------KIKELETILETQKVERS 1138
Cdd:PTZ00121 1156 IARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAedarkaeaarkaeeerkaeearKAEDAKKAEAVKKAEEA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1139 HSAKLEQDILEKE---SIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQL--TNNLQDMKHLLQLKEEEEETN 1213
Cdd:PTZ00121 1236 KKDAEEAKKAEEErnnEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1214 RQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKltDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQE 1293
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE--AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1294 LDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWK 1373
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1374 E-KCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEkmmlitqAKEAENIRNKEMKKYAEDRE 1452
Cdd:PTZ00121 1474 EaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE-------AKKAEEAKKADEAKKAEEKK 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1453 RFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQiMDIKPKRI 1532
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEEL 1625
|
570 580
....*....|....*....|....*.
gi 5911999 1533 SSADPDKLQTEPLSTSFEISRNKIED 1558
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
883-1322 |
1.18e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 883 EKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRTLDSVSQIs 962
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 963 nidllnLRDLSNGSEEDNLPNTQLDLLGNDYlvsKQVKEYRIQEPNRENSFHSSIEAIWEECKEIvkaSSKKSHQIEELE 1042
Cdd:COG4717 131 ------YQELEALEAELAELPERLEELEERL---EELRELEEELEELEAELAELQEELEELLEQL---SLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1043 QQIEKLQAEVKGYKDENNRLK-EKEHKNQDDLLKEKETLIQQLKEELQEKNVTL------------DVQIQHVVEGKRAL 1109
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQeELEELEEELEQLENELEAAALEERLKEARLLLliaaallallglGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1110 SELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDILEKESIILKLERNLKEFQE-----HLQDSVKNTKDLNVKELK 1184
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeellELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1185 LKEEItQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEE---------DYADLKEKLTDA 1255
Cdd:COG4717 359 LEEEL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGeleellealDEEELEEELEEL 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5911999 1256 KKQIKQVQKEVSVMRDEDKLLRIKINELEKkknqcSQELDMKQRTIQQLKEQLNN------------QKVEEAIQQYER 1322
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRElaeewaalklalELLEEAREEYRE 511
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
887-1490 |
1.79e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 887 LTLSKEVQQIQSNYdiAIAELHVQKSKNQEQEEKIMKLSNEIETATRsitnnvsQIKLMHTKIDELRTldsvsqisniDL 966
Cdd:COG1196 216 RELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEA-------ELAELEAELEELRL----------EL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 967 LNLRDLSNgseednlpntqldllgndylvSKQVKEYRIQepnrensfhSSIEAIWEECKEIVKASSKKSHQIEELEQQIE 1046
Cdd:COG1196 277 EELELELE---------------------EAQAEEYELL---------AELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1047 KLQAEVKGYKDENNRLKEkEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKEL 1126
Cdd:COG1196 327 ELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1127 ETILETQKVERshsAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLK 1206
Cdd:COG1196 406 EEAEEALLERL---ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1207 EEEEETNRQETEKLKE-----ELSASSARTQNLKADLQRKEEDYADL--KEKLTDAKKQIKQVQKEVSVMRDEDKLLRIK 1279
Cdd:COG1196 483 LEELAEAAARLLLLLEaeadyEGFLEGVKAALLLAGLRGLAGAVAVLigVEAAYEAALEAALAAALQNIVVEDDEVAAAA 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1280 INELEKKKNQCSQELDM-KQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIED---MRMTLEEQEQTQVEQDQVL 1355
Cdd:COG1196 563 IEYLKAAKAGRATFLPLdKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllGRTLVAARLEAALRRAVTL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1356 EAKLEEVERLATELEKWKEKcndLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKE 1435
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSL---TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 5911999 1436 AENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDS---DLQKWREERDQLVAALE 1490
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppDLEELERELERLEREIE 777
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
623-1332 |
2.56e-07 |
|
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: 56.00 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 623 TLLQEREILEENAERRLAIFKDLVGKCDTREEAAKDICAT-KVETEEATACLElkfNQIKAELAKTKGELIKTKEELKKR 701
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQEtSAELNQLLRTLD---DQWKEKRDELNGELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 702 ENESDSLiqeletSNKKIITQNQRIKELINIIDQKEDTINEFQNL-KSHMENTFKCND-KADTSSLIINNKLICNETVEV 779
Cdd:pfam12128 321 RSELEAL------EDQHGAFLDADIETAAADQEQLPSWQSELENLeERLKALTGKHQDvTAKYNRRRSKIKEQNNRDIAG 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 780 PKDSKSKICSERKR---VNENELQQDEPPAKkgsihvssaitedqkksEEVRPNIAEIEDIRVLQENNEGLRAFLLTIEN 856
Cdd:pfam12128 395 IKDKLAKIREARDRqlaVAEDDLQALESELR-----------------EQLEAGKLEFNEEEYRLKSRLGELKLRLNQAT 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 857 ELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIA-----IAELHVQKSKNQEQEEKIMkLSNEIETA 931
Cdd:pfam12128 458 ATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQAsealrQASRRLEERQSALDELELQ-LFPQAGTL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 932 TRSITNNVSQIKlmhtkiDELRTLDSVSQISNIDLLNLRDLSNGSEEDNLPNTQLDLLG---NDYLVSKQVKEYRIqepn 1008
Cdd:pfam12128 537 LHFLRKEAPDWE------QSIGKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRidvPEWAASEEELRERL---- 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1009 reNSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEEL 1088
Cdd:pfam12128 607 --DKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1089 QeknvTLDVQIQHVVEGKRALSELTQGvTCYKAKIKELETILEtqkVERSHSAKLEQDILEKESIILKLERNLKEFQEHL 1168
Cdd:pfam12128 685 N----SLEAQLKQLDKKHQAWLEEQKE-QKREARTEKQAYWQV---VEGALDAQLALLKAAIAARRSGAKAELKALETWY 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1169 QDSVKNTKDLNVKELKLKEEITQLTNNL----QDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEd 1244
Cdd:pfam12128 757 KRDLASLGVDPDVIAKLKREIRTLERKIeriaVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIA- 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1245 yadlkekltDAKKQIKQVQKEvsvmRDEDKLLRIKINELEKKknqcsqeLDMKQRTIQQLKEQLNNQKVEEAIQQYERAC 1324
Cdd:pfam12128 836 ---------DTKLRRAKLEME----RKASEKQQVRLSENLRG-------LRCEMSKLATLKEDANSEQAQGSIGERLAQL 895
|
....*...
gi 5911999 1325 KDLNVKEK 1332
Cdd:pfam12128 896 EDLKLKRD 903
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
808-1126 |
2.82e-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: 55.83 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 808 KGSIHVSSAITEDQKKSEEVRPNIAEIE-DIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKN 886
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEeKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 887 LTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRtldsvsqiSNIDL 966
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR--------AELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 967 LNLRDLSNGSEEDNLPNTQLDLLGNDYLVSKQVKEYR--IQEPNRE-NSFHSSIEAIWEECKEIVKASSKKSHQIEELEQ 1043
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSedIESLAAEiEELEELIEELESELEALLNERASLEEALALLRS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1044 QIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETL------IQQLKEELQEK-NVTLDVQIQHVVEGKRALSELTQGV 1116
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLeglevrIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRL 974
|
330
....*....|
gi 5911999 1117 TCYKAKIKEL 1126
Cdd:TIGR02168 975 KRLENKIKEL 984
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
523-1244 |
3.31e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 55.75 E-value: 3.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 523 ENSLEDLMEDEDLVEELENAEETQNVETKLLDEDLDKTLEENKAFISHEEKRKLLDLIEDLKKKLINEKKEKLTLEFKIR 602
Cdd:pfam02463 307 RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 603 EEVTQEFTQYWAQREADFKE--TLLQEREILEENAERRLAIFKDLVGKCDTREEAAKDICATKVETEEATACLELKFNQI 680
Cdd:pfam02463 387 SSAAKLKEEELELKSEEEKEaqLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELE 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 681 KAELAKTKGELIKTKEELKKRENESDSLIQELETSNKKIitQNQRIKELINIIDQKEDTINEFQNLKShmentfkcndKA 760
Cdd:pfam02463 467 LKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKA--RSGLKVLLALIKDGVGGRIISAHGRLG----------DL 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 761 DTSSLIINNKLICNETVEVPKDSKSKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVRPNIAeIEDIRVL 840
Cdd:pfam02463 535 GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLA-QLDKATL 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 841 QENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEK 920
Cdd:pfam02463 614 EADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 921 IMKLSNEIETATRSITNNVSQIKLMHTKIDELRTLDSVSQISNIDLLNLRDLSNGSEEDNLPNTQLDLLGNDYlvsKQVK 1000
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEK---SELS 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1001 EYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETL 1080
Cdd:pfam02463 771 LKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEK 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1081 IQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQgVTCYKAKIKELETILETQKVERSHSAKLEQDILEKESIILKLERN 1160
Cdd:pfam02463 851 LAEEELERLEEEITKEELLQELLLKEEELEEQKL-KDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEI 929
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1161 LKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQ---------DMKHLLQLKEEEEETNRQETEKLKEELSASSART 1231
Cdd:pfam02463 930 LLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLlakeelgkvNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIR 1009
|
730
....*....|...
gi 5911999 1232 QNLKADLQRKEED 1244
Cdd:pfam02463 1010 AIIEETCQRLKEF 1022
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1037-1511 |
5.31e-07 |
|
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: 54.97 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1037 QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDllKEKETLIQQLKEELQEKNVTLDVQIQHVvEGKRALSELTQGV 1116
Cdd:TIGR00618 450 TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE--TRKKAVVLARLLELQEEPCPLCGSCIHP-NPARQDIDNPGPL 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1117 TCykakikELETILETQKvershsaKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNL 1196
Cdd:TIGR00618 527 TR------RMQRGEQTYA-------QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1197 QDMKHLLQLKEEEEETNRQETEKLKEELsassartqNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLL 1276
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKL--------QPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1277 RIKINELEKkknqcSQELDMKQRTIQQLKEQLNNQKveEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLE 1356
Cdd:TIGR00618 666 SIRVLPKEL-----LASRQLALQKMQSEKEQLTYWK--EMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARE 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1357 AKLEEVERLATELEKWKEKCNDLEtknNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEA 1436
Cdd:TIGR00618 739 DALNQSLKELMHQARTVLKARTEA---HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD 815
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5911999 1437 ENIRNKEMKKYAEDRERFfkqQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKalISSNVQKDNEIEQLK 1511
Cdd:TIGR00618 816 EDILNLQCETLVQEEEQF---LSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK--IIQLSDKLNGINQIK 885
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1246-1530 |
5.92e-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: 54.69 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1246 ADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRtIQQLKEQLNNQKVEEAIQQYERACK 1325
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE-KREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1326 DLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLAT-ELEKWKEKCNDLETKNNQRSNKEHENNTDvlgkltnl 1404
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1405 QDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRErffkqqnEMEILTAQLTEKDSDLQKWREERDQ 1484
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE-------ELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 5911999 1485 LVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPK 1530
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1038-1528 |
6.19e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.44 E-value: 6.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1038 IEELEQQIEKLQAE-VKGYKDENNRLKEKE-HKNQDDLLKEKetlIQQLKEELQEKNVTLdvqiqhvVEGKRALSELTQG 1115
Cdd:pfam10174 249 IRDLEDEVQMLKTNgLLHTEDREEEIKQMEvYKSHSKFMKNK---IDQLKQELSKKESEL-------LALQTKLETLTNQ 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1116 VTCYKAKIKELETILeTQKVERSHSAKLEQDIL-----EKESIilklernLKEFQEHLQDsvkntkdlnvkelkLKEEIT 1190
Cdd:pfam10174 319 NSDCKQHIEVLKESL-TAKEQRAAILQTEVDALrlrleEKESF-------LNKKTKQLQD--------------LTEEKS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1191 QLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEED-------YADLKEKLTDAKKQIKQVQ 1263
Cdd:pfam10174 377 TLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtaLTTLEEALSEKERIIERLK 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1264 KEVS----VMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQ------------KVEEAIQQYERACKDL 1327
Cdd:pfam10174 457 EQREredrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLassglkkdsklkSLEIAVEQKKEECSKL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1328 NVKEKIIEDMRMTlEEQEQTQVEQDQVLEA----KLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTN 1403
Cdd:pfam10174 537 ENQLKKAHNAEEA-VRTNPEINDRIRLLEQevarYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELESLTLRQMKE 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1404 LQDELQESEQKYNADRKKWLEEkmMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLT-------EKDSDLQ 1476
Cdd:pfam10174 616 QNKKVANIKHGQQEMKKKGAQL--LEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSstqqslaEKDGHLT 693
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 5911999 1477 KWR-EERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIK 1528
Cdd:pfam10174 694 NLRaERRKQLEEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALK 746
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
822-1369 |
7.13e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.30 E-value: 7.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 822 KKSEEVRPNIAEIEDIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLsKEVQQIQSNYD 901
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 902 IAIAELHVQKSKNQEQEEKIMKLSNEIETATRSI---TNNVSQIKLMHTKIDELRtldsvsqisnidllnlRDLSNGSEE 978
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkelEEKEERLEELKKKLKELE----------------KRLEELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 979 DNLPNTQLDLLGNDYLVSKQVKEYRIQEPNREnsfhssIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQA---EVKGY 1055
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGLTPEKLEKE------LEELEKAKEEIEEEISKITARIGELKKEIKELKKaieELKKA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1056 K------------DENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKnvtldVQIQHVVEGKRALSELTQGVTcykaKI 1123
Cdd:PRK03918 435 KgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL-----RELEKVLKKESELIKLKELAE----QL 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1124 KELETILETQKVERSHSAKLEQDILEKESIILKLErnlkefQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLL 1203
Cdd:PRK03918 506 KELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1204 QLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINE- 1282
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEe 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1283 ----LEKKKNQCSQELDMKQRTIQQLKEQL-----NNQKVEEAIQQYERACKDLNVKEKIIEDMRmtlEEQEQTQVEQDQ 1353
Cdd:PRK03918 660 eyeeLREEYLELSRELAGLRAELEELEKRReeikkTLEKLKEELEEREKAKKELEKLEKALERVE---ELREKVKKYKAL 736
|
570
....*....|....*.
gi 5911999 1354 VLEAKLEEVERLATEL 1369
Cdd:PRK03918 737 LKERALSKVGEIASEI 752
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1022-1490 |
7.31e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1022 EECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEK--EHKNQ--------DDLLKEKE------TLIQQLK 1085
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEvrDLRERleeleeerDDLLAEAGlddadaEAVEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1086 EELQEKnvtlDVQIQHVVEGKR-ALSELTQGVTCYKAKIK--------------ELETILETQKVE----RSHSAKLEQD 1146
Cdd:PRK02224 317 EELEDR----DEELRDRLEECRvAAQAHNEEAESLREDADdleeraeelreeaaELESELEEAREAvedrREEIEELEEE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1147 ILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSA 1226
Cdd:PRK02224 393 IEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEE 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1227 SSARTQNLKADLQRKEEDYADLKEKLT---DAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQ 1303
Cdd:PRK02224 473 DRERVEELEAELEDLEEEVEEVEERLEraeDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAE 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1304 LKEQLNN-QKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEqeqtqveqdqvLEAKLEEVERLATELEKWKEKCNDLETK 1382
Cdd:PRK02224 553 AEEKREAaAEAEEEAEEAREEVAELNSKLAELKERIESLER-----------IRTLLAAIADAEDEIERLREKREALAEL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1383 NNQRsnKEhenntdvlgKLTNLQDELQESEQKYNADRkkwleekmmlITQAKeaenirnkemkkyaEDRERFFKQQNEME 1462
Cdd:PRK02224 622 NDER--RE---------RLAEKRERKRELEAEFDEAR----------IEEAR--------------EDKERAEEYLEQVE 666
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 5911999 1463 ILTAQLTEKDSDLQK--------------WREERDQLVAALE 1490
Cdd:PRK02224 667 EKLDELREERDDLQAeigaveneleeleeLRERREALENRVE 708
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1037-1259 |
7.94e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.86 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1037 QIEELEQQIEKLQAEVKGYKDENNRLKEK------EHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEgkrALS 1110
Cdd:PHA02562 182 QIQTLDMKIDHIQQQIKTYNKNIEEQRKKngeniaRKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSA---ALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1111 ELTQGVTCYKAKIKELETILETQKvERSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKElklkEEIT 1190
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFQKVIKMYE-KGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIM----DEFN 333
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5911999 1191 QLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQI 1259
Cdd:PHA02562 334 EQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1219-1421 |
8.09e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.23 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1219 KLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQ 1298
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1299 RTIQQLKEQ------LNNQKVEEAIQQYERACKDLNVKEKIIEDMRMT---LEEQEQTQVEQDQVLEAKLEEVERLATEL 1369
Cdd:COG4942 111 RALYRLGRQpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADlaeLAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5911999 1370 EKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKK 1421
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1234-1538 |
1.09e-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: 53.92 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1234 LKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKV 1313
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL--SSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1314 EEAIQQYERACKDLnvkEKIIEDMRMTLEEqeqtqveqdqvLEAKLEEVERLATElEKWKEKCNDLETKNNQRSNKEhen 1393
Cdd:TIGR02169 750 EQEIENVKSELKEL---EARIEELEEDLHK-----------LEEALNDLEARLSH-SRIPEIQAELSKLEEEVSRIE--- 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1394 ntdvlGKLTNLQDELQESEQK--YNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKqqnEMEILTAQLTEK 1471
Cdd:TIGR02169 812 -----ARLREIEQKLNRLTLEkeYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE---ELEAALRDLESR 883
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5911999 1472 DSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPKRISSADPD 1538
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1119-1448 |
1.62e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1119 YKAKIKELETILETQKVERSHS--AKLEQDILEKESIILKLERNLKEFQEHLQDsvkntkdLNVKELKLKEEITQLTNNL 1196
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREelEELQEELKEAEEELEELTAELQELEEKLEE-------LRLEVSELEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1197 QDMKHLLQlkeeeeetnrqeteKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKevsvmrdedkll 1276
Cdd:TIGR02168 291 YALANEIS--------------RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE------------ 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1277 riKINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKEKIIEdmrmtleeqeqtqveqdqvle 1356
Cdd:TIGR02168 345 --KLEELKEELESLEAELEELEAELEELESRL--EELEEQLETLRSKVAQLELQIASLN--------------------- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1357 aklEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEA 1436
Cdd:TIGR02168 400 ---NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330
....*....|..
gi 5911999 1437 ENIRNKEMKKYA 1448
Cdd:TIGR02168 477 LDAAERELAQLQ 488
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
543-1195 |
1.62e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 543 EETQNVETKLLDEDLDKTLEENKAFISHEEKRKLLDLIEDLKKKLINEKKEklTLEFKIREEVTQEFTQywaQREADFKE 622
Cdd:PTZ00121 1247 EERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKK--AEEKKKADEAKKKAEE---AKKADEAK 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 623 TLLQEREILEENAERRLAIFKDLVGKCDTREEAAKDIcATKVETEEATACLELKFNQIKAELAKTKGELIKTKEELKKRE 702
Cdd:PTZ00121 1322 KKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE-AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKA 1400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 703 NESDSLIQELetsnKKIITQNQRIKELiniiDQKEDTINEFQNLKSHMENTFKCNDKADTSSLIINNKLICNETVEVPKD 782
Cdd:PTZ00121 1401 EEDKKKADEL----KKAAAAKKKADEA----KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 783 SKSKICSERKRVNEnELQQDEPPAKKGSIHVSSAiTEDQKKSEEVRpNIAEIEDIRVLQENNEGLRAFLL----TIENEL 858
Cdd:PTZ00121 1473 DEAKKKAEEAKKAD-EAKKKAEEAKKKADEAKKA-AEAKKKADEAK-KAEEAKKADEAKKAEEAKKADEAkkaeEKKKAD 1549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 859 KNEKEEKAELNKQIVHFQQELSLSEKKNLTLSK--EVQQIQSNYDIAIAELHVQKSKNQ-EQEEKIMKLSNEIETATRSI 935
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKaeEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEAKIKAEELKKAE 1629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 936 TNNVSQIKLMHTKIDELRTLDSVSQISNIDLLNLRDLSNGSEEDNLPNTQLDLLGNDYLVSKQVKEYRIQEPNRENSFHS 1015
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1016 SIEAIWEECKEIVKASSKKSHQIEEL--EQQIEKLQAEV----KGYKDENNRLKEKEHKNQDDLLKEKETLIQQ-LKEEL 1088
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEAkkEAEEDKKKAEEakkdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEED 1789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1089 QEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDILEKESIILKLERNLKEFQEHL 1168
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEAD 1869
|
650 660
....*....|....*....|....*..
gi 5911999 1169 QDSVKNTKDLNVKELKLKEEITQLTNN 1195
Cdd:PTZ00121 1870 FNKEKDLKEDDEEEIEEADEIEKIDKD 1896
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1224-1453 |
1.71e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1224 LSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQ 1303
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1304 LKEQLNNQKveEAIQQYERACKDLNVKEKI-----------IEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKW 1372
Cdd:COG4942 95 LRAELEAQK--EELAELLRALYRLGRQPPLalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1373 KEKCNDLETKNNQRSNkehenntdvlgKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRE 1452
Cdd:COG4942 173 RAELEALLAELEEERA-----------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
.
gi 5911999 1453 R 1453
Cdd:COG4942 242 R 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
997-1511 |
2.12e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.22 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 997 KQVKEYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKShQIEELEQQIEKLQ--AEVKGYKDENNRLKEKEHKNQDDLL 1074
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK-KAEEAKKKADAAKkkAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1075 KEKETLIQQLKEELQEKNVTLDVQiqhvVEGKRALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQ----DILEK 1150
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKK----AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkkkaDEAKK 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1151 ESIILKLERNLKEFQEHLQDSVKNTKDLNVK----ELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSA 1226
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkadEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1227 SSARtqnlKADLQRKEEDYADLKE-KLTDAKKQIKQVQKEVSVMRDEDKllrikiNELEKKKNQcSQELDMKQRTIQQLK 1305
Cdd:PTZ00121 1519 EEAK----KADEAKKAEEAKKADEaKKAEEKKKADELKKAEELKKAEEK------KKAEEAKKA-EEDKNMALRKAEEAK 1587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1306 eQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQV--LEAKLEEVERLATELEKWKEkcnDLETKN 1383
Cdd:PTZ00121 1588 -KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVeqLKKKEAEEKKKAEELKKAEE---ENKIKA 1663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1384 NQRSNKEHENNTdvlgKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERF----FKQQN 1459
Cdd:PTZ00121 1664 AEEAKKAEEDKK----KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIkaeeAKKEA 1739
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 5911999 1460 EMEILTAQLTEKDSD----LQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLK 1511
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEekkkIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1032-1521 |
4.96e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1032 SKKSHQIEELEQQIEklqaevkgykdennrlkEKEHKNQDDLLKEKETLIQQLKEELQEKnvtldvqiqhvvEGKRALSE 1111
Cdd:PRK02224 183 SDQRGSLDQLKAQIE-----------------EKEEKDLHERLNGLESELAELDEEIERY------------EEQREQAR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1112 LTQGvtcykakikELETILETQKVERSHSAKLEQDILEKESIILKLERNLKEFQEHLQDsvkntkdlnvkelkLKEEITQ 1191
Cdd:PRK02224 234 ETRD---------EADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRD--------------LRERLEE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1192 LTNNLQDMKHLLQLKEEeeetnrqeteklkeELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRD 1271
Cdd:PRK02224 291 LEEERDDLLAEAGLDDA--------------DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1272 EDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLnnqkvEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEq 1351
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEI-----EELRERFGDAPVDLGNAEDFLEELREERDELREREAE- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1352 dqvLEAKLEEVERLATELEKWKE--KC----NDLETKNNQRSNKEHEnntdvlGKLTNLQDELQESEQKyNADRKKWLEE 1425
Cdd:PRK02224 431 ---LEATLRTARERVEEAEALLEagKCpecgQPVEGSPHVETIEEDR------ERVEELEAELEDLEEE-VEEVEERLER 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1426 KMMLITQAKEAENIRNKE---MKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREE----RDQLVAALEiQLKALIS 1498
Cdd:PRK02224 501 AEDLVEAEDRIERLEERRedlEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAaaeaEEEAEEARE-EVAELNS 579
|
490 500
....*....|....*....|...
gi 5911999 1499 SNVQKDNEIEQLKRIISETSKIE 1521
Cdd:PRK02224 580 KLAELKERIESLERIRTLLAAIA 602
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1030-1286 |
5.71e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.53 E-value: 5.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1030 ASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLlKEKETLIQQLKEELQEKNVTLDVQiqhvvegKRAL 1109
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-AALERRIAALARRIRALEQELAAL-------EAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1110 SELTQgvtcykaKIKELETILETQKVERSHSAKLEQDILEKESIILKLErnlkefQEHLQDSVKNTKDLNVKELKLKEEI 1189
Cdd:COG4942 86 AELEK-------EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLS------PEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1190 TQLTNNLQDMKhllqlkeeeeetnrqeteKLKEELSASSARTQNLKADLQRKEEDYADLKEK----LTDAKKQIKQVQKE 1265
Cdd:COG4942 153 EELRADLAELA------------------ALRAELEAERAELEALLAELEEERAALEALKAErqklLARLEKELAELAAE 214
|
250 260
....*....|....*....|.
gi 5911999 1266 VSVMRDEDKLLRIKINELEKK 1286
Cdd:COG4942 215 LAELQQEAEELEALIARLEAE 235
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1073-1569 |
8.45e-06 |
|
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: 50.98 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1073 LLKEKETLIQQLKEELQEKNVTLD-----VQIQHVVEGKRA-LSELTQGvtcykakIKELETILETQKversHSAKLEQD 1146
Cdd:pfam10174 200 LLDQKEKENIHLREELHRRNQLQPdpaktKALQTVIEMKDTkISSLERN-------IRDLEDEVQMLK----TNGLLHTE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1147 ILEKESIILKLERNLKEFQEHLQDSVKntKDLNVKE---LKLKEEITQLTNNLQDMKHLLQLkeeeeetnrqetekLKEE 1223
Cdd:pfam10174 269 DREEEIKQMEVYKSHSKFMKNKIDQLK--QELSKKEselLALQTKLETLTNQNSDCKQHIEV--------------LKES 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1224 LSASSARTQNLKAD-------LQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDM 1296
Cdd:pfam10174 333 LTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRD 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1297 KQRTIQQLKE-----QLNNQKVEEAIQQYERACKDlnvKEKIIEDMRMTLEEQEqtqveqdqvlEAKLEEVERLATELEK 1371
Cdd:pfam10174 413 KDKQLAGLKErvkslQTDSSNTDTALTTLEEALSE---KERIIERLKEQRERED----------RERLEELESLKKENKD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1372 WKEKCNDLETKNNQRSN-----KEHENNTDVLG-----KLTNLQDELQESEQ---KYNADRKKWLEEKMMLITQAKEAEN 1438
Cdd:pfam10174 480 LKEKVSALQPELTEKESslidlKEHASSLASSGlkkdsKLKSLEIAVEQKKEecsKLENQLKKAHNAEEAVRTNPEINDR 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1439 IRN--KEMKKYAEDRErffKQQNEMEILTAQLTEKDSDlqkwREERDQLVAALEIQLKALISSNVQKdneIEQLKRIISE 1516
Cdd:pfam10174 560 IRLleQEVARYKEESG---KAQAEVERLLGILREVENE----KNDKDKKIAELESLTLRQMKEQNKK---VANIKHGQQE 629
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 5911999 1517 TSKIETQIMD--IKPKRISSADPDKLQTEPLSTSFEISRNKIEDGSVVLDSCEVS 1569
Cdd:pfam10174 630 MKKKGAQLLEeaRRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQS 684
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1219-1470 |
1.10e-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: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1219 KLKEELSASSARTQNLKADL------QRKEEDYAD-LKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCS 1291
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELsslqseLRRIENRLDeLSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1292 QELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKE-----KIIEDMRMTLEEQEQTQVEQDQVLEAKLEEV---- 1362
Cdd:TIGR02169 751 QEIENVKSELKELEARI--EELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLtlek 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1363 ERLATELEKWKEKCNDLETKNNQRSNKEHENNTDvLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNK 1442
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK-KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
250 260
....*....|....*....|....*...
gi 5911999 1443 EMKKYAEDRERFFKQQNEMEILTAQLTE 1470
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
884-1531 |
2.66e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.13 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 884 KKNLTLSKEVQQIQSNYDI---AIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELrtlDSVSQ 960
Cdd:PRK01156 152 KKILDEILEINSLERNYDKlkdVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERL---SIEYN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 961 ISNIDLLNLRdlsngsEEDNLPNTQLDLLgNDYLVSKQVKEYRIQEPNRENSFHSSIEaiwEECKEIVKASSKKSH---- 1036
Cdd:PRK01156 229 NAMDDYNNLK------SALNELSSLEDMK-NRYESEIKTAESDLSMELEKNNYYKELE---ERHMKIINDPVYKNRnyin 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1037 -------QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKEtliqqlKEELqeknvtldvqiqhvvegKRAL 1109
Cdd:PRK01156 299 dyfkyknDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSR------YDDL-----------------NNQI 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1110 SELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDILEKESI------ILKLERNlkEFQEHLQDSVKNTKDLNVKEL 1183
Cdd:PRK01156 356 LELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIqeidpdAIKKELN--EINVKLQDISSKVSSLNQRIR 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1184 KLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARtqnLKADLQRKEEDYADLKEKLTDAKKQIKQVQ 1263
Cdd:PRK01156 434 ALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSR---LEEKIREIEIEVKDIDEKIVDLKKRKEYLE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1264 -KEVSVMRDEDKLLRIKINELEKKKNQCSqELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIiedmrmtle 1342
Cdd:PRK01156 511 sEEINKSINEYNKIESARADLEDIKIKIN-ELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLI--------- 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1343 eqeqtqveqdqvleakleEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNAdrkkw 1422
Cdd:PRK01156 581 ------------------DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNE----- 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1423 LEEKMMLITQAKEaeniRNKEMKKYAEDRERFFKQQNEmeiLTAQLTEKDSDLQKWREERDQLVAALEiQLKALISSNVQ 1502
Cdd:PRK01156 638 IQENKILIEKLRG----KIDNYKKQIAEIDSIIPDLKE---ITSRINDIEDNLKKSRKALDDAKANRA-RLESTIEILRT 709
|
650 660 670
....*....|....*....|....*....|...
gi 5911999 1503 KDNEIEQ----LKRIISETSKIETQIMDIKPKR 1531
Cdd:PRK01156 710 RINELSDrindINETLESMKKIKKAIGDLKRLR 742
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1219-1341 |
3.56e-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: 47.23 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1219 KLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQV--QKEVSVMRDEDKLLRIKINELEKKKNQCSQELDM 1296
Cdd:COG1579 42 ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEE 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 5911999 1297 KQRTIQQLKEQLNNQK--VEEAIQQYERACKDLNVKEKIIEDMRMTL 1341
Cdd:COG1579 122 LEEELAELEAELAELEaeLEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1037-1268 |
4.59e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1037 QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLlKEKETLIQQLKEELQEKNVTLDVQIQHVveGKRALSELTQGV 1116
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-EALQAEIDKLQAEIAEAEAEIEERREEL--GERARALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1117 TcykakIKELETILETQKVershsakleQDILEKESIILKL-ERNLKEFQEHLQDsvknTKDLNVKELKLKEEITQLTNN 1195
Cdd:COG3883 101 S-----VSYLDVLLGSESF---------SDFLDRLSALSKIaDADADLLEELKAD----KAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5911999 1196 LQDMKhllqlkeeeeetnrqeteKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSV 1268
Cdd:COG3883 163 KAELE------------------AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1187-1371 |
4.69e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1187 EEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEV 1266
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1267 SVMRDEdklLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN-----NQKVEEAIQQYERACKDLNVKEKIIEDMRMTL 1341
Cdd:COG4942 100 EAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|
gi 5911999 1342 EEQEQTQVEQDQVLEAKLEEVERLATELEK 1371
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEK 206
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1355-1543 |
4.70e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1355 LEAKLEEVERLATELEKWKEKCNDLETKNNQRSnkehenntdvlGKLTNLQDELQESEQKYNADRKKWLE--------EK 1426
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELE-----------EKLEELRLEVSELEEEIEELQKELYAlaneisrlEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1427 MMLITQAKEAENIRNKEMkkYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISSNVQKDNE 1506
Cdd:TIGR02168 303 QKQILRERLANLERQLEE--LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190
....*....|....*....|....*....|....*..
gi 5911999 1507 IEQLKRIISETSKIETQIMdikpKRISSADPDKLQTE 1543
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLN----NEIERLEARLERLE 413
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1124-1328 |
4.73e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1124 KELETILETQKVERSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLL 1203
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1204 QlKEEEEETNRQETEKLKEELSASSA-RTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEdklLRIKINE 1282
Cdd:COG4942 107 A-ELLRALYRLGRQPPLALLLSPEDFlDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE---LEALLAE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 5911999 1283 LEKKKNQCSQELDMKQRTIQQLKEQLNNQkvEEAIQQYERACKDLN 1328
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAEL--AAELAELQQEAEELE 226
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1107-1556 |
5.80e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1107 RALSELTQGVTCYKAKIKELETILETQKVE---------RSHSAKLEQDILEKESIILKLER----------NLKEFQEH 1167
Cdd:pfam15921 224 KILRELDTEISYLKGRIFPVEDQLEALKSEsqnkielllQQHQDRIEQLISEHEVEITGLTEkassarsqanSIQSQLEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1168 LQDSVKNTKDLNVKEL-KLKEEITQLTNNLQDMKHLLQLKEEeeetnrqeteKLKEELSASSARTQNLKADLQRKEEDYA 1246
Cdd:pfam15921 304 IQEQARNQNSMYMRQLsDLESTVSQLRSELREAKRMYEDKIE----------ELEKQLVLANSELTEARTERDQFSQESG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1247 DLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKvEEAIQQYERACKD 1326
Cdd:pfam15921 374 NLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMK-SECQGQMERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1327 LNVKEKiiedmrmtleeqeqtqveqdqvleaKLEEVERLATELEKWKEKCNDL-ETKNNQRSNKEHENNTdvlgkLTNLQ 1405
Cdd:pfam15921 453 IQGKNE-------------------------SLEKVSSLTAQLESTKEMLRKVvEELTAKKMTLESSERT-----VSDLT 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1406 DELQESEQKYNADRKKwleekmmlITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERD-- 1483
Cdd:pfam15921 503 ASLQEKERAIEATNAE--------ITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnm 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1484 -QLV--------------AALE-------IQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPKRISSADPDKLQ 1541
Cdd:pfam15921 575 tQLVgqhgrtagamqvekAQLEkeindrrLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQE 654
|
490
....*....|....*
gi 5911999 1542 TEPLSTSFEISRNKI 1556
Cdd:pfam15921 655 RDQLLNEVKTSRNEL 669
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1017-1415 |
1.23e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1017 IEAIWEECKEIVKASSKKS----HQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKnqddlLKEKETLIQQLKEELQEKN 1092
Cdd:COG4717 48 LERLEKEADELFKPQGRKPelnlKELKELEEELKEAEEKEEEYAELQEELEELEEE-----LEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1093 VTLDVQ--IQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDI--------LEKESIILKLERNLK 1162
Cdd:COG4717 123 KLLQLLplYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELeelleqlsLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1163 EFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEE------------------------------- 1211
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflv 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1212 -----TNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKL-----------TDAKKQIKQVQKEVSVMRDEDKL 1275
Cdd:COG4717 283 lgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspeelLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1276 LRIKINELEKK----KNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKII--EDMRMTLEEQEQTQV 1349
Cdd:COG4717 363 LQLEELEQEIAallaEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELE 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5911999 1350 EQDQVLEAKLEEVERLATELEKWKEKCN------DLETKNNQRSNKEHENNTDVLGkLTNLQDELQESEQKY 1415
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEDGElaellqELEELKAELRELAEEWAALKLA-LELLEEAREEYREER 513
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1355-1528 |
1.66e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1355 LEAKLEEVERlatELEKWKEKCNDLETknNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKwLEEKMMLITQAK 1434
Cdd:COG3206 187 LRKELEEAEA---ALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ-LGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1435 EAENIRNKemkkyaedRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQL-----------VAALEIQLKALISSNVQK 1503
Cdd:COG3206 261 QSPVIQQL--------RAQLAELEAELAELSARYTPNHPDVIALRAQIAALraqlqqeaqriLASLEAELEALQAREASL 332
|
170 180
....*....|....*....|....*
gi 5911999 1504 DNEIEQLKRIISETSKIETQIMDIK 1528
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELRRLE 357
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1025-1509 |
2.28e-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: 46.25 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1025 KEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLiQQLKEELQEKNVTLDvqiqhvve 1104
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQL-KIITMELQKKSSELE-------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1105 gkralsELTQGVTCYKAKIKELETILETQKvershsaKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELK 1184
Cdd:pfam05483 395 ------EMTKFKNNKEVELEELKKILAEDE-------KLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTA 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1185 LKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQK 1264
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1265 EVSVMRDEDKLLRikiNELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNV----KEKIIEDMRMT 1340
Cdd:pfam05483 542 KEMNLRDELESVR---EEFIQKGDEVKCKLDKSEENARSIEYEV--LKKEKQMKILENKCNNLKKqienKNKNIEELHQE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1341 LEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLeTKNNQRSNKEHENNTDvlgkltNLQDELQESeqKYNADRK 1420
Cdd:pfam05483 617 NKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEI-IDNYQKEIEDKKISEE------KLLEEVEKA--KAIADEA 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1421 KWLEEKMMLITQAKEAENIRNKEMKKYAEDRerffkqqnemeiltaQLTEKDSDLQKWR---EERDQLVAALEIQLKALI 1497
Cdd:pfam05483 688 VKLQKEIDKRCQHKIAEMVALMEKHKHQYDK---------------IIEERDSELGLYKnkeQEQSSAKAALEIELSNIK 752
|
490
....*....|....
gi 5911999 1498 SS--NVQKDNEIEQ 1509
Cdd:pfam05483 753 AEllSLKKQLEIEK 766
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1037-1268 |
2.45e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1037 QIEELEQQIEKLQAEVKGYKDENNRLK-EKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQG 1115
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGLVDlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1116 VTcykakIKELETILETQKVERshsAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELK-LKEEITQLTN 1194
Cdd:COG3206 263 PV-----IQQLRAQLAELEAEL---AELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEaLQAREASLQA 334
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5911999 1195 NLQDMKHLLQlkeeeeetnrqeteklkeELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSV 1268
Cdd:COG3206 335 QLAQLEARLA------------------ELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRV 390
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1184-1322 |
2.70e-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: 44.13 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1184 KLKEEITQLTNNLQDMKHLLQlkeeeeeTNRQETEKLKEELsassARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQ 1263
Cdd:pfam13851 30 SLKEEIAELKKKEERNEKLMS-------EIQQENKRLTEPL----QKAQEEVEELRKQLENYEKDKQSLKNLKARLKVLE 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5911999 1264 KEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQ---LKEQLNNQKVEEAIQQYER 1322
Cdd:pfam13851 99 KELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktgLKNLLLEKKLQALGETLEK 160
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1461-1747 |
3.27e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 45.81 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1461 MEILTAQLTEKDSDLQK---------WREERDQLVAALEiqlkaliSSNVQKDNEIEQLKRIISETSKIETQIMDIKPKR 1531
Cdd:PTZ00108 1104 VEKLNAELEKKEKELEKlknttpkdmWLEDLDKFEEALE-------EQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKK 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1532 ISSADPDKLQTEPLSTSFEISRNKIEDGSVVLDSCEVSTENDQSTRFPKPELEIQFTplqpnKMAVKHPGCTTPVTVEIP 1611
Cdd:PTZ00108 1177 KEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKT-----KPKKSSVKRLKSKKNNSS 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1612 KARKRKSNEMEEDLVKCENKKNATPRTNLKFPISDDRNSSVKKEQKVAIRPSS--KKTYSLRSQASIIGVNLATKKKEGT 1689
Cdd:PTZ00108 1252 KSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSptKKKVKKRLEGSLAALKKKKKSEKKT 1331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5911999 1690 LQKfgdflqhspsilqskakkiietmSSSKLSNVEASKENVSQPKRAKRKLYTSEISS 1747
Cdd:PTZ00108 1332 ARK-----------------------KKSKTRVKQASASQSSRLLRRPRKKKSDSSSE 1366
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1037-1328 |
3.38e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1037 QIEELEQQIEKLQAEvkgykdennrlkekehknqddllkeketlIQQLKEELQEknvtLDVQIQHVVEGKRALSELTQgv 1116
Cdd:COG4913 611 KLAALEAELAELEEE-----------------------------LAEAEERLEA----LEAELDALQERREALQRLAE-- 655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1117 tcykakikELETILETQKVERSHsAKLEQDI--LEKESIILK-LERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLT 1193
Cdd:COG4913 656 --------YSWDEIDVASAEREI-AELEAELerLDASSDDLAaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAE 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1194 NNLQDMKHLLQLKEEEEETNRQET--EKLKEELSASSART--QNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVM 1269
Cdd:COG4913 727 EELDELQDRLEAAEDLARLELRALleERFAAALGDAVERElrENLEERIDALRARLNRAEEELERAMRAFNREWPAETAD 806
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5911999 1270 RD---------EDKLLRIKINELEKKKnqcSQELDMKQRTIQQLKEQLnNQKVEEAIQQYERACKDLN 1328
Cdd:COG4913 807 LDadleslpeyLALLDRLEEDGLPEYE---ERFKELLNENSIEFVADL-LSKLRRAIREIKERIDPLN 870
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
915-1311 |
3.74e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 915 QEQEEKIMKLSNEIETATRSITNNVSQIklmhtkiDELRTLDSVSQISNIDLLNLRDLSNGSEE--DNLPNTQLDLLG-N 991
Cdd:PRK11281 76 DRQKEETEQLKQQLAQAPAKLRQAQAEL-------EALKDDNDEETRETLSTLSLRQLESRLAQtlDQLQNAQNDLAEyN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 992 DYLVSKQVKEYRIQEPNRENSFHS-SIEAI---WEECKEIVKASSKKSHQIEE--LEQQIEKLQAEVKGykdeNNRLKEK 1065
Cdd:PRK11281 149 SQLVSLQTQPERAQAALYANSQRLqQIRNLlkgGKVGGKALRPSQRVLLQAEQalLNAQNDLQRKSLEG----NTQLQDL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1066 EHKnQDDLLKEKetlIQQLKEELQEknvtldvqIQHVVEGKR-ALSELTqgvtcykakIKELETILETQKV--------E 1136
Cdd:PRK11281 225 LQK-QRDYLTAR---IQRLEHQLQL--------LQEAINSKRlTLSEKT---------VQEAQSQDEAARIqanplvaqE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1137 RSHSAKLEQDILEKEsiilklERNLKEFQEHLQdsVKNTKD-LNVKELKLKEEITQLTNNLQDMKHLLQLKeeeeetnrq 1215
Cdd:PRK11281 284 LEINLQLSQRLLKAT------EKLNTLTQQNLR--VKNWLDrLTQSERNIKEQISVLKGSLLLSRILYQQQ--------- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1216 eteklkeelsassartQNLKADlqrkeedyaDLKEKLTDAKKQIKQVQKEVSVMRDE--------DKLLRIKINELEKK- 1286
Cdd:PRK11281 347 ----------------QALPSA---------DLIEGLADRIADLRLEQFEINQQRDAlfqpdayiDKLEAGHKSEVTDEv 401
|
410 420
....*....|....*....|....*
gi 5911999 1287 KNQCSQELDMKQRTIQQLKEQLNNQ 1311
Cdd:PRK11281 402 RDALLQLLDERRELLDQLNKQLNNQ 426
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1219-1371 |
4.61e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1219 KLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINEL---EKKKNQCSQELD 1295
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraLYRSGGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1296 M------------KQRTIQQLKEQLNnqkveEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVE 1363
Cdd:COG3883 107 VllgsesfsdfldRLSALSKIADADA-----DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
....*...
gi 5911999 1364 RLATELEK 1371
Cdd:COG3883 182 ALLAQLSA 189
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
65-190 |
6.81e-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: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 65 IRPFTQSEKELESEGCVHILDsqtvvlkepqcilGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQ--GCIMQPVkdlLK 142
Cdd:pfam16796 22 IRVFARVRPELLSEAQIDYPD-------------ETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQeiSQLVQSC---LD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 5911999 143 GQSRLIFTYGLTNSGktytfqgteENIGILPRTLNVLFDSLQERLYTK 190
Cdd:pfam16796 86 GYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGW 124
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
542-737 |
7.16e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 7.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 542 AEETQNVETKLLDEDLDKTLEENKAFISHEEKRKLLDLIEDLKKKLINEKKEKLTLEFKIREEVTQEFTqywAQREADFK 621
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE---ALRAAAEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 622 ETLLQEREILEENAERRLAifkdlvgkcdTREEAAKDICATKVETEEATACLELKFNQIKAELAKTKGELIKTKEELKKR 701
Cdd:COG1196 399 AAQLEELEEAEEALLERLE----------RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
170 180 190
....*....|....*....|....*....|....*.
gi 5911999 702 ENESDSLIQELETSNKKIITQNQRIKELINIIDQKE 737
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1185-1320 |
7.26e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.80 E-value: 7.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1185 LKEEIT-------QLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSA---RTQNLKADLQRK----EEDYADLKE 1250
Cdd:PRK09039 44 LSREISgkdsaldRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAersRLQALLAELAGAgaaaEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5911999 1251 KLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN---NQKVEEaIQQY 1320
Cdd:PRK09039 124 ELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNvalAQRVQE-LNRY 195
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1120-1337 |
8.06e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.98 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1120 KAKIKELETILETQKVERshsAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDM 1199
Cdd:COG4942 33 QQEIAELEKELAALKKEE---KALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1200 KHLLQlkeeeeetNRQETEKLKEELSASSArtqnlkADLQRKEEDYADLKEKLTDAKKQIKQVQKEvsvmrdedklLRIK 1279
Cdd:COG4942 110 LRALY--------RLGRQPPLALLLSPEDF------LDAVRRLQYLKYLAPARREQAEELRADLAE----------LAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5911999 1280 INELEKKKNQCSQELDMKQRTIQQLKEQLNNQ-----KVEEAIQQYERACKDLNVKEKIIEDM 1337
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERqkllaRLEKELAELAAELAELQQEAEELEAL 228
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1141-1481 |
8.28e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 8.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1141 AKLEqdILEKEsiILKLERNLKEFQEHLQDsVKNTKDLNVKELKLKEEITQLTNNLQDM----KHLLQLKEEeeetnrqe 1216
Cdd:COG4913 610 AKLA--ALEAE--LAELEEELAEAEERLEA-LEAELDALQERREALQRLAEYSWDEIDVasaeREIAELEAE-------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1217 teklKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQcSQELDM 1296
Cdd:COG4913 677 ----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL-ELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1297 KQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATEL------- 1369
Cdd:COG4913 752 EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLeedglpe 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1370 --EKWKEKCNDLETKN----NQRSNKEHENNTDVLGKLtNlqDELQESEqkYNADRKKWLEEKMMLITQAKE----AENI 1439
Cdd:COG4913 832 yeERFKELLNENSIEFvadlLSKLRRAIREIKERIDPL-N--DSLKRIP--FGPGRYLRLEARPRPDPEVREfrqeLRAV 906
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 5911999 1440 RNKEMKKYAEDRERFFKQQNE-MEILTAQLTEKDsdlQKWREE 1481
Cdd:COG4913 907 TSGASLFDEELSEARFAALKRlIERLRSEEEESD---RRWRAR 946
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1015-1279 |
8.37e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1015 SSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDE----NNRLKE-----KEHKNQDDLLKEKetlIQQLK 1085
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKrdelNAQVKElreeaQELREKRDELNEK---VKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1086 EELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKA---KIKELETILETQKVERSHSAKLEQDILEKESIILKLERnLK 1162
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGGSIDKlrkEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKK-AL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1163 EFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKE 1242
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 5911999 1243 EDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIK 1279
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
556-1318 |
8.41e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.66 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 556 DLDKTLEENKAFISHEEKRKLLDLIEDLKKKlinekkekltleFKIREEVTQEFTQYWaqrEADFKETLLQEREILEENA 635
Cdd:TIGR01612 624 DLKKIIENNNAYIDELAKISPYQVPEHLKNK------------DKIYSTIKSELSKIY---EDDIDALYNELSSIVKENA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 636 ERRL---AIFKDLVGKCDTREEAAKDICATKVETEEATacLELKFNQIKAELAKTK--------GELIKTKEELKKRENE 704
Cdd:TIGR01612 689 IDNTedkAKLDDLKSKIDKEYDKIQNMETATVELHLSN--IENKKNELLDIIVEIKkhihgeinKDLNKILEDFKNKEKE 766
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 705 SDSLIQELETSNKKIITQNQRIKEL-------INIIDQKEDTINefQNLKSHMENTFKCNDKADTSSLIIN--------- 768
Cdd:TIGR01612 767 LSNKINDYAKEKDELNKYKSKISEIknhyndqINIDNIKDEDAK--QNYDKSKEYIKTISIKEDEIFKIINemkfmkddf 844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 769 -NKLicNETVEVPKDSKSKICSERKRVNE------NELQQDEPPAKKGSIHVSSAITEDQKKSEEvrpniAEIEDIRVLQ 841
Cdd:TIGR01612 845 lNKV--DKFINFENNCKEKIDSEHEQFAEltnkikAEISDDKLNDYEKKFNDSKSLINEINKSIE-----EEYQNINTLK 917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 842 ENNEGLRAFLLT---IENELKNEKEEKAELNKQIVHFQQ----ELSLSEKKNLTLSKEVQQIQSNYdiAIAELHVQKSKN 914
Cdd:TIGR01612 918 KVDEYIKICENTkesIEKFHNKQNILKEILNKNIDTIKEsnliEKSYKDKFDNTLIDKINELDKAF--KDASLNDYEAKN 995
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 915 QE----------------------QEEKIMKLSNEIETATRSITNNVSQIKL-MHTKI----DELRTLDSvsqiSNIDLL 967
Cdd:TIGR01612 996 NElikyfndlkanlgknkenmlyhQFDEKEKATNDIEQKIEDANKNIPNIEIaIHTSIyniiDEIEKEIG----KNIELL 1071
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 968 NlrdlSNGSEEDNLPNTQLDLLGND---YLVSKQVKEYRIQEPNRENSFHSSIEAIWEEC----KEIVKASSKKSHQIEE 1040
Cdd:TIGR01612 1072 N----KEILEEAEINITNFNEIKEKlkhYNFDDFGKEENIKYADEINKIKDDIKNLDQKIdhhiKALEEIKKKSENYIDE 1147
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1041 LEQQIEKLQaEVKGYKDENNRLKEKEHKNQDDLLK--EKETLIQQLKEELQEknvtldvqIQHVVEGKRALSELTQGVTC 1118
Cdd:TIGR01612 1148 IKAQINDLE-DVADKAISNDDPEEIEKKIENIVTKidKKKNIYDEIKKLLNE--------IAEIEKDKTSLEEVKGINLS 1218
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1119 YKAKIKE--LETILETQKvERSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNL 1196
Cdd:TIGR01612 1219 YGKNLGKlfLEKIDEEKK-KSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHD 1297
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1197 QDMKHLLQ--LKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKE--KLTDAKKQIKQVQKEVsvmrde 1272
Cdd:TIGR01612 1298 ENISDIREksLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANIYNilKLNKIKKIIDEVKEYT------ 1371
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 5911999 1273 dkllrikiNELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQ 1318
Cdd:TIGR01612 1372 --------KEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIE 1409
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
996-1512 |
9.60e-04 |
|
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: 44.01 E-value: 9.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 996 SKQVKEYRIQEpNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEqqiEKLQAEVKGYKD--ENNRLKEKEHKNQDDL 1073
Cdd:pfam01576 148 SKLSKERKLLE-ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLE---ERLKKEEKGRQEleKAKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1074 LKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDILEK-ES 1152
Cdd:pfam01576 224 IAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEElEA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1153 IILKLERNLKefQEHLQDSVKNTKDLNVKELK--LKEEITQLTNNLQDM--KHLLQLKEEEEETNRQETEK--------- 1219
Cdd:pfam01576 304 LKTELEDTLD--TTAAQQELRSKREQEVTELKkaLEEETRSHEAQLQEMrqKHTQALEELTEQLEQAKRNKanlekakqa 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1220 -------LKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQ 1292
Cdd:pfam01576 382 lesenaeLQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSK 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1293 ELDmkqrtiqQLKEQLnnQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLE--------------AK 1358
Cdd:pfam01576 462 DVS-------SLESQL--QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVErqlstlqaqlsdmkKK 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1359 LEEVERLATELEKWKEKC-NDLETKNNQRSNKEHE------NNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLit 1431
Cdd:pfam01576 533 LEEDAGTLEALEEGKKRLqRELEALTQQLEEKAAAydklekTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQML-- 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1432 qaKEAENIRNKemkkYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISS--NVQKD-NEIE 1508
Cdd:pfam01576 611 --AEEKAISAR----YAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSkdDVGKNvHELE 684
|
....
gi 5911999 1509 QLKR 1512
Cdd:pfam01576 685 RSKR 688
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1033-1322 |
9.61e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 44.06 E-value: 9.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1033 KKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKEtLIQQLKEELQEKNVT-------LDVQIQH---- 1101
Cdd:PRK04778 102 KAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKD-LYRELRKSLLANRFSfgpaldeLEKQLENleee 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1102 ------------VVEGKRALSELTQGVTCYKAKIKELETILETQKVE-RSHSAKLE---QDILEKESII--LKLERNLKE 1163
Cdd:PRK04778 181 fsqfveltesgdYVEAREILDQLEEELAALEQIMEEIPELLKELQTElPDQLQELKagyRELVEEGYHLdhLDIEKEIQD 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1164 FQEHLQDSVKNTKDLNVKElkLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEE 1243
Cdd:PRK04778 261 LKEQIDENLALLEELDLDE--AEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQ 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1244 DY---ADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNN-----QKVEE 1315
Cdd:PRK04778 339 SYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGlrkdeLEARE 418
|
....*..
gi 5911999 1316 AIQQYER 1322
Cdd:PRK04778 419 KLERYRN 425
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1032-1341 |
9.82e-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: 44.34 E-value: 9.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1032 SKKSHQIEELEQQIEKLQAEVKGYKDENN-RLKEKEH-KNQDDLLKEKETLIQQLKEELQEKNVTLDV---QIQHVVE-- 1104
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVDlKLQELQHlKNEGDHLRNVQTECEALKLQMAEKDKVIEIlrqQIENMTQlv 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1105 ---GKRA------LSELTQGVTCYKAKIKELETILETQKVE-RSHSAKLEQDILEKESII------LKLERNLKEFQEHL 1168
Cdd:pfam15921 579 gqhGRTAgamqveKAQLEKEINDRRLELQEFKILKDKKDAKiRELEARVSDLELEKVKLVnagserLRAVKDIKQERDQL 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1169 QDSVKNTK-DLNvkelKLKEEITQLTNNLQDMKHLLQLkeeeeetnrqETEKLKEELSASSARTQNLKADLQRKE----- 1242
Cdd:pfam15921 659 LNEVKTSRnELN----SLSEDYEVLKRNFRNKSEEMET----------TTNKLKMQLKSAQSELEQTRNTLKSMEgsdgh 724
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1243 --EDYADLKEKLTDAKKQIKQVQ--------------KEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKE 1306
Cdd:pfam15921 725 amKVAMGMQKQITAKRGQIDALQskiqfleeamtnanKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
330 340 350
....*....|....*....|....*....|....*..
gi 5911999 1307 QLNNQKV--EEAIQQYERaCKDLnVKEKIIEDMRMTL 1341
Cdd:pfam15921 805 KVANMEValDKASLQFAE-CQDI-IQRQEQESVRLKL 839
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
555-1160 |
9.93e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 555 EDLDKTLEENKAFISHEEKrKLLDLIEDLKKKLINEKKEKLTLEfKIREEVTQeftqywAQREadfKETLLQEREILEEN 634
Cdd:PRK03918 192 EELIKEKEKELEEVLREIN-EISSELPELREELEKLEKEVKELE-ELKEEIEE------LEKE---LESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 635 AERRLAIFKDLVGKCDTREEAAKDICATKVETEEAtacleLKFNQIKAELAKTKGELIKTKEELKKRENESDSLIQELET 714
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEEY-----IKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 715 SNKKIITQNQRIKELINIIDQKEDTINEFQNLKSHMEN------TFKCNDKADTSSLIINNKLICNETVEVPKDSKSKIC 788
Cdd:PRK03918 336 KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEElerlkkRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 789 SERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVRPNIAEIEDIRV-LQENNEGLRaflltienelkneKEEKAE 867
Cdd:PRK03918 416 ELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKeLKEIEEKER-------------KLRKEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 868 LNKQIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAElhvqksKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHT 947
Cdd:PRK03918 483 RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELE------KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKK 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 948 KIDEL-RTLDSVSQISNIDLLNLRDLSNGS-EEDNLPNTQLDLLGNDYLVSKQVKEyRIQEPNREnsfhssIEAIWEECK 1025
Cdd:PRK03918 557 KLAELeKKLDELEEELAELLKELEELGFESvEELEERLKELEPFYNEYLELKDAEK-ELEREEKE------LKKLEEELD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1026 EIVKASSKKSHQIEELEQQIEKLQaevKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEG 1105
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELE---KKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEER 706
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5911999 1106 KRALSELT------QGVTCYKAKIKELETILET---QKVERSHSAKLEQDILEKES-IILKLERN 1160
Cdd:PRK03918 707 EKAKKELEklekalERVEELREKVKKYKALLKEralSKVGEIASEIFEELTEGKYSgVRVKAEEN 771
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1165-1416 |
1.03e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1165 QEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEED 1244
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1245 YADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERAC 1324
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1325 KDLNVKEKIIEDMRMTLEEQEQ-TQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTN 1403
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESlPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250
....*....|...
gi 5911999 1404 LQDELQESEQKYN 1416
Cdd:COG4372 270 EKDTEEEELEIAA 282
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1026-1494 |
1.29e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.63 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1026 EIVKASSKKshqiEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDdLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEG 1105
Cdd:pfam01576 13 ELQKVKERQ----QKAESELKELEKKHQQLCEEKNALQEQLQAETE-LCAEAEEMRARLAARKQELEEILHELESRLEEE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1106 KRALSELTQGVTCYKAKIKELETILETQKVER-----------SHSAKLEQDILEKESIILKLERNLKEFQEHLQDSvkn 1174
Cdd:pfam01576 88 EERSQQLQNEKKKMQQHIQDLEEQLDEEEAARqklqlekvtteAKIKKLEEDILLLEDQNSKLSKERKLLEERISEF--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1175 TKDLNVKELKLKEeITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASS-----------ARTQNLKADLQRKEE 1243
Cdd:pfam01576 165 TSNLAEEEEKAKS-LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGEStdlqeqiaelqAQIAELRAQLAKKEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1244 DYADLKEKLTD-------AKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELdmkqrtiQQLKEQLNNQKVEEA 1316
Cdd:pfam01576 244 ELQAALARLEEetaqknnALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL-------EALKTELEDTLDTTA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1317 IQQYERAckdlnVKEKIIEDMRMTLEEQEQTQVEQDQVLEAK-LEEVERLATELEKWKEKCNDLEtKNNQRSNKEhenNT 1395
Cdd:pfam01576 317 AQQELRS-----KREQEVTELKKALEEETRSHEAQLQEMRQKhTQALEELTEQLEQAKRNKANLE-KAKQALESE---NA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1396 DVLGKLTNLQDELQESEQKynadRKKWLEEKMMLITQAKEAENIRNkemkkyaEDRERFFKQQNEMEILTAQLTEKDSDL 1475
Cdd:pfam01576 388 ELQAELRTLQQAKQDSEHK----RKKLEGQLQELQARLSESERQRA-------ELAEKLSKLQSELESVSSLLNEAEGKN 456
|
490
....*....|....*....
gi 5911999 1476 QKWREErdqlVAALEIQLK 1494
Cdd:pfam01576 457 IKLSKD----VSSLESQLQ 471
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1233-1371 |
1.32e-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: 42.22 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1233 NLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCS--QELDMKQRTIQQLKEQLN- 1309
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEIESLKRRISd 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5911999 1310 -NQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEK 1371
Cdd:COG1579 108 lEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1017-1199 |
1.70e-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: 42.83 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1017 IEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLlKEKETLIQQLKEELQEKNVTLD 1096
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI-AELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1097 VQIQH--------------VVEGKRALSELTQG----VTCYKAKIKELETILETQKVERshsAKLEQDILEKESIILKLE 1158
Cdd:COG4942 115 RLGRQpplalllspedfldAVRRLQYLKYLAPArreqAEELRADLAELAALRAELEAER---AELEALLAELEEERAALE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 5911999 1159 RNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDM 1199
Cdd:COG4942 192 ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1022-1426 |
1.83e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1022 EECKEIVKASSKKSHQIEELEQQIEKLQAEVKgykdennrLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQH 1101
Cdd:TIGR00606 709 DKLKSTESELKKKEKRRDEMLGLAPGRQSIID--------LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1102 VVEGKRALSELTQgVTCYKAKIKELETILETQKVERSHS------AKLEQDILEKESIILKLERNLKEFQEHLQDSVKNT 1175
Cdd:TIGR00606 781 EESAKVCLTDVTI-MERFQMELKDVERKIAQQAAKLQGSdldrtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1176 KDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDA 1255
Cdd:TIGR00606 860 QHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKA 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1256 KKQIKQVQKEVSVMRDEDKLLRIKINElEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIE 1335
Cdd:TIGR00606 940 QDKVNDIKEKVKNIHGYMKDIENKIQD-GKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQ 1018
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1336 DmrmtleeqeqtqVEQDQVLEAKLEEVERlatELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKY 1415
Cdd:TIGR00606 1019 D------------NLTLRKRENELKEVEE---ELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKE 1083
|
410
....*....|.
gi 5911999 1416 NADRKKWLEEK 1426
Cdd:TIGR00606 1084 IKHFKKELREP 1094
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1246-1386 |
1.87e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1246 ADLKEKLTDAKKQIKQVQKEVSVMRDEdKLLRIKiNELEKKKNQCSQELDMKQRTIQQLKEQLNnQKVEeaiqQYERACK 1325
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKE-ALLEAK-EEIHKLRNEFEKELRERRNELQKLEKRLL-QKEE----NLDRKLE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5911999 1326 DLNVKEKIiedmrmtleeqeqtqveqdqvLEAKLEEVERLATELEKWKEKCNDLETKNNQR 1386
Cdd:PRK12704 104 LLEKREEE---------------------LEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1080-1519 |
2.50e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1080 LIQQLKEELQE----KNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDI--LEKESI 1153
Cdd:COG4717 47 LLERLEKEADElfkpQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELekLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1154 ILKLERNLKEFQEHLQDsvkntkdlnvkelkLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQN 1233
Cdd:COG4717 127 LLPLYQELEALEAELAE--------------LPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1234 lkaDLQRKEEDYADLKEKLTDAKKQIKQVQKEVsvmrdedKLLRIKINELEKKknqcsQELDMKQRTIQQLKEQLN---- 1309
Cdd:COG4717 193 ---ELQDLAEELEELQQRLAELEEELEEAQEEL-------EELEEELEQLENE-----LEAAALEERLKEARLLLLiaaa 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1310 -----------------------------------NQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVeqdqv 1354
Cdd:COG4717 258 llallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPP----- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1355 lEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDE-----LQESEQKYNADRKKWLEEKMML 1429
Cdd:COG4717 333 -DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelraALEQAEEYQELKEELEELEEQL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1430 ITQAKEAENIRNKEMKKYAEDrerffkqqnEMEILTAQLTEKDSDLQKWREERdqlvAALEIQLKALISSN--VQKDNEI 1507
Cdd:COG4717 412 EELLGELEELLEALDEEELEE---------ELEELEEELEELEEELEELREEL----AELEAELEQLEEDGelAELLQEL 478
|
490
....*....|..
gi 5911999 1508 EQLKRIISETSK 1519
Cdd:COG4717 479 EELKAELRELAE 490
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1033-1322 |
2.79e-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: 42.53 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1033 KKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKEtLIQQLKEELQEKNVT-------LDVQIQHV--- 1102
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKD-KYRELRKTLLANRFSygpaideLEKQLAEIeee 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1103 -------------VEGKRALSELTQGVTCYKAKIKELETILETQKVE--------RSHSAKLEQD--ILEKesiiLKLER 1159
Cdd:pfam06160 162 fsqfeeltesgdyLEAREVLEKLEEETDALEELMEDIPPLYEELKTElpdqleelKEGYREMEEEgyALEH----LNVDK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1160 NLKEFQEHLQDSVKNTKDLNVKElkLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQ 1239
Cdd:pfam06160 238 EIQQLEEQLEENLALLENLELDE--AEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELE 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1240 RKEEDY---ADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNN-----Q 1311
Cdd:pfam06160 316 RVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSlrkdeL 395
|
330
....*....|.
gi 5911999 1312 KVEEAIQQYER 1322
Cdd:pfam06160 396 EAREKLDEFKL 406
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
568-745 |
2.82e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.62 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 568 ISHEEKRKLLDL----IEDLKKKLINEKKEKLTLEFKIREEVTQEftqywAQREADfKETLLQEREILEENAERRLAIFK 643
Cdd:COG1196 218 LKEELKELEAELlllkLRELEAELEELEAELEELEAELEELEAEL-----AELEAE-LEELRLELEELELELEEAQAEEY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 644 DLVGKcdtREEAAKDIcatKVETEEATAcLELKFNQIKAELAKTKGELIKTKEELKKRENESDSLIQELETSNKKIITQN 723
Cdd:COG1196 292 ELLAE---LARLEQDI---ARLEERRRE-LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180
....*....|....*....|..
gi 5911999 724 QRIKELINIIDQKEDTINEFQN 745
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAE 386
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1230-1520 |
2.90e-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: 42.42 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1230 RTQNLKADLQRKEEDYADLKEKLTDAKKQIKQ-----VQKEVSVMRDEDKLLRIKINELEKKKNQCSQ-ELDMKQRTIQQ 1303
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaiyAEQERMAMERERELERIRQEERKRELERIRQeEIAMEISRMRE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1304 LKE-QLNNQKVEEAIQQYERACKDLNVKEKiiEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETK 1382
Cdd:pfam17380 380 LERlQMERQQKNERVRQELEAARKVKILEE--ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1383 NNQRSNKEHENNTDVLGKLTNLQDElQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMe 1462
Cdd:pfam17380 458 RQQQVERLRQQEEERKRKKLELEKE-KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR- 535
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5911999 1463 iltaqltekdsdlQKWREERdqlvaaleiqlkalissnvQKDNEIEQLKRIISETSKI 1520
Cdd:pfam17380 536 -------------REAEEER-------------------RKQQEMEERRRIQEQMRKA 561
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1156-1536 |
3.35e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1156 KLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLK 1235
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1236 ADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKIN-------ELEKKKNQCSQELDMKQRTIQQLKEQL 1308
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNdlkkqkeELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1309 NNQK-----VEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKN 1383
Cdd:TIGR04523 197 LKLElllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1384 NQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQ----QN 1459
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEltnsES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1460 EMEILTAQLTEKDSDLQKWREERDQL----------VAALEIQLKALISSNVQKDNEIEQLKriiSETSKIETQIMDIKP 1529
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYkqeiknlesqINDLESKIQNQEKLNQQKDEQIKKLQ---QEKELLEKEIERLKE 433
|
....*..
gi 5911999 1530 KRISSAD 1536
Cdd:TIGR04523 434 TIIKNNS 440
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1237-1382 |
3.44e-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: 41.06 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1237 DLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEA 1316
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5911999 1317 IQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVE-RLATELEKWKEKCNDLETK 1382
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEaELEEKKAELDEELAELEAE 157
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1074-1387 |
3.51e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.92 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1074 LKEKETLIQQLKEELQEKNVTLDVQIQHVvegkralselTQGVTCYKAKIKELEtiletqkvershsAKLEQDILEKESI 1153
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHI----------QQQIKTYNKNIEEQR-------------KKNGENIARKQNK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1154 I---LKLERNLKEFQEHLQDSVKNtkdlnvkelkLKEEITQLTNNLQDMKHlLQLKEEEEETNRQETEKLKEELSASSAR 1230
Cdd:PHA02562 222 YdelVEEAKTIKAEIEELTDELLN----------LVMDIEDPSAALNKLNT-AAAKIKSKIEQFQKVIKMYEKGGVCPTC 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1231 TQNLKadlqrkeedyaDLKEKLTDAKKQIKQVQKEVsvmrdedKLLRIKINELEKKKNqcsqELDMKQRTIQQLKEQLNN 1310
Cdd:PHA02562 291 TQQIS-----------EGPDRITKIKDKLKELQHSL-------EKLDTAIDELEEIMD----EFNEQSKKLLELKNKIST 348
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5911999 1311 QKveEAIQQYERACKDLnvkEKIIEDMRMTLEEQEqtqveqdqvleaklEEVERLATELEKWKEKCNDLETKNNQRS 1387
Cdd:PHA02562 349 NK--QSLITLVDKAKKV---KAAIEELQAEFVDNA--------------EELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1250-1516 |
3.51e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1250 EKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN--NQKVEEAIQQYERACKDL 1327
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAalEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1328 NVKEKIIEDMRMTLEeqeqtqveqdqvleaKLEEVERLATELekwkekcndletknNQRSNKEHENNTDVLGKLTnlqDE 1407
Cdd:COG4942 100 EAQKEELAELLRALY---------------RLGRQPPLALLL--------------SPEDFLDAVRRLQYLKYLA---PA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1408 LQESEQKYNADRKKwleekmmLITQAKEAEnirnkemkkyaedrerffKQQNEMEILTAQLTEKDSDLQKWREERDQLVA 1487
Cdd:COG4942 148 RREQAEELRADLAE-------LAALRAELE------------------AERAELEALLAELEEERAALEALKAERQKLLA 202
|
250 260
....*....|....*....|....*....
gi 5911999 1488 ALEIQLKALISSNVQKDNEIEQLKRIISE 1516
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1019-1323 |
3.60e-03 |
|
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: 42.24 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1019 AIWEECKEIVKASSKKSHQIEELEQQIEKLQaeVKGYKDENnRLKEKEHKNQDDLLKeKETLIQQLKE------------ 1086
Cdd:pfam15818 75 ALEEEKGKYQLATEIKEKEIEGLKETLKALQ--VSKYSLQK-KVSEMEQKLQLHLLA-KEDHHKQLNEiekyyatitgqf 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1087 -ELQEKNVTLDVQIQHVVEGKRALSELTQG----VTCYKAKIKELETILETQKVERSHSakleqdiLEKESIILKL-ERN 1160
Cdd:pfam15818 151 gLVKENHGKLEQNVQEAIQLNKRLSALNKKqeseICSLKKELKKVTSDLIKSKVTCQYK-------MGEENINLTIkEQK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1161 LKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQlkeeeeeTNRQETEKLKEELSASSARTQNLKAD--L 1238
Cdd:pfam15818 224 FQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQ-------QQTQANTEMEAELKALKENNQTLERDneL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1239 QRK-----EEDYADLKEKLTDA----KKQIKQVQKEVSVMRDEDKLLRIKINELEKKKN-QCSQELDMKQRTIQQLKEqL 1308
Cdd:pfam15818 297 QREkvkenEEKFLNLQNEHEKAlgtwKKHVEELNGEINEIKNELSSLKETHIKLQEHYNkLCNQKKFEEDKKFQNVPE-V 375
|
330
....*....|....*
gi 5911999 1309 NNQKVEEAIQQYERA 1323
Cdd:pfam15818 376 NNENSEMSTEKSENL 390
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
115-183 |
4.07e-03 |
|
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: 40.02 E-value: 4.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5911999 115 FSKVFGPATTQKEFFQGC--IMQPVKDLLKGQSrlIFTYGLTNSGKTYTFQgteeniGILPRTLNVLFDSL 183
Cdd:cd01363 22 FYRGFRRSESQPHVFAIAdpAYQSMLDGYNNQS--IFAYGESGAGKTETMK------GVIPYLASVAFNGI 84
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
679-755 |
4.10e-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: 41.67 E-value: 4.10e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5911999 679 QIKAELAKTKGELIKTKEELKKRENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNLKSHMENTFK 755
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
542-742 |
4.68e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 542 AEETQNVETKLLDEDLDKTLEENKAFISHEEKRKLL-DLIEDLKKKLINEKKEKLTLEFKIREEVTQEftqywaQREADF 620
Cdd:COG1196 272 LRLELEELELELEEAQAEEYELLAELARLEQDIARLeERRRELEERLEELEEELAELEEELEELEEEL------EELEEE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 621 KETLLQEREILEENAERRLAIFKDLVGKCDTREEAAKDICATKVETEEATACLELKFNQIKAELAKTKGELIKTKEELKK 700
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 5911999 701 RENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINE 742
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1254-1528 |
4.72e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1254 DAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKI 1333
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1334 IEdmrmtleeqeqtqveqdqVLEAKLEEVERLATELEKWKEKCNDLETKNNQRsnkehenNTDVLGKLTNLQDELQESEQ 1413
Cdd:COG4913 687 LA------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAAED 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1414 KYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEME-----------ILTAQLTEKDSDLQKWREER 1482
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELEramrafnrewpAETADLDADLESLPEYLALL 821
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 5911999 1483 DQLVA----ALEIQLKALIssNVQKDNEIEQLKriisetSKIETQIMDIK 1528
Cdd:COG4913 822 DRLEEdglpEYEERFKELL--NENSIEFVADLL------SKLRRAIREIK 863
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1041-1179 |
5.46e-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: 41.57 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1041 LEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDL--LKEK-ETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVT 1117
Cdd:pfam10168 566 LKLQKEQQLQELQSLEEERKSLSERAEKLAEKYeeIKDKqEKLMRRCKKVLQRLNSQLPVLSDAEREMKKELETINEQLK 645
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5911999 1118 CYKAKIKELETILETQkveRSHSAKlEQDILEKESIILKLER------NLKEFQEHLQDSVKNTKDLN 1179
Cdd:pfam10168 646 HLANAIKQAKKKMNYQ---RYQIAK-SQSIRKKSSLSLSEKQrktikeILKQLGSEIDELIKQVKDIN 709
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
871-1382 |
8.74e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 8.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 871 QIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKID 950
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 951 ELRTlDSVSQISNIDLLNLRDLSNGSEEDNLpNTQLDLLGNDYLVSK----QVKEYRIQEPNRENSFHSSIEAIWEECKE 1026
Cdd:COG1196 313 ELEE-RLEELEEELAELEEELEELEEELEEL-EEELEEAEEELEEAEaelaEAEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1027 IVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGK 1106
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1107 RALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDILEKES---------------------------------- 1152
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLaglrglagavavligveaayeaaleaalaaalqn 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1153 IILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQ 1232
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAA 630
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1233 NLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLnnqk 1312
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE---- 706
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1313 vEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETK 1382
Cdd:COG1196 707 -RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1145-1558 |
8.89e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 8.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1145 QDILEKESIIlklERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKhllqlkeeeeetnrqeteKLKEEL 1224
Cdd:PRK03918 182 EKFIKRTENI---EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE------------------ELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1225 SassartqNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRiKINELEKKKNQCSQELDMKQRTIQQL 1304
Cdd:PRK03918 241 E-------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1305 KEQLnnQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEqeqtqveqdqvLEAKLEEVERLATELEKWKEKCNDLETKNN 1384
Cdd:PRK03918 313 EKRL--SRLEEEINGIEERIKELEEKEERLEELKKKLKE-----------LEKRLEELEERHELYEEAKAKKEELERLKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1385 QRSNKEHENNTDVLGKLTNLQDELQESEQKYNADR---KKWLEEKMMLITQAKEAENI------------RNKEMKKYAE 1449
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIgelKKEIKELKKAIEELKKAKGKcpvcgrelteehRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5911999 1450 DRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEI--QLKALISSnvQKDNEIEQLKRIISETSKIETQIMDI 1527
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEK--LKKYNLEELEKKAEEYEKLKEKLIKL 537
|
410 420 430
....*....|....*....|....*....|.
gi 5911999 1528 KpKRISSADPDKLQTEPLSTSFEISRNKIED 1558
Cdd:PRK03918 538 K-GEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
|
| |
