|
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 |
1.12e-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: 526.19 E-value: 1.12e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 57 DYLQVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQCILGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQP 136
Cdd:cd01368 1 DPVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 137 VKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmnlkphrsreylrlsseqekeeiask 216
Cdd:cd01368 81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 217 sallrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmansikFSVWVSFFEIYNEYIYDLFVPV-SSKFQ 295
Cdd:cd01368 130 ----------------------------------------------------YSVFVSYIEIYNEYIYDLLEPSpSSPTK 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 296 KRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSE------MSR 369
Cdd:cd01368 158 KRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSdgdvdqDKD 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 370 VIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSKFQQHVPFRESKLTHYFQSFFNGKGK 449
Cdd:cd01368 238 QITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGK 317
|
410 420
....*....|....*....|....*...
gi 546231677 450 ICMIVNISQCYLAYDETLNVLKFSAIAQ 477
Cdd:cd01368 318 ASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
64-479 |
4.02e-92 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 302.18 E-value: 4.02e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 64 RIRPFTQSEKELESEGCVHILDSQTvvlkepqcILGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLLKG 143
Cdd:pfam00225 1 RVRPLNEREKERGSSVIVSVESVDS--------ETVESSHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVLEG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 144 QSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLytkmnlkphrsreylrlsseqekeeiasksallrqi 223
Cdd:pfam00225 73 YNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK------------------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 224 kevtvhndsddtlygsltnslnisefeesikdyeqanlnmaNSIKFSVWVSFFEIYNEYIYDLFVPVSSKFQKrkmLRLS 303
Cdd:pfam00225 117 -----------------------------------------ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRK---LRIR 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 304 QDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQ-IEDSEMSRVIRVSELSLCDLA 382
Cdd:pfam00225 153 EDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQrNRSTGGEESVKTGKLNLVDLA 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 383 GSERTMKTQN-EGERLRETGNINTSLLTLGKCINVLKnsekSKFQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQCYL 461
Cdd:pfam00225 233 GSERASKTGAaGGQRLKEAANINKSLSALGNVISALA----DKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPSSS 308
|
410
....*....|....*...
gi 546231677 462 AYDETLNVLKFSAIAQKV 479
Cdd:pfam00225 309 NYEETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
60-479 |
1.92e-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: 297.95 E-value: 1.92e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 60 QVCLRIRPFTQSEKELESEGCVHILDSQTVVLkepqcilgRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:smart00129 3 RVVVRVRPLNKREKSRKSPSVVPFPDKVGKTL--------TVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 140 LLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERLYTKmnlkphrsreylrlsseqekeeiasksal 219
Cdd:smart00129 75 VLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKREEGW----------------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 220 lrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmansiKFSVWVSFFEIYNEYIYDLFVPVSSKfqkrkm 299
Cdd:smart00129 126 ------------------------------------------------QFSVKVSYLEIYNEKIRDLLNPSSKK------ 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 300 LRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSRVIRVSELSLC 379
Cdd:smart00129 152 LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNLV 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 380 DLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKskfQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQC 459
Cdd:smart00129 232 DLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSK---SRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPS 308
|
410 420
....*....|....*....|
gi 546231677 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 |
9.13e-87 |
|
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: 286.84 E-value: 9.13e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 60 QVCLRIRPFTQSEKELESEgCVHILDSQTVVLKEPqcilgrlseKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:cd00106 3 RVAVRVRPLNGREARSAKS-VISVDGGKSVVLDPP---------KNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 140 LLKGQSRLIFTYGLTNSGKTYTFQGT-EENIGILPRTLNVLFDSLQERLYTKMNlkphrsreylrlsseqekeeiasksa 218
Cdd:cd00106 73 ALEGYNGTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKRKETKSS-------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 219 llrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmansikFSVWVSFFEIYNEYIYDLFVPVsskfqKRK 298
Cdd:cd00106 127 --------------------------------------------------FSVSASYLEIYNEKIYDLLSPV-----PKK 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 299 MLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSRVIRVSELSL 378
Cdd:cd00106 152 PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVTSSKLNL 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 379 CDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKskfqQHVPFRESKLTHYFQSFFNGKGKICMIVNISQ 458
Cdd:cd00106 232 VDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN----KHIPYRDSKLTRLLQDSLGGNSKTIMIACISP 307
|
410
....*....|....*....
gi 546231677 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 |
2.56e-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: 222.47 E-value: 2.56e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 64 RIRPFTQSEkelESEGCVHIL----DSQTVVLKepqcilgrlseksSGQMAQK-FSFSKVFGPATTQKEFFQGcIMQPVK 138
Cdd:cd01366 9 RVRPLLPSE---ENEDTSHITfpdeDGQTIELT-------------SIGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQERlytkmnlkphrsreylrlsSEQekeeiasksa 218
Cdd:cd01366 72 SALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKEL-------------------KEK---------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 219 llrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmanSIKFSVWVSFFEIYNEYIYDLfvpVSSKFQKRK 298
Cdd:cd01366 123 -----------------------------------------------GWSYTIKASMLEIYNETIRDL---LAPGNAPQK 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 299 MLRLSQD-VKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKIlQIEDsEMSRVIRVSELS 377
Cdd:cd01366 153 KLEIRHDsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-SGRN-LQTGEISVGKLN 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 378 LCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSekskfQQHVPFRESKLTHYFQSFFNGKGKICMIVNIS 457
Cdd:cd01366 231 LVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQK-----QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNIS 305
|
410 420
....*....|....*....|..
gi 546231677 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 |
3.15e-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: 3.15e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 60 QVCLRIRPFTQSEKeleSEGCvhiLDSQTVVLKEPQCILGRlsekssgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:cd01372 4 RVAVRVRPLLPKEI---IEGC---RICVSFVPGEPQVTVGT---------DKSFTFDYVFDPSTEQEEVYNTCVAPLVDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 140 LLKGQSRLIFTYGLTNSGKTYTFQGT------EENIGILPRTLNVLFDSLQErlytkmnlkphrsreylrlsseqekeei 213
Cdd:cd01372 69 LFEGYNATVLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEK---------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 214 asksallrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnMANSIKFSVWVSFFEIYNEYIYDLFvpvSSK 293
Cdd:cd01372 121 -------------------------------------------------KKDTFEFQLKVSFLEIYNEEIRDLL---DPE 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 294 FQKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQ----IEDSEMSR 369
Cdd:cd01372 149 TDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQtkknGPIAPMSA 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 370 VIR----VSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKFQQHVPFRESKLTHYFQSFFN 445
Cdd:cd01372 229 DDKnstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISAL--GDESKKGAHVPYRDSKLTRLLQDSLG 306
|
410 420 430
....*....|....*....|....*....|....
gi 546231677 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 |
6.69e-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: 212.97 E-value: 6.69e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 59 LQVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQCILGRLSEKSSGQMAQ-------KFSFSKVFGPATTQKEFFQG 131
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGFFHGGSNNRDRRkrrnkelKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 132 CIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmnlkphrsreylrlsseqeke 211
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRIES-------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 212 eiasksallrqikevtvhnDSDDTlygsltnslnisefeesikdyeqanlnmansiKFSVWVSFFEIYNEYIYDLFVPVS 291
Cdd:cd01370 136 -------------------LKDEK--------------------------------EFEVSMSYLEIYNETIRDLLNPSS 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 292 skfqkrKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIE-DSEMSRV 370
Cdd:cd01370 165 ------GPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDkTASINQQ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 371 IRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKFQQHVPFRESKLTHYFQSFFNGKGKI 450
Cdd:cd01370 239 VRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINAL--ADPGKKNKHIPYRDSKLTRLLKDSLGGNCRT 316
|
410 420
....*....|....*....|....*....
gi 546231677 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 |
2.27e-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: 209.10 E-value: 2.27e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 59 LQVCLRIRPFTQSEKELESEGCVHILDSQtvvlKEPQCILGRLSEKSSgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVK 138
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVR----KEVSVRTGGLADKSS---TKTYTFDMVFGPEAKQIDVYRSVVCPILD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTE-----------ENIGILPRTLNVLFDSLqerlytkmnlkphrsreylrlsSE 207
Cdd:cd01364 77 EVLMGYNCTIFAYGQTGTGKTYTMEGDRspneeytweldPLAGIIPRTLHQLFEKL----------------------ED 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 208 QEKEeiasksallrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmansikFSVWVSFFEIYNEYIYDLF 287
Cdd:cd01364 135 NGTE---------------------------------------------------------YSVKVSYLEIYNEELFDLL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 288 VPVSSKFQKRKMLRLSQDVKGYsFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIE-DSE 366
Cdd:cd01364 158 SPSSDVSERLRMFDDPRNKRGV-IIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKEtTID 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 367 MSRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKfqqHVPFRESKLTHYFQSFFNG 446
Cdd:cd01364 237 GEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL--VERAP---HVPYRESKLTRLLQDSLGG 311
|
410 420 430
....*....|....*....|....*....|
gi 546231677 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 |
2.81e-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: 207.57 E-value: 2.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 60 QVCLRIRPFTQSEKELEsEGCVHILDSQTVVLKEPQcilgrlsekssgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:cd01374 3 TVTVRVRPLNSREIGIN-EQVAWEIDNDTIYLVEPP--------------STSFTFDHVFGGDSTNREVYELIAKPVVKS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 140 LLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQErlytkmnlkpHRSREYLrlsseqekeeiasksal 219
Cdd:cd01374 68 ALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD----------TPDREFL----------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 220 lrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmansikfsVWVSFFEIYNEYIYDLFVPVSskfqkrKM 299
Cdd:cd01374 121 ---------------------------------------------------LRVSYLEIYNEKINDLLSPTS------QN 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 300 LRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSRV-IRVSELSL 378
Cdd:cd01374 144 LKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGtVRVSTLNL 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 379 CDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNsekSKFQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQ 458
Cdd:cd01374 224 IDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE---GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITP 300
|
410 420
....*....|....*....|.
gi 546231677 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 |
3.71e-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: 3.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 59 LQVCLRIRPFTQSEKELESEGCVHILDSQTVVLkepqcilgRLSEKSSgqmaqKFSFSKVFGPATTQKEFFQGCIMQPVK 138
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVI--------ATSETGK-----TFSFDRVFDPNTTQEDVYNFAAKPIVD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 139 DLLKGQSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSLqerlytkmnlkphrsreylrlsseqekeeias 215
Cdd:cd01369 71 DVLNGYNGTIFAYGQTSSGKTYTMEGKlgdPESMGIIPRIVQDIFETI-------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 216 ksallrqikevtvhndsddtlygsltnslnisefeesikdyeqanLNMANSIKFSVWVSFFEIYNEYIYDLFVPvsskfq 295
Cdd:cd01369 119 ---------------------------------------------YSMDENLEFHVKVSYFEIYMEKIRDLLDV------ 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 296 KRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQiEDSEmSRVIRVSE 375
Cdd:cd01369 148 SKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-ENVE-TEKKKSGK 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 376 LSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSkfqqHVPFRESKLTHYFQSFFNGKGKICMIVN 455
Cdd:cd01369 226 LYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKT----HIPYRDSKLTRILQDSLGGNSRTTLIIC 301
|
410
....*....|....*..
gi 546231677 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 |
9.52e-54 |
|
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: 192.95 E-value: 9.52e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 60 QVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQcilGRLSEKSSGQMAQKFSFSKVF------GPA-TTQKEFFQGC 132
Cdd:cd01365 4 KVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQ---ADKNNKATREVPKSFSFDYSYwshdseDPNyASQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 133 IMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFdslqerlytkmnlkphrsreylrlsseqekEE 212
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLCEDLF------------------------------SR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 213 IASKSAllrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmaNSIKFSVWVSFFEIYNEYIYDLFVPvsS 292
Cdd:cd01365 131 IADTTN----------------------------------------------QNMSYSVEVSYMEIYNEKVRDLLNP--K 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 293 KFQKRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQI--EDSEMSRV 370
Cdd:cd01365 163 PKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKrhDAETNLTT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 371 IRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVL---KNSEKSKFQQHVPFRESKLTHYFQSFFNGK 447
Cdd:cd01365 243 EKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmSSGKSKKKSSFIPYRDSVLTWLLKENLGGN 322
|
410 420 430
....*....|....*....|....*....|..
gi 546231677 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 |
1.02e-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: 189.21 E-value: 1.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 57 DYLQVCLRIRPFTQSEKeleSEGCVHILD----SQTVVLKEPqcilgrlsEKSSGQMAQKFSFSKVFGPATTQKEFFQGC 132
Cdd:cd01371 1 ENVKVVVRCRPLNGKEK---AAGALQIVDvdekRGQVSVRNP--------KATANEPPKTFTFDAVFDPNSKQLDVYDET 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 133 IMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGT---EENIGILPRTLNVLFDSlqerlytkmnlkphrsreylrlsseqe 209
Cdd:cd01371 70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKredPELRGIIPNSFAHIFGH--------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 210 keeIASKSallrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmaNSIKFSVWVSFFEIYNEYIYDLFvp 289
Cdd:cd01371 123 ---IARSQ-----------------------------------------------NNQQFLVRVSYLEIYNEEIRDLL-- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 290 vsSKFQKRKM-LRLSQDVKGYsfIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKIlqiEDSEM- 367
Cdd:cd01371 151 --GKDQTKRLeLKERPDTGVY--VKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI---ECSEKg 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 368 ---SRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSeKSkfqQHVPFRESKLTHYFQSFF 444
Cdd:cd01371 224 edgENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG-KS---THIPYRDSKLTRLLQDSL 299
|
410 420 430
....*....|....*....|....*....|....*
gi 546231677 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 |
1.31e-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: 179.62 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 59 LQVCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQcilgrlseksSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVK 138
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPR----------NHGETLKYQFDAFYGEESTQEDIYAREVQPIVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLnvlfdslqerlytkmnlkphrsREYLRLSSEQekeeiasksa 218
Cdd:cd01376 72 HLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTV----------------------MDLLQMTRKE---------- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 219 llrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmanSIKFSVWVSFFEIYNEYIYDLFVPvsskfqKRK 298
Cdd:cd01376 120 -----------------------------------------------AWALSFTMSYLEIYQEKILDLLEP------ASK 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 299 MLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSRVIRvSELSL 378
Cdd:cd01376 147 ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRT-GKLNL 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 379 CDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKskfqqHVPFRESKLTHYFQSFFNGKGKICMIVNISQ 458
Cdd:cd01376 226 IDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLP-----RIPYRDSKLTRLLQDSLGGGSRCIMVANIAP 300
|
410
....*....|....*.
gi 546231677 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 |
4.24e-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: 178.86 E-value: 4.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 57 DYLQVCLRIRPFTQSEKELESEGCVHILDSQTVVLkepqcilgrlseksSGQMAQKFSFSKVFGPATTQKEFFQGCIMQP 136
Cdd:cd01373 1 DAVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVL--------------HSKPPKTFTFDHVADSNTNQESVFQSVGKPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 137 VKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENI--------GILPRTLNVLFDSLQErlytkmnlkphrsreylrlssEQ 208
Cdd:cd01373 67 VESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQR---------------------EK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 209 EKEEiasksallrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnmaNSIKFSVWVSFFEIYNEYIYDLFV 288
Cdd:cd01373 126 EKAG----------------------------------------------------EGKSFLCKCSFLEIYNEQIYDLLD 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 289 PVSSKfqkrkmLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMS 368
Cdd:cd01373 154 PASRN------LKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACF 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 369 RVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSKfQQHVPFRESKLTHYFQSFFNGKG 448
Cdd:cd01373 228 VNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGK-QRHVCYRDSKLTFLLRDSLGGNA 306
|
410 420
....*....|....*....|....
gi 546231677 449 KICMIVNISQCYLAYDETLNVLKF 472
Cdd:cd01373 307 KTAIIANVHPSSKCFGETLSTLRF 330
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
105-598 |
1.13e-43 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 169.15 E-value: 1.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 105 SSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENIGILPRTLNVLFDSLQ 184
Cdd:COG5059 50 LEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 185 ERLYTKmnlkphrsreylrlsseqekeeiasksallrqikevtvhndsddtlygsltnslnisefeesikdyeqanlnma 264
Cdd:COG5059 130 DLSMTK-------------------------------------------------------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 265 nsiKFSVWVSFFEIYNEYIYDLFVPvsSKFQKRKMLRLSQDVKgysfIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKL 344
Cdd:COG5059 136 ---DFAVSISYLEIYNEKIYDLLSP--NEESLNIREDSLLGVK----VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 345 NNASSRSHSIFTVKiLQIEDSEMSrVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSK 424
Cdd:COG5059 207 NDESSRSHSIFQIE-LASKNKVSG-TSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 425 fqqHVPFRESKLTHYFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFSA----IAQKVCVP-------------DTLNS 487
Cdd:COG5059 285 ---HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASraksIKNKIQVNsssdssreieeikFDLSE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 488 SQEKLFGPVKSSQDVSLDSNSN---SKILNVKRATISWENSLEDLMededlveeLENAEETQNVETKLLDEDLDKTLEEN 564
Cdd:COG5059 362 DRSEIEILVFREQSQLSQSSLSgifAYMQSLKKETETLKSRIDLIM--------KSIISGTFERKKLLKEEGWKYKSTLQ 433
|
490 500 510
....*....|....*....|....*....|....*
gi 546231677 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 |
4.30e-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: 160.92 E-value: 4.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 61 VCLRIRPFTQSEKELESEGCVHILDSQTVVLKEPQCILgRLSEKSSgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVKDL 140
Cdd:cd01367 4 VCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKV-DLTKYIE---NHTFRFDYVFDESSSNETVYRSTVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 141 LKGQSRLIFTYGLTNSGKTYT----FQGTEENIGILprtlnvlfdslqerlytkmnlkphrsreylrlsseqekeEIASK 216
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTmggdFSGQEESKGIY---------------------------------------ALAAR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 217 SaLLRQIKEVTVHNDsddtlygsltnslnisefeesikdyeqanlnmansikFSVWVSFFEIYNEYIYDLFvpvsskfQK 296
Cdd:cd01367 121 D-VFRLLNKLPYKDN-------------------------------------LGVTVSFFEIYGGKVFDLL-------NR 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 297 RKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSrvirvSEL 376
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTNKLH-----GKL 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 377 SLCDLAGSERTMKT-QNEGERLRETGNINTSLLTLGKCINVLKNSekskfQQHVPFRESKLTHYFQ-SFFNGKGKICMIV 454
Cdd:cd01367 231 SFVDLAGSERGADTsSADRQTRMEGAEINKSLLALKECIRALGQN-----KAHIPFRGSKLTQVLKdSFIGENSKTCMIA 305
|
410 420
....*....|....*....|.
gi 546231677 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 |
8.01e-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: 8.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 59 LQVCLRIRPFTQSEKELESEGcvhiLDSQTVVLKEPQCIlgRLSEKSSGQMAQKFSFSKVFGPATtQKEFFQGCIMQPVK 138
Cdd:cd01375 2 VQAFVRVRPTDDFAHEMIKYG----EDGKSISIHLKKDL--RRGVVNNQQEDWSFKFDGVLHNAS-QELVYETVAKDVVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTEENI---GILPRTLNVLFDSLQERlYTKMnlkphrsreylrlsseqekeeias 215
Cdd:cd01375 75 SALAGYNGTIFAYGQTGAGKTFTMTGGTENYkhrGIIPRALQQVFRMIEER-PTKA------------------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 216 ksallrqikeVTVHndsddtlygsltnslnisefeesikdyeqanlnmansikfsvwVSFFEIYNEYIYDLFVPVSSKFQ 295
Cdd:cd01375 130 ----------YTVH-------------------------------------------VSYLEIYNEQLYDLLSTLPYVGP 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 296 KRKMLRLSQDVKGYSFIKDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTVKILQIEDSEMSRVIRVSE 375
Cdd:cd01375 157 SVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTMNKNSSRSHCIFTIHLEAHSRTLSSEKYITSK 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 376 LSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKfqQHVPFRESKLTHYFQSFFNGKGKICMIVN 455
Cdd:cd01375 237 LNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIAL--SDKDR--THVPFRQSKLTHVLRDSLGGNCNTVMVAN 312
|
410
....*....|....*....
gi 546231677 456 ISQCYLAYDETLNVLKFSA 474
Cdd:cd01375 313 IYGEAAQLEETLSTLRFAS 331
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
92-479 |
4.29e-32 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 137.37 E-value: 4.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 92 KEPQCILGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQG-----TE 166
Cdd:PLN03188 113 EEGEMIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglLE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 167 ENI-----GILPRTLNVLFDslqerlytkmnlkphrsreylRLSSEQEKeeiasksallrqikevtvHNDsddtlygslt 241
Cdd:PLN03188 193 EHLsgdqqGLTPRVFERLFA---------------------RINEEQIK------------------HAD---------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 242 nslnisefeesikdyeqanlnmaNSIKFSVWVSFFEIYNEYIYDLFVPVsskfQKRKMLRlsQDVKGYSFIKDLQWIQVS 321
Cdd:PLN03188 224 -----------------------RQLKYQCRCSFLEIYNEQITDLLDPS----QKNLQIR--EDVKSGVYVENLTEEYVK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 322 DSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTV----KILQIEDSEMSrvIRVSELSLCDLAGSERTMKTQNEGERL 397
Cdd:PLN03188 275 TMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCvvesRCKSVADGLSS--FKTSRINLVDLAGSERQKLTGAAGDRL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 398 RETGNINTSLLTLGKCINVLKNSEKSKFQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFSAIAQ 477
Cdd:PLN03188 353 KEAGNINRSLSQLGNLINILAEISQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAQRAK 432
|
..
gi 546231677 478 KV 479
Cdd:PLN03188 433 AI 434
|
|
| RBD_KIF20B |
cd21786 |
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ... |
600-654 |
1.24e-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: 84.07 E-value: 1.24e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 546231677 600 KIREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREE 654
Cdd:cd21786 1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNKTAKEEE 55
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1077-1381 |
5.69e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.79 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1077 QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLkEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGV 1156
Cdd:TIGR02168 685 KIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1157 TCYKAKIKELETILETQKVEcshSAKLEQDILEKESIILKLERNLKEFQEHLQDsvkntkdLNVKELKLKEEITQLTNNL 1236
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAE---IEELEAQIEQLKEELKALREALDELRAELTL-------LNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1237 QDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLL 1316
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 546231677 1317 RIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKV---EEAIQQYERACKDLNVKEKIIEDMRMTL 1381
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltlEEAEALENKIEDDEEEARRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
629-1458 |
7.72e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 77.40 E-value: 7.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 629 EILEENAERRLAIFKDLVG--KCDTR-EEAAKDIcatkVETEEthNYVGFEDIIDSLQDNVADIKKQAEIAHLYI---AS 702
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAGisKYKERrKETERKL----ERTRE--NLDRLEDILNELERQLKSLERQAEKAERYKelkAE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 703 LPDPQEATACLELK-FNQIKAELAKTKGELIKTKEELKKRENESDSLIQELETS----NKKIITQNQRIKELINIIDQKE 777
Cdd:TIGR02168 222 LRELELALLVLRLEeLREELEELQEELKEAEEELEELTAELQELEEKLEELRLEvselEEEIEELQKELYALANEISRLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 778 DTINEFQNLKSHMENTFKcndKADTSSLIINNKLICNETVEvpKDSKSKICSERKRVNENELQQDEPPAKKGSIHvsSAI 857
Cdd:TIGR02168 302 QQKQILRERLANLERQLE---ELEAQLEELESKLDELAEEL--AELEEKLEELKEELESLEAELEELEAELEELE--SRL 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 858 TEDQKKSEEVRPNIAEIEdirvLQENneglrafLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLsKEVQQIQ 937
Cdd:TIGR02168 375 EELEEQLETLRSKVAQLE----LQIA-------SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL-KELQAEL 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 938 SNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKlmhTKIDELRTLdsvsqisnidLLNLRDLSNGse 1017
Cdd:TIGR02168 443 EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ---ARLDSLERL----------QENLEGFSEG-- 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1018 EDNLPNTQLDLLGNDYLVSKQVK---EY----------RIQEP--NRENSFHSSIEAIWEECKEIVK---ASSKKSHQIE 1079
Cdd:TIGR02168 508 VKALLKNQSGLSGILGVLSELISvdeGYeaaieaalggRLQAVvvENLNAAKKAIAFLKQNELGRVTflpLDSIKGTEIQ 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1080 ELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLL------KEKETLIQQLKE-ELQEKNVTLD---VQIQHVVEGKRAl 1149
Cdd:TIGR02168 588 GNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLggvlvvDDLDNALELAKKlRPGYRIVTLDgdlVRPGGVITGGSA- 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1150 sELTQGVTCYKAKIKELETILEtqkvecshsaKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEI 1229
Cdd:TIGR02168 667 -KTNSSILERRREIEELEEKIE----------ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1230 TQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVM 1309
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1310 RDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQV 1389
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI--ESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1390 EQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNL-QDELQESEQKYNAD 1458
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKI 963
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
740-1350 |
5.15e-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: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 740 KRENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNlkshMENTFKCNDKADTSSLIINNKLICNETVEV 819
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNN----KIKILEQQIKDLNDKLKKNKDKINKLNSDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 820 PK-DSKSKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVRPNIAEIEDIRVLQENnegLRAFLLTIENEL 898
Cdd:TIGR04523 106 SKiNSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEE---LENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 899 KNEKEEKAELNKQIVHFQQELSLSEKKN----------LTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEI 968
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKIqknkslesqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 969 ETATRSITNNVSQIKLMHTKIDELRtlDSVSQISNidllNLRDLSNGSEEDNLPNTQLDLLGNDylvsKQVKEYRIQEPN 1048
Cdd:TIGR04523 263 NKIKKQLSEKQKELEQNNKKIKELE--KQLNQLKS----EISDLNNQKEQDWNKELKSELKNQE----KKLEEIQNQISQ 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1049 RE---NSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLK------EKEHKNQDDLLKEKET 1119
Cdd:TIGR04523 333 NNkiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLEsqindlESKIQNQEKLNQQKDE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1120 LIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVECS-----------HSAKLEQDIL 1188
Cdd:TIGR04523 413 QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrsinkikqNLEQKQKELK 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1189 EKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLL---------QLKEEEEETNRQETEK 1259
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELnkddfelkkENLEKEIDEKNKEIEE 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1260 LKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQR 1339
Cdd:TIGR04523 573 LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
650
....*....|.
gi 546231677 1340 TIQQLKEQLNN 1350
Cdd:TIGR04523 653 TIKEIRNKWPE 663
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1078-1363 |
1.93e-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: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1078 IEELEQQIEKL--QAEV----KGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQH----VVEGKR 1147
Cdd:COG1196 195 LGELERQLEPLerQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAEleaeLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1148 ALSELTQGVTCYKAKIKELETILETQKVECSHSAKLEQDILEKesiILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKE 1227
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER---LEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1228 EITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVS 1307
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 546231677 1308 VMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERA 1363
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
|
| RBD_KIF20A-like |
cd21744 |
RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; ... |
600-654 |
4.10e-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: 62.47 E-value: 4.10e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 546231677 600 KIREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREE 654
Cdd:cd21744 1 RIREEVSEEFEEQFALMEEDYEERLENEKEILEERYEKRLEIRKELIKKLSAALE 55
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1076-1361 |
5.08e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.12 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1076 HQIEELEQQIEKLQAEVKGYKDENNRLKEKehknqddlLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQG 1155
Cdd:COG1196 232 LKLRELEAELEELEAELEELEAELEELEAE--------LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1156 VTCYKAKIKELETILETQKVECshsAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNN 1235
Cdd:COG1196 304 IARLEERRRELEERLEELEEEL---AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1236 LQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKL 1315
Cdd:COG1196 381 LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 546231677 1316 LRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQkvEEAIQQYE 1361
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLL--LEAEADYE 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1053-1411 |
2.49e-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: 69.33 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1053 FHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEkn 1132
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQ-- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1133 vtLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVEcsHSAKLEQDILEKESIILKLERNLKEFQEHLQDSV 1212
Cdd:TIGR02169 246 --LASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE--EQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1213 KNTKDLNVKELKLKEEITQLTNNLQDMKhllqlkeeeeetnrQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKL 1292
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEELEREIEEER--------------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1293 TDAKKQIKQVQKEvsvmrdedkllrikINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKEK 1372
Cdd:TIGR02169 388 KDYREKLEKLKRE--------------INELKRELDRLQEELQRLSEELADLNAAI--AGIEAKINELEEEKEDKALEIK 451
|
330 340 350
....*....|....*....|....*....|....*....
gi 546231677 1373 IIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEK 1411
Cdd:TIGR02169 452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQR 490
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1280-1583 |
5.77e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.04 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1280 RKEEDYADLKEKLTDAKKQIKQVQKEVsvMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN--NQKVEEAI 1357
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRE--LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEelELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1358 QQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHEnntdv 1437
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE----- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1438 lgkltnLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEmkkyAEDRERFFKQQNEMEILTAQLTEKDSDLQK 1517
Cdd:COG1196 363 ------AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQL----EELEEAEEALLERLERLEEELEELEEALAE 432
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546231677 1518 WREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPKRISSADPDKLQTE 1583
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 ... |
629-1511 |
9.47e-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: 9.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 629 EILEENAERRLAIFKDLVGKCDTREEAAKdicATKVETEETHNYVGFEDIIDSLQDNVADIKKQAEIAhlyiasLPDPQE 708
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSRLKRKKKE---ALKKLIEETENLAELIIDLEELKLQELKLKEQAKKA------LEYYQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 709 ATACLELKFNQIKAELAKTKGELIKTKEELKKRENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNLKs 788
Cdd:pfam02463 216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE- 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 789 hmentfkCNDKADTSSLIINNKLICNETVEVPKDSKSKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVR 868
Cdd:pfam02463 295 -------EEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 869 PNIAEIEDIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQSnyDIAIAELH 948
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE--SIELKQGK 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 949 VQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRTLDSVsqisniDLLNLRDLSNGSEEDNLPNTQLDL 1028
Cdd:pfam02463 446 LTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL------EERSQKESKARSGLKVLLALIKDG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1029 LGNDyLVSKQVKEYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHK 1108
Cdd:pfam02463 520 VGGR-IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLE 598
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1109 NQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKI-------KELETILETQKVECSHSA 1181
Cdd:pfam02463 599 IDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSleeglaeKSEVKASLSELTKELLEI 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1182 KLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLK 1261
Cdd:pfam02463 679 QELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1262 EELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTI 1341
Cdd:pfam02463 759 KEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1342 QQLKEQLNNQKvEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLET 1421
Cdd:pfam02463 839 ALELKEEQKLE-KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1422 KNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEM 1501
Cdd:pfam02463 918 EIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEK 997
|
890
....*....|
gi 546231677 1502 EILTAQLTEK 1511
Cdd:pfam02463 998 ERLEEEKKKL 1007
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1024-1568 |
1.13e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.01 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1024 TQLDLLGNDYLVSKQVKEYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLK 1103
Cdd:PRK03918 155 LGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1104 ----------------EKEHKNQDDLLKEKETLIQQLKEELQ--EKNVTLDVQIQHVVEGKRALSELTQGvtcYKAKIKE 1165
Cdd:PRK03918 235 elkeeieelekeleslEGSKRKLEEKIRELEERIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEE---YLDELRE 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1166 LETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQ---EHLQDSVKNTKDLNVKELKLKEEITQLTN-NLQDMKH 1241
Cdd:PRK03918 312 IEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTGlTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1242 LLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQR---------------KEEDYADLKEKLTdakKQIKQVQKEV 1306
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkakgkcpvcgrelTEEHRKELLEEYT---AELKRIEKEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1307 SVMRDEDKLLRIKINELEKKKNQCSQELDMKQrTIQQLKE------QLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMT 1380
Cdd:PRK03918 469 KEIEEKERKLRKELRELEKVLKKESELIKLKE-LAEQLKEleeklkKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1381 LEEQEQTQVEQDqVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRK 1460
Cdd:PRK03918 548 LEKLEELKKKLA-ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1461 KWLEEKMMLITQAKEAENIRNK-EMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEiQLKALISS 1539
Cdd:PRK03918 627 ELDKAFEELAETEKRLEELRKElEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE-KLKEELEE 705
|
570 580
....*....|....*....|....*....
gi 546231677 1540 NVQKDNEIEQLKRIISETSKIETQIMDIK 1568
Cdd:PRK03918 706 REKAKKELEKLEKALERVEELREKVKKYK 734
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1073-1502 |
1.31e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 66.63 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1073 KKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDdlLKEKETLIQQLKEELqeKNVTLDVQIQHVVEGKRALSEL 1152
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE--AKAKKEELERLKKRL--TGLTPEKLEKELEELEKAKEEI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1153 TQGVTCYKAKIKELETILETQK--VECSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEIT 1230
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKkaIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1231 QLTNNLQDMKHLLQLKEEEEETNRqetekLKEELSASSARtqnlkaDLQRKEEDYADLKEKLTDAKKQIKQVQKEVSvmr 1310
Cdd:PRK03918 484 ELEKVLKKESELIKLKELAEQLKE-----LEEKLKKYNLE------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELE--- 549
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1311 dedkllriKINELEKKKNQCSQELDMKQRTIQQLKEQLNN------QKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQ 1384
Cdd:PRK03918 550 --------KLEELKKKLAELEKKLDELEEELAELLKELEElgfesvEELEERLKELEPFYNEYLELKDAEKELEREEKEL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1385 EQTQVEqdqvLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGK----LTNLQDELQESEQKYNADRK 1460
Cdd:PRK03918 622 KKLEEE----LDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRelagLRAELEELEKRREEIKKTLE 697
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 546231677 1461 KWLEEKMMLITQAKEAENIrNKEMKKYAEDRERFFKQQNEME 1502
Cdd:PRK03918 698 KLKEELEEREKAKKELEKL-EKALERVEELREKVKKYKALLK 738
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
909-1569 |
2.97e-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: 65.46 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 909 NKQIVHFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTK 988
Cdd:TIGR02168 238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 989 IDEL-RTLDSVSQISNIDLLNLRDLSNGSEEDNlpnTQLDLLgndylvSKQVKEYRIQEPNRENSFHSSIEAIWEECKEI 1067
Cdd:TIGR02168 318 LEELeAQLEELESKLDELAEELAELEEKLEELK---EELESL------EAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1068 VKASSKK---SHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLK----EKETLIQQLKEELQEKNVTLDVQIQ 1140
Cdd:TIGR02168 389 AQLELQIaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQaeleELEEELEELQEELERLEEALEELRE 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1141 HVVEGKRALSELTQGVTCYKAKIKELETILETQK---------------------------------------------- 1174
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQARLDSLERLQENLEgfsegvkallknqsglsgilgvlselisvdegyeaaieaalggrlq 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1175 ---VECSHSAKLEQDILEKESIIL------------KLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQL------T 1233
Cdd:TIGR02168 549 avvVENLNAAKKAIAFLKQNELGRvtflpldsikgtEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLlggvlvV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1234 NNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSAR------TQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVS 1307
Cdd:TIGR02168 629 DDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSaktnssILERRREIEELEEKIEELEEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1308 VMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVE-----EAIQQYERACKDLNVKEKIIEDMRMTLE 1382
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKElteleAEIEELEERLEEAEEELAEAEAEIEELE 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1383 EQEQTQVEQDQVLEAKL----EEVERLATELEKWKEKCNDLE------TKNNQRSNKEHENNTDVLGKLTNLQDELQESE 1452
Cdd:TIGR02168 789 AQIEQLKEELKALREALdelrAELTLLNEEAANLRERLESLErriaatERRLEDLEEQIEELSEDIESLAAEIEELEELI 868
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1453 QKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAAL--- 1529
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsee 948
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 546231677 1530 -EIQLKALISSNVQKDNEIEQLKRiisETSKIETQIMDIKP 1569
Cdd:TIGR02168 949 ySLTLEEAEALENKIEDDEEEARR---RLKRLENKIKELGP 986
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1286-1551 |
1.18e-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: 63.54 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1286 ADLKEKLTDAKKQIKQVQKEVSVMRDEDklLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN-----NQKVEEAIQQY 1360
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELTAELQELEEKLEelrleVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1361 ERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVER----LATELEKWKEKCNDLEtknnqrsnkehENNTD 1436
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldeLAEELAELEEKLEELK-----------EELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1437 VLGKLTNLQDELQESEQKYNADRKKWLEEKmmlitqakeaenirnkemKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQ 1516
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLR------------------SKVAQLELQIASLNNEIERLEARLERLEDRRE 417
|
250 260 270
....*....|....*....|....*....|....*.
gi 546231677 1517 KWREERDQLVAAL-EIQLKALISSNVQKDNEIEQLK 1551
Cdd:TIGR02168 418 RLQQEIEELLKKLeEAELKELQAELEELEEELEELQ 453
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1054-1372 |
2.92e-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: 62.39 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1054 HSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKehknqddlLKEKETLIQQLKEELQEKNV 1133
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEAR--------IEELEEDLHKLEEALNDLEA 786
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1134 TLDVQIQHVVEGKraLSELTQGVTCYKAKIKELETILETQKVEcshSAKLEQDILEKESIILKLERNLKEFQEHLQDSVK 1213
Cdd:TIGR02169 787 RLSHSRIPEIQAE--LSKLEEEVSRIEARLREIEQKLNRLTLE---KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNG 861
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1214 NTKDLNVKELKLKEEITQLTNNLQDMKhllqlkeeeeetnrQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLT 1293
Cdd:TIGR02169 862 KKEELEEELEELEAALRDLESRLGDLK--------------KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1294 DAKKQIKQVQKEVSVMrdedkllrIKINELEKKKNQCSQELDMKQRTIQQLkEQLNNQkveeAIQQYERACKDLN-VKEK 1372
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 ... |
1078-1486 |
3.38e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.96 E-value: 3.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1078 IEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDL------LKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSE 1151
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEInektteISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1152 LTQGVTCYKAKI------------KELETILETQKVECSHS-----------AKLEQDILEKESIILKLERNLKEFQEHL 1208
Cdd:TIGR04523 286 LEKQLNQLKSEIsdlnnqkeqdwnKELKSELKNQEKKLEEIqnqisqnnkiiSQLNEQISQLKKELTNSESENSEKQREL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1209 QDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADL 1288
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1289 KEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQlnNQKVEEAIQQYERACKDLN 1368
Cdd:TIGR04523 446 TNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE--KKELEEKVKDLTKKISSLK 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1369 VKEKIiedmrmtLEEQEQTQVEQDQVLEAKLEEVerlatELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDEL 1448
Cdd:TIGR04523 524 EKIEK-------LESEKKEKESKISDLEDELNKD-----DFELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
410 420 430
....*....|....*....|....*....|....*...
gi 546231677 1449 QESEQKYNADRKKwLEEKMMLITQAKEAENIRNKEMKK 1486
Cdd:TIGR04523 592 DQKEKEKKDLIKE-IEEKEKKISSLEKELEKAKKENEK 628
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1032-1346 |
3.86e-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: 62.01 E-value: 3.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1032 DYLVSKQVKEYRIQEPNRENsFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGY-KDENNRLKEKEHKNQ 1110
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEA-IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELE 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1111 DDL--LKEKETLIQQLKEELQEKNVTLDVQIQHvvegkralseltqgvtcYKAKIKELETILETQKVEcshSAKLEQDIL 1188
Cdd:TIGR02169 301 AEIasLERSIAEKERELEDAEERLAKLEAEIDK-----------------LLAEIEELEREIEEERKR---RDKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1189 EKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLqdmkhllqlkeeeeetnrqetEKLKEELSASS 1268
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL---------------------DRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1269 ARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRD-----EDKLLRIK--INELEKKKNQCSQELDMKQRTI 1341
Cdd:TIGR02169 420 EELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAAdlskyEQELYDLKeeYDRVEKELSKLQRELAEAEAQA 499
|
....*
gi 546231677 1342 QQLKE 1346
Cdd:TIGR02169 500 RASEE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1155-1552 |
4.36e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1155 GVTCYKAKIKE-LETILETQkvecshsAKLE--QDIL-EKESIILKLER---------NLKEFQEHLQDS--VKNTKDLN 1219
Cdd:COG1196 166 GISKYKERKEEaERKLEATE-------ENLErlEDILgELERQLEPLERqaekaeryrELKEELKELEAEllLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1220 VKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQI 1299
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1300 KQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNN--QKVEEAIQQYERACKDLNVKEKIIEDM 1377
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEaeAELAEAEEELEELAEELLEALRAAAEL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1378 RMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNA 1457
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1458 DRKKwleekmmlitQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALI 1537
Cdd:COG1196 479 LAEL----------LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
410 420
....*....|....*....|
gi 546231677 1538 SSNVQKDNE-----IEQLKR 1552
Cdd:COG1196 549 QNIVVEDDEvaaaaIEYLKA 568
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1077-1421 |
1.25e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 60.47 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1077 QIEELEQQIEKLQAEVKGYKDENNRLkEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGV 1156
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRI-ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1157 TCYKAKIKELETILEtQKVECSHSAKLEQDILEKE---SIILKLERNLKEFQEHLQDSVKNTKDLNVKELKL---KEEIT 1230
Cdd:TIGR02169 754 ENVKSELKELEARIE-ELEEDLHKLEEALNDLEARlshSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLtleKEYLE 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1231 QLTNNLQDMKHLLQLKEEEeetnrqetekLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSvmr 1310
Cdd:TIGR02169 833 KEIQELQEQRIDLKEQIKS----------IEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR--- 899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1311 dedkllrikinELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEA-IQQYERACKDLNVKEKIIEDMRMTLEEQEQTQV 1389
Cdd:TIGR02169 900 -----------ELERKIEELEAQIEKKRKRLSELKAKLEALEEELSeIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIR 968
|
330 340 350
....*....|....*....|....*....|..
gi 546231677 1390 EQDQVLEAKLEEVERLATELEKWKEKCNDLET 1421
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
537-1363 |
1.29e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 60.37 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 537 EELENAEETQNVETKLLDED-------LDKTLEENKAFISHEEKRKLLDLIEDLKKKLINEKKEKLTLEFKIREEVTQEF 609
Cdd:pfam02463 173 EALKKLIEETENLAELIIDLeelklqeLKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 610 TQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREEAAKDICATKVETEETHNYVGF--------EDIIDS 681
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKEsekekkkaEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 682 LQDNVADIKKQAEIAHLYIASLPDPQEATACLELKFNQIKAELAKTKGELIKTKEELKKRENESDSLIQELETSNKKII- 760
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLe 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 761 ---TQNQRIKELINIIDQKEDTINEFQNLKSHMENtfKCNDKADTSSLIINNKLICNETVEVPKDSKSKICSERKRVNEN 837
Cdd:pfam02463 413 larQLEDLLKEEKKEELEILEEEEESIELKQGKLT--EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 838 ELQQDEPPAKKGSIHVSSAITED-QKKSEEVRPNIAEIEDIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQ 916
Cdd:pfam02463 491 SRQKLEERSQKESKARSGLKVLLaLIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 917 QELSLSEKKNLTLSKEVQQIqsnyDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRTLD 996
Cdd:pfam02463 571 TELPLGARKLRLLIPKLKLP----LKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 997 SVSQISNIDLLNLRDLSNGSEEDNLPNTQLDllgndylvskqvkeyrIQEPNRENSFHSSIEAIWEECKEIVKASSKKSH 1076
Cdd:pfam02463 647 GLRKGVSLEEGLAEKSEVKASLSELTKELLE----------------IQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1077 QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGV 1156
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1157 TCY---KAKIKELETILETQKVECSHSAKLEQDILEKESI-ILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQL 1232
Cdd:pfam02463 791 EKEeklKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIkEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQ 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1233 TNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDE 1312
Cdd:pfam02463 871 ELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEK 950
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 546231677 1313 DKLLrIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERA 1363
Cdd:pfam02463 951 EENN-KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERL 1000
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1077-1536 |
2.93e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1077 QIEELEQQIEKLQAEVKGYKDENNRLKEkEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGV 1156
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1157 TCYKAKIKELETILETQKVEcshSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNL 1236
Cdd:COG1196 396 AELAAQLEELEEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1237 QDMKHLLQLKEEEEETNRQETEKLKE-----ELSASSARTQNLKADLQRKEEDYADL--KEKLTDAKKQIKQVQKEVSVM 1309
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEaeadyEGFLEGVKAALLLAGLRGLAGAVAVLigVEAAYEAALEAALAAALQNIV 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1310 RDEDKLLRIKINELEKKKNQCSQELDM-KQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIED---MRMTLEEQE 1385
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLdKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllGRTLVAARL 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1386 QTQVEQDQVLEAKLEEVERLATELEKWKEKcndLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEE 1465
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGEGGSAGGSL---TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEEREL 709
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546231677 1466 KMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLvAALEIQLKAL 1536
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL-ERLEREIEAL 779
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1041-1598 |
1.18e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 57.07 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1041 EYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDllkeKETL 1120
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDA----KRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1121 IQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKA----------------------KIKELETILETQKVECS 1178
Cdd:PTZ00121 1156 IARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAedarkaeaarkaeeerkaeearKAEDAKKAEAVKKAEEA 1235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1179 HSAKLEQDILEKE---SIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQL--TNNLQDMKHLLQLKEEEEETN 1253
Cdd:PTZ00121 1236 KKDAEEAKKAEEErnnEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1254 RQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKltDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQE 1333
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAE--AAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKA 1393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1334 LDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWK 1413
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1414 E-KCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEkmmlitqAKEAENIRNKEMKKYAEDRE 1492
Cdd:PTZ00121 1474 EaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE-------AKKAEEAKKADEAKKAEEKK 1546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1493 RFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQiMDIKPKRI 1572
Cdd:PTZ00121 1547 KADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEEL 1625
|
570 580
....*....|....*....|....*.
gi 546231677 1573 SSADPDKLQTEPLSTSFEISRNKIED 1598
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEE 1651
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
848-1166 |
2.42e-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: 56.22 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 848 KGSIHVSSAITEDQKKSEEVRPNIAEIE-DIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKN 926
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEeKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 927 LTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRtldsvsqiSNIDL 1006
Cdd:TIGR02168 743 EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR--------AELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1007 LNLRDLSNGSEEDNLPNTQLDLLGNDYLVSKQVKEYR--IQEPNRE-NSFHSSIEAIWEECKEIVKASSKKSHQIEELEQ 1083
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSedIESLAAEiEELEELIEELESELEALLNERASLEEALALLRS 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1084 QIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETL------IQQLKEELQEK-NVTLDVQIQHVVEGKRALSELTQGV 1156
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLeglevrIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRL 974
|
330
....*....|
gi 546231677 1157 TCYKAKIKEL 1166
Cdd:TIGR02168 975 KRLENKIKEL 984
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
923-1362 |
3.32e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 923 EKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELRTLDSVSQIs 1002
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1003 nidllnLRDLSNGSEEDNLPNTQLDLLGNDYlvsKQVKEYRIQEPNRENSFHSSIEAIWEECKEIvkaSSKKSHQIEELE 1082
Cdd:COG4717 131 ------YQELEALEAELAELPERLEELEERL---EELRELEEELEELEAELAELQEELEELLEQL---SLATEEELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1083 QQIEKLQAEVKGYKDENNRLK-EKEHKNQDDLLKEKETLIQQLKEELQEKNVTL------------DVQIQHVVEGKRAL 1149
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQeELEELEEELEQLENELEAAALEERLKEARLLLliaaallallglGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1150 SELTQGVTCYKAKIKELETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQE-----HLQDSVKNTKDLNVKELK 1224
Cdd:COG4717 279 LFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSpeellELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1225 LKEEItQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEE---------DYADLKEKLTDA 1295
Cdd:COG4717 359 LEEEL-QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGeleellealDEEELEEELEEL 437
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546231677 1296 KKQIKQVQKEVSVMRDEDKLLRIKINELEKkknqcSQELDMKQRTIQQLKEQLNN------------QKVEEAIQQYER 1362
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRElaeewaalklalELLEEAREEYRE 511
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1077-1551 |
4.09e-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: 55.36 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1077 QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDllKEKETLIQQLKEELQEKNVTLDVQIQHVvEGKRALSELTQGV 1156
Cdd:TIGR00618 450 TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE--TRKKAVVLARLLELQEEPCPLCGSCIHP-NPARQDIDNPGPL 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1157 TCykakikELETILETQKvecshsaKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNL 1236
Cdd:TIGR00618 527 TR------RMQRGEQTYA-------QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNIT 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1237 QDMKHLLQLKEEEEETNRQETEKLKEELsassartqNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLL 1316
Cdd:TIGR00618 594 VRLQDLTEKLSEAEDMLACEQHALLRKL--------QPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL 665
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1317 RIKINELEKkknqcSQELDMKQRTIQQLKEQLNNQKveEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLE 1396
Cdd:TIGR00618 666 SIRVLPKEL-----LASRQLALQKMQSEKEQLTYWK--EMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAARE 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1397 AKLEEVERLATELEKWKEKCNDLEtknNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEA 1476
Cdd:TIGR00618 739 DALNQSLKELMHQARTVLKARTEA---HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSD 815
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 546231677 1477 ENIRNKEMKKYAEDRERFfkqQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKalISSNVQKDNEIEQLK 1551
Cdd:TIGR00618 816 EDILNLQCETLVQEEEQF---LSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK--IIQLSDKLNGINQIK 885
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1286-1570 |
4.67e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 55.07 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1286 ADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRtIQQLKEQLNNQKVEEAIQQYERACK 1365
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE-KREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1366 DLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLAT-ELEKWKEKCNDLETKNNQRSNKEHENNTDvlgkltnl 1444
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKERE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1445 QDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRErffkqqnEMEILTAQLTEKDSDLQKWREERDQ 1524
Cdd:TIGR02169 317 LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE-------ELEDLRAELEEVDKEFAETRDELKD 389
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 546231677 1525 LVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPK 1570
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
927-1530 |
4.69e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 927 LTLSKEVQQIQSNYdiAIAELHVQKSKNQEQEEKIMKLSNEIETATRsitnnvsQIKLMHTKIDELRTldsvsqisniDL 1006
Cdd:COG1196 216 RELKEELKELEAEL--LLLKLRELEAELEELEAELEELEAELEELEA-------ELAELEAELEELRL----------EL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1007 LNLRDLSNgseednlpntqldllgndylvSKQVKEYRIQepnrensfhSSIEAIWEECKEIVKASSKKSHQIEELEQQIE 1086
Cdd:COG1196 277 EELELELE---------------------EAQAEEYELL---------AELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1087 KLQAEVKGYKDENNRLKEkEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKEL 1166
Cdd:COG1196 327 ELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1167 ETILETQKVEcshSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLK 1246
Cdd:COG1196 406 EEAEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1247 EEEEETNRQETEKLKE-----ELSASSARTQNLKADLQRKEEDYADL--KEKLTDAKKQIKQVQKEVSVMRDEDKLLRIK 1319
Cdd:COG1196 483 LEELAEAAARLLLLLEaeadyEGFLEGVKAALLLAGLRGLAGAVAVLigVEAAYEAALEAALAAALQNIVVEDDEVAAAA 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1320 INELEKKKNQCSQELDM-KQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIED---MRMTLEEQEQTQVEQDQVL 1395
Cdd:COG1196 563 IEYLKAAKAGRATFLPLdKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllGRTLVAARLEAALRRAVTL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1396 EAKLEEVERLATELEKWKEKcndLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKE 1475
Cdd:COG1196 643 AGRLREVTLEGEGGSAGGSL---TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEE 719
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 546231677 1476 AENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDS---DLQKWREERDQLVAALE 1530
Cdd:COG1196 720 ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPeppDLEELERELERLEREIE 777
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1259-1461 |
7.40e-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: 53.61 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1259 KLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQ 1338
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1339 RTIQQLKEQ------LNNQKVEEAIQQYERACKDLNVKEKIIEDMRMT---LEEQEQTQVEQDQVLEAKLEEVERLATEL 1409
Cdd:COG4942 111 RALYRLGRQpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADlaeLAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 546231677 1410 EKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKK 1461
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1274-1578 |
8.29e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1274 LKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKV 1353
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL--SSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1354 EEAIQQYERACKDLnvkEKIIEDMRMTLEEqeqtqveqdqvLEAKLEEVERLATElEKWKEKCNDLETKNNQRSNKEhen 1433
Cdd:TIGR02169 750 EQEIENVKSELKEL---EARIEELEEDLHK-----------LEEALNDLEARLSH-SRIPEIQAELSKLEEEVSRIE--- 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1434 ntdvlGKLTNLQDELQESEQK--YNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKqqnEMEILTAQLTEK 1511
Cdd:TIGR02169 812 -----ARLREIEQKLNRLTLEkeYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE---ELEAALRDLESR 883
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 546231677 1512 DSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPKRISSADPD 1578
Cdd:TIGR02169 884 LGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEE 950
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1077-1299 |
1.01e-06 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.48 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1077 QIEELEQQIEKLQAEVKGYKDENNRLKEK------EHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEgkrALS 1150
Cdd:PHA02562 182 QIQTLDMKIDHIQQQIKTYNKNIEEQRKKngeniaRKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSA---ALN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1151 ELTQGVTCYKAKIKELETILE--TQKVECSHSAkleQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKElklkEE 1228
Cdd:PHA02562 259 KLNTAAAKIKSKIEQFQKVIKmyEKGGVCPTCT---QQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIM----DE 331
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546231677 1229 ITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQI 1299
Cdd:PHA02562 332 FNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
862-1409 |
1.04e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 862 KKSEEVRPNIAEIEDIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLsKEVQQIQSNYD 941
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKEL-KELKEKAEEYI 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 942 IAIAELHVQKSKNQEQEEKIMKLSNEIETATRSI---TNNVSQIKLMHTKIDELRtldsvsqisnidllnlRDLSNGSEE 1018
Cdd:PRK03918 297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIkelEEKEERLEELKKKLKELE----------------KRLEELEER 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1019 DNLPNTQLDLLGNDYLVSKQVKEYRIQEPNREnsfhssIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQA---EVKGY 1095
Cdd:PRK03918 361 HELYEEAKAKKEELERLKKRLTGLTPEKLEKE------LEELEKAKEEIEEEISKITARIGELKKEIKELKKaieELKKA 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1096 K------------DENNRLKEKEHKNQDDLLKEKETLIQQLKEELQEKnvtldVQIQHVVEGKRALSELTQGVTcykaKI 1163
Cdd:PRK03918 435 KgkcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKERKLRKEL-----RELEKVLKKESELIKLKELAE----QL 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1164 KELETILETQKVECSHSAKLEQDILEKESIILKLErnlkefQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLL 1243
Cdd:PRK03918 506 KELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGE------IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKEL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1244 QLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINE- 1322
Cdd:PRK03918 580 EELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEe 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1323 ----LEKKKNQCSQELDMKQRTIQQLKEQL-----NNQKVEEAIQQYERACKDLNVKEKIIEDMRmtlEEQEQTQVEQDQ 1393
Cdd:PRK03918 660 eyeeLREEYLELSRELAGLRAELEELEKRReeikkTLEKLKEELEEREKAKKELEKLEKALERVE---ELREKVKKYKAL 736
|
570
....*....|....*.
gi 546231677 1394 VLEAKLEEVERLATEL 1409
Cdd:PRK03918 737 LKERALSKVGEIASEI 752
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
707-1372 |
1.19e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 53.69 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 707 QEATACLELKFNQIKAEL----AKTKGELIKTKEELKKRENESDSLiqeletSNKKIITQNQRIKELINIIDQKEDTINE 782
Cdd:pfam12128 282 QETSAELNQLLRTLDDQWkekrDELNGELSAADAAVAKDRSELEAL------EDQHGAFLDADIETAAADQEQLPSWQSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 783 FQNL-KSHMENTFKCND-KADTSSLIINNKLICNETVEVPKDSKSKICSERKR---VNENELQQDEPPAKkgsihvssai 857
Cdd:pfam12128 356 LENLeERLKALTGKHQDvTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREARDRqlaVAEDDLQALESELR---------- 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 858 tedqkksEEVRPNIAEIEDIRVLQENNEGLRAFLLTIENELKNEKEEKAELNKQIVHFQQELSLSEKKNLTLSKEVQQIQ 937
Cdd:pfam12128 426 -------EQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 938 SNYDIA-----IAELHVQKSKNQEQEEKIMkLSNEIETATRSITNNVSQIKlmhtkiDELRTLDSVSQISNIDLLNLRDL 1012
Cdd:pfam12128 499 KRRDQAsealrQASRRLEERQSALDELELQ-LFPQAGTLLHFLRKEAPDWE------QSIGKVISPELLHRTDLDPEVWD 571
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1013 SNGSEEDNLPNTQLDLLG---NDYLVSKQVKEYRIqepnreNSFHSSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQ 1089
Cdd:pfam12128 572 GSVGGELNLYGVKLDLKRidvPEWAASEEELRERL------DKAEEALQSAREKQAAAEEQLVQANGELEKASREETFAR 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1090 AEVKGYKDENNRLKEKEHKNQDDLLKEKETLIQQLKEELQeknvTLDVQIQHVVEGKRALSELTQGvTCYKAKIKELETI 1169
Cdd:pfam12128 646 TALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLN----SLEAQLKQLDKKHQAWLEEQKE-QKREARTEKQAYW 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1170 LEtqkVECSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNL----QDMKHLLQL 1245
Cdd:pfam12128 721 QV---VEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIeriaVRRQEVLRY 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1246 KEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEdyadlkekltDAKKQIKQVQKEvsvmRDEDKLLRIKINELEK 1325
Cdd:pfam12128 798 FDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIA----------DTKLRRAKLEME----RKASEKQQVRLSENLR 863
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 546231677 1326 KknqcsqeLDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEK 1372
Cdd:pfam12128 864 G-------LRCEMSKLATLKEDANSEQAQGSIGERLAQLEDLKLKRD 903
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1062-1568 |
1.43e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.51 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1062 EECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEK--EHKNQ--------DDLLKEKE------TLIQQLK 1125
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEvrDLRERleeleeerDDLLAEAGlddadaEAVEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1126 EELQEKnvtlDVQIQHVVEGKR-ALSELTQGVTCYKAKIKELETILETQKVEcshSAKLEQDILEKESIILKLERNLKEF 1204
Cdd:PRK02224 317 EELEDR----DEELRDRLEECRvAAQAHNEEAESLREDADDLEERAEELREE---AAELESELEEAREAVEDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1205 QEHLQDsvkntkdlnvkelkLKEEITQLTNNLQDMKHLLQLkeeeeetnrqetekLKEELSASSARTQNLKADLQRKEED 1284
Cdd:PRK02224 390 EEEIEE--------------LRERFGDAPVDLGNAEDFLEE--------------LREERDELREREAELEATLRTARER 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1285 YADlKEKLTDAKK---------------QIKQVQKEVSVMRDEDKLLRIKINELEKKKNQcSQELDMKQRTIQQLKEQLN 1349
Cdd:PRK02224 442 VEE-AEALLEAGKcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLER-AEDLVEAEDRIERLEERRE 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1350 NqkVEEAIQQyerackdlnvKEKIIEDMRMTLEEQEQTQVEqdqvLEAKLEEVERLATELEKWKEKCNDlETKNNQRSNK 1429
Cdd:PRK02224 520 D--LEELIAE----------RRETIEEKRERAEELRERAAE----LEAEAEEKREAAAEAEEEAEEARE-EVAELNSKLA 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1430 EHENNTDVLGKLTNLQDELQESEQKYNADRKKwLEEKMMLITQAKEAENIRNKEMKKYAE--DRERFFKQQNEMEILTAQ 1507
Cdd:PRK02224 583 ELKERIESLERIRTLLAAIADAEDEIERLREK-REALAELNDERRERLAEKRERKRELEAefDEARIEEAREDKERAEEY 661
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 546231677 1508 LTEKDSDLQKWREERDQLVAAL-----EIQ-LKALISSNVQKDNEIEQLKRIISETSKIETQIMDIK 1568
Cdd:PRK02224 662 LEQVEEKLDELREERDDLQAEIgavenELEeLEELRERREALENRVEALEALYDEAEELESMYGDLR 728
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1264-1493 |
1.51e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1264 LSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQ 1343
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1344 LKEQLNNQKveEAIQQYERACKDLNVKEKI-----------IEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKW 1412
Cdd:COG4942 95 LRAELEAQK--EELAELLRALYRLGRQPPLalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1413 KEKCNDLETKNNQRSNkehenntdvlgKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRE 1492
Cdd:COG4942 173 RAELEALLAELEEERA-----------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
.
gi 546231677 1493 R 1493
Cdd:COG4942 242 R 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1037-1551 |
2.37e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.84 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1037 KQVKEYRIQEPNRENSFHSSIEAIWEECKEIVKASSKKShQIEELEQQIEKLQ--AEVKGYKDENNRLKEKEHKNQDDLL 1114
Cdd:PTZ00121 1284 KKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKK-KAEEAKKKADAAKkkAEEAKKAAEAAKAEAEAAADEAEAA 1362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1115 KEKETLIQQLKEELQEKNVTLDVQiqhvVEGKRALSELTQGVTCYKAKIKELETILETQKVECSHSAKLEQ----DILEK 1190
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKK----AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEkkkaDEAKK 1438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1191 ESIILKLERNLKEFQEHLQDSVKNTKDLNVK----ELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSA 1266
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkadEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKA 1518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1267 SSARtqnlKADLQRKEEDYADLKE-KLTDAKKQIKQVQKEVSVMRDEDKllrikiNELEKKKNQcSQELDMKQRTIQQLK 1345
Cdd:PTZ00121 1519 EEAK----KADEAKKAEEAKKADEaKKAEEKKKADELKKAEELKKAEEK------KKAEEAKKA-EEDKNMALRKAEEAK 1587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1346 eQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQV--LEAKLEEVERLATELEKWKEkcnDLETKN 1423
Cdd:PTZ00121 1588 -KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVeqLKKKEAEEKKKAEELKKAEE---ENKIKA 1663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1424 NQRSNKEHENNTdvlgKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERF----FKQQN 1499
Cdd:PTZ00121 1664 AEEAKKAEEDKK----KAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIkaeeAKKEA 1739
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 546231677 1500 EMEILTAQLTEKDSD----LQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLK 1551
Cdd:PTZ00121 1740 EEDKKKAEEAKKDEEekkkIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1078-1568 |
4.47e-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: 51.75 E-value: 4.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1078 IEELEQQIEKLQAE-VKGYKDENNRLKEKE-HKNQDDLLKEKetlIQQLKEELQEKNV----------TLDVQI----QH 1141
Cdd:pfam10174 249 IRDLEDEVQMLKTNgLLHTEDREEEIKQMEvYKSHSKFMKNK---IDQLKQELSKKESellalqtkleTLTNQNsdckQH 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1142 VVEGKRALSELTQGVTCYKAKIKELETILEtqkvecshsakleqdilEKESIilklernLKEFQEHLQDsvkntkdlnvk 1221
Cdd:pfam10174 326 IEVLKESLTAKEQRAAILQTEVDALRLRLE-----------------EKESF-------LNKKTKQLQD----------- 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1222 elkLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEED-------YADLKEKLTD 1294
Cdd:pfam10174 371 ---LTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtaLTTLEEALSE 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1295 AKKQIKQVQKEVS----VMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQ------------KVEEAIQ 1358
Cdd:pfam10174 448 KERIIERLKEQREredrERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLassglkkdsklkSLEIAVE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1359 QYERACKDLNVKEKIIEDMRMTlEEQEQTQVEQDQVLEA----KLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENN 1434
Cdd:pfam10174 528 QKKEECSKLENQLKKAHNAEEA-VRTNPEINDRIRLLEQevarYKEESGKAQAEVERLLGILREVENEKNDKDKKIAELE 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1435 TDVLGKLTNLQDELQESEQKYNADRKKWLEEkmMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLT----- 1509
Cdd:pfam10174 607 SLTLRQMKEQNKKVANIKHGQQEMKKKGAQL--LEEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSstqqs 684
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 546231677 1510 --EKDSDLQKWR-EERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIK 1568
Cdd:pfam10174 685 laEKDGHLTNLRaERRKQLEEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALK 746
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1113-1609 |
4.51e-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: 51.75 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1113 LLKEKETLIQQLKEELQEKNVTLD-----VQIQHVVEGKRA-LSELTQGvtcykakIKELETILETQKvecsHSAKLEQD 1186
Cdd:pfam10174 200 LLDQKEKENIHLREELHRRNQLQPdpaktKALQTVIEMKDTkISSLERN-------IRDLEDEVQMLK----TNGLLHTE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1187 ILEKESIILKLERNLKEFQEHLQDSVKntKDLNVKE---LKLKEEITQLTNNLQDMKHLLQLkeeeeetnrqetekLKEE 1263
Cdd:pfam10174 269 DREEEIKQMEVYKSHSKFMKNKIDQLK--QELSKKEselLALQTKLETLTNQNSDCKQHIEV--------------LKES 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1264 LSASSARTQNLKAD-------LQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDM 1336
Cdd:pfam10174 333 LTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRD 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1337 KQRTIQQLKE-----QLNNQKVEEAIQQYERACKDlnvKEKIIEDMRMTLEEQEqtqveqdqvlEAKLEEVERLATELEK 1411
Cdd:pfam10174 413 KDKQLAGLKErvkslQTDSSNTDTALTTLEEALSE---KERIIERLKEQRERED----------RERLEELESLKKENKD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1412 WKEKCNDLETKNNQRSN-----KEHENNTDVLG-----KLTNLQDELQESEQ---KYNADRKKWLEEKMMLITQAKEAEN 1478
Cdd:pfam10174 480 LKEKVSALQPELTEKESslidlKEHASSLASSGlkkdsKLKSLEIAVEQKKEecsKLENQLKKAHNAEEAVRTNPEINDR 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1479 IRN--KEMKKYAEDRErffKQQNEMEILTAQLTEKDSDlqkwREERDQLVAALEIQLKALISSNVQKdneIEQLKRIISE 1556
Cdd:pfam10174 560 IRLleQEVARYKEESG---KAQAEVERLLGILREVENE----KNDKDKKIAELESLTLRQMKEQNKK---VANIKHGQQE 629
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 546231677 1557 TSKIETQIMD--IKPKRISSADPDKLQTEPLSTSFEISRNKIEDGSVVLDSCEVS 1609
Cdd:pfam10174 630 MKKKGAQLLEeaRRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQS 684
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1159-1488 |
5.28e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.60 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1159 YKAKIKELETILETQKVECSHS--AKLEQDILEKESIILKLERNLKEFQEHLQDsvkntkdLNVKELKLKEEITQLTNNL 1236
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREelEELQEELKEAEEELEELTAELQELEEKLEE-------LRLEVSELEEEIEELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1237 QDMKHLLQlkeeeeetnrqeteKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKevsvmrdedkll 1316
Cdd:TIGR02168 291 YALANEIS--------------RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEE------------ 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1317 riKINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKEKIIEdmrmtleeqeqtqveqdqvle 1396
Cdd:TIGR02168 345 --KLEELKEELESLEAELEELEAELEELESRL--EELEEQLETLRSKVAQLELQIASLN--------------------- 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1397 aklEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEA 1476
Cdd:TIGR02168 400 ---NEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330
....*....|..
gi 546231677 1477 ENIRNKEMKKYA 1488
Cdd:TIGR02168 477 LDAAERELAQLQ 488
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1070-1326 |
7.80e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 50.15 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1070 ASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLlKEKETLIQQLKEELQEKNVTLDVQiqhvvegKRAL 1149
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQL-AALERRIAALARRIRALEQELAAL-------EAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1150 SELTQgvtcykaKIKELETILETQKVECSHSAKLEQDILEKESIILKLErnlkefQEHLQDSVKNTKDLNVKELKLKEEI 1229
Cdd:COG4942 86 AELEK-------EIAELRAELEAQKEELAELLRALYRLGRQPPLALLLS------PEDFLDAVRRLQYLKYLAPARREQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1230 TQLTNNLQDMKhllqlkeeeeetnrqeteKLKEELSASSARTQNLKADLQRKEEDYADLKEK----LTDAKKQIKQVQKE 1305
Cdd:COG4942 153 EELRADLAELA------------------ALRAELEAERAELEALLAELEEERAALEALKAErqklLARLEKELAELAAE 214
|
250 260
....*....|....*....|.
gi 546231677 1306 VSVMRDEDKLLRIKINELEKK 1326
Cdd:COG4942 215 LAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1259-1510 |
8.89e-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: 50.84 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1259 KLKEELSASSARTQNLKADL------QRKEEDYAD-LKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCS 1331
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELsslqseLRRIENRLDeLSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1332 QELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKE-----KIIEDMRMTLEEQEQTQVEQDQVLEAKLEEV---- 1402
Cdd:TIGR02169 751 QEIENVKSELKELEARI--EELEEDLHKLEEALNDLEARLshsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLtlek 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1403 ERLATELEKWKEKCNDLETKNNQRSNKEHENNTDvLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNK 1482
Cdd:TIGR02169 829 EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK-KEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEE 907
|
250 260
....*....|....*....|....*...
gi 546231677 1483 EMKKYAEDRERFFKQQNEMEILTAQLTE 1510
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSE 935
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1072-1561 |
1.84e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1072 SKKSHQIEELEQQIEklqaevkgykdennrlkEKEHKNQDDLLKEKETLIQQLKEELQEKNVtldvQIQHVVEGKRALSE 1151
Cdd:PRK02224 183 SDQRGSLDQLKAQIE-----------------EKEEKDLHERLNGLESELAELDEEIERYEE----QREQARETRDEADE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1152 LtqgVTCYKAKIKELETiletqkvecshsakLEQDILEKESIILKLERNLKEFQEHLQDsvkntkdlnvkelkLKEEITQ 1231
Cdd:PRK02224 242 V---LEEHEERREELET--------------LEAEIEDLRETIAETEREREELAEEVRD--------------LRERLEE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1232 LTNNLQDMKHLLQLKEEeeetnrqeteklkeELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRD 1311
Cdd:PRK02224 291 LEEERDDLLAEAGLDDA--------------DAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1312 EDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLnnqkvEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEq 1391
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEI-----EELRERFGDAPVDLGNAEDFLEELREERDELREREAE- 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1392 dqvLEAKLEEVERLATELEKWKE--KC----NDLETKNNQRSNKEHEnntdvlGKLTNLQDELQESEQKyNADRKKWLEE 1465
Cdd:PRK02224 431 ---LEATLRTARERVEEAEALLEagKCpecgQPVEGSPHVETIEEDR------ERVEELEAELEDLEEE-VEEVEERLER 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1466 KMMLITQAKEAENIRNKE---MKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREE----RDQLVAALEiQLKALIS 1538
Cdd:PRK02224 501 AEDLVEAEDRIERLEERRedlEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAaaeaEEEAEEARE-EVAELNS 579
|
490 500
....*....|....*....|...
gi 546231677 1539 SNVQKDNEIEQLKRIISETSKIE 1561
Cdd:PRK02224 580 KLAELKERIESLERIRTLLAAIA 602
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1065-1534 |
2.07e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1065 KEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENN---RLKEKEHKNQDDL------LKEKETLIQQLKEELQEKNVTL 1135
Cdd:pfam01576 26 SELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEmraRLAARKQELEEILhelesrLEEEEERSQQLQNEKKKMQQHI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1136 DVQIQHVVEGKRALSELTQGVTCYKAKIKELET---ILETQKVECSHSAKLeqdilekesiilkLERNLKEFQEHLQDSV 1212
Cdd:pfam01576 106 QDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEdilLLEDQNSKLSKERKL-------------LEERISEFTSNLAEEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1213 KNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKL 1292
Cdd:pfam01576 173 EKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1293 TD-------AKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELdmkqrtiQQLKEQLNNQKVEEAIQQYERAck 1365
Cdd:pfam01576 253 EEetaqknnALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL-------EALKTELEDTLDTTAAQQELRS-- 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1366 dlnVKEKIIEDMRMTLEEQEQTQVEQDQVLEAK-LEEVERLATELEKWKEKCNDLEtKNNQRSNKEhenNTDVLGKLTNL 1444
Cdd:pfam01576 324 ---KREQEVTELKKALEEETRSHEAQLQEMRQKhTQALEELTEQLEQAKRNKANLE-KAKQALESE---NAELQAELRTL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1445 QDELQESEQKynadRKKWLEEKMMLITQAKEAENIRNkemkkyaEDRERFFKQQNEMEILTAQLTEKDSDLQKWREErdq 1524
Cdd:pfam01576 397 QQAKQDSEHK----RKKLEGQLQELQARLSESERQRA-------ELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD--- 462
|
490
....*....|
gi 546231677 1525 lVAALEIQLK 1534
Cdd:pfam01576 463 -VSSLESQLQ 471
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1259-1381 |
2.98e-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: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1259 KLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQV--QKEVSVMRDEDKLLRIKINELEKKKNQCSQELDM 1336
Cdd:COG1579 42 ALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKEYEALQKEIESLKRRISDLEDEILELMERIEE 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 546231677 1337 KQRTIQQLKEQLNNQK--VEEAIQQYERACKDLNVKEKIIEDMRMTL 1381
Cdd:COG1579 122 LEEELAELEAELAELEaeLEEKKAELDEELAELEAELEELEAEREEL 168
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1395-1583 |
3.87e-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: 48.90 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1395 LEAKLEEVERLATELEKWKEKCNDLETKNNQRSnkehenntdvlGKLTNLQDELQESEQKYNADRKKWLE--------EK 1466
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELE-----------EKLEELRLEVSELEEEIEELQKELYAlaneisrlEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1467 MMLITQAKEAENIRNKEMkkYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISSNVQKDNE 1546
Cdd:TIGR02168 303 QKQILRERLANLERQLEE--LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190
....*....|....*....|....*....|....*..
gi 546231677 1547 IEQLKRIISETSKIETQIMdikpKRISSADPDKLQTE 1583
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLN----NEIERLEARLERLE 413
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
924-1571 |
4.13e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 4.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 924 KKNLTLSKEVQQIQSNYDI---AIAELHVQKSKNQEQEEKIMKLSNEIETATRSITNNVSQIKLMHTKIDELrtlDSVSQ 1000
Cdd:PRK01156 152 KKILDEILEINSLERNYDKlkdVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERL---SIEYN 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1001 ISNIDLLNLRdlsngsEEDNLPNTQLDLLgNDYLVSKQVKEYRIQEPNRENSFHSSIEaiwEECKEIVKASSKKSH---- 1076
Cdd:PRK01156 229 NAMDDYNNLK------SALNELSSLEDMK-NRYESEIKTAESDLSMELEKNNYYKELE---ERHMKIINDPVYKNRnyin 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1077 -------QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKEtliqqlKEELqeknvtldvqiqhvvegKRAL 1149
Cdd:PRK01156 299 dyfkyknDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSR------YDDL-----------------NNQI 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1150 SELTQGVTCYKAKIKELETI---LETQKVECSHSAKLEQDILEKESI---ILKLERNlkEFQEHLQDSVKNTKDLNVKEL 1223
Cdd:PRK01156 356 LELEGYEMDYNSYLKSIESLkkkIEEYSKNIERMSAFISEILKIQEIdpdAIKKELN--EINVKLQDISSKVSSLNQRIR 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1224 KLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARtqnLKADLQRKEEDYADLKEKLTDAKKQIKQVQ 1303
Cdd:PRK01156 434 ALRENLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSR---LEEKIREIEIEVKDIDEKIVDLKKRKEYLE 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1304 -KEVSVMRDEDKLLRIKINELEKKKNQCSqELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIiedmrmtle 1382
Cdd:PRK01156 511 sEEINKSINEYNKIESARADLEDIKIKIN-ELKDKHDKYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLI--------- 580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1383 eqeqtqveqdqvleakleEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNAdrkkw 1462
Cdd:PRK01156 581 ------------------DIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNE----- 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1463 LEEKMMLITQAKEaeniRNKEMKKYAEDRERFFKQQNEmeiLTAQLTEKDSDLQKWREERDQLVAALEiQLKALISSNVQ 1542
Cdd:PRK01156 638 IQENKILIEKLRG----KIDNYKKQIAEIDSIIPDLKE---ITSRINDIEDNLKKSRKALDDAKANRA-RLESTIEILRT 709
|
650 660 670
....*....|....*....|....*....|...
gi 546231677 1543 KDNEIEQ----LKRIISETSKIETQIMDIKPKR 1571
Cdd:PRK01156 710 RINELSDrindINETLESMKKIKKAIGDLKRLR 742
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1227-1411 |
4.33e-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: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1227 EEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEV 1306
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1307 SVMRDEdklLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN-----NQKVEEAIQQYERACKDLNVKEKIIEDMRMTL 1381
Cdd:COG4942 100 EAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|
gi 546231677 1382 EEQEQTQVEQDQVLEAKLEEVERLATELEK 1411
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEK 206
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1077-1308 |
4.35e-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: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1077 QIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLlKEKETLIQQLKEELQEKNVTLDVQIQHVveGKRALSELTQGV 1156
Cdd:COG3883 24 ELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-EALQAEIDKLQAEIAEAEAEIEERREEL--GERARALYRSGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1157 TcykakIKELETILETQKVecshsakleQDILEKESIILKL-ERNLKEFQEHLQDsvknTKDLNVKELKLKEEITQLTNN 1235
Cdd:COG3883 101 S-----VSYLDVLLGSESF---------SDFLDRLSALSKIaDADADLLEELKAD----KAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546231677 1236 LQDMKhllqlkeeeeetnrqeteKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSV 1308
Cdd:COG3883 163 KAELE------------------AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1147-1596 |
4.78e-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: 48.58 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1147 RALSELTQGVTCYKAKIKELETILETQKVECS---------HSAKLEQDILEKESIILKLER----------NLKEFQEH 1207
Cdd:pfam15921 224 KILRELDTEISYLKGRIFPVEDQLEALKSESQnkielllqqHQDRIEQLISEHEVEITGLTEkassarsqanSIQSQLEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1208 LQDSVKNTKDLNVKEL-KLKEEITQLTNNLQDMKHLLQLKEEeeetnrqeteKLKEELSASSARTQNLKADLQRKEEDYA 1286
Cdd:pfam15921 304 IQEQARNQNSMYMRQLsDLESTVSQLRSELREAKRMYEDKIE----------ELEKQLVLANSELTEARTERDQFSQESG 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1287 DLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKvEEAIQQYERACKD 1366
Cdd:pfam15921 374 NLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMK-SECQGQMERQMAA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1367 LNVKEKiiedmrmtleeqeqtqveqdqvleaKLEEVERLATELEKWKEKCNDL-ETKNNQRSNKEHENNTdvlgkLTNLQ 1445
Cdd:pfam15921 453 IQGKNE-------------------------SLEKVSSLTAQLESTKEMLRKVvEELTAKKMTLESSERT-----VSDLT 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1446 DELQESEQKYNADRKKwleekmmlITQAKEAENIRNKEMKKYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERD-- 1523
Cdd:pfam15921 503 ASLQEKERAIEATNAE--------ITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIEnm 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1524 -QLV--------------AALE-------IQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPKRISSADPDKLQ 1581
Cdd:pfam15921 575 tQLVgqhgrtagamqvekAQLEkeindrrLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQE 654
|
490
....*....|....*
gi 546231677 1582 TEPLSTSFEISRNKI 1596
Cdd:pfam15921 655 RDQLLNEVKTSRNEL 669
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1065-1549 |
1.27e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 47.02 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1065 KEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKETLiQQLKEELQEKNVTLDvqiqhvve 1144
Cdd:pfam05483 324 KTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQL-KIITMELQKKSSELE-------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1145 gkralsELTQGVTCYKAKIKELETILETQKvecshsaKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELK 1224
Cdd:pfam05483 395 ------EMTKFKNNKEVELEELKKILAEDE-------KLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTA 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1225 LKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQK 1304
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1305 EVSVMRDEDKLLRikiNELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNV----KEKIIEDMRMT 1380
Cdd:pfam05483 542 KEMNLRDELESVR---EEFIQKGDEVKCKLDKSEENARSIEYEV--LKKEKQMKILENKCNNLKKqienKNKNIEELHQE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1381 LEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLeTKNNQRSNKEHENNTDvlgkltNLQDELQESeqKYNADRK 1460
Cdd:pfam05483 617 NKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEI-IDNYQKEIEDKKISEE------KLLEEVEKA--KAIADEA 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1461 KWLEEKMMLITQAKEAENIRNKEMKKYAEDRerffkqqnemeiltaQLTEKDSDLQKWR---EERDQLVAALEIQLKALI 1537
Cdd:pfam05483 688 VKLQKEIDKRCQHKIAEMVALMEKHKHQYDK---------------IIEERDSELGLYKnkeQEQSSAKAALEIELSNIK 752
|
490
....*....|....
gi 546231677 1538 SS--NVQKDNEIEQ 1549
Cdd:pfam05483 753 AEllSLKKQLEIEK 766
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1395-1568 |
1.48e-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: 1.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1395 LEAKLEEVERlatELEKWKEKCNDLETknNQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKwLEEKMMLITQAK 1474
Cdd:COG3206 187 LRKELEEAEA---ALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ-LGSGPDALPELL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1475 EAENIRNKemkkyaedRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQL-----------VAALEIQLKALISSNVQK 1543
Cdd:COG3206 261 QSPVIQQL--------RAQLAELEAELAELSARYTPNHPDVIALRAQIAALraqlqqeaqriLASLEAELEALQAREASL 332
|
170 180
....*....|....*....|....*
gi 546231677 1544 DNEIEQLKRIISETSKIETQIMDIK 1568
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELRRLE 357
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1059-1363 |
2.18e-04 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 46.48 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1059 AIWEECKEIVKASSKKSHQIEELEQQIEKLQaeVKGYKDENnRLKEKEHKNQDDLLKeKETLIQQLKE------------ 1126
Cdd:pfam15818 75 ALEEEKGKYQLATEIKEKEIEGLKETLKALQ--VSKYSLQK-KVSEMEQKLQLHLLA-KEDHHKQLNEiekyyatitgqf 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1127 -ELQEKNVTLDVQIQHVVEGKRALSELTQG----VTCYKAKIKELETILETQKVECSHSakleqdiLEKESIILKL-ERN 1200
Cdd:pfam15818 151 gLVKENHGKLEQNVQEAIQLNKRLSALNKKqeseICSLKKELKKVTSDLIKSKVTCQYK-------MGEENINLTIkEQK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1201 LKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQlkeeeeeTNRQETEKLKEELSASSARTQNLKAD--L 1278
Cdd:pfam15818 224 FQELQERLNMELELNKKINEEITHIQEEKQDIIISFQHMQQLLQ-------QQTQANTEMEAELKALKENNQTLERDneL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1279 QRK-----EEDYADLKEKLTDA----KKQIKQVQKEVSVMRDEDKLLRIKINELEKKKN-QCSQELDMKQRTIQQLKEqL 1348
Cdd:pfam15818 297 QREkvkenEEKFLNLQNEHEKAlgtwKKHVEELNGEINEIKNELSSLKETHIKLQEHYNkLCNQKKFEEDKKFQNVPE-V 375
|
330
....*....|....*
gi 546231677 1349 NNQKVEEAIQQYERA 1363
Cdd:pfam15818 376 NNENSEMSTEKSENL 390
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1278-1429 |
2.18e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1278 LQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKIN--ELEKKKNQCSQELDMKQRTIQQLKEQLNN----- 1350
Cdd:COG4717 83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEElrele 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1351 ---QKVEEAIQQYERACKDL-----NVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETK 1422
Cdd:COG4717 163 eelEELEAELAELQEELEELleqlsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
....*..
gi 546231677 1423 NNQRSNK 1429
Cdd:COG4717 243 ERLKEAR 249
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1224-1362 |
2.23e-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: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1224 KLKEEITQLTNNLQDMKHLLQlkeeeeeTNRQETEKLKEELsassARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQ 1303
Cdd:pfam13851 30 SLKEEIAELKKKEERNEKLMS-------EIQQENKRLTEPL----QKAQEEVEELRKQLENYEKDKQSLKNLKARLKVLE 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 546231677 1304 KEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQ---LKEQLNNQKVEEAIQQYER 1362
Cdd:pfam13851 99 KELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktgLKNLLLEKKLQALGETLEK 160
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1057-1455 |
2.43e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1057 IEAIWEECKEIVKASSKKS----HQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKnqddlLKEKETLIQQLKEELQEKN 1132
Cdd:COG4717 48 LERLEKEADELFKPQGRKPelnlKELKELEEELKEAEEKEEEYAELQEELEELEEE-----LEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1133 VTLDVQ--IQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVECSHSAKLEQDI--------LEKESIILKLERNLK 1202
Cdd:COG4717 123 KLLQLLplYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELeelleqlsLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1203 EFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEE------------------------------- 1251
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflv 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1252 -----TNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKL-----------TDAKKQIKQVQKEVSVMRDEDKL 1315
Cdd:COG4717 283 lgllaLLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdlspeelLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1316 LRIKINELEKK----KNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKII--EDMRMTLEEQEQTQV 1389
Cdd:COG4717 363 LQLEELEQEIAallaEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEELEELEEELE 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 546231677 1390 EQDQVLEAKLEEVERLATELEKWKEKCN------DLETKNNQRSNKEHENNTDVLGkLTNLQDELQESEQKY 1455
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLEEDGElaellqELEELKAELRELAEEWAALKLA-LELLEEAREEYREER 513
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
524-882 |
2.65e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 524 NSLEDLMEDEDLVEELENAEETQNVETKlldEDLDKTLEEnkafisHEEKRKLLDLIEdlkkKLINEKKEKLTLEFKIRE 603
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQREQARETR---DEADEVLEE------HEERREELETLE----AEIEDLRETIAETERERE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 604 evtqeftqywaqreaDFKETLLQEREILEENAERRlaifKDLVGKCDtREEAAKDICATKVETeethnyvgFEDIIDSLQ 683
Cdd:PRK02224 276 ---------------ELAEEVRDLRERLEELEEER----DDLLAEAG-LDDADAEAVEARREE--------LEDRDEELR 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 684 DNVADIKKQAEIAHLYIASLpdpQEATACLELKFNQIKAELAKTKGELIKTKEELKKRENESDSLIQELETSNKKIitqn 763
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESL---REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF---- 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 764 qrikeliniidqkEDTINEFQNLKSHMEntfkcndkadtssLIINNKlicNETVEVPKDSKSKICSERKRVNENELQQDE 843
Cdd:PRK02224 401 -------------GDAPVDLGNAEDFLE-------------ELREER---DELREREAELEATLRTARERVEEAEALLEA 451
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 546231677 844 PPAK------KGSIHVsSAITEDQKKSEEVRpniAEIEDIRVLQE 882
Cdd:PRK02224 452 GKCPecgqpvEGSPHV-ETIEEDRERVEELE---AELEDLEEEVE 492
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1164-1368 |
2.97e-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: 45.14 E-value: 2.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1164 KELETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLL 1243
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1244 QlKEEEEETNRQETEKLKEELSASSA-RTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEdklLRIKINE 1322
Cdd:COG4942 107 A-ELLRALYRLGRQPPLALLLSPEDFlDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE---LEALLAE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 546231677 1323 LEKKKNQCSQELDMKQRTIQQLKEQLNNQkvEEAIQQYERACKDLN 1368
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAEL--AAELAELQQEAEELE 226
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
955-1351 |
3.08e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 955 QEQEEKIMKLSNEIETATRSITNNVSQIklmhtkiDELRTLDSVSQISNIDLLNLRDLSNGSEE--DNLPNTQLDLLG-N 1031
Cdd:PRK11281 76 DRQKEETEQLKQQLAQAPAKLRQAQAEL-------EALKDDNDEETRETLSTLSLRQLESRLAQtlDQLQNAQNDLAEyN 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1032 DYLVSKQVKEYRIQEPNRENSFHS-SIEAI---WEECKEIVKASSKKSHQIEE--LEQQIEKLQAEVKGykdeNNRLKEK 1105
Cdd:PRK11281 149 SQLVSLQTQPERAQAALYANSQRLqQIRNLlkgGKVGGKALRPSQRVLLQAEQalLNAQNDLQRKSLEG----NTQLQDL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1106 EHKnQDDLLKEKetlIQQLKEELQEknvtldvqIQHVVEGKR-ALSELTqgvtcykakIKELETILETQKV--------E 1176
Cdd:PRK11281 225 LQK-QRDYLTAR---IQRLEHQLQL--------LQEAINSKRlTLSEKT---------VQEAQSQDEAARIqanplvaqE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1177 CSHSAKLEQDILEKEsiilklERNLKEFQEHLQdsVKNTKD-LNVKELKLKEEITQLTNNLQDMKHLLQLKeeeeetnrq 1255
Cdd:PRK11281 284 LEINLQLSQRLLKAT------EKLNTLTQQNLR--VKNWLDrLTQSERNIKEQISVLKGSLLLSRILYQQQ--------- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1256 eteklkeelsassartQNLKADlqrkeedyaDLKEKLTDAKKQIKQVQKEVSVMRDE--------DKLLRIKINELEKK- 1326
Cdd:PRK11281 347 ----------------QALPSA---------DLIEGLADRIADLRLEQFEINQQRDAlfqpdayiDKLEAGHKSEVTDEv 401
|
410 420
....*....|....*....|....*
gi 546231677 1327 KNQCSQELDMKQRTIQQLKEQLNNQ 1351
Cdd:PRK11281 402 RDALLQLLDERRELLDQLNKQLNNQ 426
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1501-1792 |
3.14e-04 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 45.81 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1501 MEILTAQLTEKDSDLQK---------WREERDQLVAALEiqlkaliSSNVQKDNEIEQLKRIISETSKIETQIMDIKPKR 1571
Cdd:PTZ00108 1104 VEKLNAELEKKEKELEKlknttpkdmWLEDLDKFEEALE-------EQEEVEEKEIAKEQRLKSKTKGKASKLRKPKLKK 1176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1572 ISSADPDKLQTEPLSTSFEISRNKIEDGSVVLDSCEVSTENDQSTRFPKPELEIQFTplqpnKMAVKHPGCTTPVTVKIP 1651
Cdd:PTZ00108 1177 KEKKKKKSSADKSKKASVVGNSKRVDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKT-----KPKKSSVKRLKSKKNNSS 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1652 KARKRKSNEMEEDLVKCENKKNATPRTNLKFPISDDRNSSVKKEQKVAIRPSS--KKTYSLRSQASIIGVNLATKKKEGT 1729
Cdd:PTZ00108 1252 KSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSptKKKVKKRLEGSLAALKKKKKSEKKT 1331
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546231677 1730 LQKfgdflqhspsilqskakkiietmSSSKLSNVEASKENVSQPKRAKRKLYTSEISSPIDIS 1792
Cdd:PTZ00108 1332 ARK-----------------------KKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDDDDS 1371
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1259-1411 |
4.68e-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: 4.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1259 KLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINEL---EKKKNQCSQELD 1335
Cdd:COG3883 27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaraLYRSGGSVSYLD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1336 M------------KQRTIQQLKEQLNnqkveEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVE 1403
Cdd:COG3883 107 VllgsesfsdfldRLSALSKIADADA-----DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181
|
....*...
gi 546231677 1404 RLATELEK 1411
Cdd:COG3883 182 ALLAQLSA 189
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1077-1308 |
5.12e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.01 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1077 QIEELEQQIEKLQAEVKGYKDENNRLK-EKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQ- 1154
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGLVDlSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQs 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1155 -GVTCYKAKIKELETILetqkvecshsAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELK-LKEEITQL 1232
Cdd:COG3206 263 pVIQQLRAQLAELEAEL----------AELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEaLQAREASL 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 546231677 1233 TNNLQDMKHLLQlkeeeeetnrqeteklkeELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSV 1308
Cdd:COG3206 333 QAQLAQLEARLA------------------ELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRV 390
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
65-190 |
6.33e-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: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 65 IRPFTQSEKELESEGCVHILDsqtvvlkepqcilGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQ--GCIMQPVkdlLK 142
Cdd:pfam16796 22 IRVFARVRPELLSEAQIDYPD-------------ETSSDGKIGSKNKSFSFDRVFPPESEQEDVFQeiSQLVQSC---LD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 546231677 143 GQSRLIFTYGLTNSGktytfqgteENIGILPRTLNVLFDSLQERLYTK 190
Cdd:pfam16796 86 GYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLKKGW 124
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1225-1360 |
6.70e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 44.19 E-value: 6.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1225 LKEEIT-------QLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSA---RTQNLKADLQRK----EEDYADLKE 1290
Cdd:PRK09039 44 LSREISgkdsaldRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAersRLQALLAELAGAgaaaEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546231677 1291 KLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN---NQKVEEaIQQY 1360
Cdd:PRK09039 124 ELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNvalAQRVQE-LNRY 195
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1205-1456 |
7.15e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 7.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1205 QEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEED 1284
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1285 YADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERAC 1364
Cdd:COG4372 110 AEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1365 KDLNVKEKIIEDMRMTLEEQEQ-TQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTN 1443
Cdd:COG4372 190 KEANRNAEKEEELAEAEKLIESlPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILV 269
|
250
....*....|...
gi 546231677 1444 LQDELQESEQKYN 1456
Cdd:COG4372 270 EKDTEEEELEIAA 282
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1181-1521 |
7.35e-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: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1181 AKLEqdILEKEsiILKLERNLKEFQEHLQDsVKNTKDLNVKELKLKEEITQLTNNLQDM----KHLLQLKEEeeetnrqe 1256
Cdd:COG4913 610 AKLA--ALEAE--LAELEEELAEAEERLEA-LEAELDALQERREALQRLAEYSWDEIDVasaeREIAELEAE-------- 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1257 teklKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQcSQELDM 1336
Cdd:COG4913 677 ----LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL-ELRALL 751
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1337 KQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATEL------- 1409
Cdd:COG4913 752 EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLeedglpe 831
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1410 --EKWKEKCNDLETKN----NQRSNKEHENNTDVLGKLtNlqDELQESEqkYNADRKKWLEEKMMLITQAKE----AENI 1479
Cdd:COG4913 832 yeERFKELLNENSIEFvadlLSKLRRAIREIKERIDPL-N--DSLKRIP--FGPGRYLRLEARPRPDPEVREfrqeLRAV 906
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 546231677 1480 RNKEMKKYAEDRERFFKQQNE-MEILTAQLTEKDsdlQKWREE 1521
Cdd:COG4913 907 TSGASLFDEELSEARFAALKRlIERLRSEEEESD---RRWRAR 946
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1072-1381 |
1.12e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.95 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1072 SKKSHQIEELEQQIEKLQAEVKGYKDENN-RLKEKEH-KNQDDLLKEKETLIQQLKEELQEKNVTLDV---QIQHVVE-- 1144
Cdd:pfam15921 499 SDLTASLQEKERAIEATNAEITKLRSRVDlKLQELQHlKNEGDHLRNVQTECEALKLQMAEKDKVIEIlrqQIENMTQlv 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1145 ---GKRALSELTQGVTCYK--------------------AKIKELE---TILETQKVECSHSA----------KLEQDIL 1188
Cdd:pfam15921 579 gqhGRTAGAMQVEKAQLEKeindrrlelqefkilkdkkdAKIRELEarvSDLELEKVKLVNAGserlravkdiKQERDQL 658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1189 EKESIILKLERN-LKEFQEHLQDSVKN-TKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSA 1266
Cdd:pfam15921 659 LNEVKTSRNELNsLSEDYEVLKRNFRNkSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITA 738
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1267 SSARTQNLKADLQRkeedyadLKEKLTDAkkqikqvQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKE 1346
Cdd:pfam15921 739 KRGQIDALQSKIQF-------LEEAMTNA-------NKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKE 804
|
330 340 350
....*....|....*....|....*....|....*..
gi 546231677 1347 QLNNQKV--EEAIQQYERaCKDLnVKEKIIEDMRMTL 1381
Cdd:pfam15921 805 KVANMEValDKASLQFAE-CQDI-IQRQEQESVRLKL 839
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1273-1411 |
1.25e-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: 42.60 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1273 NLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCS--QELDMKQRTIQQLKEQLN- 1349
Cdd:COG1579 28 ELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEALQKEIESLKRRISd 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 546231677 1350 -NQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEK 1411
Cdd:COG1579 108 lEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1055-1319 |
1.26e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1055 SSIEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDE----NNRLKE-----KEHKNQDDLLKEKetlIQQLK 1125
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKrdelNAQVKElreeaQELREKRDELNEK---VKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1126 EELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKA---KIKELETILETQKVECSHSAKLEQDILEKESIILKLERnLK 1202
Cdd:COG1340 78 EERDELNEKLNELREELDELRKELAELNKAGGSIDKlrkEIERLEWRQQTEVLSPEEEKELVEKIKELEKELEKAKK-AL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1203 EFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKE 1282
Cdd:COG1340 157 EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 546231677 1283 EDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIK 1319
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1062-1466 |
1.35e-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: 43.88 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1062 EECKEIVKASSKKSHQIEELEQQIEKLQAEVKgykdennrLKEKEHKNQDDLLKEKETLIQQLKEELQEKNVTLDVQIQH 1141
Cdd:TIGR00606 709 DKLKSTESELKKKEKRRDEMLGLAPGRQSIID--------LKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPE 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1142 VVEGKRALSELTQgVTCYKAKIKELETILETQKVECSHS------AKLEQDILEKESIILKLERNLKEFQEHLQDSVKNT 1215
Cdd:TIGR00606 781 EESAKVCLTDVTI-MERFQMELKDVERKIAQQAAKLQGSdldrtvQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQI 859
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1216 KDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEEDYADLKEKLTDA 1295
Cdd:TIGR00606 860 QHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKA 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1296 KKQIKQVQKEVSVMRDEDKLLRIKINElEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIE 1375
Cdd:TIGR00606 940 QDKVNDIKEKVKNIHGYMKDIENKIQD-GKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQ 1018
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1376 DmrmtleeqeqtqVEQDQVLEAKLEEVERlatELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDELQESEQKY 1455
Cdd:TIGR00606 1019 D------------NLTLRKRENELKEVEE---ELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKE 1083
|
410
....*....|.
gi 546231677 1456 NADRKKWLEEK 1466
Cdd:TIGR00606 1084 IKHFKKELREP 1094
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1286-1426 |
1.80e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1286 ADLKEKLTDAKKQIKQVQKEVSVMRDEdKLLRIKiNELEKKKNQCSQELDMKQRTIQQLKEQLNnQKVEeaiqQYERACK 1365
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIKKE-ALLEAK-EEIHKLRNEFEKELRERRNELQKLEKRLL-QKEE----NLDRKLE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546231677 1366 DLNVKEKIiedmrmtleeqeqtqveqdqvLEAKLEEVERLATELEKWKEKCNDLETKNNQR 1426
Cdd:PRK12704 104 LLEKREEE---------------------LEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1270-1560 |
1.90e-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: 43.19 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1270 RTQNLKADLQRKEEDYADLKEKLTDAKKQIKQ-----VQKEVSVMRDEDKLLRIKINELEKKKNQCSQ-ELDMKQRTIQQ 1343
Cdd:pfam17380 300 RLRQEKEEKAREVERRRKLEEAEKARQAEMDRqaaiyAEQERMAMERERELERIRQEERKRELERIRQeEIAMEISRMRE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1344 LKE-QLNNQKVEEAIQQYERACKDLNVKEKiiEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETK 1422
Cdd:pfam17380 380 LERlQMERQQKNERVRQELEAARKVKILEE--ERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1423 NNQRSNKEHENNTDVLGKLTNLQDElQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEMe 1502
Cdd:pfam17380 458 RQQQVERLRQQEEERKRKKLELEKE-KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR- 535
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 546231677 1503 iltaqltekdsdlQKWREERdqlvaaleiqlkalissnvQKDNEIEQLKRIISETSKI 1560
Cdd:pfam17380 536 -------------REAEEER-------------------RKQQEMEERRRIQEQMRKA 561
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1073-1362 |
1.91e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.90 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1073 KKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKEtLIQQLKEELQEKNVT-------LDVQIQH---- 1141
Cdd:PRK04778 102 KAKHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQLKD-LYRELRKSLLANRFSfgpaldeLEKQLENleee 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1142 ------------VVEGKRALSELTQGVTCYKAKIKELETILETQKVEC-SHSAKLE---QDILEKESII--LKLERNLKE 1203
Cdd:PRK04778 181 fsqfveltesgdYVEAREILDQLEEELAALEQIMEEIPELLKELQTELpDQLQELKagyRELVEEGYHLdhLDIEKEIQD 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1204 FQEHLQDSVKNTKDLNVKElkLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKADLQRKEE 1283
Cdd:PRK04778 261 LKEQIDENLALLEELDLDE--AEEKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQ 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1284 DY---ADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNN-----QKVEE 1355
Cdd:PRK04778 339 SYtlnESELESVRQLEKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGlrkdeLEARE 418
|
....*..
gi 546231677 1356 AIQQYER 1362
Cdd:PRK04778 419 KLERYRN 425
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1120-1559 |
2.13e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1120 LIQQLKEELQE----KNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETiLETQKVEcshsakLEQDILEKESIIL 1195
Cdd:COG4717 47 LLERLEKEADElfkpQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEE------LEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1196 KLERnLKEFQEHLQDSVKNTKDLNvkelKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNlk 1275
Cdd:COG4717 120 KLEK-LLQLLPLYQELEALEAELA----ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1276 aDLQRKEEDYADLKEKLTDAKKQIKQVQKEVsvmrdedKLLRIKINELEKKknqcsQELDMKQRTIQQLKEQLN------ 1349
Cdd:COG4717 193 -ELQDLAEELEELQQRLAELEEELEEAQEEL-------EELEEELEQLENE-----LEAAALEERLKEARLLLLiaaall 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1350 ---------------------------------NQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVeqdqvlE 1396
Cdd:COG4717 260 allglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPP------D 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1397 AKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHENNTDVLGKLTNLQDE-----LQESEQKYNADRKKWLEEKMMLIT 1471
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelraALEQAEEYQELKEELEELEEQLEE 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1472 QAKEAENIRNKEMKKYAEDrerffkqqnEMEILTAQLTEKDSDLQKWREERdqlvAALEIQLKALISSN--VQKDNEIEQ 1549
Cdd:COG4717 414 LLGELEELLEALDEEELEE---------ELEELEEELEELEEELEELREEL----AELEAELEQLEEDGelAELLQELEE 480
|
490
....*....|
gi 546231677 1550 LKRIISETSK 1559
Cdd:COG4717 481 LKAELRELAE 490
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1181-1377 |
2.18e-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: 42.44 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1181 AKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQlkeEEEETNRQETEKL 1260
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1261 KEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRT 1340
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 546231677 1341 IQQLKEQLNNQ-----KVEEAIQQYERACKDLNVKEKIIEDM 1377
Cdd:COG4942 187 RAALEALKAERqkllaRLEKELAELAAELAELQQEAEELEAL 228
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1196-1576 |
2.44e-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: 42.70 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1196 KLERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLK 1275
Cdd:TIGR04523 37 QLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1276 ADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKIN-------ELEKKKNQCSQELDMKQRTIQQLKEQL 1348
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNdlkkqkeELENELNLLEKEKLNIQKNIDKIKNKL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1349 NNQK-----VEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKN 1423
Cdd:TIGR04523 197 LKLElllsnLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1424 NQRSNKEHENNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQ----QN 1499
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEltnsES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1500 EMEILTAQLTEKDSDLQKWREERDQL----------VAALEIQLKALISSNVQKDNEIEQLKriiSETSKIETQIMDIKP 1569
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYkqeiknlesqINDLESKIQNQEKLNQQKDEQIKKLQ---QEKELLEKEIERLKE 433
|
....*..
gi 546231677 1570 KRISSAD 1576
Cdd:TIGR04523 434 TIIKNNS 440
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1049-1203 |
2.58e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1049 RENSFHSSIEAIWEECKEIVKASSKKshqIEELEQQIEkLQAevkgyKDENNRLK---EKEHKNQDDLLKEKETLIQQLK 1125
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKE---AEAIKKEAL-LEA-----KEEIHKLRnefEKELRERRNELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 546231677 1126 EELQEKNVTLDVQIQHVVEGKRALSELTQGVtcyKAKIKELETILETQKVECSHSAKLEQDilE-KESIILKLERNLKE 1203
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQEL---EKKEEELEELIEEQLQELERISGLTAE--EaKEILLEKVEEEARH 169
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1073-1362 |
2.86e-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: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1073 KKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLLKEKEtLIQQLKEELQEKNVT-------LDVQIQHV--- 1142
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKD-KYRELRKTLLANRFSygpaideLEKQLAEIeee 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1143 -------------VEGKRALSELTQGVTCYKAKIKELETILETQKVEcshsakLEQDILEKESII------------LKL 1197
Cdd:pfam06160 162 fsqfeeltesgdyLEAREVLEKLEEETDALEELMEDIPPLYEELKTE------LPDQLEELKEGYremeeegyalehLNV 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1198 ERNLKEFQEHLQDSVKNTKDLNVKElkLKEEITQLTNNLQDMKHLLQLKEEEEETNRQETEKLKEELSASSARTQNLKAD 1277
Cdd:pfam06160 236 DKEIQQLEEQLEENLALLENLELDE--AEEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1278 LQRKEEDY---ADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNN---- 1350
Cdd:pfam06160 314 LERVQQSYtlnENELERVRGLEKQLEELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIEEEQEEFKESLQSlrkd 393
|
330
....*....|...
gi 546231677 1351 -QKVEEAIQQYER 1362
Cdd:pfam06160 394 eLEAREKLDEFKL 406
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1290-1556 |
2.97e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1290 EKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN--NQKVEEAIQQYERACKDL 1367
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAalEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1368 NVKEKIIEDMRMTLEeqeqtqveqdqvleaKLEEVERLATELekwkekcndletknNQRSNKEHENNTDVLGKLTnlqDE 1447
Cdd:COG4942 100 EAQKEELAELLRALY---------------RLGRQPPLALLL--------------SPEDFLDAVRRLQYLKYLA---PA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1448 LQESEQKYNADRKKwleekmmLITQAKEAEnirnkemkkyaedrerffKQQNEMEILTAQLTEKDSDLQKWREERDQLVA 1527
Cdd:COG4942 148 RREQAEELRADLAE-------LAALRAELE------------------AERAELEALLAELEEERAALEALKAERQKLLA 202
|
250 260
....*....|....*....|....*....
gi 546231677 1528 ALEIQLKALISSNVQKDNEIEQLKRIISE 1556
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1114-1427 |
3.14e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1114 LKEKETLIQQLKEELQEKNVTLDVQIQHVvegkralselTQGVTCYKAKIKELEtiletqkvecshsAKLEQDILEKESI 1193
Cdd:PHA02562 165 LSEMDKLNKDKIRELNQQIQTLDMKIDHI----------QQQIKTYNKNIEEQR-------------KKNGENIARKQNK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1194 I---LKLERNLKEFQEHLQDSVKNtkdlnvkelkLKEEITQLTNNLQDMKHlLQLKEEEEETNRQETEKLKEELSASSAR 1270
Cdd:PHA02562 222 YdelVEEAKTIKAEIEELTDELLN----------LVMDIEDPSAALNKLNT-AAAKIKSKIEQFQKVIKMYEKGGVCPTC 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1271 TQNLKadlqrkeedyaDLKEKLTDAKKQIKQVQKEVsvmrdedKLLRIKINELEKKKNqcsqELDMKQRTIQQLKEQLNN 1350
Cdd:PHA02562 291 TQQIS-----------EGPDRITKIKDKLKELQHSL-------EKLDTAIDELEEIMD----EFNEQSKKLLELKNKIST 348
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 546231677 1351 QKveEAIQQYERACKDLnvkEKIIEDMRMTLEEQEqtqveqdqvleaklEEVERLATELEKWKEKCNDLETKNNQRS 1427
Cdd:PHA02562 349 NK--QSLITLVDKAKKV---KAAIEELQAEFVDNA--------------EELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
542-1235 |
3.34e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 542 AEETQNVETKLLDEDLDKTLEENKA--------FISHEEKRKLLDL--------------IEDLKKKLINEKKEKLTLEF 599
Cdd:PTZ00121 1172 AEDAKKAEAARKAEEVRKAEELRKAedarkaeaARKAEEERKAEEArkaedakkaeavkkAEEAKKDAEEAKKAEEERNN 1251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 600 KIREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREEAAKDICATKVETEETHNYVGFEDII 679
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKA 1331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 680 DSLQDNVADIKKQAEIAHLYIASLPDPQEAT------ACLELKFNQIKAELAKTKGELIKTKEELKKRENESDSLIQELe 753
Cdd:PTZ00121 1332 DAAKKKAEEAKKAAEAAKAEAEAAADEAEAAeekaeaAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADEL- 1410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 754 tsnKKIITQNQRIKELiniiDQKEDTINEFQNLKSHMENTFKCNDKADTSSLIINNKLICNETVEVPKDSKSKICSERKR 833
Cdd:PTZ00121 1411 ---KKAAAAKKKADEA----KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK 1483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 834 VNEnELQQDEPPAKKGSIHVSSAiTEDQKKSEEVRpNIAEIEDIRVLQENNEGLRAFLL----TIENELKNEKEEKAELN 909
Cdd:PTZ00121 1484 KAD-EAKKKAEEAKKKADEAKKA-AEAKKKADEAK-KAEEAKKADEAKKAEEAKKADEAkkaeEKKKADELKKAEELKKA 1560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 910 KQIVHFQQELSLSEKKNLTLSK--EVQQIQSNYDIAIAELHVQKSKNQ-EQEEKIMKLSNEIETATRSITNNVSQIKLMH 986
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKaeEAKKAEEARIEEVMKLYEEEKKMKaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKK 1640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 987 TKIDELRTLDSVSQISNIDLLNLRDLSNGSEEDNLPNTQLDLLGNDYLVSKQVKEYRIQEPNRENSFHSSIEAIWEECKE 1066
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE 1720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1067 IVKASSKKSHQIEEL--EQQIEKLQAEV----KGYKDENNRLKEKEHKNQDDLLKEKETLIQQ-LKEELQEKNVTLDVQI 1139
Cdd:PTZ00121 1721 LKKAEEENKIKAEEAkkEAEEDKKKAEEakkdEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEEDEKRRMEVDKKI 1800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1140 QHVVEGKRALSELTQGVTCYKAKIKELETILETQKVECSHSAKLEQDILEKESIILKLERNLKEFQEHLQDSVKNTKDLN 1219
Cdd:PTZ00121 1801 KDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDD 1880
|
730
....*....|....*.
gi 546231677 1220 VKELKLKEEITQLTNN 1235
Cdd:PTZ00121 1881 EEEIEEADEIEKIDKD 1896
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1277-1422 |
3.49e-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: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1277 DLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEA 1356
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 546231677 1357 IQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVE-RLATELEKWKEKCNDLETK 1422
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEaELEEKKAELDEELAELEAE 157
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
719-795 |
3.92e-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: 3.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 546231677 719 QIKAELAKTKGELIKTKEELKKRENESDSLIQELETSNKKIITQNQRIKELINIIDQKEDTINEFQNLKSHMENTFK 795
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1294-1568 |
4.12e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1294 DAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKI 1373
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1374 IEdmrmtleeqeqtqveqdqVLEAKLEEVERLATELEKWKEKCNDLETKNNQRsnkehenNTDVLGKLTNLQDELQESEQ 1453
Cdd:COG4913 687 LA------------------ALEEQLEELEAELEELEEELDELKGEIGRLEKE-------LEQAEEELDELQDRLEAAED 741
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1454 KYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFFKQQNEME-----------ILTAQLTEKDSDLQKWREER 1522
Cdd:COG4913 742 LARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELEramrafnrewpAETADLDADLESLPEYLALL 821
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 546231677 1523 DQLVA----ALEIQLKALIssNVQKDNEIEQLKriisetSKIETQIMDIK 1568
Cdd:COG4913 822 DRLEEdglpEYEERFKELL--NENSIEFVADLL------SKLRRAIREIK 863
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
115-183 |
4.12e-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: 4.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 546231677 115 FSKVFGPATTQKEFFQGC--IMQPVKDLLKGQSrlIFTYGLTNSGKTYTFQgteeniGILPRTLNVLFDSL 183
Cdd:cd01363 22 FYRGFRRSESQPHVFAIAdpAYQSMLDGYNNQS--IFAYGESGAGKTETMK------GVIPYLASVAFNGI 84
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1185-1598 |
5.04e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.97 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1185 QDILEKESIIlklERNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDMKhllqlkeeeeetnrqeteKLKEEL 1264
Cdd:PRK03918 182 EKFIKRTENI---EELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE------------------ELKEEI 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1265 SassartqNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRiKINELEKKKNQCSQELDMKQRTIQQL 1344
Cdd:PRK03918 241 E-------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1345 KEQLnnQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEqeqtqveqdqvLEAKLEEVERLATELEKWKEKCNDLETKNN 1424
Cdd:PRK03918 313 EKRL--SRLEEEINGIEERIKELEEKEERLEELKKKLKE-----------LEKRLEELEERHELYEEAKAKKEELERLKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1425 QRSNKEHENNTDVLGKLTNLQDELQESEQKYNADR---KKWLEEKMMLITQAKEAENI------------RNKEMKKYAE 1489
Cdd:PRK03918 380 RLTGLTPEKLEKELEELEKAKEEIEEEISKITARIgelKKEIKELKKAIEELKKAKGKcpvcgrelteehRKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1490 DRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEI--QLKALISSnvQKDNEIEQLKRIISETSKIETQIMDI 1567
Cdd:PRK03918 460 ELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEK--LKKYNLEELEKKAEEYEKLKEKLIKL 537
|
410 420 430
....*....|....*....|....*....|.
gi 546231677 1568 KpKRISSADPDKLQTEPLSTSFEISRNKIED 1598
Cdd:PRK03918 538 K-GEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1057-1239 |
5.59e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 5.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1057 IEAIWEECKEIVKASSKKSHQIEELEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDLlKEKETLIQQLKEELQEKNVTLD 1136
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI-AELRAELEAQKEELAELLRALY 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1137 VQIQH--------------VVEGKRALSELTQG----VTCYKAKIKELETILETQKVEcshSAKLEQDILEKESIILKLE 1198
Cdd:COG4942 115 RLGRQpplalllspedfldAVRRLQYLKYLAPArreqAEELRADLAELAALRAELEAE---RAELEALLAELEEERAALE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 546231677 1199 RNLKEFQEHLQDSVKNTKDLNVKELKLKEEITQLTNNLQDM 1239
Cdd:COG4942 192 ALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1036-1552 |
6.75e-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: 41.31 E-value: 6.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1036 SKQVKEYRIQEpNRENSFHSSIEAIWEECKEIVKASSKKSHQIEELEqqiEKLQAEVKGYKD--ENNRLKEKEHKNQDDL 1113
Cdd:pfam01576 148 SKLSKERKLLE-ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLE---ERLKKEEKGRQEleKAKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1114 LKEKETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVTCYKAKIKELETILETQKVECSHSAKLEQDILEK-ES 1192
Cdd:pfam01576 224 IAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEElEA 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1193 IILKLERNLKefQEHLQDSVKNTKDLNVKELK--LKEEITQLTNNLQDM--KHLLQLKEEEEETNRQETEK--------- 1259
Cdd:pfam01576 304 LKTELEDTLD--TTAAQQELRSKREQEVTELKkaLEEETRSHEAQLQEMrqKHTQALEELTEQLEQAKRNKanlekakqa 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1260 -------LKEELSASSARTQNLKADLQRKEEDYADLKEKLTDAKKQIKQVQKEVSVMRDEDKLLRIKINELEKKKNQCSQ 1332
Cdd:pfam01576 382 lesenaeLQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSK 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1333 ELDmkqrtiqQLKEQLnnQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLE--------------AK 1398
Cdd:pfam01576 462 DVS-------SLESQL--QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVErqlstlqaqlsdmkKK 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1399 LEEVERLATELEKWKEKC-NDLETKNNQRSNKEHE------NNTDVLGKLTNLQDELQESEQKYNADRKKWLEEKMMLit 1471
Cdd:pfam01576 533 LEEDAGTLEALEEGKKRLqRELEALTQQLEEKAAAydklekTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQML-- 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1472 qaKEAENIRNKemkkYAEDRERFFKQQNEMEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISS--NVQKD-NEIE 1548
Cdd:pfam01576 611 --AEEKAISAR----YAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSkdDVGKNvHELE 684
|
....
gi 546231677 1549 QLKR 1552
Cdd:pfam01576 685 RSKR 688
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1081-1219 |
8.19e-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: 41.18 E-value: 8.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 546231677 1081 LEQQIEKLQAEVKGYKDENNRLKEKEHKNQDDL--LKEK-ETLIQQLKEELQEKNVTLDVQIQHVVEGKRALSELTQGVT 1157
Cdd:pfam10168 566 LKLQKEQQLQELQSLEEERKSLSERAEKLAEKYeeIKDKqEKLMRRCKKVLQRLNSQLPVLSDAEREMKKELETINEQLK 645
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 546231677 1158 CYKAKIKELETILETQKvecSHSAKlEQDILEKESIILKLER------NLKEFQEHLQDSVKNTKDLN 1219
Cdd:pfam10168 646 HLANAIKQAKKKMNYQR---YQIAK-SQSIRKKSSLSLSEKQrktikeILKQLGSEIDELIKQVKDIN 709
|
|
| |
