|
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 |
8.17e-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: 523.88 E-value: 8.17e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 57 DYLQVCLRIRPFTQSEKEHESEGCVHILDSQTVVLKEPQCILGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQP 136
Cdd:cd01368 1 DPVKVYLRVRPLSKDELESEDEGCIEVINSTTVVLHPPKGSAANKSERNGGQKETKFSFSKVFGPNTTQKEFFQGTALPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 137 VKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENMGILPRTLNVLFDSLQErlytkmnlkphrsreylrlsseqekeeiagk 216
Cdd:cd01368 81 VQDLLHGKNGLLFTYGVTNSGKTYTMQGSPGDGGILPRSLDVIFNSIGG------------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 217 sallrqikevtmhndgddtlygsltnslnisefeesikdceqaslnmandikFSVWVSFFEIYNEYIYDLFVPV-SSKFQ 295
Cdd:cd01368 130 ----------------------------------------------------YSVFVSYIEIYNEYIYDLLEPSpSSPTK 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 296 KRKMLRLSQDVKGYSFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKILQIEDSE------MSR 369
Cdd:cd01368 158 KRQSLRLREDHNGNMYVAGLTEIEVKSTEEARKVLKRGQKNRSVAGTKLNRESSRSHSVFTIKLVQAPGDSdgdvdqDKD 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 370 VIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSKFQQHVPFRESKLTHYFQSFFNGKGK 449
Cdd:cd01368 238 QITVSQLSLVDLAGSERTSRTQNTGERLKEAGNINTSLMTLGTCIEVLRENQLQGTNKMVPFRDSKLTHLFQNYFDGEGK 317
|
410 420
....*....|....*....|....*...
gi 1622966431 450 ICMIVNISQCYLAYDETLNVLKFSAIAQ 477
Cdd:cd01368 318 ASMIVNVNPCASDYDETLHVMKFSAIAQ 345
|
|
| Kinesin |
pfam00225 |
Kinesin motor domain; |
64-479 |
1.70e-92 |
|
Kinesin motor domain;
Pssm-ID: 459720 [Multi-domain] Cd Length: 326 Bit Score: 303.34 E-value: 1.70e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 64 RIRPFTQSEKE--HESEGCVHILDSQTVVLkepqcilgrlSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLL 141
Cdd:pfam00225 1 RVRPLNEREKErgSSVIVSVESVDSETVES----------SHLTNKNRTKTFTFDKVFDPEATQEDVYEETAKPLVESVL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 142 KGQSRLIFTYGLTNSGKTYTFQGTEENMGILPRTLNVLFDSLQERLytkmnlkphrsreylrlsseqekeeiagksallr 221
Cdd:pfam00225 71 EGYNVTIFAYGQTGSGKTYTMEGSDEQPGIIPRALEDLFDRIQKTK---------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 222 qikevtmhndgddtlygsltnslnisefeesikdceqaslnmaNDIKFSVWVSFFEIYNEYIYDLFVPVSSKFQKrkmLR 301
Cdd:pfam00225 117 -------------------------------------------ERSEFSVKVSYLEIYNEKIRDLLSPSNKNKRK---LR 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 302 LSQDVKGYSFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKILQ-IEDSEMSRVIRVSELSLCD 380
Cdd:pfam00225 151 IREDPKKGVYVKGLTEVEVSSAEEVLELLQLGNKNRTVAATKMNEESSRSHAIFTITVEQrNRSTGGEESVKTGKLNLVD 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 381 LAGSERTMKTQN-EGERLRETGNINTSLLTLGKCINVLKnsekSKFQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQC 459
Cdd:pfam00225 231 LAGSERASKTGAaGGQRLKEAANINKSLSALGNVISALA----DKKSKHIPYRDSKLTRLLQDSLGGNSKTLMIANISPS 306
|
410 420
....*....|....*....|
gi 1622966431 460 YLAYDETLNVLKFSAIAQKV 479
Cdd:pfam00225 307 SSNYEETLSTLRFASRAKNI 326
|
|
| KISc |
smart00129 |
Kinesin motor, catalytic domain. ATPase; Microtubule-dependent molecular motors that play ... |
60-479 |
2.74e-91 |
|
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: 300.26 E-value: 2.74e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 60 QVCLRIRPFTQSEKEHESEGCVHILDSQTVVLkepqcilgRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:smart00129 3 RVVVRVRPLNKREKSRKSPSVVPFPDKVGKTL--------TVRSPKNRQGEKKFTFDKVFDATASQEDVFEETAAPLVDS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 140 LLKGQSRLIFTYGLTNSGKTYTFQGTEENMGILPRTLNVLFDSLQERlytkmnlkphrsreylrlsseqekeeiagksal 219
Cdd:smart00129 75 VLEGYNATIFAYGQTGSGKTYTMIGTPDSPGIIPRALKDLFEKIDKR--------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 220 lrqikevtmhndgddtlygsltnslnisefeesikdceqaslnmANDIKFSVWVSFFEIYNEYIYDLFVPVSSKfqkrkm 299
Cdd:smart00129 122 --------------------------------------------EEGWQFSVKVSYLEIYNEKIRDLLNPSSKK------ 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 300 LRLSQDVKGYSFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKILQIEDSEMSRVIRVSELSLC 379
Cdd:smart00129 152 LEIREDEKGGVYVKGLTEISVSSFEEVYNLLEKGNKNRTVAATKMNEESSRSHAVFTITVEQKIKNSSSGSGKASKLNLV 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 380 DLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKskfQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQC 459
Cdd:smart00129 232 DLAGSERAKKTGAEGDRLKEAGNINKSLSALGNVINALAQHSK---SRHIPYRDSKLTRLLQDSLGGNSKTLMIANVSPS 308
|
410 420
....*....|....*....|
gi 1622966431 460 YLAYDETLNVLKFSAIAQKV 479
Cdd:smart00129 309 SSNLEETLSTLRFASRAKEI 328
|
|
| KISc |
cd00106 |
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity ... |
60-477 |
1.60e-86 |
|
Kinesin motor domain; Kinesin motor domain. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type), in some its is found in the middle (M-type), or C-terminal (C-type). N-type and M-type kinesins are (+) end-directed motors, while C-type kinesins are (-) end-directed motors, i.e. they transport cargo towards the (-) end of the microtubule. Kinesin motor domains hydrolyze ATP at a rate of about 80 per second, and move along the microtubule at a speed of about 6400 Angstroms per second. To achieve that, kinesin head groups work in pairs. Upon replacing ADP with ATP, a kinesin motor domain increases its affinity for microtubule binding and locks in place. Also, the neck linker binds to the motor domain, which repositions the other head domain through the coiled-coil domain close to a second tubulin dimer, about 80 Angstroms along the microtubule. Meanwhile, ATP hydrolysis takes place, and when the second head domain binds to the microtubule, the first domain again replaces ADP with ATP, triggering a conformational change that pulls the first domain forward.
Pssm-ID: 276812 [Multi-domain] Cd Length: 326 Bit Score: 286.07 E-value: 1.60e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 60 QVCLRIRPFTQSEKEHESEgCVHILDSQTVVLKEPqcilgrlseKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:cd00106 3 RVAVRVRPLNGREARSAKS-VISVDGGKSVVLDPP---------KNRVAPPKTFAFDAVFDSTSTQEEVYEGTAKPLVDS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 140 LLKGQSRLIFTYGLTNSGKTYTFQGT-EENMGILPRTLNVLFDSLQERLYTKMNlkphrsreylrlsseqekeeiagksa 218
Cdd:cd00106 73 ALEGYNGTIFAYGQTGSGKTYTMLGPdPEQRGIIPRALEDIFERIDKRKETKSS-------------------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 219 llrqikevtmhndgddtlygsltnslnisefeesikdceqaslnmandikFSVWVSFFEIYNEYIYDLFVPVsskfqKRK 298
Cdd:cd00106 127 --------------------------------------------------FSVSASYLEIYNEKIYDLLSPV-----PKK 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 299 MLRLSQDVKGYSFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKILQIEDSEMSRVIRVSELSL 378
Cdd:cd00106 152 PLSLREDPKRGVYVKGLTEVEVGSLEDALELLDAGNKNRTTASTNMNEHSSRSHAVFTIHVKQRNREKSGESVTSSKLNL 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 379 CDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKskfqQHVPFRESKLTHYFQSFFNGKGKICMIVNISQ 458
Cdd:cd00106 232 VDLAGSERAKKTGAEGDRLKEGGNINKSLSALGKVISALADGQN----KHIPYRDSKLTRLLQDSLGGNSKTIMIACISP 307
|
410
....*....|....*....
gi 1622966431 459 CYLAYDETLNVLKFSAIAQ 477
Cdd:cd00106 308 SSENFEETLSTLRFASRAK 326
|
|
| KISc_C_terminal |
cd01366 |
Kinesin motor domain, KIFC2/KIFC3/ncd-like carboxy-terminal kinesins; Kinesin motor domain, ... |
64-479 |
3.07e-65 |
|
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: 225.17 E-value: 3.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 64 RIRPFTQSEkehESEGCVHIL----DSQTVVLKepqcilgrlseksSGQMAQK-FSFSKVFGPATTQKEFFQGcIMQPVK 138
Cdd:cd01366 9 RVRPLLPSE---ENEDTSHITfpdeDGQTIELT-------------SIGAKQKeFSFDKVFDPEASQEDVFEE-VSPLVQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTEENMGILPRTLNVLFDSLQERlytkmnlkphrsreylrlsSEQekeeiagksa 218
Cdd:cd01366 72 SALDGYNVCIFAYGQTGSGKTYTMEGPPESPGIIPRALQELFNTIKEL-------------------KEK---------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 219 llrqikevtmhndgddtlygsltnslnisefeesikdceqaslnmanDIKFSVWVSFFEIYNEYIYDLfvpVSSKFQKRK 298
Cdd:cd01366 123 -----------------------------------------------GWSYTIKASMLEIYNETIRDL---LAPGNAPQK 152
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 299 MLRLSQD-VKGYSFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKIlQIEDsEMSRVIRVSELS 377
Cdd:cd01366 153 KLEIRHDsEKGDTTVTNLTEVKVSSPEEVRQLLKKASKNRSTASTAMNEHSSRSHSVFILHI-SGRN-LQTGEISVGKLN 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 378 LCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSekskfQQHVPFRESKLTHYFQSFFNGKGKICMIVNIS 457
Cdd:cd01366 231 LVDLAGSERLNKSGATGDRLKETQAINKSLSALGDVISALRQK-----QSHIPYRNSKLTYLLQDSLGGNSKTLMFVNIS 305
|
410 420
....*....|....*....|..
gi 1622966431 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 |
2.43e-64 |
|
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: 222.98 E-value: 2.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 60 QVCLRIRPFTQSEKeheSEGCvhiLDSQTVVLKEPQCILGRlsekssgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:cd01372 4 RVAVRVRPLLPKEI---IEGC---RICVSFVPGEPQVTVGT---------DKSFTFDYVFDPSTEQEEVYNTCVAPLVDG 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 140 LLKGQSRLIFTYGLTNSGKTYTFQGT------EENMGILPRTLNVLFDSLQErlytkmnlkphrsreylrlsseqekeei 213
Cdd:cd01372 69 LFEGYNATVLAYGQTGSGKTYTMGTAytaeedEEQVGIIPRAIQHIFKKIEK---------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 214 agksallrqikevtmhndgddtlygsltnslnisefeesikdceqaslnMANDIKFSVWVSFFEIYNEYIYDLFvpvSSK 293
Cdd:cd01372 121 -------------------------------------------------KKDTFEFQLKVSFLEIYNEEIRDLL---DPE 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 294 FQKRKMLRLSQDVKGYSFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKILQ----IEDSEMSR 369
Cdd:cd01372 149 TDKKPTISIREDSKGGITIVGLTEVTVLSAEDMMSCLEQGSLSRTTASTAMNSQSSRSHAIFTITLEQtkknGPIAPMSA 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 370 VIR----VSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKFQQHVPFRESKLTHYFQSFFN 445
Cdd:cd01372 229 DDKnstfTSKFHFVDLAGSERLKRTGATGDRLKEGISINSGLLALGNVISAL--GDESKKGAHVPYRDSKLTRLLQDSLG 306
|
410 420 430
....*....|....*....|....*....|....
gi 1622966431 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 |
2.02e-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: 214.52 E-value: 2.02e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 59 LQVCLRIRPFTQSEKEHESEGCVHILDSQTVVLKEPQCILGRLSEKSSGQMAQ-------KFSFSKVFGPATTQKEFFQG 131
Cdd:cd01370 2 LTVAVRVRPFSEKEKNEGFRRIVKVMDNHMLVFDPKDEEDGFFHGGSNNRDRRkrrnkelKYVFDRVFDETSTQEEVYEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 132 CIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENMGILPRTLNVLFDSLqerlytkmnlkphrsreylrlsseqeke 211
Cdd:cd01370 82 TTKPLVDGVLNGYNATVFAYGATGAGKTHTMLGTPQEPGLMVLTMKELFKRI---------------------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 212 eiagksallrqikevtmhndgddtlygsltnslnisefeESIKDceqaslnmanDIKFSVWVSFFEIYNEYIYDLFVPVS 291
Cdd:cd01370 134 ---------------------------------------ESLKD----------EKEFEVSMSYLEIYNETIRDLLNPSS 164
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 292 skfqkrKMLRLSQDVKGYSFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKILQIE-DSEMSRV 370
Cdd:cd01370 165 ------GPLELREDAQNGIVVAGLTEHSPKSAEEILELLMKGNRNRTQEPTDANATSSRSHAVLQITVRQQDkTASINQQ 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 371 IRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKFQQHVPFRESKLTHYFQSFFNGKGKI 450
Cdd:cd01370 239 VRQGKLSLIDLAGSERASATNNRGQRLKEGANINRSLLALGNCINAL--ADPGKKNKHIPYRDSKLTRLLKDSLGGNCRT 316
|
410 420
....*....|....*....|....*....
gi 1622966431 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 |
1.00e-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: 209.87 E-value: 1.00e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 59 LQVCLRIRPFTQSEKEHESEGCVHILDSQtvvlKEPQCILGRLSEKSSgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVK 138
Cdd:cd01364 4 IQVVVRCRPFNLRERKASSHSVVEVDPVR----KEVSVRTGGLADKSS---TKTYTFDMVFGPEAKQIDVYRSVVCPILD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTE-----------ENMGILPRTLNVLFDSLQErlytkmnlkphrsreylrlsse 207
Cdd:cd01364 77 EVLMGYNCTIFAYGQTGTGKTYTMEGDRspneeytweldPLAGIIPRTLHQLFEKLED---------------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 208 qekeeiagksallrqikevtmhndgddtlygsltnslnisefeesikdceqaslnmaNDIKFSVWVSFFEIYNEYIYDLF 287
Cdd:cd01364 135 ---------------------------------------------------------NGTEYSVKVSYLEIYNEELFDLL 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 288 VPVSSKFQKRKMLRLSQDVKGYsFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKILQIE-DSE 366
Cdd:cd01364 158 SPSSDVSERLRMFDDPRNKRGV-IIKGLEEITVHNKDEVYQILEKGAAKRKTAATLMNAQSSRSHSVFSITIHIKEtTID 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 367 MSRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSKfqqHVPFRESKLTHYFQSFFNG 446
Cdd:cd01364 237 GEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITAL--VERAP---HVPYRESKLTRLLQDSLGG 311
|
410 420 430
....*....|....*....|....*....|
gi 1622966431 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 |
1.61e-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: 208.34 E-value: 1.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 60 QVCLRIRPFTQSEKEhESEGCVHILDSQTVVLKEPQcilgrlsekssgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVKD 139
Cdd:cd01374 3 TVTVRVRPLNSREIG-INEQVAWEIDNDTIYLVEPP--------------STSFTFDHVFGGDSTNREVYELIAKPVVKS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 140 LLKGQSRLIFTYGLTNSGKTYTFQGTEENMGILPRTLNVLFDSLQErlytkmnlkpHRSREYLrlsseqekeeiagksal 219
Cdd:cd01374 68 ALEGYNGTIFAYGQTSSGKTFTMSGDEDEPGIIPLAIRDIFSKIQD----------TPDREFL----------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 220 lrqikevtmhndgddtlygsltnslnisefeesikdceqaslnmandikfsVWVSFFEIYNEYIYDLFVPVSskfqkrKM 299
Cdd:cd01374 121 ---------------------------------------------------LRVSYLEIYNEKINDLLSPTS------QN 143
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 300 LRLSQDVKGYSFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKILQIEDSEMSRV-IRVSELSL 378
Cdd:cd01374 144 LKIRDDVEKGVYVAGLTEEIVSSPEHALSLIARGEKNRHVGETDMNERSSRSHTIFRITIESSERGELEEGtVRVSTLNL 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 379 CDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNsekSKFQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQ 458
Cdd:cd01374 224 IDLAGSERAAQTGAAGVRRKEGSHINKSLLTLGTVISKLSE---GKVGGHIPYRDSKLTRILQPSLGGNSRTAIICTITP 300
|
410 420
....*....|....*....|.
gi 1622966431 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 |
1.72e-56 |
|
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: 199.48 E-value: 1.72e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 59 LQVCLRIRPFTQSEKEHESEGCVHILDSQTVVLkepqcilgRLSEKSSgqmaqKFSFSKVFGPATTQKEFFQGCIMQPVK 138
Cdd:cd01369 4 IKVVCRFRPLNELEVLQGSKSIVKFDPEDTVVI--------ATSETGK-----TFSFDRVFDPNTTQEDVYNFAAKPIVD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 139 DLLKGQSRLIFTYGLTNSGKTYTFQGT---EENMGILPRTLNVLFDSLqerlytkmnlkphrsreylrlsseqekeeiag 215
Cdd:cd01369 71 DVLNGYNGTIFAYGQTSSGKTYTMEGKlgdPESMGIIPRIVQDIFETI-------------------------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 216 ksallrqikevtmhndgddtlygsltnslnisefeesikdceqasLNMANDIKFSVWVSFFEIYNEYIYDLFVPvsskfq 295
Cdd:cd01369 119 ---------------------------------------------YSMDENLEFHVKVSYFEIYMEKIRDLLDV------ 147
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 296 KRKMLRLSQDVKGYSFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKILQiEDSEmSRVIRVSE 375
Cdd:cd01369 148 SKTNLSVHEDKNRGPYVKGATERFVSSPEEVLDVIDEGKSNRHVAVTNMNEESSRSHSIFLINVKQ-ENVE-TEKKKSGK 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 376 LSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSkfqqHVPFRESKLTHYFQSFFNGKGKICMIVN 455
Cdd:cd01369 226 LYLVDLAGSEKVSKTGAEGAVLDEAKKINKSLSALGNVINALTDGKKT----HIPYRDSKLTRILQDSLGGNSRTTLIIC 301
|
410
....*....|....*..
gi 1622966431 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 |
2.65e-53 |
|
Kinesin motor domain, KIF1_like proteins; Kinesin motor domain, KIF1_like proteins. KIF1A (Unc104) transports synaptic vesicles to the nerve terminal, KIF1B has been implicated in transport of mitochondria. Both proteins are expressed in neurons. This catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Kinesins are microtubule-dependent molecular motors that play important roles in intracellular transport and in cell division. In most kinesins, the motor domain is found at the N-terminus (N-type). N-type kinesins are (+) end-directed motors, i.e. they transport cargo towards the (+) end of the microtubule. In contrast to the majority of dimeric kinesins, most KIF1A/Unc104 kinesins are monomeric motors. A lysine-rich loop in KIF1A binds to the negatively charged C-terminus of tubulin and compensates for the lack of a second motor domain, allowing KIF1A to move processively.
Pssm-ID: 276816 [Multi-domain] Cd Length: 361 Bit Score: 191.80 E-value: 2.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 60 QVCLRIRPFTQSEKEHESEGCVHILDSQTVVLKEPQcilGRLSEKSSGQMAQKFSFSKVF------GPA-TTQKEFFQGC 132
Cdd:cd01365 4 KVAVRVRPFNSREKERNSKCIVQMSGKETTLKNPKQ---ADKNNKATREVPKSFSFDYSYwshdseDPNyASQEQVYEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 133 IMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENMGILPRTLnvlfdslqERLYTKMNLKPhrsreylrlsseqekee 212
Cdd:cd01365 81 GEELLQHAFEGYNVCLFAYGQTGSGKSYTMMGTQEQPGIIPRLC--------EDLFSRIADTT----------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 213 iagksallrqikevtmhndgddtlygsltnslnisefeesikdceqaslnmANDIKFSVWVSFFEIYNEYIYDLFVPvsS 292
Cdd:cd01365 136 ---------------------------------------------------NQNMSYSVEVSYMEIYNEKVRDLLNP--K 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 293 KFQKRKMLRLSQDVKGYSFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKILQI--EDSEMSRV 370
Cdd:cd01365 163 PKKNKGNLKVREHPVLGPYVEDLSKLAVTSYEDIQDLMDEGNKSRTVAATNMNDTSSRSHAVFTIVLTQKrhDAETNLTT 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 371 IRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVL---KNSEKSKFQQHVPFRESKLTHYFQSFFNGK 447
Cdd:cd01365 243 EKVSKISLVDLAGSERASSTGATGDRLKEGANINKSLTTLGKVISALadmSSGKSKKKSSFIPYRDSVLTWLLKENLGGN 322
|
410 420 430
....*....|....*....|....*....|..
gi 1622966431 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 |
9.66e-53 |
|
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: 9.66e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 57 DYLQVCLRIRPFTQSEKeheSEGCVHILD----SQTVVLKEPqcilgrlsEKSSGQMAQKFSFSKVFGPATTQKEFFQGC 132
Cdd:cd01371 1 ENVKVVVRCRPLNGKEK---AAGALQIVDvdekRGQVSVRNP--------KATANEPPKTFTFDAVFDPNSKQLDVYDET 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 133 IMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGT---EENMGILPRTLNVLFDSlqerlytkmnlkphrsreylrlsseqe 209
Cdd:cd01371 70 ARPLVDSVLEGYNGTIFAYGQTGTGKTYTMEGKredPELRGIIPNSFAHIFGH--------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 210 keeIAGKSallrqikevtmhndgddtlygsltnslnisefeesikdceqaslnmaNDIKFSVWVSFFEIYNEYIYDLFvp 289
Cdd:cd01371 123 ---IARSQ-----------------------------------------------NNQQFLVRVSYLEIYNEEIRDLL-- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 290 vsSKFQKRKM-LRLSQDVKGYsfIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKIlqiEDSEM- 367
Cdd:cd01371 151 --GKDQTKRLeLKERPDTGVY--VKDLSMFVVKNADEMEHVMNLGNKNRSVGATNMNEDSSRSHAIFTITI---ECSEKg 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 368 ---SRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSeKSkfqQHVPFRESKLTHYFQSFF 444
Cdd:cd01371 224 edgENHIRVGKLNLVDLAGSERQSKTGATGERLKEATKINLSLSALGNVISALVDG-KS---THIPYRDSKLTRLLQDSL 299
|
410 420 430
....*....|....*....|....*....|....*
gi 1622966431 445 NGKGKICMIVNISQCYLAYDETLNVLKFSAIAQKV 479
Cdd:cd01371 300 GGNSKTVMCANIGPADYNYDETLSTLRYANRAKNI 334
|
|
| KISc_KLP2_like |
cd01373 |
Kinesin motor domain, KIF15-like subgroup; Kinesin motor domain, KIF15-like subgroup. Members ... |
57-472 |
3.34e-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: 179.24 E-value: 3.34e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 57 DYLQVCLRIRPFTQSEKEHESEGCVHILDSQTVVLkepqcilgrlseksSGQMAQKFSFSKVFGPATTQKEFFQGCIMQP 136
Cdd:cd01373 1 DAVKVFVRIRPPAEREGDGEYGQCLKKLSSDTLVL--------------HSKPPKTFTFDHVADSNTNQESVFQSVGKPI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 137 VKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENM--------GILPRTLNVLFDSLQErlytkmnlkphrsreylrlssEQ 208
Cdd:cd01373 67 VESCLSGYNGTIFAYGQTGSGKTYTMWGPSESDnesphglrGVIPRIFEYLFSLIQR---------------------EK 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 209 EKEEiagksallrqikevtmhndgddtlygsltnslnisefeesikdceqaslnmaNDIKFSVWVSFFEIYNEYIYDLFV 288
Cdd:cd01373 126 EKAG----------------------------------------------------EGKSFLCKCSFLEIYNEQIYDLLD 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 289 PVSSKfqkrkmLRLSQDVKGYSFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKILQIEDSEMS 368
Cdd:cd01373 154 PASRN------LKLREDIKKGVYVENLVEEYVTSAEDVYQVLSKGWSNRKVAATSMNRESSRSHAVFTCTIESWEKKACF 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 369 RVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSKfQQHVPFRESKLTHYFQSFFNGKG 448
Cdd:cd01373 228 VNIRTSRLNLVDLAGSERQKDTHAEGVRLKEAGNINKSLSCLGHVINALVDVAHGK-QRHVCYRDSKLTFLLRDSLGGNA 306
|
410 420
....*....|....*....|....
gi 1622966431 449 KICMIVNISQCYLAYDETLNVLKF 472
Cdd:cd01373 307 KTAIIANVHPSSKCFGETLSTLRF 330
|
|
| KISc_KID_like |
cd01376 |
Kinesin motor domain, KIF22/Kid-like subgroup; Kinesin motor domain, KIF22/Kid-like subgroup. ... |
59-474 |
3.69e-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: 178.08 E-value: 3.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 59 LQVCLRIRPFTQSEKEHESEGCVHILDSQTVVLKEPQcilgrlseksSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVK 138
Cdd:cd01376 2 VRVAVRVRPFVDGTAGASDPSCVSGIDSCSVELADPR----------NHGETLKYQFDAFYGEESTQEDIYAREVQPIVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 139 DLLKGQSRLIFTYGLTNSGKTYTFQGTEENMGILPRTLnvlfdslqerlytkmnlkphrsREYLRLSSEQEKeeiagksa 218
Cdd:cd01376 72 HLLEGQNATVFAYGSTGAGKTFTMLGSPEQPGLMPLTV----------------------MDLLQMTRKEAW-------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 219 llrqikevtmhndgddtlygsltnslnisefeesikdceqaslnmandiKFSVWVSFFEIYNEYIYDLFVPvsskfqKRK 298
Cdd:cd01376 122 -------------------------------------------------ALSFTMSYLEIYQEKILDLLEP------ASK 146
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 299 MLRLSQDVKGYSFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKILQIEDSEMSRVIRvSELSL 378
Cdd:cd01376 147 ELVIREDKDGNILIPGLSSKPIKSMAEFEEAFLPASKNRTVAATRLNDNSSRSHAVLLIKVDQRERLAPFRQRT-GKLNL 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 379 CDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKskfqqHVPFRESKLTHYFQSFFNGKGKICMIVNISQ 458
Cdd:cd01376 226 IDLAGSEDNRRTGNEGIRLKESGAINSSLFVLSKVVNALNKNLP-----RIPYRDSKLTRLLQDSLGGGSRCIMVANIAP 300
|
410
....*....|....*.
gi 1622966431 459 CYLAYDETLNVLKFSA 474
Cdd:cd01376 301 ERTFYQDTLSTLNFAA 316
|
|
| KIP1 |
COG5059 |
Kinesin-like protein [Cytoskeleton]; |
105-598 |
1.56e-43 |
|
Kinesin-like protein [Cytoskeleton];
Pssm-ID: 227392 [Multi-domain] Cd Length: 568 Bit Score: 168.76 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 105 SSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENMGILPRTLNVLFDSLQ 184
Cdd:COG5059 50 LEKSKEGTYAFDKVFGPSATQEDVYEETIKPLIDSLLLGYNCTVFAYGQTGSGKTYTMSGTEEEPGIIPLSLKELFSKLE 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 185 ERLYTKmnlkphrsreylrlsseqekeeiagksallrqikevtmhndgddtlygsltnslnisefeesikdceqaslnma 264
Cdd:COG5059 130 DLSMTK-------------------------------------------------------------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 265 ndiKFSVWVSFFEIYNEYIYDLFVPvsSKFQKRKMLRLSQDVKgysfIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKL 344
Cdd:COG5059 136 ---DFAVSISYLEIYNEKIYDLLSP--NEESLNIREDSLLGVK----VAGLTEKHVSSKEEILDLLRKGEKNRTTASTEI 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 345 NNASSRSHSIFTIKiLQIEDSEMSrVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLKNSEKSK 424
Cdd:COG5059 207 NDESSRSHSIFQIE-LASKNKVSG-TSETSKLSLVDLAGSERAARTGNRGTRLKEGASINKSLLTLGNVINALGDKKKSG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 425 fqqHVPFRESKLTHYFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFSA----IAQKVCVP-------------DTLNS 487
Cdd:COG5059 285 ---HIPYRESKLTRLLQDSLGGNCNTRVICTISPSSNSFEETINTLKFASraksIKNKIQVNsssdssreieeikFDLSE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 488 SQEKLFGPVRSSQDVSLD---NNSNNKILNVKRATISWENSLEDLMededlveeLENSEETQNVETKLIDEDLDKTLEEN 564
Cdd:COG5059 362 DRSEIEILVFREQSQLSQsslSGIFAYMQSLKKETETLKSRIDLIM--------KSIISGTFERKKLLKEEGWKYKSTLQ 433
|
490 500 510
....*....|....*....|....*....|....*
gi 1622966431 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 |
3.88e-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: 3.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 61 VCLRIRPFTQSEKEHESEGCVHILDSQTVVLKEPQCILgRLSEKSSgqmAQKFSFSKVFGPATTQKEFFQGCIMQPVKDL 140
Cdd:cd01367 4 VCVRKRPLNKKEVAKKEIDVVSVPSKLTLIVHEPKLKV-DLTKYIE---NHTFRFDYVFDESSSNETVYRSTVKPLVPHI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 141 LKGQSRLIFTYGLTNSGKTYT----FQGTEENMGILprtlnvlfdslqerlytkmnlkphrsreylrlsseqekeEIAGK 216
Cdd:cd01367 80 FEGGKATCFAYGQTGSGKTYTmggdFSGQEESKGIY---------------------------------------ALAAR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 217 SaLLRQIKEVTMHNDgddtlygsltnslnisefeesikdceqaslnmandikFSVWVSFFEIYNEYIYDLFvpvsskfQK 296
Cdd:cd01367 121 D-VFRLLNKLPYKDN-------------------------------------LGVTVSFFEIYGGKVFDLL-------NR 155
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 297 RKMLRLSQDVKGYSFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTIKILQIEDSEMSrvirvSEL 376
Cdd:cd01367 156 KKRVRLREDGKGEVQVVGLTEKPVTSAEELLELIESGSSLRTTGQTSANSQSSRSHAILQIILRDRGTNKLH-----GKL 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 377 SLCDLAGSERTMKT-QNEGERLRETGNINTSLLTLGKCINVLKNSekskfQQHVPFRESKLTHYFQ-SFFNGKGKICMIV 454
Cdd:cd01367 231 SFVDLAGSERGADTsSADRQTRMEGAEINKSLLALKECIRALGQN-----KAHIPFRGSKLTQVLKdSFIGENSKTCMIA 305
|
410 420
....*....|....*....|.
gi 1622966431 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 ... |
108-474 |
3.47e-38 |
|
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: 146.96 E-value: 3.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 108 QMAQKFSFSKVFGPATtQKEFFQGCIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQGTEENM---GILPRTLNVLFDSLQ 184
Cdd:cd01375 45 QEDWSFKFDGVLHNAS-QELVYETVAKDVVSSALAGYNGTIFAYGQTGAGKTFTMTGGTENYkhrGIIPRALQQVFRMIE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 185 ERlYTKMnlkphrsreylrlsseqekeeiagksallrqikevtmhndgddtlygsltnslnisefeesikdceqaslnma 264
Cdd:cd01375 124 ER-PTKA------------------------------------------------------------------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 265 ndikFSVWVSFFEIYNEYIYDLFVPVSSKFQKRKMLRLSQDVKGYSFIRDLQWIQVSDSKEAYRLLKLGIKHQSVAFTKL 344
Cdd:cd01375 130 ----YTVHVSYLEIYNEQLYDLLSTLPYVGPSVTPMTILEDSPQNIFIKGLSLHLTSQEEEALSLLFLGETNRIIASHTM 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 345 NNASSRSHSIFTIKILQIEDSEMSRVIRVSELSLCDLAGSERTMKTQNEGERLRETGNINTSLLTLGKCINVLknSEKSK 424
Cdd:cd01375 206 NKNSSRSHCIFTIHLEAHSRTLSSEKYITSKLNLVDLAGSERLSKTGVEGQVLKEATYINKSLSFLEQAIIAL--SDKDR 283
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1622966431 425 fqQHVPFRESKLTHYFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFSA 474
Cdd:cd01375 284 --THVPFRQSKLTHVLRDSLGGNCNTVMVANIYGEAAQLEETLSTLRFAS 331
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
92-522 |
3.74e-33 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 140.84 E-value: 3.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 92 KEPQCILGRLSEKSSGQMAQKFSFSKVFGPATTQKEFFQGCIMQPVKDLLKGQSRLIFTYGLTNSGKTYTFQG-----TE 166
Cdd:PLN03188 113 EEGEMIVQKMSNDSLTINGQTFTFDSIADPESTQEDIFQLVGAPLVENCLAGFNSSVFAYGQTGSGKTYTMWGpanglLE 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 167 ENM-----GILPRTLNVLFDslqerlytkmnlkphrsreylRLSSEQEKeeiagksallrqikevtmHNDgddtlygslt 241
Cdd:PLN03188 193 EHLsgdqqGLTPRVFERLFA---------------------RINEEQIK------------------HAD---------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 242 nslnisefeesikdceqaslnmaNDIKFSVWVSFFEIYNEYIYDLFVPVsskfQKRKMLRlsQDVKGYSFIRDLQWIQVS 321
Cdd:PLN03188 224 -----------------------RQLKYQCRCSFLEIYNEQITDLLDPS----QKNLQIR--EDVKSGVYVENLTEEYVK 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 322 DSKEAYRLLKLGIKHQSVAFTKLNNASSRSHSIFTI----KILQIEDSEMSrvIRVSELSLCDLAGSERTMKTQNEGERL 397
Cdd:PLN03188 275 TMKDVTQLLIKGLSNRRTGATSINAESSRSHSVFTCvvesRCKSVADGLSS--FKTSRINLVDLAGSERQKLTGAAGDRL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 398 RETGNINTSLLTLGKCINVLKNSEKSKFQQHVPFRESKLTHYFQSFFNGKGKICMIVNISQCYLAYDETLNVLKFS---- 473
Cdd:PLN03188 353 KEAGNINRSLSQLGNLINILAEISQTGKQRHIPYRDSRLTFLLQESLGGNAKLAMVCAISPSQSCKSETFSTLRFAqrak 432
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1622966431 474 AIAQKVCVPDTLNSSQEKLFGPVRSSQD--VSLDNNSNNKILNVKRATISW 522
Cdd:PLN03188 433 AIKNKAVVNEVMQDDVNFLREVIRQLRDelQRVKANGNNPTNPNVAYSTAW 483
|
|
| RBD_KIF20B |
cd21786 |
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B ... |
600-655 |
1.45e-19 |
|
RAB6 binding domain (RBD) found in kinesin-like protein KIF20B, and similar proteins; KIF20B (also called cancer/testis antigen 90 (CT90), kinesin family member 20B, kinesin-related motor interacting with PIN1, or M-phase phosphoprotein 1 (MPP1)) is a plus-end-directed motor enzyme that is required for completion of cytokinesis. It is required for proper midbody organization and abscission in polarized cortical stem cells. KIF20B plays a role in the regulation of neuronal polarization by mediating the transport of specific cargos. It participates in the mobilization of SHTN1 (shootin 1) and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, KIF20B cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. KIF20B acts as an oncogene for promoting bladder cancer cell proliferation, apoptosis inhibition, and carcinogenic progression. This model corresponds to a conserved region in KIF20B that shows some sequence similarity to the RAB6 binding domain (RBD) of KIF20A. KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.
Pssm-ID: 409644 [Multi-domain] Cd Length: 56 Bit Score: 83.68 E-value: 1.45e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622966431 600 KIREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREET 655
Cdd:cd21786 1 KIREEVTQEFTELFSEMEKDYSERLEREREILEERAEKRLEIFKNLVNKTAKEEEE 56
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1067-1383 |
6.20e-17 |
|
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: 87.42 E-value: 6.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1067 IVKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQI----- 1141
Cdd:TIGR02168 661 ITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarlea 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1142 ------QHVVEGNRALSELTQGVTCYKAKIKELETILETQKVERshsAKLEQDILEKESVILKLERNLKELQAHLQDsvk 1215
Cdd:TIGR02168 741 eveqleERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI---EELEAQIEQLKEELKALREALDELRAELTL--- 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1216 ntkdLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLT 1295
Cdd:TIGR02168 815 ----LNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1296 DAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKV---EEAIQQYERACKDLNVK 1372
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSltlEEAEALENKIEDDEEEA 970
|
330
....*....|.
gi 1622966431 1373 EKIIEDMRMTL 1383
Cdd:TIGR02168 971 RRRLKRLENKI 981
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1124-1457 |
8.48e-17 |
|
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: 87.03 E-value: 8.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1124 QQLKEELqeKNASLDIQIQHVVEGNRALSELTQGVTCYKAKIKELETILETqkvershsakLEQDILEKESVILKLERNL 1203
Cdd:TIGR02168 216 KELKAEL--RELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE----------LEEKLEELRLEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1204 KELQAHLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRK 1283
Cdd:TIGR02168 284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1284 EEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYE 1363
Cdd:TIGR02168 364 EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1364 RACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLEtkNNQRSNKEHEDNTDVLGKL 1443
Cdd:TIGR02168 444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE--GFSEGVKALLKNQSGLSGI 521
|
330
....*....|....
gi 1622966431 1444 SNLQDELQESEQKY 1457
Cdd:TIGR02168 522 LGVLSELISVDEGY 535
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
575-1424 |
1.12e-16 |
|
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: 86.65 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 575 KLLDLIEDLKKKLIN-EKKEKLTLEFK-IREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVgKCDTR 652
Cdd:TIGR02168 190 RLEDILNELERQLKSlERQAEKAERYKeLKAELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQ-ELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 653 EETTKDvcaTIVETEEThnyvgFEDIIDSLQDNVADI-KKQAEIAHLyiaslpdpQEAIACLELKFNQIKAELTKTKEEL 731
Cdd:TIGR02168 269 LEELRL---EVSELEEE-----IEELQKELYALANEIsRLEQQKQIL--------RERLANLERQLEELEAQLEELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 732 IKTKEELKKRENETDSLIQELETSNKKIITQNQRIQELINTIDQKEGIINEFQNLKSHMEKTFKcndkadtsslIINNKL 811
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA----------SLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 812 ICNEtvevpqdsktkicSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVQPNIAEnedirvLQKNNEGLKALL 891
Cdd:TIGR02168 403 ERLE-------------ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEE------LQEELERLEEAL 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 892 LTIENELKNEKEEKAELNKQIVRFQQElslsekknLTLSKEVQQIQSNYDIAIAELhvqkSKNQEQEEKIM--------- 962
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQAR--------LDSLERLQENLEGFSEGVKAL----LKNQSGLSGILgvlselisv 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 963 --KLSHEIETATRSITNNVsqikLMHTKIDQLRTFDSVSQISN-----IDLLNLRDLSNGSEEDNLPNTQLHLLGNDYLV 1035
Cdd:TIGR02168 532 deGYEAAIEAALGGRLQAV----VVENLNAAKKAIAFLKQNELgrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1036 SKQVKEYRI------------------QEPNRESSFHSSI----EAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAEVK 1093
Cdd:TIGR02168 608 VKFDPKLRKalsyllggvlvvddldnaLELAKKLRPGYRIvtldGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1094 GYKDENNRLKVEENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQI-----------QHVVEGNRALSELTQGVTCYK 1162
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLarleaeveqleERIAQLSKELTELEAEIEELE 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1163 AKIKELETILETQKVERshsAKLEQDILEKESVILKLERNLKELQAHLQDsvkntkdlsvkevkLKEEITQLTNNLQDMK 1242
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEI---EELEAQIEQLKEELKALREALDELRAELTL--------------LNEEAANLRERLESLE 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1243 HLLQLKEEEKETNRQETEKLKEELSAssactqhLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKI 1322
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIES-------LAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1323 NELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAiqqyerackdlNVKEKIIEDMRMTleeqeqtqveqdqvLEAKLE 1402
Cdd:TIGR02168 904 RELESKRSELRRELEELREKLAQLELRLEGLEVRID-----------NLQERLSEEYSLT--------------LEEAEA 958
|
890 900
....*....|....*....|..
gi 1622966431 1403 EVERLATELEKWKEKCNDLETK 1424
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENK 980
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
629-1553 |
8.95e-15 |
|
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: 80.49 E-value: 8.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 629 EILEENAERRLAIFKDLVG--KCDTR-EETTKDvcatIVETEEthNYVGFEDIIDSLQDNVADIKKQAEIAHLYI---AS 702
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAGisKYKERrKETERK----LERTRE--NLDRLEDILNELERQLKSLERQAEKAERYKelkAE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 703 LPDPQEAIACLELK-FNQIKAELTKTKEELIKTKEELKKRENETDSLIQELETsnkkiitqnqRIQELINTIDQKEGIIN 781
Cdd:TIGR02168 222 LRELELALLVLRLEeLREELEELQEELKEAEEELEELTAELQELEEKLEELRL----------EVSELEEEIEELQKELY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 782 EFQNLKSHMEKtfkcndkadtssliinnklicnetvevpqdsKTKICSERKRVNENELQQdeppakkgsihVSSAITEDQ 861
Cdd:TIGR02168 292 ALANEISRLEQ-------------------------------QKQILRERLANLERQLEE-----------LEAQLEELE 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 862 KKSEEVQPNIAENED-IRVLQKNNEGLKALLLTIENELKNEKEEKAELNKQIVRFQQELSLSEKKNLTLSKEVQ------ 934
Cdd:TIGR02168 330 SKLDELAEELAELEEkLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIErlearl 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 935 -QIQSNYDIAIAELHVQKSKNQEQEEKimKLSHEIETATRSITNNVSQIKLMHTKIDQLRtfDSVSQISNIDLLNLRDL- 1012
Cdd:TIGR02168 410 eRLEDRRERLQQEIEELLKKLEEAELK--ELQAELEELEEELEELQEELERLEEALEELR--EELEEAEQALDAAERELa 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1013 SNGSEEDNLPNTQLHLLGNDYLVsKQVKEYRIQEPNRESSFHSSI--EAIWEECKEIVKSSSKKSHQIQELEQQIEKLQA 1090
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEGV-KALLKNQSGLSGILGVLSELIsvDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAF 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1091 EVKGykdENNRLKVEENEHKNQDDLLKEKETLIQQLKEELQeknaSLDIQIQHVVEGNRALSELTQGVTCykakIKELET 1170
Cdd:TIGR02168 565 LKQN---ELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLG----VAKDLVKFDPKLRKALSYLLGGVLV----VDDLDN 633
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1171 ILETQKVERSH--------------------SAKLEQDILEKESVILKLERNLKELQahlqdsvkntkdlsvkevklkEE 1230
Cdd:TIGR02168 634 ALELAKKLRPGyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELE---------------------EK 692
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1231 ITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSV 1310
Cdd:TIGR02168 693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1311 MRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQ--YERACKDLNVKEKIIEDMRMTleeqeq 1388
Cdd:TIGR02168 773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRerLESLERRIAATERRLEDLEEQ------ 846
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1389 tqveqdqvLEAKLEEVERLATELEKWKEKCNDLEtknnqrsnKEHEDNTDVLGKLSNLQDELQESEQKYNADRKKWLEEK 1468
Cdd:TIGR02168 847 --------IEELSEDIESLAAEIEELEELIEELE--------SELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1469 MMLITQAKEAENIRNKEMKKYAE---DRERFLKQQNEVEILTAQLTEK-----DSDLQKWREErdqlVAALEIQLKALIS 1540
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGlevRIDNLQERLSEEYSLTLEEAEAlenkiEDDEEEARRR----LKRLENKIKELGP 986
|
970
....*....|...
gi 1622966431 1541 SNVQKDNEIEQLK 1553
Cdd:TIGR02168 987 VNLAAIEEYEELK 999
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1078-1358 |
2.53e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 2.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1078 IQELEQQIEKL--QAEV----KGYKDENNRLKVE---------ENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQIQ 1142
Cdd:COG1196 195 LGELERQLEPLerQAEKaeryRELKEELKELEAEllllklrelEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1143 HVVEGNRALSELTQGVTCYKAKIKELETILETQKVERSHsakLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSV 1222
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE---LEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1223 KEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIE 1302
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622966431 1303 QVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEA 1358
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1079-1363 |
3.43e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.44 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1079 QELEQQIEKLQAEVKGYKDENNRLKVE---------ENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQIQHVVEGNR 1149
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEeleaeleelEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1150 ALSELTQGVTCYKAKIKELETILETQKVERshsAKLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKE 1229
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEEL---AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1230 EITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVS 1309
Cdd:COG1196 373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1622966431 1310 VMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQkvEEAIQQYE 1363
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL--LEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
910-1571 |
7.57e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.94 E-value: 7.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 910 KQIVRFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSHEIETATRSITNNVSQIKLMHTKI 989
Cdd:TIGR02168 232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 990 DQLRtfDSVSQISNIDLLNLRDLSNGSEEDNLPNTQLHLLGNDY-LVSKQVKEYRIQEPNRESSFHSS---IEAIWEECK 1065
Cdd:TIGR02168 312 ANLE--RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELeSLEAELEELEAELEELESRLEELeeqLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1066 EIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRL--KVEENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQIQH 1143
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1144 VVEGNRALSELTQGVTCYKAKIKELETILE----------TQKVERSHSAKLEQDILEKESVILKLERNLKE-LQAHLQD 1212
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQEnlegfsegvkALLKNQSGLSGILGVLSELISVDEGYEAAIEAaLGGRLQA 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1213 SVKNTKDLSVKEVK-LKE---------EITQLTNNLQDMKHLLQLKEEEK-----------------------------E 1253
Cdd:TIGR02168 550 VVVENLNAAKKAIAfLKQnelgrvtflPLDSIKGTEIQGNDREILKNIEGflgvakdlvkfdpklrkalsyllggvlvvD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1254 TNRQETEKLKEELSASSACTQ------------------------------HLKADLQRKEEDYAELKEKLTDAKKQIEQ 1303
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRIVTLdgdlvrpggvitggsaktnssilerrreieELEEKIEELEEKIAELEKALAELRKELEE 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1304 VQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKI--IEDMRM 1381
Cdd:TIGR02168 710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEaeIEELEA 789
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1382 TLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLE------TKNNQRSNKEHEDNTDVLGKLSNLQDELQESEQ 1455
Cdd:TIGR02168 790 QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLErriaatERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1456 KYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFLKQQNEVEILTAQLTEKDSDLQKWREERDQLVAAL---- 1531
Cdd:TIGR02168 870 ELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLseey 949
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1622966431 1532 EIQLKALISSNVQKDNEIEQLKRiisETSKIETQIMDIKP 1571
Cdd:TIGR02168 950 SLTLEEAEALENKIEDDEEEARR---RLKRLENKIKELGP 986
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1049-1570 |
1.00e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.56 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1049 RESSFHSSIEAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAEVKGY---KDENNRLKVE----ENEHKNQDDLLKEKET 1121
Cdd:PRK03918 187 RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelKEEIEELEKEleslEGSKRKLEEKIRELEE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1122 LIQQLKEELQ--EKNASLDIQIQHVVEGNRALSELTQGvtcYKAKIKELETILETQKVERSHSAKLEQDILEKESVILKL 1199
Cdd:PRK03918 267 RIEELKKEIEelEEKVKELKELKEKAEEYIKLSEFYEE---YLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEEL 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1200 ERNLKELQ---AHLQDSVKNTKDLSVKEVKLKEEITQLTN-NLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQH 1275
Cdd:PRK03918 344 KKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRLTGlTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1276 LKADLQR---------------KEEDYAELKEKLTdakKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQ 1340
Cdd:PRK03918 424 LKKAIEElkkakgkcpvcgrelTEEHRKELLEEYT---AELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1341 rTIQQLKE------QLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDqVLEAKLEEVERLATELEKW 1414
Cdd:PRK03918 501 -LAEQLKEleeklkKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLA-ELEKKLDELEEELAELLKE 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1415 KEKCNDLETKNNQRSNKEHEDNTDVLGKLSNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNK--EMKK---- 1488
Cdd:PRK03918 579 LEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKEleELEKkyse 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1489 --YAEDRERFLKQQNEVEILTAQLTEkdsdLQKWREERDQLVAALEIQLKALissnVQKDNEIEQLKRIISETSKIETQI 1566
Cdd:PRK03918 659 eeYEELREEYLELSRELAGLRAELEE----LEKRREEIKKTLEKLKEELEER----EKAKKELEKLEKALERVEELREKV 730
|
....
gi 1622966431 1567 MDIK 1570
Cdd:PRK03918 731 KKYK 734
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1053-1365 |
1.35e-12 |
|
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: 73.18 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1053 FHSSIEAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAE---VKGYKDENNRL-KVEENEH-KNQDDLLKEKETL----- 1122
Cdd:TIGR02169 168 FDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRErekAERYQALLKEKrEYEGYELlKEKEALERQKEAIerqla 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1123 -----IQQLKEELQEKNASLDIQIQHVVEGNRALSELTQG-VTCYKAKIKELETilETQKVERSHSAK-LEQDILEKESV 1195
Cdd:TIGR02169 248 sleeeLEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEeQLRVKEKIGELEA--EIASLERSIAEKeRELEDAEERLA 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1196 ILKLERNlkELQAHLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQET-------EKLKEELSA 1268
Cdd:TIGR02169 326 KLEAEID--KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELkdyreklEKLKREINE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1269 SSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKE 1348
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
330
....*....|....*..
gi 1622966431 1349 QLnnqkvEEAIQQYERA 1365
Cdd:TIGR02169 484 EL-----SKLQRELAEA 495
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1282-1558 |
4.44e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.51 E-value: 4.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1282 RKEEDYAELKEKLTdaKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN--NQKVEEAI 1359
Cdd:COG1196 210 EKAERYRELKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEelELELEEAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1360 QQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHEdntdv 1439
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE----- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1440 lgklsnLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKE------MKKYAEDRERFLKQQNEVEILTAQLTEK 1513
Cdd:COG1196 363 ------AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLeeleeaEEALLERLERLEEELEELEEALAELEEE 436
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1622966431 1514 DSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISE 1558
Cdd:COG1196 437 EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| RBD_KIF20A-like |
cd21744 |
RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; ... |
600-654 |
5.40e-12 |
|
RAB6 binding domain (RBD) found in kinesin-like proteins KIF20A, KIF20B, and similar proteins; This family includes kinesin-like proteins KIF20A and KIF20B. KIF20A (also called GG10_2, mitotic kinesin-like protein 2 (MKlp2), Rab6-interacting kinesin-like protein, or rabkinesin-6) is a mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1 (polo-like kinase 1), it is involved in recruitment of PLK1 to the central spindle. KIF20A interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. It may act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. KIF20A has a microtubule plus-end-directed motility. KIF20B (also called cancer/testis antigen 90 (CT90), kinesin family member 20B, kinesin-related motor interacting with PIN1, or M-phase phosphoprotein 1 (MPP1)) is a plus-end-directed motor enzyme that is required for completion of cytokinesis. It is required for proper midbody organization and abscission in polarized cortical stem cells. KIF20B plays a role in the regulation of neuronal polarization by mediating the transport of specific cargoes. It participates in the mobilization of SHTN1 and in the accumulation of PIP3 in the growth cone of primary hippocampal neurons in a tubulin and actin-dependent manner. In the developing telencephalon, KIF20B cooperates with SHTN1 to promote both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex. This model corresponds to a conserved domain in the KIF20A subfamily, that shows RAB6 binding ability and has been called the RAB6 binding domain (RBD). KIF20A-RBD is a dimer composed of two parallel alpha helices that form a right-handed coiled-coil additionally stabilized by an inter-helical cysteine bridge.
Pssm-ID: 409643 [Multi-domain] Cd Length: 56 Bit Score: 62.09 E-value: 5.40e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1622966431 600 KIREEVTQEFTQYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREE 654
Cdd:cd21744 1 RIREEVSEEFEEQFALMEEDYEERLENEKEILEERYEKRLEIRKELIKKLSAALE 55
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1057-1423 |
1.10e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1057 IEAIWEECKEIVkssSKKSHQIQELEQQIEKLQAEVKGYKDEnnrlkvEENEHKNQDDLLKEKEtliqQLKEELQEKNAS 1136
Cdd:PRK02224 368 LESELEEAREAV---EDRREEIEELEEEIEELRERFGDAPVD------LGNAEDFLEELREERD----ELREREAELEAT 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1137 LDiQIQHVVEGNRALSELTQGVTCykakikeletileTQKVERS-HSAKLEqdilEKESVILKLERNLKELQAHlQDSVK 1215
Cdd:PRK02224 435 LR-TARERVEEAEALLEAGKCPEC-------------GQPVEGSpHVETIE----EDRERVEELEAELEDLEEE-VEEVE 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1216 NTKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKE---EEKETNRQETEKLKEELSAS------SACTQHLKADlqRKEED 1286
Cdd:PRK02224 496 ERLERAEDLVEAEDRIERLEERREDLEELIAERRetiEEKRERAEELRERAAELEAEaeekreAAAEAEEEAE--EAREE 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1287 YAELKEKLTDAKKQIEQVQKEVSVM------RDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQ 1360
Cdd:PRK02224 574 VAELNSKLAELKERIESLERIRTLLaaiadaEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDEARIEEARE 653
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622966431 1361 QYERACKDL-NVKEKIIEdmrmtLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLET 1423
Cdd:PRK02224 654 DKERAEEYLeQVEEKLDE-----LREERDDLQAEIGAVENELEELEELRERREALENRVEALEA 712
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1062-1532 |
1.14e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1062 EECKEIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQ--------DDLLKEKE------TLIQQLK 1127
Cdd:PRK02224 237 DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERleeleeerDDLLAEAGlddadaEAVEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1128 EELQEKNASLDiqiQHVVEGNRALSELTQGVTCYKAKIKELEtilETQKVERSHSAKLEQDILEKESVILKLERNLKELQ 1207
Cdd:PRK02224 317 EELEDRDEELR---DRLEECRVAAQAHNEEAESLREDADDLE---ERAEELREEAAELESELEEAREAVEDRREEIEELE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1208 AHLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSA--CTQHLK-----ADL 1280
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCpeCGQPVEgsphvETI 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1281 QRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRiKINELEKKKNQCSQELDMKQRTIQQLKEQ---LNNQKVE- 1356
Cdd:PRK02224 471 EEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED-RIERLEERREDLEELIAERRETIEEKRERaeeLRERAAEl 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1357 --EAIQQYERACKdlnvKEKIIEDMRMTLEEQEQTQVEqdqvLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEhE 1434
Cdd:PRK02224 550 eaEAEEKREAAAE----AEEEAEEAREEVAELNSKLAE----LKERIESLERIRTLLAAIADAEDEIERLREKREALA-E 620
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1435 DNTDVLGKLSNLQDELQESEQKYNADRkkwleekmmlITQAKeaenirnkemkkyaEDRERFLKQQNEVEILTAQLTEKD 1514
Cdd:PRK02224 621 LNDERRERLAEKRERKRELEAEFDEAR----------IEEAR--------------EDKERAEEYLEQVEEKLDELREER 676
|
490 500 510
....*....|....*....|....*....|..
gi 1622966431 1515 SDLQK--------------WREERDQLVAALE 1532
Cdd:PRK02224 677 DDLQAeigaveneleeleeLRERREALENRVE 708
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1040-1504 |
2.27e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1040 KEYRIQEpnRESSFHSSIEAIWEECKEIvkssSKKSHQIQELEQQIEKLQ---AEVKGYKDENNRLKVEENEHKNQDDLL 1116
Cdd:PRK03918 308 ELREIEK--RLSRLEEEINGIEERIKEL----EEKEERLEELKKKLKELEkrlEELEERHELYEEAKAKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1117 KEKEtlIQQLKEELQE-KNASLDIQiqhvvegnRALSELTQGVTCYKAKIKELETILETQKvershSAKLEQDILEKESV 1195
Cdd:PRK03918 382 TGLT--PEKLEKELEElEKAKEEIE--------EEISKITARIGELKKEIKELKKAIEELK-----KAKGKCPVCGRELT 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1196 ILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETnrqetEKLKEELSassactQH 1275
Cdd:PRK03918 447 EEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQL-----KELEEKLK------KY 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1276 LKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSvmrdeekllriKINELEKKKNQCSQELDMKQRTIQQLKEQLNN--- 1352
Cdd:PRK03918 516 NLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELE-----------KLEELKKKLAELEKKLDELEEELAELLKELEElgf 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1353 ---QKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEqdqvLEAKLEEVERLATELEKWKEKCNDLETKNNQRS 1429
Cdd:PRK03918 585 esvEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEE----LDKAFEELAETEKRLEELRKELEELEKKYSEEE 660
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622966431 1430 NKEHEDNTDVLGK-LSNLQDELQESEQKYN---ADRKKWLEEKMMLITQAKEAENIrNKEMKKYAEDRERFLKQQNEVE 1504
Cdd:PRK03918 661 YEELREEYLELSReLAGLRAELEELEKRREeikKTLEKLKEELEEREKAKKELEKL-EKALERVEELREKVKKYKALLK 738
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1124-1412 |
3.03e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.81 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1124 QQLKEELQEKNASLdiqiqHVVEGNRALSELTQgvtcYKAKIKELETILETQKVERshsAKLEQDILEKESVILKLERNL 1203
Cdd:COG1196 216 RELKEELKELEAEL-----LLLKLRELEAELEE----LEAELEELEAELEELEAEL---AELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1204 KELQAHLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRK 1283
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1284 EEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQL--NNQKVEEAIQQ 1361
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALaeLEEEEEEEEEA 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1622966431 1362 YERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELE 1412
Cdd:COG1196 444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1077-1538 |
4.92e-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: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1077 QIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQddlLKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRALSELTQ 1156
Cdd:COG1196 317 RLEELEEELAELEEELEELEEELEELEEELEEAEEE---LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1157 GVTCYKAKIKELETILETQKVERshsAKLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQLTN 1236
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERL---ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1237 NLQDMKHLLQLKEEEKETNRQETEKLKE-----ELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQV--QKEVS 1309
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEaeadyEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaAALQN 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1310 VMRDEEKLLRIKINELEKKKNQCSQELDM-KQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIED---MRMTLEE 1385
Cdd:COG1196 551 IVVEDDEVAAAAIEYLKAAKAGRATFLPLdKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllGRTLVAA 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1386 QEQTQVEQDQVLEAKLEEVERLATELEKWKEKcndLETKNNQRSNKEHEDNTDVLGKLSNLQDELQESEQKYNADRKKWL 1465
Cdd:COG1196 631 RLEAALRRAVTLAGRLREVTLEGEGGSAGGSL---TGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEER 707
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622966431 1466 EEKMMLITQAKEAENIRNKEMKKYAEDRERFLKQQNEVEILTAQLTEKDSDLQKWREERDQLvAALEIQLKAL 1538
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL-ERLEREIEAL 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1080-1423 |
6.64e-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: 67.79 E-value: 6.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1080 ELEQQIEKLQAEVKGYKDENNRLKVEENEHKNqddLLKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRALSELtqgvt 1159
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIEN---RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL----- 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1160 cyKAKIKELETILETQKVERshsAKLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSVKEVK-----LKEEITQL 1234
Cdd:TIGR02169 743 --EEDLSSLEQEIENVKSEL---KELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEeevsrIEARLREI 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1235 TNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDE 1314
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1315 EKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACkdlnvkEKIIEDMRMTLEEQEQTQVEQD 1394
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE------ELSLEDVQAELQRVEEEIRALE 971
|
330 340
....*....|....*....|....*....
gi 1622966431 1395 QVLEAKLEEVERLATELEKWKEKCNDLET 1423
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDELKEKRAKLEE 1000
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
708-1513 |
1.38e-10 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 66.53 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 708 EAIACLELKFNQIKAELTKTKEELIKTKEELKKRENETDSLIQELETSNKKIITQNQRIQELINTIDQKEGIINEFQNLK 787
Cdd:pfam02463 205 QAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQ 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 788 SHM--EKTFKCNDKADTSSLIINNKLICNETVEVPQDSKTKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSE 865
Cdd:pfam02463 285 EEElkLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 866 EVQPNIAENEDIRVLQKNNEGLKALLLTIENELKNEKEEKAELNKQIVRFQQELSLSEKKNLTLSKEVQQIQSnyDIAIA 945
Cdd:pfam02463 365 QEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE--SIELK 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 946 ELHVQKSKNQEQEEKIMKLSHEIETATRSITNNVSQIKLMHTKIDQLRtfdsvsQISNIDLLNLRDLSNGSEEDNLPNTQ 1025
Cdd:pfam02463 443 QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL------SRQKLEERSQKESKARSGLKVLLALI 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1026 LHLLGNDyLVSKQVKEYRIQEPNRESSFHSSIEAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVE 1105
Cdd:pfam02463 517 KDGVGGR-IISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIA 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1106 ENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQIQHVV----------EGNRALSELTQGVTCYKAKIKELETILETQ 1175
Cdd:pfam02463 596 VLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTklkesakakeSGLRKGVSLEEGLAEKSEVKASLSELTKEL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1176 KVERSHSAKLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETN 1255
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKS 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1256 RQETEKLKEELSASSactqhLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQE 1335
Cdd:pfam02463 756 RLKKEEKEEEKSELS-----LKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1336 LDMKQRTIQQLKEQLNNQKvEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWK 1415
Cdd:pfam02463 831 KEEELEELALELKEEQKLE-KLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKL 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1416 EKCNDLETKNNQRSNKEHEDNTDVLGKLSNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRER 1495
Cdd:pfam02463 910 NLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989
|
810
....*....|....*...
gi 1622966431 1496 FLKQQNEVEILTAQLTEK 1513
Cdd:pfam02463 990 YNKDELEKERLEEEKKKL 1007
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
934-1532 |
1.99e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 934 QQIQSNYDIAIAELHVQKSKNQEQEEKimKLSHEIETATRSITNNVSQIKLMHTKIDQLRTfdsvsqisniDLLNLRDLS 1013
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELE--ELEAELEELEAELEELEAELAELEAELEELRL----------ELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1014 NgseednlpntqlhllgndylvSKQVKEYRIQepnressfhSSIEAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAEVK 1093
Cdd:COG1196 284 E---------------------EAQAEEYELL---------AELARLEQDIARLEERRRELEERLEELEEELAELEEELE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1094 GYKDENNRLKVEENEHKNQddlLKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRALSELTQGVTCYKAKIKELETILE 1173
Cdd:COG1196 334 ELEEELEELEEELEEAEEE---LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1174 TQKVERshsAKLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKE 1253
Cdd:COG1196 411 ALLERL---ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1254 TNRQETEKLKE-----ELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQV--QKEVSVMRDEEKLLRIKINELE 1326
Cdd:COG1196 488 EAAARLLLLLEaeadyEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaAALQNIVVEDDEVAAAAIEYLK 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1327 KKKNQCSQELDM-KQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIED---MRMTLEEQEQTQVEQDQVLEAKLE 1402
Cdd:COG1196 568 AAKAGRATFLPLdKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDtllGRTLVAARLEAALRRAVTLAGRLR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1403 EVERLATELEKWKEKCNDLETKNNQRSNKEHEDNTDVLGKLSNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIR 1482
Cdd:COG1196 648 EVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1483 NKEMKKYAEDRERFLKQQNEVEILTAQLTEKDSDLQKWREERDQLVAALE 1532
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1073-1570 |
3.68e-10 |
|
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: 65.04 E-value: 3.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1073 KKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQddlLKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRALS 1152
Cdd:TIGR04523 208 KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTE---ISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIK 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1153 ELTQGVTCYKAKIKEL--ETILETQKVERSHSAKLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEE 1230
Cdd:TIGR04523 285 ELEKQLNQLKSEISDLnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1231 ITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSV 1310
Cdd:TIGR04523 365 LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1311 MRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEeaIQQYERACKDLNVKEKIIEdmrmtleeqeqtq 1390
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE--LKSKEKELKKLNEEKKELE------------- 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1391 veqdqvleaklEEVERLATELEKWKEKCNDLETKNNQRSNKehedntdvlgkLSNLQDELQESEQKYNADrkkwleekmm 1470
Cdd:TIGR04523 510 -----------EKVKDLTKKISSLKEKIEKLESEKKEKESK-----------ISDLEDELNKDDFELKKE---------- 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1471 litQAKEAENIRNKEMKKYAEDRERFLKQQNEVEILTAQLTEKDSDLQKWREERDQLVAALEiqlkalissnvqkdneiE 1550
Cdd:TIGR04523 558 ---NLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE-----------------K 617
|
490 500
....*....|....*....|
gi 1622966431 1551 QLKRIISETSKIETQIMDIK 1570
Cdd:TIGR04523 618 ELEKAKKENEKLSSIIKNIK 637
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1077-1553 |
7.40e-10 |
|
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: 64.22 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1077 QIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQddllKEKETLIQQLKEELQEKNASLDIQIQHVvEGNRALSELTQ 1156
Cdd:TIGR00618 450 TAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQE----TRKKAVVLARLLELQEEPCPLCGSCIHP-NPARQDIDNPG 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1157 GVTCykakikELETILETQKvershsaKLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQLTN 1236
Cdd:TIGR00618 525 PLTR------RMQRGEQTYA-------QLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1237 NLQDMKHLLQLKEEEKETNRQETEKLKEELsassactqHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEK 1316
Cdd:TIGR00618 592 ITVRLQDLTEKLSEAEDMLACEQHALLRKL--------QPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREH 663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1317 LLRIKINELEKkknqcSQELDMKQRTIQQLKEQLNNQKveEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQV 1396
Cdd:TIGR00618 664 ALSIRVLPKEL-----LASRQLALQKMQSEKEQLTYWK--EMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAA 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1397 LEAKLEEVERLATELEKWKEKCNDLEtknNQRSNKEHEDNTDVLGKLSNLQDELQESEQKYNADRKKWLEEKMMLITQAK 1476
Cdd:TIGR00618 737 REDALNQSLKELMHQARTVLKARTEA---HFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIP 813
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622966431 1477 EAENIRNKEMKKYAEDRERFLkqqNEVEILTAQLTEKDSDLQKWREERDQLVAALEIQLKalISSNVQKDNEIEQLK 1553
Cdd:TIGR00618 814 SDEDILNLQCETLVQEEEQFL---SRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAK--IIQLSDKLNGINQIK 885
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1062-1553 |
1.60e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 63.24 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1062 EECKEIVKSSSKKSHQIQELEQQIEKlQAEVKGYKDENNRLKVEENEHKNQDDLLKEKETliQQLKEELQEKnasldiqi 1141
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKK-AAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA--KKKADAAKKK-------- 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1142 qhvVEGNRALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQdILEKESVILKLERNLKELQAHLQDSVKNTKDLS 1221
Cdd:PTZ00121 1387 ---AEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE-KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEA 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1222 VKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETnRQETEKLKEELSASSACTQHLKADLQRKEEDY--AELKEKLTDAKK 1299
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA-KKKADEAKKAAEAKKKADEAKKAEEAKKADEAkkAEEAKKADEAKK 1541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1300 QiEQVQKEVSVMRDEEKLLRIKINELEKKKNQcSQELDMKQRTIQQLKeQLNNQKVEEAIQQYERACKDLNVKEKIIEDM 1379
Cdd:PTZ00121 1542 A-EEKKKADELKKAEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAK-KAEEARIEEVMKLYEEEKKMKAEEAKKAEEA 1618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1380 RMTLEEQEQTQVEQDQV--LEAKLEEVERLATELEKWKEkcnDLETKNNQRSNKEHEDNTdvlgKLSNLQDELQESEQKY 1457
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVeqLKKKEAEEKKKAEELKKAEE---ENKIKAAEEAKKAEEDKK----KAEEAKKAEEDEKKAA 1691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1458 NADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERF----LKQQNEVEILTAQLTEKDSD----LQKWREERDQLVA 1529
Cdd:PTZ00121 1692 EALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIkaeeAKKEAEEDKKKAEEAKKDEEekkkIAHLKKEEEKKAE 1771
|
490 500
....*....|....*....|....
gi 1622966431 1530 ALEIQLKALISSNVQKDNEIEQLK 1553
Cdd:PTZ00121 1772 EIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
740-1484 |
4.52e-09 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 740 KRENETDSLIQELETSNKKIITQNQRIQELINTIDQKEGIINEFQNLKSHMEKTFK-CNDKADTSSLIINNklICNETVE 818
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKdLNDKLKKNKDKINK--LNSDLSK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 819 VPQDSKTKIcsERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVqpnIAENEDIRVLQKNNEGLKALLLTIENEL 898
Cdd:TIGR04523 108 INSEIKNDK--EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKEL---EKLNNKYNDLKKQKEELENELNLLEKEK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 899 KNEKEEKAELNKQIVRFQQELSLSEKKNltlskevqQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSHEIETATRSITNN 978
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLELLLSNLKKKI--------QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQ 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 979 VSQIKLMHTKI-DQLRTFDSVSQISNIDLLNLRDlsngseednlpntQLHLLGNDYLVSKQVKEyriqePNRESSFHSSI 1057
Cdd:TIGR04523 255 LNQLKDEQNKIkKQLSEKQKELEQNNKKIKELEK-------------QLNQLKSEISDLNNQKE-----QDWNKELKSEL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1058 EAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEenehknqddlLKEKETLIQQLKEELQEknasl 1137
Cdd:TIGR04523 317 KNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE----------LEEKQNEIEKLKKENQS----- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1138 diqiqhvvegnralseltqgvtcYKAKIKELEtiletqkverSHSAKLEQDILEKESVILKLERNLKELQAHLQDSVKNT 1217
Cdd:TIGR04523 382 -----------------------YKQEIKNLE----------SQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1218 KDLSVKEVKLKEEITQLTNNLQDmkhllqlKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDA 1297
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSV-------KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1298 KKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQyerackdlnvKEKIIE 1377
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDE----------KNKEIE 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1378 DMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLEtKNNQRSNKEHEDNTDVLGKLSNLQDELQESEQKY 1457
Cdd:TIGR04523 572 ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLE-KELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQI 650
|
730 740
....*....|....*....|....*..
gi 1622966431 1458 NADRKKWLEEKMMLITQAKEAENIRNK 1484
Cdd:TIGR04523 651 KETIKEIRNKWPEIIKKIKESKTKIDD 677
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1276-1573 |
1.54e-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: 60.08 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1276 LKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKV 1355
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL--SSL 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1356 EEAIQQYERACKDLnvkEKIIEDMRMTLEEqeqtqveqdqvLEAKLEEVERLATElEKWKEKCNDLETKNNQRSNKEHED 1435
Cdd:TIGR02169 750 EQEIENVKSELKEL---EARIEELEEDLHK-----------LEEALNDLEARLSH-SRIPEIQAELSKLEEEVSRIEARL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1436 NtDVLGKLSNLQDELQ--ESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFLKQ-QNEVEILTAQLTE 1512
Cdd:TIGR02169 815 R-EIEQKLNRLTLEKEylEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDlESRLGDLKKERDE 893
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622966431 1513 KDSDLQKWREERDQLVAALEI------QLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIKPRC 1573
Cdd:TIGR02169 894 LEAQLRELERKIEELEAQIEKkrkrlsELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAEL 960
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1062-1513 |
2.34e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.38 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1062 EECKEIVKSSSKKSHQIQELEQQIEKLQAEVKG----------YKDENNRLKVEENEHKNQDDLLKEKETLIQQLKEELQ 1131
Cdd:PTZ00121 1414 AAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAdeakkkaeeaKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAE 1493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1132 EKNASLDiQIQHVVEGNRALSELTQGVTCYKAKikELETILETQKVERSHSA--KLEQDILEKESVILKLERNLKELQAH 1209
Cdd:PTZ00121 1494 EAKKKAD-EAKKAAEAKKKADEAKKAEEAKKAD--EAKKAEEAKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAK 1570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1210 LQDSVKN-----TKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEE-----KETNRQETEKLKEELSASSACTQHLKAD 1279
Cdd:PTZ00121 1571 KAEEDKNmalrkAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikaEELKKAEEEKKKVEQLKKKEAEEKKKAE 1650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1280 LQRKEEDY-----AELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINElEKKKNQCSQELDMKQRTIQQLK--EQLNN 1352
Cdd:PTZ00121 1651 ELKKAEEEnkikaAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEE-AKKAEELKKKEAEEKKKAEELKkaEEENK 1729
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1353 QKVEEAIQQ-------YERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKN 1425
Cdd:PTZ00121 1730 IKAEEAKKEaeedkkkAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAN 1809
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1426 NQRSNKEhedNTDVLgklsNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAED--RERFLKQQNEV 1503
Cdd:PTZ00121 1810 IIEGGKE---GNLVI----NDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADfnKEKDLKEDDEE 1882
|
490
....*....|
gi 1622966431 1504 EILTAQLTEK 1513
Cdd:PTZ00121 1883 EIEEADEIEK 1892
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1198-1566 |
2.49e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1198 KLERNLKELQAHLQDSVKNTKDLSvkevKLKEEITQLTNNLQDMKHLLQLKEEEKE--TNRQETEKLKEELSASSACTQH 1275
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1276 LKA---DLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEE--------KLLRIKINELEKKKNQCSQELDMKQRTIQ 1344
Cdd:COG4717 151 LEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeelEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1345 QLKEQLNNQKVEEAIQQYER-------------ACKDLNVKEKIIEDMRMT----LEEQEQTQVEQDQVLEAKLEEVERL 1407
Cdd:COG4717 231 QLENELEAAALEERLKEARLllliaaallallgLGGSLLSLILTIAGVLFLvlglLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1408 AT----ELEKWKEKCNDLETKNNQrSNKEHEDNTDVLGKLSNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRN 1483
Cdd:COG4717 311 PAleelEEEELEELLAALGLPPDL-SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRA 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1484 KemkkyAEDRERFLKQQNEVEILTAQLTEKDSDLQKWREERDqlvaalEIQLKALISSNVQKDNEI-EQLKRIISETSKI 1562
Cdd:COG4717 390 A-----LEQAEEYQELKEELEELEEQLEELLGELEELLEALD------EEELEEELEELEEELEELeEELEELREELAEL 458
|
....
gi 1622966431 1563 ETQI 1566
Cdd:COG4717 459 EAEL 462
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1041-1600 |
3.17e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 59.00 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1041 EYRIQEPNRESSFHSSIEAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRlKVEENEHKNQDdllkeKE 1120
Cdd:PTZ00121 1080 DFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR-KAEEARKAEDA-----KR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1121 TLIQQLKEELQEKNASLDIQIQHVVEGNRALSELTQGVTCYKA----------------------KIKELETILETQKVE 1178
Cdd:PTZ00121 1154 VEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAedarkaeaarkaeeerkaeearKAEDAKKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1179 RSHSAKLEQDILEKE---SVILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQL--TNNLQDMKHLLQLKEEEKE 1253
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEErnnEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1254 TNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKllRIKINELEKKKNQCS 1333
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA--KKKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1334 QELDMKQRTIQQLKE-------QLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVER 1406
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKadelkkaAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1407 LATELEKWKEKCNDLETKNNQRSNKEHEDNTDVLGKLSNLQDELQESEQKYNADRKKWLEEKMMlITQAKEAENIRNKEM 1486
Cdd:PTZ00121 1472 ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK-ADEAKKAEEKKKADE 1550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1487 KKYAE-----DRERFLKQQNEVEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISSNVQKDNE----IEQLKRIIS 1557
Cdd:PTZ00121 1551 LKKAEelkkaEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakikAEELKKAEE 1630
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1622966431 1558 ETSKIETQIMDIKPRCISSADPDKLQTEPQLTSFEISRNKVED 1600
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
923-1364 |
5.50e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 923 EKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSHEIETATRSITNNVSQIKLMHTKIDQLRTFDSVSQIs 1002
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPL- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1003 nidllnLRDLSNGSEEDNLPNTQLHLLGNDYlvsKQVKEYRIQEPNRESSfhssIEAIWEECKEIVKSSS-KKSHQIQEL 1081
Cdd:COG4717 131 ------YQELEALEAELAELPERLEELEERL---EELRELEEELEELEAE----LAELQEELEELLEQLSlATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1082 EQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLLkEKETLIQQLKEELQEKN------------ASLDIQIQHVVEGNR 1149
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQL-ENELEAAALEERLKEARlllliaaallalLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1150 ALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDILEKESVILKLERNLKELQ-----AHLQDSVKNTKDLSVKE 1224
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLspeelLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1225 VKLKEEItQLTNNLQDMKHLLQLKE-------EEKETNRQETEKLKEEL-SASSACTQHLKADLQRKE-EDYAELKEKLT 1295
Cdd:COG4717 357 EELEEEL-QLEELEQEIAALLAEAGvedeeelRAALEQAEEYQELKEELeELEEQLEELLGELEELLEaLDEEELEEELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1296 DAKKQIEQVQKEVSVMRDEEKLLRIKINELEKkknqcSQELDMKQRTIQQLKEQLNN------------QKVEEAIQQYE 1363
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRElaeewaalklalELLEEAREEYR 510
|
.
gi 1622966431 1364 R 1364
Cdd:COG4717 511 E 511
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1288-1570 |
6.11e-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: 58.16 E-value: 6.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1288 AELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRtIQQLKEQLNNQKVEEAIQQYERACK 1367
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKE-KREYEGYELLKEKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1368 DLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLAT-ELEKWKEKCNDLETK--NNQRSNKEHEDNtdvlgkls 1444
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEiaSLERSIAEKERE-------- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1445 nlQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRErflkqqnEVEILTAQLTEKDSDLQKWREER 1524
Cdd:TIGR02169 317 --LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE-------ELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1622966431 1525 DQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIK 1570
Cdd:TIGR02169 388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1227-1493 |
8.31e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1227 LKEEITQLTNNLQDMkhllqlkEEEKETNRQETEKLKEELSASSACTQH---------LKADLQRKEEDYAELKE---KL 1294
Cdd:COG4913 615 LEAELAELEEELAEA-------EERLEALEAELDALQERREALQRLAEYswdeidvasAEREIAELEAELERLDAssdDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1295 TDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKE- 1373
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVEREl 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1374 -KIIEDMRMTLEEQeqtqveqdqvLEAKLEEVERLATE-LEKWKEKCNDLETKNnqrsnkehEDNTDVLGKLSNLQ-DEL 1450
Cdd:COG4913 768 rENLEERIDALRAR----------LNRAEEELERAMRAfNREWPAETADLDADL--------ESLPEYLALLDRLEeDGL 829
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1622966431 1451 QESEQKYNADRKKWLEEKM-MLITQAKEA-ENIR------NKEMKK--YAEDR 1493
Cdd:COG4913 830 PEYEERFKELLNENSIEFVaDLLSKLRRAiREIKeridplNDSLKRipFGPGR 882
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1077-1351 |
9.85e-08 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 57.23 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1077 QIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDL---LKEKETLIQQLKEELQEKNASLdIQIQHVVEgnRALSE 1153
Cdd:PRK11281 88 QLAQAPAKLRQAQAELEALKDDNDEETRETLSTLSLRQLesrLAQTLDQLQNAQNDLAEYNSQL-VSLQTQPE--RAQAA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1154 LTQGVTcykaKIKELETILETQKVERSHSAKLEQDILEKESVIL--KLERNLKELQAH--LQDSVKNTKDLsvkevkLKE 1229
Cdd:PRK11281 165 LYANSQ----RLQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLnaQNDLQRKSLEGNtqLQDLLQKQRDY------LTA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1230 EITQLTNNLQDmkhllqLKEEEKETNRQETEKLKEELsASSACTQHLKAD--LQRKEEDYAELKEKLtdakkqIEQVQKE 1307
Cdd:PRK11281 235 RIQRLEHQLQL------LQEAINSKRLTLSEKTVQEA-QSQDEAARIQANplVAQELEINLQLSQRL------LKATEKL 301
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1622966431 1308 VSVMRDEeklLRIKinelekkknqcsQELDMKQRTIQQLKEQLN 1351
Cdd:PRK11281 302 NTLTQQN---LRVK------------NWLDRLTQSERNIKEQIS 330
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1075-1309 |
1.02e-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: 56.31 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1075 SHQIQELEQQIEKLQAEVKgykDENNRLKVEENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQiqhvvegNRALSEL 1154
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIA---ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL-------EAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1155 TQgvtcykaKIKELETILETQKVE---------RSHSAKLEQDILEKESvILKLERNLKELQAHLQDSVKNTKDLSVKEV 1225
Cdd:COG4942 89 EK-------EIAELRAELEAQKEElaellralyRLGRQPPLALLLSPED-FLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1226 KLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQ 1305
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
....
gi 1622966431 1306 KEVS 1309
Cdd:COG4942 241 ERTP 244
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1077-1570 |
1.13e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 56.75 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1077 QIQELEQQIEKLQAEVKGYKDENNRLKvEENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRAL-SELT 1155
Cdd:pfam10174 186 RIAEAEMQLGHLEVLLDQKEKENIHLR-EELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLkTNGL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1156 QGVTCYKAKIKELETILETQKVERSHSAKLEQDILEKESVILKLERNLKELQAHLQDSVKNTkdlsvkEVkLKEEIT--- 1232
Cdd:pfam10174 265 LHTEDREEEIKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHI------EV-LKESLTake 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1233 QLTNNLQDMKHLLQLKEEEKETNRQETEK----LKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEV 1308
Cdd:pfam10174 338 QRAAILQTEVDALRLRLEEKESFLNKKTKqlqdLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1309 SVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQ--LNNQKVEEAIQQYERACKDL----NVKEKIIEDMRMT 1382
Cdd:pfam10174 418 AGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQreREDRERLEELESLKKENKDLkekvSALQPELTEKESS 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1383 LEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLET--KNNQRSNKEHEDNTDVLGKLSNLQDE----------- 1449
Cdd:pfam10174 498 LIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENqlKKAHNAEEAVRTNPEINDRIRLLEQEvarykeesgka 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1450 ----------LQESEQKYNADRKKWLEEKMMLITQAKE----AENIR---NKEMKKYAEDRERFLK---------QQNEV 1503
Cdd:pfam10174 578 qaeverllgiLREVENEKNDKDKKIAELESLTLRQMKEqnkkVANIKhgqQEMKKKGAQLLEEARRrednladnsQQLQL 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1504 EILTAQ---------------------LTEKDSDLQKWR-EERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSK 1561
Cdd:pfam10174 658 EELMGAlektrqeldatkarlsstqqsLAEKDGHLTNLRaERRKQLEEILEMKQEALLAAISEKDANIALLELSSSKKKK 737
|
....*....
gi 1622966431 1562 IETQIMDIK 1570
Cdd:pfam10174 738 TQEEVMALK 746
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1114-1563 |
1.51e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1114 DLLKEKETLIQQLKEELQEKNAsldiqiqhvvegnralSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQdilEKE 1193
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEEKEE----------------KDLHERLNGLESELAELDEEIERYEEQREQARETRD---EAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1194 SVILKLERNLKELQAHLQDSVKNTKDLSVKEVK---LKEEITQLTNNLQDMkhllqlkEEEKETNRQETEKLKEELSASS 1270
Cdd:PRK02224 241 EVLEEHEERREELETLEAEIEDLRETIAETEREreeLAEEVRDLRERLEEL-------EEERDDLLAEAGLDDADAEAVE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1271 ACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQL 1350
Cdd:PRK02224 314 ARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1351 nnqkvEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEqdqvLEAKLEEVERLATELEKWKE--KC----NDLETK 1424
Cdd:PRK02224 394 -----EELRERFGDAPVDLGNAEDFLEELREERDELREREAE----LEATLRTARERVEEAEALLEagKCpecgQPVEGS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1425 NNQRSNKEHEDntdvlgKLSNLQDELQESEQKyNADRKKWLEEKMMLITQAKEAENIRNKE---MKKYAEDRERFLKQQN 1501
Cdd:PRK02224 465 PHVETIEEDRE------RVEELEAELEDLEEE-VEEVEERLERAEDLVEAEDRIERLEERRedlEELIAERRETIEEKRE 537
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622966431 1502 EVEILTAQLTEKDSDLQKWREE----RDQLVAALEiQLKALISSNVQKDNEIEQLKRIISETSKIE 1563
Cdd:PRK02224 538 RAEELRERAAELEAEAEEKREAaaeaEEEAEEARE-EVAELNSKLAELKERIESLERIRTLLAAIA 602
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
537-1365 |
1.52e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.90 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 537 EELENSEETQNVETKLIDE------DLDKTLEENKAFISHEEKRKLLDLIEDLKKKLINEKKEKLTLEFKIREEVTQEFT 610
Cdd:pfam02463 173 EALKKLIEETENLAELIIDleelklQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 611 QYWAQREADFKETLLQEREILEENAERRLAIFKDLVGKCDTREETTKDVCATIVETEETHNYVG---------FEDIIDS 681
Cdd:pfam02463 253 IESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLkesekekkkAEKELKK 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 682 LQDNVADIKKQAEIAHLYIASLPDPQEAIACLELKFNQIKAELTKTKEELIKTKEELKKRENETDSLIQELETSNKKII- 760
Cdd:pfam02463 333 EKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLe 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 761 ---TQNQRIQELINTIDQKEGIINEFQNLKShmEKTFKCNDKADTSSLIINNKLICNETVEVPQDSKTKICSERKRVNEN 837
Cdd:pfam02463 413 larQLEDLLKEEKKEELEILEEEEESIELKQ--GKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 838 ELQQDEPPAKKGSIHVSSAITED-QKKSEEVQPNIAENEDIRVLQKNNEGLKALLLTIENELKNEKEEKAELNKQIVRFQ 916
Cdd:pfam02463 491 SRQKLEERSQKESKARSGLKVLLaLIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 917 QELSLSEKKNLTLSKEVQQIqsnyDIAIAELHVQKSKNQEQEEKIMKLSHEIETATRSITNNVSQIKLMHTKIDQLRTFD 996
Cdd:pfam02463 571 TELPLGARKLRLLIPKLKLP----LKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 997 SVSQISNIDLLNLRDLSNGSEEDNLPNTQLhllgndylvskqvkeyRIQEPNRESSFHSSIEAIWEECKEIVKSSSKKSH 1076
Cdd:pfam02463 647 GLRKGVSLEEGLAEKSEVKASLSELTKELL----------------EIQELQEKAESELAKEEILRRQLEIKKKEQREKE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1077 QIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRALSELTQ 1156
Cdd:pfam02463 711 ELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEE 790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1157 GVTCYKAKIKELETILETQKVERSHSAKLEQDILEKESVI--LKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQL 1234
Cdd:pfam02463 791 EKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIkeEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQ 870
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1235 TNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTdakKQIEQVQKEVSVMRDE 1314
Cdd:pfam02463 871 ELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILL---KYEEEPEELLLEEADE 947
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1622966431 1315 EKLLRIKINELEKKKNQCSQ--ELDMKQRTIQQLKEQLNNQKVEEAIQQYERA 1365
Cdd:pfam02463 948 KEKEENNKEEEEERNKRLLLakEELGKVNLMAIEEFEEKEERYNKDELEKERL 1000
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1078-1567 |
1.71e-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: 56.52 E-value: 1.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1078 IQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRALSE---- 1153
Cdd:TIGR00618 302 VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLtqhi 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1154 --LTQGVTCYKAKIKELETILETQ-----KVERSHSAK--LEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSVKE 1224
Cdd:TIGR00618 382 htLQQQKTTLTQKLQSLCKELDILqreqaTIDTRTSAFrdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1225 VKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKAD-------------LQRKEEDYAELK 1291
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPArqdidnpgpltrrMQRGEQTYAQLE 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1292 E-------KLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQ--------------LKEQL 1350
Cdd:TIGR00618 542 TseedvyhQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKlseaedmlaceqhaLLRKL 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1351 NNQKVEEAIQQYERACKDLNVKEKII----------EDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCN- 1419
Cdd:TIGR00618 622 QPEQDLQDVRLHLQQCSQELALKLTAlhalqltltqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAq 701
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1420 ------DLETKNNQRSNKEHEDNTDVLGKLSNLQ---DELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYA 1490
Cdd:TIGR00618 702 cqtllrELETHIEEYDREFNEIENASSSLGSDLAareDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELS 781
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1491 EDRERFLKQQNEVEILTAQLTEKDSDLQKWREE-------RDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIE 1563
Cdd:TIGR00618 782 HLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSdedilnlQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQL 861
|
....
gi 1622966431 1564 TQIM 1567
Cdd:TIGR00618 862 AQLT 865
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1077-1310 |
1.97e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.18 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1077 QIQELEQQIEKLQAEVKGYKDENNRLKVEEnEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRALSELTQ 1156
Cdd:COG3206 183 QLPELRKELEEAEAALEEFRQKNGLVDLSE-EAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1157 GVTcykakIKELETILETQKVERshsAKLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSVKEVK-LKEEITQLT 1235
Cdd:COG3206 262 SPV-----IQQLRAQLAELEAEL---AELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEaLQAREASLQ 333
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622966431 1236 NNLQdmkhllQLKEEEKETNRQETEkLKEelsassactqhLKADLQRKEEDYAELKEKLTDAkkQIEQVQKEVSV 1310
Cdd:COG3206 334 AQLA------QLEARLAELPELEAE-LRR-----------LEREVEVARELYESLLQRLEEA--RLAEALTVGNV 388
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1072-1527 |
2.86e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1072 SKKSHQIQELEQQIEklQAEVKGYKDENNRLKVEENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRAL 1151
Cdd:PRK02224 183 SDQRGSLDQLKAQIE--EKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEI 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1152 SELTQGVT-------CYKAKIKELETILETQKVERSHS-AKLEQDILEKESVILKLErNLKELQAHLQDSVKntkDLSVK 1223
Cdd:PRK02224 261 EDLRETIAeterereELAEEVRDLRERLEELEEERDDLlAEAGLDDADAEAVEARRE-ELEDRDEELRDRLE---ECRVA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1224 EVKLKEEITQLTNNLQDMkhllqlkEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQ 1303
Cdd:PRK02224 337 AQAHNEEAESLREDADDL-------EERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1304 VQKEVSVMRDEEKLLRIKINELEKKKnqcsQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKdlnVKEKiiEDMRMTL 1383
Cdd:PRK02224 410 AEDFLEELREERDELREREAELEATL----RTARERVEEAEALLEAGKCPECGQPVEGSPHVET---IEED--RERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1384 EEQEQTQVEQDQVLEAKLEEVERL---ATELEKWKEKCNDLETKNNQRSNKEHEDNTdvlgKLSNLQDELQESEQKYNAD 1460
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLveaEDRIERLEERREDLEELIAERRETIEEKRE----RAEELRERAAELEAEAEEK 556
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622966431 1461 RKKwLEEKMMLITQAKEAENIRNKEMKKYAEDRERFlkqqNEVEILTAQLTEKDSDLQKWREERDQL 1527
Cdd:PRK02224 557 REA-AAEAEEEAEEAREEVAELNSKLAELKERIESL----ERIRTLLAAIADAEDEIERLREKREAL 618
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1079-1611 |
4.12e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 55.21 E-value: 4.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1079 QELEQQIEKLQAEVKGYKDENNRLK-------------------VEEN---EHKNQDDLLKEKETLIQQLKE-----ELQ 1131
Cdd:pfam10174 70 QHLQLTIQALQDELRAQRDLNQLLQqdfttspvdgedkfstpelTEENfrrLQSEHERQAKELFLLRKTLEEmelriETQ 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1132 EKN-ASLDIQIQHVVE----------GNRALSELTQGVTCYKAKIKELETILETQKVERSH--------------SAK-- 1184
Cdd:pfam10174 150 KQTlGARDESIKKLLEmlqskglpkkSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHlreelhrrnqlqpdPAKtk 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1185 -LEQDILEKESVILKLERNLKELQAHLQdSVKNTKDLSVKEvkLKEEITQL----------TNNLQDMKHLLQLKEEEKE 1253
Cdd:pfam10174 230 aLQTVIEMKDTKISSLERNIRDLEDEVQ-MLKTNGLLHTED--REEEIKQMevykshskfmKNKIDQLKQELSKKESELL 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1254 T--------------NRQETEKLKEELSAS---SACTQ----HLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMR 1312
Cdd:pfam10174 307 AlqtkletltnqnsdCKQHIEVLKESLTAKeqrAAILQtevdALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLK 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1313 DEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKE-----QLNNQKVEEAIQQYERACKDlnvKEKIIEDMRMTLEEQE 1387
Cdd:pfam10174 387 DMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKErvkslQTDSSNTDTALTTLEEALSE---KERIIERLKEQRERED 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1388 qtqveqdqvlEAKLEEVERLATELEKWKEKCNDLETKNNQRSN-----KEHEDNTDVLG-----KLSNLQDELQESEQ-- 1455
Cdd:pfam10174 464 ----------RERLEELESLKKENKDLKEKVSALQPELTEKESslidlKEHASSLASSGlkkdsKLKSLEIAVEQKKEec 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1456 -KYNADRKKWLEEKMMLITQAKEAENIRN--KEMKKYAEDRErflKQQNEVEILTAQLTEKDSDlqkwREERDQLVAALE 1532
Cdd:pfam10174 534 sKLENQLKKAHNAEEAVRTNPEINDRIRLleQEVARYKEESG---KAQAEVERLLGILREVENE----KNDKDKKIAELE 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1533 IQLKALISSNVQKdneIEQLKRIISETSKIETQIMD--IKPRCISSADPDKLQTEPQLTSFEISRNKVEDGSVVLDSCEV 1610
Cdd:pfam10174 607 SLTLRQMKEQNKK---VANIKHGQQEMKKKGAQLLEeaRRREDNLADNSQQLQLEELMGALEKTRQELDATKARLSSTQQ 683
|
.
gi 1622966431 1611 S 1611
Cdd:pfam10174 684 S 684
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1250-1463 |
5.95e-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: 54.00 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1250 EEKETNRQETEKLKEELSAssactqhLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKK 1329
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAE-------LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1330 NQCSQELDMKQ-------RTIQQLKEQ------LNNQKVEEAIQQYERACKDLNVKEKIIEDMRMT---LEEQEQTQVEQ 1393
Cdd:COG4942 93 AELRAELEAQKeelaellRALYRLGRQpplallLSPEDFLDAVRRLQYLKYLAPARREQAEELRADlaeLAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1394 DQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHEDNTDVLGKLSNLQDELQESEQKYNADRKK 1463
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1079-1536 |
7.90e-07 |
|
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: 54.41 E-value: 7.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1079 QELEQQIEKLQAEVKGYKDENNRLKVEEnehknqddllKEKETLIQQLKEELQEKnasldiqiqhvvEGNRALSELTQgV 1158
Cdd:pfam01576 71 QELEEILHELESRLEEEEERSQQLQNEK----------KKMQQHIQDLEEQLDEE------------EAARQKLQLEK-V 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1159 TCyKAKIKELET---ILETQKVERSHSAKLeqdilekesvilkLERNLKELQAHLQDSVKNTKDLSvkevKLKEEITQLT 1235
Cdd:pfam01576 128 TT-EAKIKKLEEdilLLEDQNSKLSKERKL-------------LEERISEFTSNLAEEEEKAKSLS----KLKNKHEAMI 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1236 NNLQDmkhllQLKEEEKetNRQETEKLKEELSASSACTQ-----------HLKADLQRKEEDYAELKEKLTD-------A 1297
Cdd:pfam01576 190 SDLEE-----RLKKEEK--GRQELEKAKRKLEGESTDLQeqiaelqaqiaELRAQLAKKEEELQAALARLEEetaqknnA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1298 KKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELdmkqrtiQQLKEQLNNQKVEEAIQQYERAckdlnVKEKIIE 1377
Cdd:pfam01576 263 LKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEL-------EALKTELEDTLDTTAAQQELRS-----KREQEVT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1378 DMRMTLEEQEQTQVEQDQVLEAK-LEEVERLATELEKWKEKCNDLEtKNNQRSNKEhedNTDVLGKLSNLQDELQESEQK 1456
Cdd:pfam01576 331 ELKKALEEETRSHEAQLQEMRQKhTQALEELTEQLEQAKRNKANLE-KAKQALESE---NAELQAELRTLQQAKQDSEHK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1457 ynadRKKWLEEKMMLITQAKEAENIRNkemkkyaEDRERFLKQQNEVEILTAQLTEKDSDLQKWREErdqlVAALEIQLK 1536
Cdd:pfam01576 407 ----RKKLEGQLQELQARLSESERQRA-------ELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD----VSSLESQLQ 471
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1122-1537 |
8.55e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1122 LIQQLKEELQE----KNASLDIQIQHVVEGNRALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDI--LEKESV 1195
Cdd:COG4717 47 LLERLEKEADElfkpQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELekLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1196 ILKLERNLKELQAHLQDsvkntkdLSVKEVKLKEEITQLTNNLQDMKHLlqlkEEEKETNRQETEKLKEELSASSactqh 1275
Cdd:COG4717 127 LLPLYQELEALEAELAE-------LPERLEELEERLEELRELEEELEEL----EAELAELQEELEELLEQLSLAT----- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1276 lKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQ------------------------ 1331
Cdd:COG4717 191 -EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLkearlllliaaallallglggsll 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1332 -------------------CSQELDMKQRTIQQLKEQLNNQKVEEAIQQYE--RACKDLNVKEkiiedmrmtleeqeqtq 1390
Cdd:COG4717 270 sliltiagvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEEleELLAALGLPP----------------- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1391 veqdqvlEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHEDNTDVLGKLSNLQDE-----LQESEQKYNADRKKWL 1465
Cdd:COG4717 333 -------DLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEeelraALEQAEEYQELKEELE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1466 EEKMMLITQAKEAENIR---------------NKEMKKYAEDRERFLKQQNEVEILTAQLtEKDSDLQKWREERDQLVAA 1530
Cdd:COG4717 406 ELEEQLEELLGELEELLealdeeeleeeleelEEELEELEEELEELREELAELEAELEQL-EEDGELAELLQELEELKAE 484
|
....*..
gi 1622966431 1531 LEIQLKA 1537
Cdd:COG4717 485 LRELAEE 491
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1054-1331 |
1.40e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 53.53 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1054 HSSIEAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLLKEKETLIQQLKEELQEK 1133
Cdd:TIGR02169 790 HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1134 NASldiqiqhvvegnralseltqgvtcYKAKIKELETILEtqkvershsaKLEQDILEKESVILKLERNLKELQAHLQDS 1213
Cdd:TIGR02169 870 LEE------------------------LEAALRDLESRLG----------DLKKERDELEAQLRELERKIEELEAQIEKK 915
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1214 VKNTKDLSVKEVKLKEEITQLTNNLQDMkhllqlkeEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEK 1293
Cdd:TIGR02169 916 RKRLSELKAKLEALEEELSEIEDPKGED--------EEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKR 987
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622966431 1294 LTDAKKQIEQVQKevsvmrdEEKLLRIKINELEKKKNQ 1331
Cdd:TIGR02169 988 LDELKEKRAKLEE-------ERKAILERIEEYEKKKRE 1018
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1051-1478 |
1.44e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1051 SSFHSSIEAIWE-----ECKEIVKSSSKKS----HQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLLKEKET 1121
Cdd:COG4717 37 STLLAFIRAMLLerlekEADELFKPQGRKPelnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1122 LIQQLKEELQ-----EKNASLDIQIQHVVEgnrALSELTQGVTCYKAKIKELETILET-QKVERSHSAKLEQDILEKESV 1195
Cdd:COG4717 117 ELEKLEKLLQllplyQELEALEAELAELPE---RLEELEERLEELRELEEELEELEAElAELQEELEELLEQLSLATEEE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1196 ILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEE------------------------- 1250
Cdd:COG4717 194 LQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllliaaallallglggsllslil 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1251 ----------------------EKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEV 1308
Cdd:COG4717 274 tiagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1309 SVMRDEEKLLRIKINELEKK----KNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKII--EDMRMT 1382
Cdd:COG4717 354 REAEELEEELQLEELEQEIAallaEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeEELEEE 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1383 LEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKcndletknnqrsnkehedntdvlGKLSNLQDELQESEQKYNADRK 1462
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELEQLEED-----------------------GELAELLQELEELKAELRELAE 490
|
490
....*....|....*...
gi 1622966431 1463 KWLEEKM--MLITQAKEA 1478
Cdd:COG4717 491 EWAALKLalELLEEAREE 508
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1036-1554 |
1.45e-06 |
|
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: 53.64 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1036 SKQVKEYRIQEpNRESSFHSSIEAIWEECKEIVKSSSKKSHQIQELEqqiEKLQAEVKGYKD-ENNRLKVEENEHKNQDD 1114
Cdd:pfam01576 148 SKLSKERKLLE-ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLE---ERLKKEEKGRQElEKAKRKLEGESTDLQEQ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1115 LLkEKETLIQQLKEELQEKNASLDIQIQHVVEGNRALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDILEK-E 1193
Cdd:pfam01576 224 IA-ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEElE 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1194 SVILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDM--KHLLQLKEEEK------------ETNRQET 1259
Cdd:pfam01576 303 ALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMrqKHTQALEELTEqleqakrnkanlEKAKQAL 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1260 EKLKEELSASSACTQHLKADLQRK----EEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQE 1335
Cdd:pfam01576 383 ESENAELQAELRTLQQAKQDSEHKrkklEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKD 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1336 LDmkqrtiqQLKEQLnnQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLE--------------AKL 1401
Cdd:pfam01576 463 VS-------SLESQL--QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVErqlstlqaqlsdmkKKL 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1402 EEVERLATELEKWKEKC-NDLETKNNQRSNKEHE------DNTDVLGKLSNLQDELQESEQKYNADRKKWLEEKMMLitq 1474
Cdd:pfam01576 534 EEDAGTLEALEEGKKRLqRELEALTQQLEEKAAAydklekTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQML--- 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1475 aKEAENIRNkemkKYAEDRERFLKQQNEVEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISS--NVQKD-NEIEQ 1551
Cdd:pfam01576 611 -AEEKAISA----RYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSkdDVGKNvHELER 685
|
...
gi 1622966431 1552 LKR 1554
Cdd:pfam01576 686 SKR 688
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1280-1572 |
1.65e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.38 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1280 LQRKEEDYAELKEKLTDAKKQIEQVQkevsvmrDEEKLLRIKINELEKKKNQCSQELDMK--QRTIQQLKEQL-----NN 1352
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALE-------AELDALQERREALQRLAEYSWDEIDVAsaEREIAELEAELerldaSS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1353 QKVEEAIQQYERAckdlnvkEKIIEDMRmtleeqeqtqveqdQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNK- 1431
Cdd:COG4913 685 DDLAALEEQLEEL-------EAELEELE--------------EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLa 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1432 EHEDNTDVLGKLSNLQDELQESEQkynadrKKWLEEkmmlitQAKEAENIRNKEMKKYAEDRERFLKQQNEVeilTAQLT 1511
Cdd:COG4913 744 RLELRALLEERFAAALGDAVEREL------RENLEE------RIDALRARLNRAEEELERAMRAFNREWPAE---TADLD 808
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622966431 1512 EKDSDLQKWREERDQLVA----ALEIQLKALIssNVQKDNEIEQLKriisetSKIETQIMDIKPR 1572
Cdd:COG4913 809 ADLESLPEYLALLDRLEEdglpEYEERFKELL--NENSIEFVADLL------SKLRRAIREIKER 865
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1229-1413 |
1.82e-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: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1229 EEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEV 1308
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1309 SVMRDEeklLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN-----NQKVEEAIQQYERACKDLNVKEKIIEDMRMTL 1383
Cdd:COG4942 100 EAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkylAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190
....*....|....*....|....*....|
gi 1622966431 1384 EEQEQTQVEQDQVLEAKLEEVERLATELEK 1413
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEK 206
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1062-1411 |
2.32e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1062 EECKEIVKSSSKKSHQIQELEQQIEKLQAEVKgykdenNRLKVEENEHKNQDDLLKEKETL--IQQLKEELQEKNasldi 1139
Cdd:PRK03918 448 EHRKELLEEYTAELKRIEKELKEIEEKERKLR------KELRELEKVLKKESELIKLKELAeqLKELEEKLKKYN----- 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1140 qIQHVVEGNRALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDILEKESVILKLERNLKELQAHLQDSVKntkd 1219
Cdd:PRK03918 517 -LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE---- 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1220 lsvKEVKLKEEITQLTNNLQDMKHLLQLKEEEKEtnrqeteKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDakK 1299
Cdd:PRK03918 592 ---ERLKELEPFYNEYLELKDAEKELEREEKELK-------KLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--E 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1300 QIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCsqeldmkQRTIQQLKEQLNN-QKVEEAIQQYERACKDLNVKEKIIED 1378
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEI-------KKTLEKLKEELEErEKAKKELEKLEKALERVEELREKVKK 732
|
330 340 350
....*....|....*....|....*....|...
gi 1622966431 1379 MRMTLEeqeqtqveqdqvlEAKLEEVERLATEL 1411
Cdd:PRK03918 733 YKALLK-------------ERALSKVGEIASEI 752
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1266-1495 |
3.35e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.30 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1266 LSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQ 1345
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1346 LKEQLNNQKveEAIQQYERACKDLNVKEKI-----------IEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKW 1414
Cdd:COG4942 95 LRAELEAQK--EELAELLRALYRLGRQPPLalllspedfldAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1415 KEKCNDLETKNNQRSNkehedntdvlgKLSNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRE 1494
Cdd:COG4942 173 RAELEALLAELEEERA-----------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
.
gi 1622966431 1495 R 1495
Cdd:COG4942 242 R 242
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1199-1536 |
3.65e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 51.94 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1199 LERNLKELQAHLqDSVKNTKDLSvkevklkeeitqLTNNLQDMK--HLLQLKEEEKETNRQETEKLKEELSASsacTQHL 1276
Cdd:NF033838 67 LEKILSEIQKSL-DKRKHTQNVA------------LNKKLSDIKteYLYELNVLKEKSEAELTSKTKKELDAA---FEQF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1277 KADLQRKEEDYAELKEKLTDAKK---------------------QIEQVQKEVSVMRDEEKLLRIKINEL--EKKKNQCS 1333
Cdd:NF033838 131 KKDTLEPGKKVAEATKKVEEAEKkakdqkeedrrnyptntyktlELEIAESDVEVKKAELELVKEEAKEPrdEEKIKQAK 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1334 QELDMKQRTIQQLKE-QLNNQKVEEaiqqyerackdlNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELE 1412
Cdd:NF033838 211 AKVESKKAEATRLEKiKTDREKAEE------------EAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1413 KW-KEKCND-------LETKNNQRSNKEHEDNTDVLGKLSNLQDELQESEQKYNADRKKWLE-EKMMLITQAKEAENIRN 1483
Cdd:NF033838 279 KEnDAKSSDssvgeetLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKTLElEIAESDVKVKEAELELV 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1622966431 1484 KEMKKYAEDRERFLKQQNEVEILTAQLT--EKDSDLQKWREERDQLVAALEIQLK 1536
Cdd:NF033838 359 KEEAKEPRNEEKIKQAKAKVESKKAEATrlEKIKTDRKKAEEEAKRKAAEEDKVK 413
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1288-1566 |
4.34e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1288 AELKEKLTDAKKQIEQVqkevsvmrdEEKLLRIK--INELEKKKNQCSqeldmKQRTI----QQLKEQLNNQKVEEAIQQ 1361
Cdd:COG1196 168 SKYKERKEEAERKLEAT---------EENLERLEdiLGELERQLEPLE-----RQAEKaeryRELKEELKELEAELLLLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1362 YERACKDLNVKEKIIEDmrmtLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHEDNTDVLG 1441
Cdd:COG1196 234 LRELEAELEELEAELEE----LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1442 KLSNLQDELQESEQkynaDRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFLKQQNEVEILTAQLTEKDSDLQKWR 1521
Cdd:COG1196 310 RRRELEERLEELEE----ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1622966431 1522 EERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQI 1566
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1162-1341 |
5.88e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.45 E-value: 5.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1162 KAKIKELETILETQKVERshsAKLEQDILEKEsvILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQL-TNNLQD 1240
Cdd:COG4913 268 RERLAELEYLRAALRLWF---AQRRLELLEAE--LEELRAELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1241 MKHLLQLKEEEKETNRQETEKLKEELsassactQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEeklLRI 1320
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALL-------AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAE---AEA 412
|
170 180
....*....|....*....|..
gi 1622966431 1321 KINELEKKKNQCSQELD-MKQR 1341
Cdd:COG4913 413 ALRDLRRELRELEAEIAsLERR 434
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1229-1562 |
6.43e-06 |
|
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: 51.28 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1229 EEITQLTNNLQDMKHLLQLKEEEKeTNRQETEKLKEElsassactqhlKADLQRKEEDYAELKEKLTDAKKQIEQ----- 1303
Cdd:pfam17380 269 EFLNQLLHIVQHQKAVSERQQQEK-FEKMEQERLRQE-----------KEEKAREVERRRKLEEAEKARQAEMDRqaaiy 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1304 VQKEVSVMRDEEKLLRIKINELEKKKNQCSQ-ELDMKQRTIQQLKE-QLNNQKVEEAIQQYERACKDLNVKEKiiEDMRM 1381
Cdd:pfam17380 337 AEQERMAMERERELERIRQEERKRELERIRQeEIAMEISRMRELERlQMERQQKNERVRQELEAARKVKILEE--ERQRK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1382 TLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHEDNTDVLGKLSNLQDElQESEQKYNADR 1461
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE-KRDRKRAEEQR 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1462 KKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFLKQQNEveiltaqltekdsdLQKWREERdqlvaaleiqlkaliss 1541
Cdd:pfam17380 494 RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEER--------------RREAEEER----------------- 542
|
330 340
....*....|....*....|.
gi 1622966431 1542 nvQKDNEIEQLKRIISETSKI 1562
Cdd:pfam17380 543 --RKQQEMEERRRIQEQMRKA 561
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1148-1572 |
7.98e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.89 E-value: 7.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1148 NRALSELTQGVTCYKAKIKELETILETQKVE---------RSHSAKLEQDILEKESVILKLERNLKELQAH--------- 1209
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALKSEsqnkielllQQHQDRIEQLISEHEVEITGLTEKASSARSQansiqsqle 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1210 -LQDSVKNTKDLSVKEV-KLKEEITQLTNNLQDMKHLLQLKEEEKEtnrqeteklKEELSASSACTQhlkadlQRKEED- 1286
Cdd:pfam15921 303 iIQEQARNQNSMYMRQLsDLESTVSQLRSELREAKRMYEDKIEELE---------KQLVLANSELTE------ARTERDq 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1287 YAELKEKLTDakkqieQVQKEVSVMRDEEKLLrikinELEKKKNQCSQELDMKQR-TIQQLKEQLNNQKVEeaIQQYERA 1365
Cdd:pfam15921 368 FSQESGNLDD------QLQKLLADLHKREKEL-----SLEKEQNKRLWDRDTGNSiTIDHLRRELDDRNME--VQRLEAL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1366 CKDLNVKEKIIEDMRMTLEEQEQTqveqdqvleaKLEEVERLATELEKWKEKCNDL-ETKNNQRSNKEHEDNTdvlgkLS 1444
Cdd:pfam15921 435 LKAMKSECQGQMERQMAAIQGKNE----------SLEKVSSLTAQLESTKEMLRKVvEELTAKKMTLESSERT-----VS 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1445 NLQDELQESEQKYNADRKKwleekmmlITQAKEAENIRNKEMKKYAEDRERFLKQQNEVEILTAQLTEKDSDLQKWREER 1524
Cdd:pfam15921 500 DLTASLQEKERAIEATNAE--------ITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQI 571
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1622966431 1525 D---QLVAALEIQLKALISSNVQKDNEIEQlKRIISETSKIETQIMDIKPR 1572
Cdd:pfam15921 572 EnmtQLVGQHGRTAGAMQVEKAQLEKEIND-RRLELQEFKILKDKKDAKIR 621
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1007-1361 |
1.10e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 50.40 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1007 LNLRDLSNGSEEDNLPNTQLHLLGNDYLVSKQVKEYRIQEPNRESSfhSSIEAIWEECKEIVKSSSKK---------SHQ 1077
Cdd:COG3206 68 VLLSGLSSLSASDSPLETQIEILKSRPVLERVVDKLNLDEDPLGEE--ASREAAIERLRKNLTVEPVKgsnvieisyTSP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1078 IQELEQQIekLQAEVKGYKDENNRLKVEENEhkNQDDLLKEKetlIQQLKEELQEKNASL-DIQIQHvveGNRALSELTQ 1156
Cdd:COG3206 146 DPELAAAV--ANALAEAYLEQNLELRREEAR--KALEFLEEQ---LPELRKELEEAEAALeEFRQKN---GLVDLSEEAK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1157 GVTcykAKIKELETILETQKVERShSAKLEQDILEKesvilKLERNLKELQAHLQDSVKNT--KDLSVKEVKLKEEITQL 1234
Cdd:COG3206 216 LLL---QQLSELESQLAEARAELA-EAEARLAALRA-----QLGSGPDALPELLQSPVIQQlrAQLAELEAELAELSARY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1235 TNNLQDMKHLLQLKEEEKETNRQETEKLKEELSAssactqhlkadlqrkeeDYAELKEKLTDAKKQIEQVQKEVSVMRDE 1314
Cdd:COG3206 287 TPNHPDVIALRAQIAALRAQLQQEAQRILASLEA-----------------ELEALQAREASLQAQLAQLEARLAELPEL 349
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1622966431 1315 EkllrIKINELEkkknqcsQELDMKQRTIQQLKEQLNNQKVEEAIQQ 1361
Cdd:COG3206 350 E----AELRRLE-------REVEVARELYESLLQRLEEARLAEALTV 385
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1069-1310 |
1.10e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1069 KSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEenehknqddlLKEKETLIQQLKEELQEKNASLDIQIQHVveGN 1148
Cdd:COG3883 23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAE----------LEALQAEIDKLQAEIAEAEAEIEERREEL--GE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1149 RALSELTQGVTcykakIKELETILETQKVershsakleQDILEKESVILKLERNLKELQahlqdsvkntkdlsvkevklk 1228
Cdd:COG3883 91 RARALYRSGGS-----VSYLDVLLGSESF---------SDFLDRLSALSKIADADADLL--------------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1229 EEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEV 1308
Cdd:COG3883 136 EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAA 215
|
..
gi 1622966431 1309 SV 1310
Cdd:COG3883 216 AA 217
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1037-1457 |
1.15e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1037 KQVKEYRiQEPNRESSFHSSIEAIWEECKEIVKSSSKKSHQIQ--ELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDD 1114
Cdd:COG4717 85 EKEEEYA-ELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELAELPERLEELEERLEELRELEE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1115 LLKEKETLIQQLKEELQEKNASLDIQIQhvvegnRALSELTQGVTCYKAKIKELETILETQKvERSHSAKLEQDILEKES 1194
Cdd:COG4717 164 ELEELEAELAELQEELEELLEQLSLATE------EELQDLAEELEELQQRLAELEEELEEAQ-EELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1195 VILKLERNLKELQ------------AHLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKL 1262
Cdd:COG4717 237 EAAALEERLKEARlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1263 KEELSASSACTQHLKADLQRKE-----EDYAELKEKLTDAKKQIEQVQKEVSV-----------MRDEEKLLRI-----K 1321
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEEllellDRIEELQELLREAEELEEELQLEELEqeiaallaeagVEDEEELRAAleqaeE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1322 INELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERAckdLNVKEKIIEDMRMTLEEqeqtqveqdqvLEAKL 1401
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEE---LEELEEELEELREELAE-----------LEAEL 462
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622966431 1402 EEVERlATELEKWKEKcndLETKNNQRSNKEHEDNTDVLGkLSNLQDELQESEQKY 1457
Cdd:COG4717 463 EQLEE-DGELAELLQE---LEELKAELRELAEEWAALKLA-LELLEEAREEYREER 513
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
916-1166 |
1.23e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.76 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 916 QQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSHEIETATRSITNNVSQIKLMHTKID----- 990
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEaqkee 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 991 ---QLRTFDSVSQISNIDLLnlrdLSNGSEEDNLPNTQLHllgndylvsKQVKEYRIQEpnressfhssIEAIWEECKEI 1067
Cdd:COG4942 106 laeLLRALYRLGRQPPLALL----LSPEDFLDAVRRLQYL---------KYLAPARREQ----------AEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1068 VKssskkshQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQIQHVVEG 1147
Cdd:COG4942 163 AA-------LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
250
....*....|....*....
gi 1622966431 1148 NRALSELTQGVTCYKAKIK 1166
Cdd:COG4942 236 AAAAAERTPAAGFAALKGK 254
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1055-1321 |
1.25e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.14 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1055 SSIEAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLLKEKE----TLIQQLKEEL 1130
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRdelnEKVKELKEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1131 QEKNASLDIQIQHVVEGNRALSELTQGVTCYKAKIKELETILETQKVErSHSAKLEQDILEKesvILKLERNLKELQA-- 1208
Cdd:COG1340 81 DELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTE-VLSPEEEKELVEK---IKELEKELEKAKKal 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1209 ----HLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKE 1284
Cdd:COG1340 157 ekneKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQ 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 1622966431 1285 EDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIK 1321
Cdd:COG1340 237 KELRELRKELKKLRKKQRALKREKEKEELEEKAEEIF 273
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1162-1429 |
1.43e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.01 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1162 KAKIKELETILETQKVERSHsakLEQDILEKESVILKLER----NLKELQAHLQDSVKNTKDLSVKEVKLKEEITQL--- 1234
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDH---IQQQIKTYNKNIEEQRKkngeNIARKQNKYDELVEEAKTIKAEIEELTDELLNLvmd 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1235 ----TNNLQDMKHLLQLKEEEKETNRQEtEKLKEELSASSACTQHLkadlqrkeEDYAELKEKLTDAKKQIEQvqkevsv 1310
Cdd:PHA02562 250 iedpSAALNKLNTAAAKIKSKIEQFQKV-IKMYEKGGVCPTCTQQI--------SEGPDRITKIKDKLKELQH------- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1311 mrdEEKLLRIKINELEKKKNqcsqELDMKQRTIQQLKEQLNNQKveEAIQQYERACKDLnvkEKIIEDMrmtleeqeqtq 1390
Cdd:PHA02562 314 ---SLEKLDTAIDELEEIMD----EFNEQSKKLLELKNKISTNK--QSLITLVDKAKKV---KAAIEEL----------- 370
|
250 260 270
....*....|....*....|....*....|....*....
gi 1622966431 1391 vEQDQVLEAklEEVERLATELEKWKEKCNDLETKNNQRS 1429
Cdd:PHA02562 371 -QAEFVDNA--EELAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1227-1459 |
2.00e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1227 LKEEITQLTNNLQDM-------KHLLQLKEeeketNRQETEKLKEELSASSACTQHLkaDLQRKEEDYAELKEKLTDAKK 1299
Cdd:COG4913 230 LVEHFDDLERAHEALedareqiELLEPIRE-----LAERYAAARERLAELEYLRAAL--RLWFAQRRLELLEAELEELRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1300 QIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCS-QELDMKQRTIQQLKEQLnnQKVEEAIQQYERACKDLNVKEKIIED 1378
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLEREL--EERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1379 mrmtleeqeqtqveqdqVLEAKLEEVERLATELEKWKEKCNDLETKNNQRsnkehedntdvlgkLSNLQDELQESEQKYN 1458
Cdd:COG4913 381 -----------------EFAALRAEAAALLEALEEELEALEEALAEAEAA--------------LRDLRRELRELEAEIA 429
|
.
gi 1622966431 1459 A 1459
Cdd:COG4913 430 S 430
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1146-1553 |
2.09e-05 |
|
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: 49.72 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1146 EGNRALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDILE-KESVILKLERNLKELQAHLQDSVKNTKDLSVKE 1224
Cdd:pfam05483 71 ENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEaQRKAIQELQFENEKVSLKLEEEIQENKDLIKEN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1225 VKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKE-EDYAELKEKLTDAKKQIEQ 1303
Cdd:pfam05483 151 NATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARlEMHFKLKEDHEKIQHLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1304 VQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQ--LNNQKVEEAIQQYERACKDLnvkekiiEDMRM 1381
Cdd:pfam05483 231 YKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKtkLQDENLKELIEKKDHLTKEL-------EDIKM 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1382 TLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSnkehednTDVLGKLSNLQDELQESEQKYNADr 1461
Cdd:pfam05483 304 SLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVV-------TEFEATTCSLEELLRTEQQRLEKN- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1462 kkwlEEKMMLITQAKEAENIRNKEMKKYAEDRE--------------RFLKQQNEVEILTAQLTEKDSDLQKWREERDQL 1527
Cdd:pfam05483 376 ----EDQLKIITMELQKKSSELEEMTKFKNNKEveleelkkilaedeKLLDEKKQFEKIAEELKGKEQELIFLLQAREKE 451
|
410 420
....*....|....*....|....*.
gi 1622966431 1528 VAALEIQLKALISSNVQKDNEIEQLK 1553
Cdd:pfam05483 452 IHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1206-1458 |
2.14e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1206 LQAHLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEE 1285
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1286 DYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERA 1365
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1366 CKDLNVKEKIIEDMRMTLEEQEQ-TQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHEDNTDVLGKLS 1444
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESlPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIL 268
|
250
....*....|....
gi 1622966431 1445 NLQDELQESEQKYN 1458
Cdd:COG4372 269 VEKDTEEEELEIAA 282
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1078-1361 |
2.20e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 49.67 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1078 IQELEQQIEKLQAEVKGYkdeNNRLKVEENEHK-----NQddlLKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRALS 1152
Cdd:PRK10929 81 SAELRQQLNNERDEPRSV---PPNMSTDALEQEilqvsSQ---LLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLN 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1153 ELTQGvtcykakikeletiLETQKVERSHSAKLEQDILEKESVILKLERNLKELQahlQDSVKNTKDLSVKEVKL-KEEI 1231
Cdd:PRK10929 155 EIERR--------------LQTLGTPNTPLAQAQLTALQAESAALKALVDELELA---QLSANNRQELARLRSELaKKRS 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1232 TQLTNNLQDMKHLLQ-LKEEEKETNRQETEKLKEE-------LSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQ 1303
Cdd:PRK10929 218 QQLDAYLQALRNQLNsQRQREAERALESTELLAEQsgdlpksIVAQFKINRELSQALNQQAQRMDLIASQQRQAASQTLQ 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622966431 1304 VQKEVSVMRDEEK----------LLRIKINEL-EKKKnqcSQELD--MKQRTIQQLK--EQLNNQKVEEAIQQ 1361
Cdd:PRK10929 298 VRQALNTLREQSQwlgvsnalgeALRAQVARLpEMPK---PQQLDteMAQLRVQRLRyeDLLNKQPQLRQIRQ 367
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1227-1362 |
2.24e-05 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 48.81 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1227 LKEEIT-------QLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRK-------EEDYAELKE 1292
Cdd:PRK09039 44 LSREISgkdsaldRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELagagaaaEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622966431 1293 KLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLN---NQKVEEaIQQY 1362
Cdd:PRK09039 124 ELDSEKQVSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNvalAQRVQE-LNRY 195
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1226-1364 |
2.34e-05 |
|
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: 47.21 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1226 KLKEEITQLTNNLQDMKHLLQLKEEEketNRQETEKLKEelsassacTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQ 1305
Cdd:pfam13851 30 SLKEEIAELKKKEERNEKLMSEIQQE---NKRLTEPLQK--------AQEEVEELRKQLENYEKDKQSLKNLKARLKVLE 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622966431 1306 KEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQ---LKEQLNNQKVEEAIQQYER 1364
Cdd:pfam13851 99 KELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQktgLKNLLLEKKLQALGETLEK 160
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
555-1243 |
3.00e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 555 EDLDKTLEENKafishEEKRKLLDLIEDLKKKLINEKKEK--LTLEFKIREEVTQEFTQYWAQREADFKET---LLQERE 629
Cdd:TIGR02169 318 EDAEERLAKLE-----AEIDKLLAEIEELEREIEEERKRRdkLTEEYAELKEELEDLRAELEEVDKEFAETrdeLKDYRE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 630 ILEENAERRLAIFKDLVGKCDTREETTKDVcativeteethnyvgfEDIIDSLQDNVADIKKqaeiahlYIASLPDPQEA 709
Cdd:TIGR02169 393 KLEKLKREINELKRELDRLQEELQRLSEEL----------------ADLNAAIAGIEAKINE-------LEEEKEDKALE 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 710 IACLELKFNQIKAELTKTKEELIKTKEELKKRENETDSLIQELET--SNKKIITQNQR----IQELINtiDQKEGIINEF 783
Cdd:TIGR02169 450 IKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEaeAQARASEERVRggraVEEVLK--ASIQGVHGTV 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 784 QNLKSHMEKTFKCNDKADTSSL---IINNKLICNETVEVPQDSK----TKICSERKRVNENELqqdEPPAKKGSIHV--- 853
Cdd:TIGR02169 528 AQLGSVGERYATAIEVAAGNRLnnvVVEDDAVAKEAIELLKRRKagraTFLPLNKMRDERRDL---SILSEDGVIGFavd 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 854 -----------------------------------------------SSAITEDQKKSEEVQPN-IAENEDIRVLQKNNE 885
Cdd:TIGR02169 605 lvefdpkyepafkyvfgdtlvvedieaarrlmgkyrmvtlegelfekSGAMTGGSRAPRGGILFsRSEPAELQRLRERLE 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 886 GLKALLLTIENELKNEKeekaelnKQIVRFQQELSLSEKKNLTLSKEVQQIQsnydiaiAELHVQKSKNQEQEEKIMKLS 965
Cdd:TIGR02169 685 GLKRELSSLQSELRRIE-------NRLDELSQELSDASRKIGEIEKEIEQLE-------QEEEKLKERLEELEEDLSSLE 750
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 966 HEIETATRSITNNVSQIKLMHTKIDQLRtfdsvsqisnidlLNLRDLSNGSEEDNLPNTQLHLLGNDYLVSKQVK----- 1040
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKLE-------------EALNDLEARLSHSRIPEIQAELSKLEEEVSRIEArlrei 817
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1041 EYRIQEPNRESSFHSS----IEAIWEECKEIVKSSSKKSH----QIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQ 1112
Cdd:TIGR02169 818 EQKLNRLTLEKEYLEKeiqeLQEQRIDLKEQIKSIEKEIEnlngKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1113 ddllkeketlIQQLKEELQEKNASLDIQIQHVVEGNRALSELTQGVTCYKAKIKELETILETQKVERshsaKLEQDILEK 1192
Cdd:TIGR02169 898 ----------LRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE----DVQAELQRV 963
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1622966431 1193 ESVILKLER-NLKELQAHlQDSVKNTKDLSVKEVKLKEE---ITQLTNNLQDMKH 1243
Cdd:TIGR02169 964 EEEIRALEPvNMLAIQEY-EEVLKRLDELKEKRAKLEEErkaILERIEEYEKKKR 1017
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
911-1518 |
3.43e-05 |
|
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: 48.89 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 911 QIVRFQQELSLSEKKNLTLSKEVQQIQ------SNYDIAIAELHVQKSKNQEQEEKIMKLSHEIETATRSITNNVSQIKL 984
Cdd:TIGR00606 180 SATRYIKALETLRQVRQTQGQKVQEHQmelkylKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEH 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 985 MHTKIDQLRTFDSVSQISNIDLLNLRDLSNGSEEDNLPNTQLHLLGNDYLVSKQVKEYRiqepNRESSFHSSIEAIWEEC 1064
Cdd:TIGR00606 260 NLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKE----RELVDCQRELEKLNKER 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1065 KEIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDE--NNRLKVEENEHKNQDDLLKEKETLIqQLKEELQEKNASLDIQIQ 1142
Cdd:TIGR00606 336 RLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLiqSLATRLELDGFERGPFSERQIKNFH-TLVIERQEDEAKTAAQLC 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1143 HVVEGN-----RALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDILEKESVILKLERNLKELQAHLQDSVKNt 1217
Cdd:TIGR00606 415 ADLQSKerlkqEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKN- 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1218 kdlSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRqETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTD- 1296
Cdd:TIGR00606 494 ---SLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNH-HTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYf 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1297 -AKKQIE----QVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQyerackDLNV 1371
Cdd:TIGR00606 570 pNKKQLEdwlhSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEES------DLER 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1372 KEKIIEDMRMTLeeqeqtqveqdQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHEDNTDVLGKLSNLQDELQ 1451
Cdd:TIGR00606 644 LKEEIEKSSKQR-----------AMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLK 712
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622966431 1452 ESEQKYnadrKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFLKQQNEVEILTAQLTEKDSDLQ 1518
Cdd:TIGR00606 713 STESEL----KKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG 775
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1113-1365 |
3.60e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1113 DDLLKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRALSELtqgvtcyKAKIKELETILEtqkvershsaKLEQDILEK 1192
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNEL-------QAELEALQAEID----------KLQAEIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1193 ESVILKLERNLKELQAHLQDSVKNTKDLSVkeVKLKEEITQLTNNLQDMKHLLqlkeeekETNRQETEKLKEELSASsac 1272
Cdd:COG3883 78 EAEIEERREELGERARALYRSGGSVSYLDV--LLGSESFSDFLDRLSALSKIA-------DADADLLEELKADKAEL--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1273 tQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEeklLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNN 1352
Cdd:COG3883 146 -EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQ---LSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
250
....*....|...
gi 1622966431 1353 QKVEEAIQQYERA 1365
Cdd:COG3883 222 AAAAAAAAAAAAA 234
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1056-1364 |
4.61e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1056 SIEAIWEECKEIVKSSSKKSHQIQELEQQIEKL-------QAEVKGYKDENNR----LKVEENEHKNQDDLLKEKETLIQ 1124
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLtqrvlerETELERMKERAKKagaqRKEEEAERKQLQAKLQQTEEELR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1125 QLKEELQEKNASLDIQIQHVVEGNRALSELTQGVTCYKAKIKELETILETQKV--ERSHSAkleqdilekesvilklERN 1202
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSlqERLNAS----------------ERK 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1203 LKELQAHLQdSVKNTKDLSVKEV-KLKEEITQLTNNLQDMKhlLQLKEE------EKETNRQETEKLKEELsassactQH 1275
Cdd:pfam07888 253 VEGLGEELS-SMAAQRDRTQAELhQARLQAAQLTLQLADAS--LALREGrarwaqERETLQQSAEADKDRI-------EK 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1276 LKADLQRKEEDYAElkekltdakKQIEQVQKEVSVMRdEEKLLRIKINELEKKknqcSQELDMKQRTIQQLKEQLNNQKV 1355
Cdd:pfam07888 323 LSAELQRLEERLQE---------ERMEREKLEVELGR-EKDCNRVQLSESRRE----LQELKASLRVAQKEKEQLQAEKQ 388
|
330
....*....|.
gi 1622966431 1356 E--EAIQQYER 1364
Cdd:pfam07888 389 EllEYIRQLEQ 399
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1163-1314 |
7.50e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1163 AKIKELETILETQKVERshsAKLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQLTNN--LQD 1240
Cdd:COG1579 17 SELDRLEHRLKELPAEL---AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeYEA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622966431 1241 MKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDE 1314
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1161-1493 |
7.67e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.66 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1161 YKAKIKELETILETQKVERSHSAKL------EQDILEKESVILKLERNLKELQAHLQDSVKNTKdLSVKEVKLKEEITQL 1234
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLeelklqELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY-LKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1235 TNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSactqhlkadLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDE 1314
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK---------LQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1315 EKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERAckdlNVKEKIIEDMRMTLEEQEQTQVEQD 1394
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL----EQLEEELLAKKKLESERLSSAAKLK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1395 QVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHEDNTDVLGKLSNLQDELQESEQKYNADRKKWLEEKMMLITQ 1474
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL 473
|
330
....*....|....*....
gi 1622966431 1475 AKEAENIRNKEMKKYAEDR 1493
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSR 492
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
722-1303 |
1.13e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 722 AELTKTKEELIKTKEELKKRENETDSLIQELETSNKKIITQNQRIQELINTIDQKEGIINEFQNLKSHMEKTFKCNDkad 801
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE--- 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 802 tssliinnklICNETVEVPQDSKTKICSERKRVNENELQQDEPPAKKGSI-HVSSAITEDQKKSEEVQPNIAENEDIRVL 880
Cdd:PRK03918 301 ----------FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLeELKKKLKELEKRLEELEERHELYEEAKAK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 881 QKNNEGLKALLltienelknekeekaeLNKQIVRFQQELSLSEKKNLTLSKEVQQIQSNydiaIAELHVQKSKNQEQEEK 960
Cdd:PRK03918 371 KEELERLKKRL----------------TGLTPEKLEKELEELEKAKEEIEEEISKITAR----IGELKKEIKELKKAIEE 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 961 IMKLSHEIETATRSITNnvsqiklmHTKIDQLRTFdsvsqisnidLLNLRDLSNGSEEdnLPNTQLHLLGNDYLVSKQVK 1040
Cdd:PRK03918 431 LKKAKGKCPVCGRELTE--------EHRKELLEEY----------TAELKRIEKELKE--IEEKERKLRKELRELEKVLK 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1041 EYRIQEPNRESSfhSSIEAIWEECKEI-VKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEENE----HKNQDDL 1115
Cdd:PRK03918 491 KESELIKLKELA--EQLKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKlaelEKKLDEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1116 LKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRALSELtqgvtcyKAKIKELETILETQKVERSHSAKLEQDILEKESV 1195
Cdd:PRK03918 569 EEELAELLKELEELGFESVEELEERLKELEPFYNEYLEL-------KDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1196 ILKLERNLKELQahlqdsvkntKDLSVKEVK-LKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQ 1274
Cdd:PRK03918 642 LEELRKELEELE----------KKYSEEEYEeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
570 580
....*....|....*....|....*....
gi 1622966431 1275 HLKaDLQRKEEDYAELKEKLTDAKKQIEQ 1303
Cdd:PRK03918 712 ELE-KLEKALERVEELREKVKKYKALLKE 739
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1288-1491 |
1.14e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1288 AELKEKLTDAKKQIEQVQKEVSVMRdEEKLLRIKiNELEKKKNQCSQELDMKQRTIQQLKEQLNnQKVEeaiqQYERACK 1367
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKEAEAIK-KEALLEAK-EEIHKLRNEFEKELRERRNELQKLEKRLL-QKEE----NLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1368 DLNVKEKIiedmrmtleeqeqtqveqdqvLEAKLEEVERLATELEKWKEKCNDLETKNNQRsnkehedntdvLGKLSNLQ 1447
Cdd:PRK12704 104 LLEKREEE---------------------LEKKEKELEQKQQELEKKEEELEELIEEQLQE-----------LERISGLT 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1448 DE------LQESEQKYNAdrkkwleEKMMLItqaKEAENIRNKEMKKYAE 1491
Cdd:PRK12704 152 AEeakeilLEKVEEEARH-------EAAVLI---KEIEEEAKEEADKKAK 191
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1077-1355 |
1.49e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1077 QIQELEQQIEKLQAEVkgykdenNRLKVEENEHKNQDDLLKEKETLIQQL--------KEELQEKNASLDIQIQhvvegn 1148
Cdd:PRK04863 838 ELRQLNRRRVELERAL-------ADHESQEQQQRSQLEQAKEGLSALNRLlprlnllaDETLADRVEEIREQLD------ 904
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1149 rALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDILEKEsvilKLERNLKELQAHLQDSVKNTKDLSVKE-VKL 1227
Cdd:PRK04863 905 -EAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQ----QTQRDAKQQAFALTEVVQRRAHFSYEDaAEM 979
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1228 KEEITQLTNNLqdmKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQI-EQVQK 1306
Cdd:PRK04863 980 LAKNSDLNEKL---RQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPAdSGAEE 1056
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622966431 1307 EVSVMRDE-EKLL---RIKINELEKKknQCSQELDMK---------QRTIQQLKEQLNNQKV 1355
Cdd:PRK04863 1057 RARARRDElHARLsanRSRRNQLEKQ--LTFCEAEMDnltkklrklERDYHEMREQVVNAKA 1116
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1177-1475 |
1.50e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.76 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1177 VERSHSAKLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQLTNnlqdmkhllQLKEEEKETNr 1256
Cdd:pfam12128 238 KIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDD---------QWKEKRDELN- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1257 QETEKLKEELSASSACTQHLKADLQRKEEDYAelkEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQEL 1336
Cdd:pfam12128 308 GELSAADAAVAKDRSELEALEDQHGAFLDADI---ETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKI 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1337 DMK-QRTIQQLKEQLNNQKvEEAIQQYERACKDLnvkEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEV----------E 1405
Cdd:pfam12128 385 KEQnNRDIAGIKDKLAKIR-EARDRQLAVAEDDL---QALESELREQLEAGKLEFNEEEYRLKSRLGELklrlnqatatP 460
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622966431 1406 RLATELEKWKEKCNDLETKNNQRsNKEHEDNTDVLGKLSNLQDE----LQESEQKYNADRKKWLEEKMMLITQA 1475
Cdd:pfam12128 461 ELLLQLENFDERIERAREEQEAA-NAEVERLQSELRQARKRRDQaseaLRQASRRLEERQSALDELELQLFPQA 533
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1397-1570 |
2.00e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1397 LEAKLEEVERlatELEKWKEKCNDLETKnnqrsnkehEDNTDVLGKLSNLQDELQESEQKYNADRKKWLEEKMMLITQAK 1476
Cdd:COG3206 187 LRKELEEAEA---ALEEFRQKNGLVDLS---------EEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPD 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1477 EAENIRNKEMkkYAEDRERFLKQQNEVEILTAQLTEKDSDLQKWREERDQL-----------VAALEIQLKALISSNVQK 1545
Cdd:COG3206 255 ALPELLQSPV--IQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALraqlqqeaqriLASLEAELEALQAREASL 332
|
170 180
....*....|....*....|....*
gi 1622966431 1546 DNEIEQLKRIISETSKIETQIMDIK 1570
Cdd:COG3206 333 QAQLAQLEARLAELPELEAELRRLE 357
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1245-1459 |
2.24e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1245 LQLKEEEKETNRQETEKLKEELSAssactqhLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINE 1324
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDA-------LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1325 LekkknqcSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDmrmtLEEQEQTQVEQDQVLEAKLEEV 1404
Cdd:COG3883 91 R-------ARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEE----LKADKAELEAKKAELEAKLAEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622966431 1405 ERLATELEKWKEKCNDLETKNNQRSNKEHEDNTDVLGKLSNLQDELQESEQKYNA 1459
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAA 214
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1078-1350 |
2.60e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.98 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1078 IQELEQQIEKLQAEVKGYKDENNRlkvEENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQI----------QHVVEG 1147
Cdd:pfam12128 250 FNTLESAELRLSHLHFGYKSDETL---IASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELsaadaavakdRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1148 --NRALSELTQGVTCYKAKIKELETIL-ETQKVERSHSAKLE--QDILEK-ESVILKLERNLKELQAHLQDSVKNTKDLS 1221
Cdd:pfam12128 327 leDQHGAFLDADIETAAADQEQLPSWQsELENLEERLKALTGkhQDVTAKyNRRRSKIKEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1222 VKEVKLKEEITQLTNNLQDMKHLLQLKE--EEKETNRQETEKLKEELSASSAcTQHLKADLQRKEEDYAELKEKLTDAKK 1299
Cdd:pfam12128 407 DRQLAVAEDDLQALESELREQLEAGKLEfnEEEYRLKSRLGELKLRLNQATA-TPELLLQLENFDERIERAREEQEAANA 485
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1622966431 1300 QIEQVQkevsvmrDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQL 1350
Cdd:pfam12128 486 EVERLQ-------SELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1077-1238 |
2.73e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.53 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1077 QIQELEQQIEKLQAEVKGYKDE----NNRLKVEENEHKNQDDLLKEKETLIQQLKEELQEKNASLDiqiqhVVEGNRALS 1152
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDElaalEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLG-----NVRNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1153 ELTQGVTCYKAKIKELETILETQKVERshsAKLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDlsvKEVKLKEEIT 1232
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERI---EELEEELAELEAELAELEAELEEKKAELDEELAELEA---ELEELEAERE 166
|
....*.
gi 1622966431 1233 QLTNNL 1238
Cdd:COG1579 167 ELAAKI 172
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1162-1533 |
2.76e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 45.44 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1162 KAKIKELETILETqkvERSHSAKLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDM 1241
Cdd:pfam19220 47 KSRLLELEALLAQ---ERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELRIELRDKTAQAEAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1242 KHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSV----MRDEEKL 1317
Cdd:pfam19220 124 ERQLAAETEQNRALEEENKALREEAQAAEKALQRAEGELATARERLALLEQENRRLQALSEEQAAELAEltrrLAELETQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1318 LRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQ--QYERACKDLNVKEKIIEDMRMTLEEqeqtqveqdq 1395
Cdd:pfam19220 204 LDATRARLRALEGQLAAEQAERERAEAQLEEAVEAHRAERASLrmKLEALTARAAATEQLLAEARNQLRD---------- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1396 vLEAKLEEVERLATELEkwkekcndLETKNNQRSNKEHE-DNTDVLGKLSNLQDELQESEQKYNADRKKwLEEKMMLITQ 1474
Cdd:pfam19220 274 -RDEAIRAAERRLKEAS--------IERDTLERRLAGLEaDLERRTQQFQEMQRARAELEERAEMLTKA-LAAKDAALER 343
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622966431 1475 AKEAENIRNKEMkkyAEDRERFLKQQNEVEILTAQLTEkdsDLQKWREERDQLVAALEI 1533
Cdd:pfam19220 344 AEERIASLSDRI---AELTKRFEVERAALEQANRRLKE---ELQRERAERALAQGALEI 396
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1079-1514 |
2.95e-04 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 45.45 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1079 QELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDL-------LKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRAL 1151
Cdd:pfam05622 17 HELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSgtpggkkYLLLQKQLEQLQEENFRLETARDDYRIKCEELEKEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1152 SELTQgvtcykaKIKELetileTQKVERSHSAKLEQDILEKESvilkleRNLKELQAHLQDSVKNTKDLS--VKEVKLKE 1229
Cdd:pfam05622 97 LELQH-------RNEEL-----TSLAEEAQALKDEMDILRESS------DKVKKLEATVETYKKKLEDLGdlRRQVKLLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1230 EitqltNNLQDMKHLLQLKEEEKETN---------RQETEKLKEELSASSACTQHLKADLQRKEEDYAEL-KEK------ 1293
Cdd:pfam05622 159 E-----RNAEYMQRTLQLEEELKKANalrgqletyKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALqKEKerliie 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1294 --------------------LTDAKKQIEQVQKEVSVMRDE-------EKLLRIkinELEKKKNQCSQE----------- 1335
Cdd:pfam05622 234 rdtlretneelrcaqlqqaeLSQADALLSPSSDPGDNLAAEimpaeirEKLIRL---QHENKMLRLGQEgsyrerltelq 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1336 --LDMKQRTIQQLKEQ--LNNQKVEEAIQQYERACKDLNVKEKIIEDmrmtleeqeqtQVEQDQVLEAKLEEVERLATEL 1411
Cdd:pfam05622 311 qlLEDANRRKNELETQnrLANQRILELQQQVEELQKALQEQGSKAED-----------SSLLKQKLEEHLEKLHEAQSEL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1412 EKWKEKCNDLETKNNQRSNKEhedntdvlgklsnlQDELQESEQKYNADRKKWLEEKMMLITQAKEAenIRNKEMKKYAe 1491
Cdd:pfam05622 380 QKKKEQIEELEPKQDSNLAQK--------------IDELQEALRKKDEDMKAMEERYKKYVEKAKSV--IKTLDPKQNP- 442
|
490 500
....*....|....*....|...
gi 1622966431 1492 drerflKQQNEVEILTAQLTEKD 1514
Cdd:pfam05622 443 ------ASPPEIQALKNQLLEKD 459
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1279-1479 |
3.01e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1279 DLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQkveeA 1358
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER----A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1359 IQQYeRACKDLNVKEKI-----IEDM--RMTLeeqeqtqveQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNK 1431
Cdd:COG3883 93 RALY-RSGGSVSYLDVLlgsesFSDFldRLSA---------LSKIADADADLLEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622966431 1432 EhEDNTDVLGKLSNLQDELQESEQKYNADRKKWLEEKMMLITQAKEAE 1479
Cdd:COG3883 163 K-AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1077-1370 |
3.16e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1077 QIQELEQQIEKLQAEVkgykdenNRLKVEENEHKNQDDLLKEKETLIQQLKEELQEknaslDIQIQHVVegnRALSELTQ 1156
Cdd:COG4913 611 KLAALEAELAELEEEL-------AEAEERLEALEAELDALQERREALQRLAEYSWD-----EIDVASAE---REIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1157 gvtcykakikELETILETqkvershSAKLEQdilekesvilkLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQLTN 1236
Cdd:COG4913 676 ----------ELERLDAS-------SDDLAA-----------LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEE 727
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1237 NLQDMKHLLQLKEEEKETN-RQETEKLKEELSAsSACTQHLKADLQrkeEDYAELKEKLTDAKKQIEQVQKE-------- 1307
Cdd:COG4913 728 ELDELQDRLEAAEDLARLElRALLEERFAAALG-DAVERELRENLE---ERIDALRARLNRAEEELERAMRAfnrewpae 803
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622966431 1308 -VSVMRD-------EEKLLRIKINELEKKKnqcSQELDMKQRTIQQLKEQLnNQKVEEAIQQYERACKDLN 1370
Cdd:COG4913 804 tADLDADleslpeyLALLDRLEEDGLPEYE---ERFKELLNENSIEFVADL-LSKLRRAIREIKERIDPLN 870
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
1077-1307 |
3.25e-04 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 45.02 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1077 QIQELEQQIEKLQAEVKGYKDENNRLKVEENEhknQDDLLKeketlIQQLKEELQEKNASLDIQIQHvvegNRALSELTQ 1156
Cdd:pfam04849 95 QNSVLTERNEALEEQLGSAREEILQLRHELSK---KDDLLQ-----IYSNDAEESETESSCSTPLRR----NESFSSLHG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1157 GVT--CYKAKIKELETILETQKVERSHsAKLEQDILEKESVILKLErNLKELQAHLQDSVKNTKDLSVKE---VKLKEEI 1231
Cdd:pfam04849 163 CVQldALQEKLRGLEEENLKLRSEASH-LKTETDTYEEKEQQLMSD-CVEQLSEANQQMAELSEELARKMeenLRQQEEI 240
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622966431 1232 TQLTNNLQDMKHLLQlkeeekeTNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKE 1307
Cdd:pfam04849 241 TSLLAQIVDLQHKCK-------ELGIENEELQQHLQASKEAQRQLTSELQELQDRYAECLGMLHEAQEELKELRKK 309
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
543-1304 |
3.57e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.82 E-value: 3.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 543 EETQNVETKLIDEDLDKTLEENKAFISHEEKR----KLLDLIEDLKKKLINEKKEKLTLEFKIR------EEVTQEFTQY 612
Cdd:TIGR02168 242 EELQEELKEAEEELEELTAELQELEEKLEELRlevsELEEEIEELQKELYALANEISRLEQQKQilrerlANLERQLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 613 WAQREadfkeTLLQEREILEENAERRLAIFKDLVGKCDTREETTKDVCATIVETEEThnYVGFEDIIDSLQDNVADIKKQ 692
Cdd:TIGR02168 322 EAQLE-----ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESR--LEELEEQLETLRSKVAQLELQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 693 AEIAHLYIASLPDPQEAIA----------------CLELKFNQIKAELTKTKEELIKTKEELKKRENETDSLIQELETSN 756
Cdd:TIGR02168 395 IASLNNEIERLEARLERLEdrrerlqqeieellkkLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 757 KKIITQNQRIQELINTIDQKEGIINEFQNL----KSHMEKTFKCNDKADTSS-----------------------LIINN 809
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEGFsegvKALLKNQSGLSGILGVLSelisvdegyeaaieaalggrlqaVVVEN 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 810 KLICNETVEVPQDSKTKICS--ERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVQPN---------IAENED-- 876
Cdd:TIGR02168 555 LNAAKKAIAFLKQNELGRVTflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlVVDDLDna 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 877 IRVLQKNNEGL-----------------------KALLLTIENELKNEKeekaelnKQIVRFQQELSLSEKKNLTLSKEV 933
Cdd:TIGR02168 635 LELAKKLRPGYrivtldgdlvrpggvitggsaktNSSILERRREIEELE-------EKIEELEEKIAELEKALAELRKEL 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 934 QQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSHEIETATRSItnnvsqiklmhtkidqlrtfdsvsqisnidllnlrdls 1013
Cdd:TIGR02168 708 EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI-------------------------------------- 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1014 ngseednlpnTQLHLLGNDYLVSKQVKEYRIQEPNRESsfhSSIEAIWEECKEIVKSSSKkshQIQELEQQIEKLQAEVK 1093
Cdd:TIGR02168 750 ----------AQLSKELTELEAEIEELEERLEEAEEEL---AEAEAEIEELEAQIEQLKE---ELKALREALDELRAELT 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1094 GYKDENNRLKVEENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRALSELTQGVTcykakiKELETILE 1173
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL------NERASLEE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1174 TQKVERSHSAKLEQDILEKESVILKLERNLKELQAHLQDSVkntKDLSVKEVKLKEEITQLTN----NLQDMKHLLQLKE 1249
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLE---LRLEGLEVRIDNLQERLSEeyslTLEEAEALENKIE 964
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622966431 1250 EEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAEL---KEKLTDAKKQIEQV 1304
Cdd:TIGR02168 965 DDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLtaqKEDLTEAKETLEEA 1022
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1228-1363 |
3.59e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1228 KEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELsassactQHLKADLQ-RKEEDYAELKEKltdAKKQIEQVQK 1306
Cdd:PRK00409 515 KEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEEL-------EEKKEKLQeEEDKLLEEAEKE---AQQAIKEAKK 584
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622966431 1307 EVsvmrdEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYE 1363
Cdd:PRK00409 585 EA-----DEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1279-1424 |
3.61e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1279 DLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEA 1358
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622966431 1359 IQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVE-RLATELEKWKEKCNDLETK 1424
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEaELEEKKAELDEELAELEAE 157
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
914-1439 |
4.05e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.49 E-value: 4.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 914 RFQQELSLSEKKNLTLSKE---VQQIQSNYDI---AIAELHVQKSKNQEQEEKIMKLSHEIETATRSITNNVSQIKLMHT 987
Cdd:pfam15921 445 QMERQMAAIQGKNESLEKVsslTAQLESTKEMlrkVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRS 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 988 KIDqlrtfdsvsqisnIDLLNLRDLSNgsEEDNLPNTQ-------LHLLGNDYLVS--KQVKEYRIQEPNR--------- 1049
Cdd:pfam15921 525 RVD-------------LKLQELQHLKN--EGDHLRNVQtecealkLQMAEKDKVIEilRQQIENMTQLVGQhgrtagamq 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1050 --ESSFHSSIEAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAE-VKGYKDENNRLKVEENEHKNQDDLLKEKETLIQQL 1126
Cdd:pfam15921 590 veKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNEL 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1127 KEELQEknasldiqiQHVVEGNralseltqgvtcYKAKIKELETILETQKVE-RSHSAKLEQDilekesvilklERNLKE 1205
Cdd:pfam15921 670 NSLSED---------YEVLKRN------------FRNKSEEMETTTNKLKMQlKSAQSELEQT-----------RNTLKS 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1206 LQAHLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEE 1285
Cdd:pfam15921 718 MEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRS 797
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1286 DYAELKEKLTDAKKQIEQVQKEVS-----VMRDEEKLLRIKINE-LEKKKNQ---CSQELDMKQRTIQ--QLKEQLNNQK 1354
Cdd:pfam15921 798 QERRLKEKVANMEVALDKASLQFAecqdiIQRQEQESVRLKLQHtLDVKELQgpgYTSNSSMKPRLLQpaSFTRTHSNVP 877
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1355 VEEAIQQY--ERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERlATELEKWKEKCNDLETKNNQRSNKE 1432
Cdd:pfam15921 878 SSQSTASFlsHHSRKTNALKEDPTRDLKQLLQELRSVINEEPTVQLSKAEDKGR-APSLGALDDRVRDCIIESSLRSDIC 956
|
....*..
gi 1622966431 1433 HEDNTDV 1439
Cdd:pfam15921 957 HSSSNSL 963
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1164-1264 |
4.21e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1164 KIKELETiletqKVER--SHSAKLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSvkevKLKEEITQLtnnlqdm 1241
Cdd:COG2433 414 EIRRLEE-----QVERleAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREIS----RLDREIERL------- 477
|
90 100
....*....|....*....|...
gi 1622966431 1242 KHLLQLKEEEKETNRQETEKLKE 1264
Cdd:COG2433 478 ERELEEERERIEELKRKLERLKE 500
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1057-1329 |
4.35e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 45.21 E-value: 4.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1057 IEAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDE--------NNRLKVEE------NEHKNQDDLLKEKETL 1122
Cdd:PRK04778 121 IEQILEELQELLESEEKNREEVEQLKDLYRELRKSLLANRFSfgpaldelEKQLENLEeefsqfVELTESGDYVEAREIL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1123 iQQLKEELQEKNASLDI--------------QIQHVVEGNRALSE---------LTQGVTCYKAKIKELETILETQKVER 1179
Cdd:PRK04778 201 -DQLEEELAALEQIMEEipellkelqtelpdQLQELKAGYRELVEegyhldhldIEKEIQDLKEQIDENLALLEELDLDE 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1180 ShSAKLEQ---------DILEKEsVILK--LERNLKELQAHLQDSVKNTKdlsvkevKLKEEITQLTNNLQ----DMKHL 1244
Cdd:PRK04778 280 A-EEKNEEiqeridqlyDILERE-VKARkyVEKNSDTLPDFLEHAKEQNK-------ELKEEIDRVKQSYTlnesELESV 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1245 LQLKEEEKETNRQeTEKLKEELSASSACTQHLKADLQrkeedyaELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINE 1324
Cdd:PRK04778 351 RQLEKQLESLEKQ-YDEITERIAEQEIAYSELQEELE-------EILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLER 422
|
....*
gi 1622966431 1325 LEKKK 1329
Cdd:PRK04778 423 YRNKL 427
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1224-1532 |
4.81e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1224 EVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDA-KKQIE 1302
Cdd:pfam12128 599 EEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKAlAERKD 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1303 QVQKEVSVMRDEEKLLRIKINE-LEKKKNQCSQELDMKQRTIQQLKEQLNNQ--KVEEAI---------------QQYER 1364
Cdd:pfam12128 679 SANERLNSLEAQLKQLDKKHQAwLEEQKEQKREARTEKQAYWQVVEGALDAQlaLLKAAIaarrsgakaelkaleTWYKR 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1365 ACKDLNVKEKIIEDMRMTLEEqeqtqveqdqvLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHEdntDVLGKLS 1444
Cdd:pfam12128 759 DLASLGVDPDVIAKLKREIRT-----------LERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLS---NIERAIS 824
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1445 NLQDELQESEQKYNADRKKWLEEKmmlitQAKEAENIRNKEMKKYAEDRER---FLKQQNEVEILTAQLTEKDSDLQKWR 1521
Cdd:pfam12128 825 ELQQQLARLIADTKLRRAKLEMER-----KASEKQQVRLSENLRGLRCEMSklaTLKEDANSEQAQGSIGERLAQLEDLK 899
|
330
....*....|.
gi 1622966431 1522 EERDQLVAALE 1532
Cdd:pfam12128 900 LKRDYLSESVK 910
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1227-1417 |
4.89e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.66 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1227 LKEEITQLTNNLQDMKHLL-QLKEEEKETNRQetekLKEELSASSACTQHLKADLQRKEEDYA--------ELKEKLTDA 1297
Cdd:COG1842 28 LDQAIRDMEEDLVEARQALaQVIANQKRLERQ----LEELEAEAEKWEEKARLALEKGREDLArealerkaELEAQAEAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1298 KKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMkQRTIQQLKEQLNNQKVEEAIQQYERackdlnVKEKIie 1377
Cdd:COG1842 104 EAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKA-AKAQEKVNEALSGIDSDDATSALER------MEEKI-- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622966431 1378 dMRMTLEEQEQTQVEQDQVLEAKLEEVE---RLATELEKWKEK 1417
Cdd:COG1842 175 -EEMEARAEAAAELAAGDSLDDELAELEadsEVEDELAALKAK 216
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1077-1373 |
5.21e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.89 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1077 QIQE-LEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLLKEKETLIQQLKEEL------------------------- 1130
Cdd:pfam07888 35 RLEEcLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELrqsrekheeleekykelsasseels 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1131 QEKNASLDIQIQHVVEgnraLSELTQGVTCYKAKIKELETILE--TQKVERSHsAKLEQDILEKESVILKLERNLKELQA 1208
Cdd:pfam07888 115 EEKDALLAQRAAHEAR----IRELEEDIKTLTQRVLERETELErmKERAKKAG-AQRKEEEAERKQLQAKLQQTEEELRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1209 HLQD--SVKNTKDLSVKEV-KLKEEITQLTNNL----------QDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQH 1275
Cdd:pfam07888 190 LSKEfqELRNSLAQRDTQVlQLQDTITTLTQKLttahrkeaenEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1276 LKADLQRKEEDYAELKEKLTDAKKQIE----QVQKEVSVMRDEEKLLRIKINELekkknqcSQELDMKQRTIQqlKEQLN 1351
Cdd:pfam07888 270 TQAELHQARLQAAQLTLQLADASLALRegraRWAQERETLQQSAEADKDRIEKL-------SAELQRLEERLQ--EERME 340
|
330 340
....*....|....*....|..
gi 1622966431 1352 NQKVEEAIQQyERACKDLNVKE 1373
Cdd:pfam07888 341 REKLEVELGR-EKDCNRVQLSE 361
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1140-1428 |
5.69e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 44.73 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1140 QIQHVVEGNRALSELTQGVTCYK-----------AKIKELETILETQKVERSHSAKLE-QDILEKESVILKLERNlKELQ 1207
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKmeqerlrqekeEKAREVERRRKLEEAEKARQAEMDrQAAIYAEQERMAMERE-RELE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1208 AHLQDSVKNTKdlsvkEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETE-----KLKEELSASSACTQHLKADLQR 1282
Cdd:pfam17380 352 RIRQEERKREL-----ERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEaarkvKILEEERQRKIQQQKVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1283 KEEDYA---ELKEKLTDAKKQIEQVQKEVsvMRDEEKLLRIKINELEKKKNQCSQEldmKQRTIQQLKEQLNNQKVEEAI 1359
Cdd:pfam17380 427 AEQEEArqrEVRRLEEERAREMERVRLEE--QERQQQVERLRQQEEERKRKKLELE---KEKRDRKRAEEQRRKILEKEL 501
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622966431 1360 QQYERACKDLNVKEKIIED-----MRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQR 1428
Cdd:pfam17380 502 EERKQAMIEEERKRKLLEKemeerQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERER 575
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1057-1267 |
5.75e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 44.37 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1057 IEAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQddlLKEKETLIQQLKEELQEKNAS 1136
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE---IAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1137 LDIQIQH--------------VVEGNRALSELTQG----VTCYKAKIKELETILETQKVERshsAKLEQDILEKESVILK 1198
Cdd:COG4942 113 LYRLGRQpplalllspedfldAVRRLQYLKYLAPArreqAEELRADLAELAALRAELEAER---AELEALLAELEEERAA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622966431 1199 LERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQLTNNLQDMKHllQLKEEEKETNRQETEKLKEELS 1267
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA--EAAAAAERTPAAGFAALKGKLP 256
|
|
| Motor_domain |
cd01363 |
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ... |
61-183 |
7.85e-04 |
|
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: 42.33 E-value: 7.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 61 VCLRIRPFTQSEKEHESEgcvhildsqtvvlkepqCIlgrlsekssgqmaqkfSFSKVFGPATTQKEFFQGC--IMQPVK 138
Cdd:cd01363 1 VLVRVNPFKELPIYRDSK-----------------II----------------VFYRGFRRSESQPHVFAIAdpAYQSML 47
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1622966431 139 DLLKGQSrlIFTYGLTNSGKTYTfqgteeNMGILPRTLNVLFDSL 183
Cdd:cd01363 48 DGYNNQS--IFAYGESGAGKTET------MKGVIPYLASVAFNGI 84
|
|
| Microtub_bd |
pfam16796 |
Microtubule binding; This motor homology domain binds microtubules and lacks an ATP-binding ... |
110-190 |
8.20e-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: 41.44 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 110 AQKFSFSKVFGPATTQKEFFQ--GCIMQPVkdlLKGQSRLIFTYGLTNSGktytfqgteENMGILPRTLNVLFDSLQERL 187
Cdd:pfam16796 54 NKSFSFDRVFPPESEQEDVFQeiSQLVQSC---LDGYNVCIFAYGQTGSG---------SNDGMIPRAREQIFRFISSLK 121
|
...
gi 1622966431 188 YTK 190
Cdd:pfam16796 122 KGW 124
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1230-1374 |
9.19e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1230 EITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSAssactqhLKADLQRKEEDYAELKEKLTDAKKQIEQV--QKE 1307
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED-------LEKEIKRLELEIEEVEARIKKYEEQLGNVrnNKE 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622966431 1308 VSVMRDEEKLLRIKINELEKKknqcsqELDMKQRtIQQLKEQLnnqkvEEAIQQYERACKDLNVKEK 1374
Cdd:COG1579 91 YEALQKEIESLKRRISDLEDE------ILELMER-IEELEEEL-----AELEAELAELEAELEEKKA 145
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1246-1357 |
1.03e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1246 QLKEEEKETNRQ-ETEKLKEELSASSACTQHLKADLqrkEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINE 1324
Cdd:COG3096 520 QLAELEQRLRQQqNAERLLEEFCQRIGQQLDAAEEL---EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKE 596
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1325 LEKK--------------KNQCSQELDMKQ---RTIQQLKEQLNNQKVEE 1357
Cdd:COG3096 597 LAARapawlaaqdalerlREQSGEALADSQevtAAMQQLLEREREATVER 646
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1198-1364 |
1.03e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 44.27 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1198 KLERNLKELQAHLQDSVKN-TKDLSVKEvkLKEEITQLTNNLQDMKHLLQ---------------LKEEEKETNRQETEK 1261
Cdd:PRK10929 79 KLSAELRQQLNNERDEPRSvPPNMSTDA--LEQEILQVSSQLLEKSRQAQqeqdrareisdslsqLPQQQTEARRQLNEI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1262 LKEELSASSACTQHLKADLqrkeedyAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKInELEKKKnqcSQELDMKqr 1341
Cdd:PRK10929 157 ERRLQTLGTPNTPLAQAQL-------TALQAESAALKALVDELELAQLSANNRQELARLRS-ELAKKR---SQQLDAY-- 223
|
170 180
....*....|....*....|...
gi 1622966431 1342 tIQQLKEQLNNQKVEEAIQQYER 1364
Cdd:PRK10929 224 -LQALRNQLNSQRQREAERALES 245
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
908-1504 |
1.06e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 908 LNKQIVRFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSknqeQEEKIMKLSHEIetatRSITNNVSQIKLMHT 987
Cdd:PRK01156 202 IKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSS----LEDMKNRYESEI----KTAESDLSMELEKNN 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 988 KIDQLRtfDSVSQISNIDLLNLRDLSNGSEEDNlpntqlhllgNDYLVSKQVKEYRIQEPNRESSFHSSIEAIWEECKEI 1067
Cdd:PRK01156 274 YYKELE--ERHMKIINDPVYKNRNYINDYFKYK----------NDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDY 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1068 VKSSSKK---SHQIQELEQQIEKLQAEVKGYkdENNRLKVEENEhknqddllKEKETLIQQLKEELQEKNASLDIQIQHV 1144
Cdd:PRK01156 342 IKKKSRYddlNNQILELEGYEMDYNSYLKSI--ESLKKKIEEYS--------KNIERMSAFISEILKIQEIDPDAIKKEL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1145 VEGNRALSELTQGVTCYKAKIKELetiletqkveRSHSAKLEQD--ILEKESVILKLERNLKElqahlQDSVKNTKDLSV 1222
Cdd:PRK01156 412 NEINVKLQDISSKVSSLNQRIRAL----------RENLDELSRNmeMLNGQSVCPVCGTTLGE-----EKSNHIINHYNE 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1223 KEVKLKEEITQLTNNLQDMKHllQLKEEEKETNRQETEKLkEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIE 1302
Cdd:PRK01156 477 KKSRLEEKIREIEIEVKDIDE--KIVDLKKRKEYLESEEI-NKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKN 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1303 QVQKevsvmrdeekllrIKINELEKKKNQCSQELDMkqrtIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMT 1382
Cdd:PRK01156 554 RYKS-------------LKLEDLDSKRTSWLNALAV----ISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSY 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1383 LEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNDLETKNNQRSNKEHEDNTdVLGKLSNLQDELQESE---QKYNA 1459
Cdd:PRK01156 617 IDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKE-ITSRINDIEDNLKKSRkalDDAKA 695
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1622966431 1460 DRKKWlEEKMMLITQAKEAENIRNKEMKKYAEDRERFLKQQNEVE 1504
Cdd:PRK01156 696 NRARL-ESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLK 739
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1327-1577 |
1.45e-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: 43.21 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1327 KKKNQCSQELDMKQRTIQQLKEQLNNQKVEE--AIQQYERACKDLNVKEKIIEDMRMTLEEqeqtqveqdqvLEAKLEEV 1404
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEkaLLKQLAALERRIAALARRIRALEQELAA-----------LEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1405 ERLATELEKwkekcndlETKNNQRSNKEHEDNTDVLGKLSNLQDELQESEQKYNADRKKWLEEkmMLITQAKEAENIRnK 1484
Cdd:COG4942 89 EKEIAELRA--------ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY--LAPARREQAEELR-A 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1485 EMKKYAEDRERFLKQQNEVEILTAQLTEKDSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIIsetSKIET 1564
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI---ARLEA 234
|
250
....*....|...
gi 1622966431 1565 QIMDIKPRCISSA 1577
Cdd:COG4942 235 EAAAAAERTPAAG 247
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
556-1360 |
1.48e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 556 DLDKTLEENKAFISHEEKRKLLDLIEDLKKKlinekkekltleFKIREEVTQEFTQYWaqrEADFKETLLQEREILEENA 635
Cdd:TIGR01612 624 DLKKIIENNNAYIDELAKISPYQVPEHLKNK------------DKIYSTIKSELSKIY---EDDIDALYNELSSIVKENA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 636 ERRL---AIFKDLVGKCDTREETTKDVCATIVETeethNYVGFEDIIDSLQDNVADIKK--QAEIAHLYIASLPDPQEAI 710
Cdd:TIGR01612 689 IDNTedkAKLDDLKSKIDKEYDKIQNMETATVEL----HLSNIENKKNELLDIIVEIKKhiHGEINKDLNKILEDFKNKE 764
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 711 ACLELKFNqikaELTKTKEELIKTKEELKKRENETDSLIQELETSNKKIITQNQRIQELINTIDQKEG----IINEFQNL 786
Cdd:TIGR01612 765 KELSNKIN----DYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDeifkIINEMKFM 840
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 787 KshmektfkcNDKADTSSLIINNKLICNETVEVPQDSKTKICSERKrvneNELQQDEPPAKKGSIHVSSAITEDQKKSEE 866
Cdd:TIGR01612 841 K---------DDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIK----AEISDDKLNDYEKKFNDSKSLINEINKSIE 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 867 vqpniAENEDIRVLQKNNEGLKALLLT---IENELKNEKEEKAELNKQIVRFQQ----ELSLSEKKNLTLSKEVQQIQSN 939
Cdd:TIGR01612 908 -----EEYQNINTLKKVDEYIKICENTkesIEKFHNKQNILKEILNKNIDTIKEsnliEKSYKDKFDNTLIDKINELDKA 982
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 940 YdiAIAELHVQKSKNQEQEEKIMKLSHEIETATRSITNNVSQIKLMHTKIDQLRTFDSVSQISNIDLLNLRDLSNGSEE- 1018
Cdd:TIGR01612 983 F--KDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEi 1060
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1019 DNLPNTQLHLLGNDYL------------VSKQVKEYRIQEPNRESSFHSSIEAiwEECKEIVKSSSKK-SHQIQELEQQI 1085
Cdd:TIGR01612 1061 EKEIGKNIELLNKEILeeaeinitnfneIKEKLKHYNFDDFGKEENIKYADEI--NKIKDDIKNLDQKiDHHIKALEEIK 1138
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1086 EKLQAEVKGYKDENNRL-KVEENEHKNQDdlLKEKETLIQQLKEELQEKNASLDiqiqhvvEGNRALSELtqgvtcykAK 1164
Cdd:TIGR01612 1139 KKSENYIDEIKAQINDLeDVADKAISNDD--PEEIEKKIENIVTKIDKKKNIYD-------EIKKLLNEI--------AE 1201
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1165 IKELETILETQK-VERSHSAKLEQDILEK--------ESVILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQLT 1235
Cdd:TIGR01612 1202 IEKDKTSLEEVKgINLSYGKNLGKLFLEKideekkksEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNI 1281
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1236 NNLQDMKHLLQLKEEEKETN--RQETEKLKEELSASSACTqhlkaDLQRkeedyaELKEKLTDAKK---QIEQVQKEVSV 1310
Cdd:TIGR01612 1282 SHDDDKDHHIISKKHDENISdiREKSLKIIEDFSEESDIN-----DIKK------ELQKNLLDAQKhnsDINLYLNEIAN 1350
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622966431 1311 MRDEEKLLRIK---------INELEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQ 1360
Cdd:TIGR01612 1351 IYNILKLNKIKkiidevkeyTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKIE 1409
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
719-795 |
1.49e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622966431 719 QIKAELTKTKEELIKTKEELKKRENETDSLIQELETSNKKIITQNQRIQELINTIDQKEGIINEFQNLKSHMEKTFK 795
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
1277-1362 |
1.55e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 41.36 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1277 KADLQRKEEDY-AELKEKLTDAKKQIEQVQKEVSVMRDEEKllRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNNQ-- 1353
Cdd:COG2825 45 QKKLEKEFKKRqAELQKLEKELQALQEKLQKEAATLSEEER--QKKERELQKKQQELQRKQQEAQQDLQKRQQELLQPil 122
|
90
....*....|
gi 1622966431 1354 -KVEEAIQQY 1362
Cdd:COG2825 123 eKIQKAIKEV 132
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
930-1475 |
1.57e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 43.27 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 930 SKEVQQIQSNYDIAIAELhvqKSKNQEQEEKIMKLSHEIETATRSITNNVSQI-------KLMHTKIDQLRtfdsvsqis 1002
Cdd:pfam10174 228 TKALQTVIEMKDTKISSL---ERNIRDLEDEVQMLKTNGLLHTEDREEEIKQMevykshsKFMKNKIDQLK--------- 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1003 nidllnlRDLSNGSEEDNLPNTQLHLLGNDYLVSKQ----VKEYRIQEPNRESSFHSSIEAIWEECKEIVKSSSKKSHQI 1078
Cdd:pfam10174 296 -------QELSKKESELLALQTKLETLTNQNSDCKQhievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1079 QELEQQIEKLQAEVKGYKDennRLKVEEnehKNQDDLLKEKETLIQQLKEElqeknasldiqiqhvvegNRALSELtqgv 1158
Cdd:pfam10174 369 QDLTEEKSTLAGEIRDLKD---MLDVKE---RKINVLQKKIENLQEQLRDK------------------DKQLAGL---- 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1159 tcyKAKIKELETILETQKverSHSAKLEQDILEKESVILKL----ERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQL 1234
Cdd:pfam10174 421 ---KERVKSLQTDSSNTD---TALTTLEEALSEKERIIERLkeqrEREDRERLEELESLKKENKDLKEKVSALQPELTEK 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1235 TNNLQDMKHLLQ------LKEEEKETNRQ-ETEKLKEELSASSacTQHLKAdlqRKEEDYAELKEKLTDakkQIEQVQKE 1307
Cdd:pfam10174 495 ESSLIDLKEHASslassgLKKDSKLKSLEiAVEQKKEECSKLE--NQLKKA---HNAEEAVRTNPEIND---RIRLLEQE 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1308 VSVMRDE--------EKLLRIkINELEKKKNQCSQEL-DMKQRTIQQLKEQLNNQKVEEAIQQYERackdlnvKEKIIED 1378
Cdd:pfam10174 567 VARYKEEsgkaqaevERLLGI-LREVENEKNDKDKKIaELESLTLRQMKEQNKKVANIKHGQQEMK-------KKGAQLL 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1379 MRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKCNdletkNNQRSNKEHEdntdvlGKLSNLQdelqeseqkyn 1458
Cdd:pfam10174 639 EEARRREDNLADNSQQLQLEELMGALEKTRQELDATKARLS-----STQQSLAEKD------GHLTNLR----------- 696
|
570
....*....|....*..
gi 1622966431 1459 ADRKKWLEEKMMLITQA 1475
Cdd:pfam10174 697 AERRKQLEEILEMKQEA 713
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1280-1561 |
1.61e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1280 LQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRikinELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAI 1359
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIK----EKEKELEEVLREINEISSELPELREEL--EKLEKEV 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1360 QQYERACKDLNVKEKIIEDMR---MTLEEQEQTQVEQDQVLEAKLEEVERLATELEKWKEKC------NDLETKNNQRSN 1430
Cdd:PRK03918 231 KELEELKEEIEELEKELESLEgskRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAeeyiklSEFYEEYLDELR 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1431 KEHEDNTDVLGKLSNLQDELQESEQKYNadRKKWLEEKMmlitqaKEAENiRNKEMKKYAEDRERFLKQQNEVEILTAQL 1510
Cdd:PRK03918 311 EIEKRLSRLEEEINGIEERIKELEEKEE--RLEELKKKL------KELEK-RLEELEERHELYEEAKAKKEELERLKKRL 381
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622966431 1511 TEKD-SDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSK 1561
Cdd:PRK03918 382 TGLTpEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1224-1456 |
1.63e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1224 EVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQ 1303
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1304 VQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKE---QLNNQKVEEaiqQYERacKDLNVKEKIIEDMR 1380
Cdd:pfam07888 113 LSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKErakKAGAQRKEE---EAER--KQLQAKLQQTEEEL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622966431 1381 MTLEEQEQtqveqdqvlEAKLEEVERlATELEKWKEKCNDLETKNNQRSNKEHEdNTDVLGKLSNLQDELQESEQK 1456
Cdd:pfam07888 188 RSLSKEFQ---------ELRNSLAQR-DTQVLQLQDTITTLTQKLTTAHRKEAE-NEALLEELRSLQERLNASERK 252
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1191-1367 |
1.84e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1191 EKESVILKLERNLKELQAHLQDsvkntkdLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASS 1270
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAE-------LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1271 acTQHLKADLQRKEEDyaeLKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQL 1350
Cdd:COG1579 87 --NNKEYEALQKEIES---LKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEEL 161
|
170 180
....*....|....*....|....
gi 1622966431 1351 NNQKVE-------EAIQQYERACK 1367
Cdd:COG1579 162 EAEREElaakippELLALYERIRK 185
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1055-1527 |
1.86e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 43.24 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1055 SSIEAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLLKEKETLIQQLKEElqEKN 1134
Cdd:pfam01576 538 GTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAE--EKA 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1135 ASLdiqiQHVVEGNRALSELTQGVTCYKAKIKELETILETQKvershsakleqdilekesvilKLERNLKELQAHLQDSV 1214
Cdd:pfam01576 616 ISA----RYAEERDRAEAEAREKETRALSLARALEEALEAKE---------------------ELERTNKQLRAEMEDLV 670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1215 KNTKDLSVKEVKLKEEITQLTNNLQDMKhlLQLKEEEKETNRQETEKLKEELSASSACTQHLKaDLQRKEEDYAElkekl 1294
Cdd:pfam01576 671 SSKDDVGKNVHELERSKRALEQQVEEMK--TQLEELEDELQATEDAKLRLEVNMQALKAQFER-DLQARDEQGEE----- 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1295 tdAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKknqcsQELDMKQrtiqqLKEQLN--NQKVEEAIQQYERACKDLNVK 1372
Cdd:pfam01576 743 --KRRQLVKQVRELEAELEDERKQRAQAVAAKKK-----LELDLKE-----LEAQIDaaNKGREEAVKQLKKLQAQMKDL 810
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1373 EKIIEDMRMTLEEQEQTQVEQdqvlEAKLEEVERLATELEKwkekcnDLETKNNQRSNKEHEdntdvlgklsnlQDELQE 1452
Cdd:pfam01576 811 QRELEEARASRDEILAQSKES----EKKLKNLEAELLQLQE------DLAASERARRQAQQE------------RDELAD 868
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622966431 1453 SEQKYNADRKKWLEEKMMLITQAKEAENIRNKEMKKYAEDRERFLKQQNEVEILTAQLTEKDSDLQKWREERDQL 1527
Cdd:pfam01576 869 EIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQL 943
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1074-1368 |
1.93e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 43.09 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1074 KSHQIQELE------QQIEKLQAEVKGYKDENNrlKVEENEHKNQDDLLKEKEtLIQQLK--------EELQEKNASLDI 1139
Cdd:pfam05701 27 KAHRIQTVErrklveLELEKVQEEIPEYKKQSE--AAEAAKAQVLEELESTKR-LIEELKlnleraqtEEAQAKQDSELA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1140 QIQhvvegnraLSELTQGVTcYKAKIkELETILETQK------VERSHSAKLEQDILEKESVILKLERNL-----KELQA 1208
Cdd:pfam05701 104 KLR--------VEEMEQGIA-DEASV-AAKAQLEVAKarhaaaVAELKSVKEELESLRKEYASLVSERDIaikraEEAVS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1209 HLQDSVKNTKDLSVKEVKLKEEIT---------------------QLTNNLQdmKHLLQLKEEEKETNRQ--ETEKLKEE 1265
Cdd:pfam05701 174 ASKEIEKTVEELTIELIATKESLEsahaahleaeehrigaalareQDKLNWE--KELKQAEEELQRLNQQllSAKDLKSK 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1266 LSASSACTQHLKADL---------------QRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKI----NELE 1326
Cdd:pfam05701 252 LETASALLLDLKAELaaymesklkeeadgeGNEKKTSTSIQAALASAKKELEEVKANIEKAKDEVNCLRVAAaslrSELE 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1327 KKKnqcsQELD-MKQR------TIQQLKEQLNNQKVE-EAIQQYERACKD 1368
Cdd:pfam05701 332 KEK----AELAsLRQRegmasiAVSSLEAELNRTKSEiALVQAKEKEARE 377
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
910-1319 |
2.19e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.02 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 910 KQIVRFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAEL--HVQKSKNQEQEEKIMKLSHEIETATRSITNNVSQIKLMHT 987
Cdd:PRK04863 786 KRIEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIgsHLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQRS 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 988 KIDQLRTfdsvsqisNIDLLN-LRDLSNGSEEDNLPNtqlhllgndylvskqvkeyRIQEpnressfhssIEAIWEECKE 1066
Cdd:PRK04863 866 QLEQAKE--------GLSALNrLLPRLNLLADETLAD-------------------RVEE----------IREQLDEAEE 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1067 IVKSSSKKSHQIQELEQQIEKLQAEVKGYkdENNRLKVEENEHKNQDdlLKEKetlIQQLKEELQEKNASLDIQIQHVVE 1146
Cdd:PRK04863 909 AKRFVQQHGNALAQLEPIVSVLQSDPEQF--EQLKQDYQQAQQTQRD--AKQQ---AFALTEVVQRRAHFSYEDAAEMLA 981
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1147 GNRALSELtqgvtcYKAKIKELETILETQKVE-RSHSAKLEQdilekesvilklernLKELQAHLQDSvkntkdLSVKEV 1225
Cdd:PRK04863 982 KNSDLNEK------LRQRLEQAEQERTRAREQlRQAQAQLAQ---------------YNQVLASLKSS------YDAKRQ 1034
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1226 KLKEeitqLTNNLQDMKhlLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQ 1305
Cdd:PRK04863 1035 MLQE----LKQELQDLG--VPADSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMR 1108
|
410 420
....*....|....*....|....*...
gi 1622966431 1306 KEV--------SVMR------DEEKLLR 1319
Cdd:PRK04863 1109 EQVvnakagwcAVLRlvkdngVERRLHR 1136
|
|
| GOLGA2L5 |
pfam15070 |
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ... |
1077-1351 |
2.25e-03 |
|
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.
Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 42.74 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1077 QIQELEQQIEKLQaevkgykdenNRLKVEENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQIQHVVEGNRALSELTQ 1156
Cdd:pfam15070 51 QVQELETSLAELK----------NQAAVPPAEEEQPPAGPSEEEQRLQEEAEQLQKELEALAGQLQAQVQDNEQLSRLNQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1157 GvtcYKAKIKELETILETQkverSHSAKLEQDILEKE-------SVILKLERNLKELQAHLQDS-VKNTKD--------L 1220
Cdd:pfam15070 121 E---QEQRLLELERAAERW----GEQAEDRKQILEDMqsdratiSRALSQNRELKEQLAELQNGfVKLTNEnmeltsalQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1221 SVKEVK--LKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKAD---LQRKEEDYAELKEKLt 1295
Cdd:pfam15070 194 SEQHVKkeLAKKLGQLQEELGELKETLELKSQEAQSLQEQRDQYLAHLQQYVAAYQQLASEkeeLHKQYLLQTQLMDRL- 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622966431 1296 dakkQIEQVQKEVSVmrdeekllrikinELEKKKNQCSQE-LDMKQRTIQQLKEQLN 1351
Cdd:pfam15070 273 ----QHEEVQGKVAA-------------EMARQELQETQErLEALTQQNQQLQAQLS 312
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1077-1314 |
2.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1077 QIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKnqDDLLKEKETLIQQLKEELQEKNASLDIQIQHVvegnralseltq 1156
Cdd:COG4913 256 PIRELAERYAAARERLAELEYLRAALRLWFAQRR--LELLEAELEELRAELARLEAELERLEARLDAL------------ 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1157 gvtcyKAKIKELETILETQKVERShsAKLEQDILEKESVILKLERNLKELQAHLQDSvkntkdlsvkEVKLKEEITQLTN 1236
Cdd:COG4913 322 -----REELDELEAQIRGNGGDRL--EQLEREIERLERELEERERRRARLEALLAAL----------GLPLPASAEEFAA 384
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622966431 1237 NLQDMKHLLQ-LKEEEKETNRQETEklkeelsassactqhLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDE 1314
Cdd:COG4913 385 LRAEAAALLEaLEEELEALEEALAE---------------AEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
572-1312 |
2.42e-03 |
|
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: 43.03 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 572 EKRKLLDLIEDLKKKLINEKKEKLTLEFKIREEVTQEFTQYWAQREADFKETLLQEREILEenaerrlaifkdlvgkcdt 651
Cdd:TIGR00618 176 DQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQ------------------- 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 652 reettkdvcativETEETHNYVGFEDII----DSLQDNVADIKKQAEIAHLYIASLPDPQEAI--ACLELKFNQIKAELT 725
Cdd:TIGR00618 237 -------------QTQQSHAYLTQKREAqeeqLKKQQLLKQLRARIEELRAQEAVLEETQERInrARKAAPLAAHIKAVT 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 726 KTKEELIKTKEELKKRENETDSLIQELETSNKKIITQNQRiQELINTIDQKEgIINEFQNLKSHMEKTFKCNDKADTSSL 805
Cdd:TIGR00618 304 QIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ-RRLLQTLHSQE-IHIRDAHEVATSIREISCQQHTLTQHI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 806 IINNKLICNETvEVPQDSKTKICSERKRVNENELQQDEPPAKKGSIHVSSAITEDQKKSEEVQPNIAENEDIRVLQKN-- 883
Cdd:TIGR00618 382 HTLQQQKTTLT-QKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKih 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 884 -NEGLKALLLTIENELKNEKEEKAELNKQIVRFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAElhVQKSKNQEQEEKIM 962
Cdd:TIGR00618 461 lQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPG--PLTRRMQRGEQTYA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 963 KLSHEIETATRSITNNVSQIKLMHTKIDQLRTfdsvsqisniDLLNLRDLSNGSEEDNLPNTQLHLLGNDYLVSKQVKEY 1042
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQMQEIQQ----------SFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAED 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1043 RIQEPNRESSFHSSIEAiweECKEIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHK---NQDDLLKEK 1119
Cdd:TIGR00618 609 MLACEQHALLRKLQPEQ---DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKEllaSRQLALQKM 685
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1120 ETLIQQL---KEELQEKNASLDIQIQHVVEGNRALSELTQGVTCYKAKIKELETIL--------ETQKVERSHSAKLEQD 1188
Cdd:TIGR00618 686 QSEKEQLtywKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALnqslkelmHQARTVLKARTEAHFN 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1189 ILEKESVILKLERNLKELQAHLQDSVKNTKDLSVKEVKLKEEITqltnnlQDMKHLLQLKEEEKETNRQETEKLKEELSA 1268
Cdd:TIGR00618 766 NNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIG------QEIPSDEDILNLQCETLVQEEEQFLSRLEE 839
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1622966431 1269 SSAcTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMR 1312
Cdd:TIGR00618 840 KSA-TLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGIN 882
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1079-1297 |
2.50e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1079 QELEQQIEKLQAEVKGYKDENNRLkveENEHKNQDDLLKEKETLIQQLKEELQEKNASLDIQIQHVV-----EGNRALSE 1153
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEA---EALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIkeakkEADEIIKE 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1154 LTQGVTCYKAKIKELETIlETQKvershsaKLEQDILEKESVILKLERNLKELQAHlqDSVK----NTKD--LSV---KE 1224
Cdd:PRK00409 593 LRQLQKGGYASVKAHELI-EARK-------RLNKANEKKEKKKKKQKEKQEELKVG--DEVKylslGQKGevLSIpddKE 662
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622966431 1225 VKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKeelsassacTQHLKADL--QRKEEDYAELKEKLTDA 1297
Cdd:PRK00409 663 AIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPR---------TVSLELDLrgMRYEEALERLDKYLDDA 728
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1065-1468 |
2.84e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.73 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1065 KEIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLLKEKETLIQQLKEELQ-EKNASLDIQIqh 1143
Cdd:TIGR00606 716 SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEEsAKVCLTDVTI-- 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1144 vvegnraLSELTQGVTCYKAKIKELETILETQKVERSHSaKLEQDILEKESVILKLERNLKELQAHLQDSVKNTKDLSVK 1223
Cdd:TIGR00606 794 -------MERFQMELKDVERKIAQQAAKLQGSDLDRTVQ-QVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSK 865
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1224 EVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQ 1303
Cdd:TIGR00606 866 TNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVND 945
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1304 VQKEVSVMRDEEKLLRIKINElEKKKNQCSQELDMKQRTIQQLKEQLNNQKVEEAIQQYERACKDLNVKEKIIEDmrmtl 1383
Cdd:TIGR00606 946 IKEKVKNIHGYMKDIENKIQD-GKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQD----- 1019
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1384 eeqeqtqVEQDQVLEAKLEEVERlatELEKWKEKCNDLETKNNQRSNKEHEDNTDVLGKLSNLQDELQESEQKYNADRKK 1463
Cdd:TIGR00606 1020 -------NLTLRKRENELKEVEE---ELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKK 1089
|
....*
gi 1622966431 1464 WLEEK 1468
Cdd:TIGR00606 1090 ELREP 1094
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1201-1565 |
3.98e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1201 RNLKELQAHLQDSVKNTKDLSVKEVKLKEEITQLTNnlqdmkhllqLKEEEKETNRQETEkLKEELSASSACTQHLKADL 1280
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAAEQYRLVE----------MARELAELNEAESD-LEQDYQAASDHLNLVQTAL 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1281 --QRKEEDYAELKEKLTDakkQIEQvQKEVSVMRDEEKLlrikinELEKKKNQCSQELDmkqrtiqQLKEQLNN-QKVEE 1357
Cdd:PRK04863 345 rqQEKIERYQADLEELEE---RLEE-QNEVVEEADEQQE------ENEARAEAAEEEVD-------ELKSQLADyQQALD 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1358 AIQ----QYERACKDLNVKEKIIEDMRMTLEEqeqtqveqdqvLEAKLEEverLATELEKWKEKCNDLETKNNQrSNKEH 1433
Cdd:PRK04863 408 VQQtraiQYQQAVQALERAKQLCGLPDLTADN-----------AEDWLEE---FQAKEQEATEELLSLEQKLSV-AQAAH 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1434 EDNTDVLGKLSNLQDELQESEQKYNADRK--KWLEEKMmlitQAKEAENIRNKemkkYAEDRERFLKQQNEVEILT---- 1507
Cdd:PRK04863 473 SQFEQAYQLVRKIAGEVSRSEAWDVARELlrRLREQRH----LAEQLQQLRMR----LSELEQRLRQQQRAERLLAefck 544
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622966431 1508 ---AQLTEKDsDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQ 1565
Cdd:PRK04863 545 rlgKNLDDED-ELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPA 604
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1210-1413 |
4.29e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1210 LQDSVKNTKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSAssactqhLKADLQRKEEDYAE 1289
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE-------AEAEIEERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1290 L-------------------KEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKnqcsQELDMKQRTIQQLKEQL 1350
Cdd:COG3883 91 RaralyrsggsvsyldvllgSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKK----AELEAKLAELEALKAEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622966431 1351 NNQK--VEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEK 1413
Cdd:COG3883 167 EAAKaeLEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
877-1413 |
4.56e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 877 IRVLQKNNEGLKALLLTIENELKNEKEEKAELNKQIVRFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQE 956
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 957 QEEKIMKLSHEIETATRSITNNVSQIKLMHTKIDQLRTFDSVSQISNIDLLNLRDLSNGSEEDnlpntQLHLLGNDYLVS 1036
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE-----AEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1037 KQVKEYRIQEPNRESSFHSSIEAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLL 1116
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1117 KEKETLIQQLKEELQEKNASLDIQIQHVVEGNRALSELTQGVTcYKAKIKELETILETQKVERSHSAKLEQDILEKES-- 1194
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK-AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAaa 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1195 ---VILKLERNLKELQAHLQDSVKNTKD-LSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASS 1270
Cdd:COG1196 548 lqnIVVEDDEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTL 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1271 ACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMK----QRTIQQL 1346
Cdd:COG1196 628 VAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEeallAEEEEER 707
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622966431 1347 KEQLNNQKVEEAIQQYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEK 1413
Cdd:COG1196 708 ELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1284-1551 |
4.88e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1284 EEDYAELKEKLTDAKKQIEQVQKEVSVMRDEekllrikINELEKKKNQCSQELDMKQRTIQQLKEQLnnQKVEEAIQQYe 1363
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAE-------LEELNEEYNELQAELEALQAEIDKLQAEI--AEAEAEIEER- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1364 rackdlnvKEKIIEDMRmTLEEQEQTQVEQDQVLEAKleeverlatelekwkekcnDLETKNNQRS--NKEHEDNTDVLG 1441
Cdd:COG3883 85 --------REELGERAR-ALYRSGGSVSYLDVLLGSE-------------------SFSDFLDRLSalSKIADADADLLE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1442 KLSNLQDELQESEQKYNADRKKwleekmmLITQAKEAEnirnkEMKKYAEdrerflKQQNEVEILTAQLTEKDSDLQkwr 1521
Cdd:COG3883 137 ELKADKAELEAKKAELEAKLAE-------LEALKAELE-----AAKAELE------AQQAEQEALLAQLSAEEAAAE--- 195
|
250 260 270
....*....|....*....|....*....|
gi 1622966431 1522 EERDQLVAALEIQLKALISSNVQKDNEIEQ 1551
Cdd:COG3883 196 AQLAELEAELAAAEAAAAAAAAAAAAAAAA 225
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
910-1563 |
4.91e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 41.96 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 910 KQIVRFQQELSLSEKKNLTLSKEVQQIQSNYDIAIAELHVQKSKNQEQEEKIMKLSHEIETATRSI-------TNNVSQI 982
Cdd:TIGR01612 558 KLIHEIKKELEEENEDSIHLEKEIKDLFDKYLEIDDEIIYINKLKLELKEKIKNISDKNEYIKKAIdlkkiieNNNAYID 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 983 KLMHTKIDQ----LRTFDSV--------SQISNIDLLNL-RDLSNGSEEDNLPNTQLHLLGNDyLVSKQVKEY-RIQEPN 1048
Cdd:TIGR01612 638 ELAKISPYQvpehLKNKDKIystikselSKIYEDDIDALyNELSSIVKENAIDNTEDKAKLDD-LKSKIDKEYdKIQNME 716
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1049 RES--SFHSSIEAIWEECKEIVKSSSKKSHQiqELEQQIEKLqaeVKGYKDENNRLKVEENEHKNQDDLLKEKETLIQQL 1126
Cdd:TIGR01612 717 TATveLHLSNIENKKNELLDIIVEIKKHIHG--EINKDLNKI---LEDFKNKEKELSNKINDYAKEKDELNKYKSKISEI 791
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1127 KEELQEKNASLDIQIQHVVEGNRALSELTQGVTcykakIKELETILETQKVErshsaKLEQDILEKESVILKLERNLKEL 1206
Cdd:TIGR01612 792 KNHYNDQINIDNIKDEDAKQNYDKSKEYIKTIS-----IKEDEIFKIINEMK-----FMKDDFLNKVDKFINFENNCKEK 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1207 QAHLQDSVKNTKDLSVKEVKlKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACtQHLKADLQRKEED 1286
Cdd:TIGR01612 862 IDSEHEQFAELTNKIKAEIS-DDKLNDYEKKFNDSKSLINEINKSIEEEYQNINTLKKVDEYIKIC-ENTKESIEKFHNK 939
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1287 YAELKEKLTDAKKQIEQVQK-EVSVMRDEEKLLRIKINELEKKKNQCS-QELDMKQRTIQQ----LKEQLNNQKVEEAIQ 1360
Cdd:TIGR01612 940 QNILKEILNKNIDTIKESNLiEKSYKDKFDNTLIDKINELDKAFKDASlNDYEAKNNELIKyfndLKANLGKNKENMLYH 1019
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1361 QYERACKDLNVKEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEE-----VERLATELekwKEKCNDLETKNNQRSNKEhed 1435
Cdd:TIGR01612 1020 QFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKeigknIELLNKEI---LEEAEINITNFNEIKEKL--- 1093
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1436 ntdvlgKLSNLQDELQESEQKYnADRKKWLEEKMMLITQAKEAENIRNKEMKKyaedrerflKQQNEVEILTAQLT--EK 1513
Cdd:TIGR01612 1094 ------KHYNFDDFGKEENIKY-ADEINKIKDDIKNLDQKIDHHIKALEEIKK---------KSENYIDEIKAQINdlED 1157
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1514 DSDLQKWREErdqlVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIE 1563
Cdd:TIGR01612 1158 VADKAISNDD----PEEIEKKIENIVTKIDKKKNIYDEIKKLLNEIAEIE 1203
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1228-1352 |
7.30e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 40.77 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1228 KEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEEL-SASSACTQHLKADLQRKEEDYAELKEKLTDAKKQIEQVQK 1306
Cdd:smart00787 160 YKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELeDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELES 239
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622966431 1307 EVSVMRDEEKLLRIKINELEKKKNQCSQeldMKQRTIQQLKEQLNN 1352
Cdd:smart00787 240 KIEDLTNKKSELNTEIAEAEKKLEQCRG---FTFKEIEKLKEQLKL 282
|
|
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
1082-1365 |
7.38e-03 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 41.47 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1082 EQQIEKLQAEVKGYKDENNRL--KVEENEHKNQDDLLKeKETLIQQLKE-------------ELQEKNASLDIQIQHVVE 1146
Cdd:pfam15818 91 EKEIEGLKETLKALQVSKYSLqkKVSEMEQKLQLHLLA-KEDHHKQLNEiekyyatitgqfgLVKENHGKLEQNVQEAIQ 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1147 GNRALSELTQG----VTCYKAKIKELETILETQKVERSHSakleqdiLEKESVILKL-ERNLKELQAHLQDSVKNTKDLS 1221
Cdd:pfam15818 170 LNKRLSALNKKqeseICSLKKELKKVTSDLIKSKVTCQYK-------MGEENINLTIkEQKFQELQERLNMELELNKKIN 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1222 VKEVKLKEEITQLTNNLQDMKHLLQlkeeeKETnrQETEKLKEELSASSACTQHLKAD--LQRK-----EEDYAELKEKL 1294
Cdd:pfam15818 243 EEITHIQEEKQDIIISFQHMQQLLQ-----QQT--QANTEMEAELKALKENNQTLERDneLQREkvkenEEKFLNLQNEH 315
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622966431 1295 TDA----KKQIEQVQKEVSVMRDEEKLLRIKINELEKKKN-QCSQELDMKQRTIQQLKEqLNNQKVEEAIQQYERA 1365
Cdd:pfam15818 316 EKAlgtwKKHVEELNGEINEIKNELSSLKETHIKLQEHYNkLCNQKKFEEDKKFQNVPE-VNNENSEMSTEKSENL 390
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1073-1364 |
7.45e-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: 40.99 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1073 KKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLLKEKetlIQQLKEELQEKNAS-------LDIQIQHVV 1145
Cdd:pfam06160 83 KAKKALDEIEELLDDIEEDIKQILEELDELLESEEKNREEVEELKDK---YRELRKTLLANRFSygpaideLEKQLAEIE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1146 EGNRALSELTQGVTCYKAK---------IKELETILET-----QKVERSHSAKLE------QDILEKESVI--LKLERNL 1203
Cdd:pfam06160 160 EEFSQFEELTESGDYLEARevlekleeeTDALEELMEDipplyEELKTELPDQLEelkegyREMEEEGYALehLNVDKEI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1204 KELQAHLQDSVKNTKDLSVKEVklKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSACTQHLKADLQRK 1283
Cdd:pfam06160 240 QQLEEQLEENLALLENLELDEA--EEALEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERV 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1284 EEDY---AELKEKLTDAKKQIEQVQKEvsVMRDEEKLLRIKI--NELEKKKNQCSQELDMKQRTIQQLKEQLNN-----Q 1353
Cdd:pfam06160 318 QQSYtlnENELERVRGLEKQLEELEKR--YDEIVERLEEKEVaySELQEELEEILEQLEEIEEEQEEFKESLQSlrkdeL 395
|
330
....*....|.
gi 1622966431 1354 KVEEAIQQYER 1364
Cdd:pfam06160 396 EAREKLDEFKL 406
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1062-1351 |
7.45e-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: 40.99 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1062 EECKEIVKSSSKKSHQIQELEQQIEKLQAEVK-GYKDENNRLKVEENEHKNQDDLLKEKETL--IQQLKEELQEKNASLD 1138
Cdd:pfam06160 175 LEAREVLEKLEEETDALEELMEDIPPLYEELKtELPDQLEELKEGYREMEEEGYALEHLNVDkeIQQLEEQLEENLALLE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1139 -IQIQHVVEGNRALSEltqgvtcykaKIKELetiletqkvershsakleQDILEKESVILK-LERNLKELQAHLQDSVKN 1216
Cdd:pfam06160 255 nLELDEAEEALEEIEE----------RIDQL------------------YDLLEKEVDAKKyVEKNLPEIEDYLEHAEEQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1217 TKDLsvkevklKEEITQLtnnlqdmKHLLQLKEEEKETNRQetekLKEELSASSACTQHLKADLQRKEEDYAELKEKLTD 1296
Cdd:pfam06160 307 NKEL-------KEELERV-------QQSYTLNENELERVRG----LEKQLEELEKRYDEIVERLEEKEVAYSELQEELEE 368
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1622966431 1297 AKKQIEQVQKEVSVMRDEEKLLRIKinelEKKKNQCSQELDMKQRTIQQLKEQLN 1351
Cdd:pfam06160 369 ILEQLEEIEEEQEEFKESLQSLRKD----ELEAREKLDEFKLELREIKRLVEKSN 419
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1022-1269 |
7.61e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 40.83 E-value: 7.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1022 PNTQLHLL---GNDylvSKQVKEYRiqepnressfhssieAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAEVkgykDE 1098
Cdd:COG0497 140 PDAQRELLdafAGL---EELLEEYR---------------EAYRAWRALKKELEELRADEAERARELDLLRFQL----EE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1099 NNRLKVEENEhknQDDLLKEKETL---------IQQLKEELQEKNASLDIQIQHVVegnRALSELTQgvtcYKAKIKELE 1169
Cdd:COG0497 198 LEAAALQPGE---EEELEEERRRLsnaeklreaLQEALEALSGGEGGALDLLGQAL---RALERLAE----YDPSLAELA 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1170 TILETQKVE--------RSHSAKLEQD------ILEKESVILKLER----NLKELQAHLQdsvkntkdlsvkevKLKEEI 1231
Cdd:COG0497 268 ERLESALIEleeaaselRRYLDSLEFDperleeVEERLALLRRLARkygvTVEELLAYAE--------------ELRAEL 333
|
250 260 270
....*....|....*....|....*....|....*...
gi 1622966431 1232 TQLTNNLQDMKHLlqlkEEEKETNRQETEKLKEELSAS 1269
Cdd:COG0497 334 AELENSDERLEEL----EAELAEAEAELLEAAEKLSAA 367
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
1198-1360 |
8.36e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 40.43 E-value: 8.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1198 KLERNLKELQAHLQDSVKNTKDLSVKEvkLKEEITQLTNNLQDmkhllqlkeeEKETNRQETEKLKEELSASSACTQHLK 1277
Cdd:cd22656 88 TIDSYYAEILELIDDLADATDDEELEE--AKKTIKALLDDLLK----------EAKKYQDKAAKVVDKLTDFENQTEKDQ 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1278 ADLQRKEEDYAEL--KEKLTDAKKQIEQVQKEV-SVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQL---KEQLN 1351
Cdd:cd22656 156 TALETLEKALKDLltDEGGAIARKEIKDLQKELeKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLIADLtaaDTDLD 235
|
170
....*....|.
gi 1622966431 1352 N--QKVEEAIQ 1360
Cdd:cd22656 236 NllALIGPAIP 246
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1053-1570 |
8.60e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1053 FHSSIEAIWEECKEIVKSSSKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLLKEKETLIQQLKEELQE 1132
Cdd:PRK01156 129 FLNSIFVGQGEMDSLISGDPAQRKKILDEILEINSLERNYDKLKDVIDMLRAEISNIDYLEEKLKSSNLELENIKKQIAD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1133 KNASLDIQIQHVVEGNRALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEQDILEKESVILKLERNLKELQAHLQD 1212
Cdd:PRK01156 209 DEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKIIND 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1213 SVKNTKDLSVKEVKLKEEITQLTNNLQDMKHLLQ------LKEEEKETNRQETEKLKEELSAssacTQHLKADLQRKEED 1286
Cdd:PRK01156 289 PVYKNRNYINDYFKYKNDIENKKQILSNIDAEINkyhaiiKKLSVLQKDYNDYIKKKSRYDD----LNNQILELEGYEMD 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1287 YAELKEKLTDAKKQIEQVQKEVSVMRDE--EKLLRIKIN--ELEKKKNQCSQELDMKQRTIQQLkeqlnNQKVEEAIQQY 1362
Cdd:PRK01156 365 YNSYLKSIESLKKKIEEYSKNIERMSAFisEILKIQEIDpdAIKKELNEINVKLQDISSKVSSL-----NQRIRALRENL 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1363 ERACKDLNV------------------KEKIIEDMRMTLEEQEQTQVEQDQVLEAKLEEVERLATELEKW-KEKCNDLET 1423
Cdd:PRK01156 440 DELSRNMEMlngqsvcpvcgttlgeekSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLeSEEINKSIN 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1424 KNNQRSNKEHE--DNTDVLGKLSNLQDELQESEQKYN--------ADRKKWLeeKMMLITQAKEAENIRNK--EMKKYAE 1491
Cdd:PRK01156 520 EYNKIESARADleDIKIKINELKDKHDKYEEIKNRYKslkledldSKRTSWL--NALAVISLIDIETNRSRsnEIKKQLN 597
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622966431 1492 DRErflKQQNEVEIltaQLTEKDSDLQKWREERDQLVAALEIQLKALISSNVQKDNEIEQLKRIISETSKIETQIMDIK 1570
Cdd:PRK01156 598 DLE---SRLQEIEI---GFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLK 670
|
|
| CDC37_N |
smart01071 |
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of ... |
1223-1330 |
8.84e-03 |
|
Cdc37 N terminal kinase binding; Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This domain corresponds to the N terminal domain which binds predominantly to protein kinases.and is found N terminal to the Hsp (Heat shocked protein) 90-binding domain. Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 results in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function.
Pssm-ID: 198139 [Multi-domain] Cd Length: 154 Bit Score: 38.94 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1223 KEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRqeteklKEELSASSACTQHLKADLQRKEEDYAELKEKltDAKKQIE 1302
Cdd:smart01071 40 ARVERMEEIKNLKYELIMNDHLNKRIDKLLKGLR------EEELSPETPTYNEMLAELQDQLKKELEEANG--DSEGLLE 111
|
90 100
....*....|....*....|....*...
gi 1622966431 1303 QVQKEVSVMRDEEKLLRIKINELEKKKN 1330
Cdd:smart01071 112 ELKKHRDKLKKEQKELRKKLDELEKEEK 139
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1072-1456 |
9.29e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1072 SKKSHQIQELEQQIEKLQAEVKGYKDENNRLKVEENEHKNQDDLLKEKETLIQ---QLKEELQEKNASL------DIQIQ 1142
Cdd:pfam05557 128 QSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQsqeQDSEIVKNSKSELaripelEKELE 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1143 HVVEGNRALSELTQGVTCYKAKIKELETILETQKVERSHSAKLEqdiLEKESVILKLERNLKELQAHLQDSVK------N 1216
Cdd:pfam05557 208 RLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREEAATLE---LEKEKLEQELQSWVKLAQDTGLNLRSpedlsrR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1217 TKDLSVKEVKLKEEITQLTNNLQDMKHLLQLKEEEKETNRQETEKLKEELSASSActqhLKADLQR------KEEDY--- 1287
Cdd:pfam05557 285 IEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKA----LVRRLQRrvllltKERDGyra 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1288 ------AELKEKLTDAKK--QIEQVQKEVSVMRDEEKLLRIKINELEKKKNQCSQELDMKQRTIQQLKEQLNN------- 1352
Cdd:pfam05557 361 ilesydKELTMSNYSPQLleRIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERELQALRQQESLadpsysk 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622966431 1353 -------QKVEEAIQQYERACKDLNVKEKIIEdmRMTLEEQEQTQVEQDQVL---------EAKLEEVERLATELEKWKE 1416
Cdd:pfam05557 441 eevdslrRKLETLELERQRLREQKNELEMELE--RRCLQGDYDPKKTKVLHLsmnpaaeayQQRKNQLEKLQAEIERLKR 518
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1622966431 1417 KCNDLETKNNQRSNKEHEDNTDVLGKLSNLQDELQESEQK 1456
Cdd:pfam05557 519 LLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELK 558
|
|
| |
