|
Name |
Accession |
Description |
Interval |
E-value |
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
25-187 |
2.33e-48 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 162.40 E-value: 2.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 25 VYDLASDIGKEYERIMDRFGTDAVSGLMPKIINTLELLEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDKEL 104
Cdd:pfam09744 1 VYDLASSIGKEFERLIDRYGEDVVKGLMPKVVNVLELLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 105 ELIEEQWRSETNELVDLVSSLQDENKRLV-KQTQDLQSSSAQSSGLGASLTEsiismtnhelhsalSDTQVLQRLKEQIY 183
Cdd:pfam09744 81 EEIEDQWEQETKDLLSQVESLEEENRRLEaDHVSRLEEKEAELKKEYSKLHE--------------RETEVLRKLKEVVD 146
|
....
gi 18543225 184 KQRD 187
Cdd:pfam09744 147 RQRD 150
|
|
| RILP-like |
cd14445 |
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in ... |
9-95 |
1.53e-32 |
|
Rab interacting lysosomal protein-like 1 and 2 (Rilpl1 and Rilpl2); This domain is found in Rab interacting lysosomal protein-like 1 and 2, and appears to be conserved in Bilateria. The Rilp-like proteins regulate the concentration of ciliary membrane proteins in the primary cilium. Rilpl2 interacts with myosin-Va and has been linked to the regulation of cellular morphology in neurons; it forms a complex with Rac1 and activates Rac1-Pak signaling, dependent on myosin-Va.
Pssm-ID: 271220 [Multi-domain] Cd Length: 89 Bit Score: 118.47 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 9 MGEMVLDAI-DDIGVVDVYDLASDIGKEYERIMDRFGTDAVSGLMPKIINTLELLEALATKNERENATIQELRDKVAQLE 87
Cdd:cd14445 1 GAESALDKSpSELTVVDVYDIASAIGKEFERLIDRYGPEAVAGLMPKVVRVLELLEALASRNERENLEIEELRLEVDRLE 80
|
....*...
gi 18543225 88 SEKLEKAE 95
Cdd:cd14445 81 LEKRERAQ 88
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
24-327 |
4.14e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 4.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 24 DVYDLASDIGKEYERIMDRFGtdAVSGLMPKIINTLELLEALATKNERENATIQELRDKVAQLESEKLEKAEFR----RR 99
Cdd:TIGR02169 143 DVTDFISMSPVERRKIIDEIA--GVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQallkEK 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 100 FDKELELIEEQWRSETNELVDL---VSSLQDENKRLVKQTQDLQSSSAQSSGLGASLTESIISMTNHElhsALSDTQVLQ 176
Cdd:TIGR02169 221 REYEGYELLKEKEALERQKEAIerqLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEE---QLRVKEKIG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 177 RLKEQIYKQRDELKHRERELQDK-------YSELEHLNIQAERLKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQS 249
Cdd:TIGR02169 298 ELEAEIASLERSIAEKERELEDAeerlaklEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18543225 250 REINQLRKRLGLAEKENEDLvasyddgqndpnrprytTRELKELISERDELLTTIDTLNEQLAELKppSQAKGKRQRH 327
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKL-----------------KREINELKRELDRLQEELQRLSEELADLN--AAIAGIEAKI 436
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
64-315 |
4.26e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 4.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 64 ALATKNEREN--ATIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQWRSETNELVDLVSSLQDENKRLVKQTQDLQS 141
Cdd:TIGR02168 672 ILERRREIEEleEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 142 SSAQSSGLGASLTE--SIISMTNHELHSALsdtQVLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASERD 219
Cdd:TIGR02168 752 LSKELTELEAEIEEleERLEEAEEELAEAE---AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 220 TRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDLVASYDDGQNDPNRPRY----TTRELKELIS 295
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSeleeLSEELRELES 908
|
250 260
....*....|....*....|
gi 18543225 296 ERDELLTTIDTLNEQLAELK 315
Cdd:TIGR02168 909 KRSELRRELEELREKLAQLE 928
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
60-315 |
6.37e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 60 ELLEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQWRSETNELVDLVSSLQDENKRLVKQTQDL 139
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 140 QSSSAQSSGLGASLTESIISMTNHELHSALSDTQVLQRLKEQIYKQRDELKHRERELQDKYSELEHLNiQAERLKASERD 219
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA-QLEELEEAEEA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 220 TRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDLVASYDDGQndpnrpryttRELKELISERDE 299
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL----------EEAALLEAALAE 481
|
250
....*....|....*.
gi 18543225 300 LLTTIDTLNEQLAELK 315
Cdd:COG1196 482 LLEELAEAAARLLLLL 497
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
54-268 |
8.19e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.02 E-value: 8.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 54 KIINTLELLEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQWRSETNELVDLVSSLQDENKRLV 133
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 134 KQTQDLQSSSAQSSGLGASLTEsiismtnhelhsalsDTQVLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERL 213
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEE---------------LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18543225 214 KASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENED 268
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
77-314 |
1.14e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.64 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 77 QELRDKVAQLESEKLEKAefRRRFDKELELIEEQWRSETNELVDLVSSLQDENKRLVKQTQDLQSSSAQSSGLGASLTES 156
Cdd:COG1196 216 RELKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 157 IISmtnhelhsalsdtqvLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASERDTRRRHKLMQAQVKTLCE 236
Cdd:COG1196 294 LAE---------------LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18543225 237 ERADFLAQLQDQSREINQLRKRLglaEKENEDLVASYDDGQNDPNRPRYTTRELKELISERDELLTTIDTLNEQLAEL 314
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEEL---EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
60-326 |
8.93e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 8.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 60 ELLEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQwRSETNELVDLVSSLQDENKRLVKQTQDL 139
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA-QAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 140 QSSSAQSSGLGASLTESIISMTNhELHSALSDTQVLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASERD 219
Cdd:COG1196 315 EERLEELEEELAELEEELEELEE-ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 220 TRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDLVASYDDGQNDpnrpryTTRELKELISERDE 299
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE------LEEEEEALLELLAE 467
|
250 260
....*....|....*....|....*..
gi 18543225 300 LLTTIDTLNEQLAELKPPSQAKGKRQR 326
Cdd:COG1196 468 LLEEAALLEAALAELLEELAEAAARLL 494
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
71-317 |
1.22e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 54.30 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 71 RENATIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQWRSETNELVDLVSSLQDENKRLVKQTQDLQSSSAQSSGLG 150
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 151 ASLTESIISMTN------------HELHSALSD-------------TQVLQRLKEQIYKQRDELKHRERELQDKYSELEH 205
Cdd:TIGR02169 751 QEIENVKSELKElearieeleedlHKLEEALNDlearlshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 206 LNIQAERLKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDLVASYDDGQNDPNRPRY 285
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA 910
|
250 260 270
....*....|....*....|....*....|..
gi 18543225 286 TTRELKELISerdELLTTIDTLNEQLAELKPP 317
Cdd:TIGR02169 911 QIEKKRKRLS---ELKAKLEALEEELSEIEDP 939
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
62-278 |
4.68e-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: 51.69 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 62 LEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQWRSETNELVDLVSSLQDENKRLVKQTQDLQS 141
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 142 SSAQSSGL----GASLTESIISMtnhELHSALsdTQVLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASE 217
Cdd:COG4942 116 LGRQPPLAlllsPEDFLDAVRRL---QYLKYL--APARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18543225 218 RDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDLVASYDDGQN 278
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAAL 251
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
62-271 |
5.32e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 62 LEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDK---ELELIEEQWRSETNELVDLVSSLQDENKRLVKQTQD 138
Cdd:TIGR02168 290 LYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESkldELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 139 LQSSSAQS-------SGLGASLTESIISMTNH--ELHSALSDTQV-LQRLKEQIYKQRDELKhrERELQDKYSELEHLNI 208
Cdd:TIGR02168 370 LESRLEELeeqletlRSKVAQLELQIASLNNEieRLEARLERLEDrRERLQQEIEELLKKLE--EAELKELQAELEELEE 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18543225 209 QAERLKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDLVA 271
Cdd:TIGR02168 448 ELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKA 510
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
60-241 |
1.24e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 60 ELLEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQWRSETNELVDLVSSLQDENKRLVKQTQDL 139
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEI 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 140 QSSSAQSSGLGASLTESIISMTNHELHSALSDtqvLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKaserD 219
Cdd:TIGR02168 424 EELLKKLEEAELKELQAELEELEEELEELQEE---LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLE----R 496
|
170 180
....*....|....*....|..
gi 18543225 220 TRRRHKLMQAQVKTLCEERADF 241
Cdd:TIGR02168 497 LQENLEGFSEGVKALLKNQSGL 518
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
58-315 |
1.49e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.83 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 58 TLELLEALATKNERENATIQELRDKVAQLESEKLEKaefrrrfDKELELIEEQWRSETNELVDLVSSLQDENKRLVKQTQ 137
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSEL-------EEEIEELQKELYALANEISRLEQQKQILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 138 DLQSSSAQSSGLGASLTESiismtnhELHSALSDTQvLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASE 217
Cdd:TIGR02168 317 QLEELEAQLEELESKLDEL-------AEELAELEEK-LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 218 RDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAE-KENEDLVASYDDGQNDPNRPRYTTRELKELISE 296
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEALEELRE 468
|
250 260
....*....|....*....|
gi 18543225 297 R-DELLTTIDTLNEQLAELK 315
Cdd:TIGR02168 469 ElEEAEQALDAAERELAQLQ 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
51-314 |
2.05e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 51 LMPKIINTLELLEALATKNERENATIQELRDKVAQLEsEKLEKAEFRR-RFDKELELIEEQWRSETNELVDLVSSLQDEN 129
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLR-ERLESLERRIaATERRLEDLEEQIEELSEDIESLAAEIEELE 865
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 130 KRLVKQTQDLQSSSAQSSGLgasltesiismtNHELHSALSDTQVLQRLKEQIYKQRDELKHRERELQDKyseLEHLNIQ 209
Cdd:TIGR02168 866 ELIEELESELEALLNERASL------------EEALALLRSELEELSEELRELESKRSELRRELEELREK---LAQLELR 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 210 AERLKASERDTRRR----HKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLG----LAEKENEDLVASYD--DGQ-N 278
Cdd:TIGR02168 931 LEGLEVRIDNLQERlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlAAIEEYEELKERYDflTAQkE 1010
|
250 260 270
....*....|....*....|....*....|....*...
gi 18543225 279 DPNRPRYTTRELKELISE--RDELLTTIDTLNEQLAEL 314
Cdd:TIGR02168 1011 DLTEAKETLEEAIEEIDReaRERFKDTFDQVNENFQRV 1048
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
53-288 |
1.06e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 53 PKIINTLELLEALATKNERENATIQELRDKVAQLEsEKLEKAEfrrrfdKELELIEEqwrsetnELVDLVSSLQDENKRL 132
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELN-EEYNELQ------AELEALQA-------EIDKLQAEIAEAEAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 133 VKQTQDL--QSSSAQSSGLGASLTESIISMTNheLHSALSDTQVLQRLKEQIYKQRDELKHRERELQDKYSELEHlniQA 210
Cdd:COG3883 82 EERREELgeRARALYRSGGSVSYLDVLLGSES--FSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEA---KL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18543225 211 ERLKASERDTRRRHKLMQAQVktlcEERADFLAQLQDQSREINQLRKRLGLAEKENEDLVASYDDGQNDPNRPRYTTR 288
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQ----AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
56-311 |
1.12e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 56 INTLEL-LEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQwrsetneLVDLVSSLQDENKRLVK 134
Cdd:TIGR02168 269 LEELRLeVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ-------LEELESKLDELAEELAE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 135 QTQDLQSSSAQSSGLGASLTESIISMTNHELHSALSDTQVLQR------LKEQIYKQRDELKHRERELQDkySELEHLNI 208
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLrskvaqLELQIASLNNEIERLEARLER--LEDRRERL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 209 QAERLKASERDTRRRHKLMQAQV-------KTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDLVASYDDGQNDPN 281
Cdd:TIGR02168 420 QQEIEELLKKLEEAELKELQAELeeleeelEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
250 260 270
....*....|....*....|....*....|
gi 18543225 282 RPRYTTRELKELISERDELLTTIDTLNEQL 311
Cdd:TIGR02168 500 NLEGFSEGVKALLKNQSGLSGILGVLSELI 529
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
166-315 |
1.69e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 166 HSALSDTQVLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASERDTRRRHKLMQAQVKTLCEERADFLAQL 245
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 246 QDQSREINQLRKRLGLAEKENEDLvasyddgqndpnrprytTRELKELISERDELLTTIDTLNEQLAELK 315
Cdd:TIGR02168 750 AQLSKELTELEAEIEELEERLEEA-----------------EEELAEAEAEIEELEAQIEQLKEELKALR 802
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
59-310 |
1.80e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 59 LELLEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFdkELELIEEQWRSETNELVDLVSSLQDENKRLVKQTQD 138
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVL--GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 139 LQSSSAQSSGLGASLTESIISMTNHELHSALSDTQVLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASER 218
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 219 DTRRRHKLMQAQV-KTLCEERADFLAQLQDQSREINQL---RKRLG----LAEKENEDLVASYDdgqndpnrprYTTREL 290
Cdd:COG1196 735 EELLEELLEEEELlEEEALEELPEPPDLEELERELERLereIEALGpvnlLAIEEYEELEERYD----------FLSEQR 804
|
250 260
....*....|....*....|
gi 18543225 291 KELISERDELLTTIDTLNEQ 310
Cdd:COG1196 805 EDLEEARETLEEAIEEIDRE 824
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
62-280 |
2.14e-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: 46.98 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 62 LEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQWRSETNELVDLVSSLQDEnkRLVKQTQDLQS 141
Cdd:TIGR02169 725 IEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS--RIPEIQAELSK 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 142 SSAQSSGLGASL--TESIISMTNHELHSALSDTQVLQR----LKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKA 215
Cdd:TIGR02169 803 LEEEVSRIEARLreIEQKLNRLTLEKEYLEKEIQELQEqridLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES 882
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18543225 216 SERDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDLVASYDDGQNDP 280
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
63-267 |
2.48e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 63 EALATKNERENATIQELRDKVAQLEsEKLEKAEFR-RRFDKELELIeeqwrSETNELVDLVSSLQDENKRLVKQTQDLQS 141
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELR-KELEEAEAAlEEFRQKNGLV-----DLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 142 SSAQSSGLGASLTESIISMtnhelhSALSDTQVLQRLKEQIYKQRDELkhreRELQDKYSElEHLNIQA--ERLKASERD 219
Cdd:COG3206 238 AEARLAALRAQLGSGPDAL------PELLQSPVIQQLRAQLAELEAEL----AELSARYTP-NHPDVIAlrAQIAALRAQ 306
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 18543225 220 TRRRHKLMQAQVKTlceERADFLAQLQDQSREINQLRKRL-GLAEKENE 267
Cdd:COG3206 307 LQQEAQRILASLEA---ELEALQAREASLQAQLAQLEARLaELPELEAE 352
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
154-326 |
2.71e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 154 TESIISMTNHELHSALSDTQVLQrlkEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASERDTRRRHKLMQAQVKT 233
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELE---EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 234 LCEERADFLAQLQDQSREINQLRKRLGLAEKENEDLVASYD----DGQNDPNRPRYTTRELKELISERDELLTTIDTLNE 309
Cdd:TIGR02168 321 LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEeleaELEELESRLEELEEQLETLRSKVAQLELQIASLNN 400
|
170
....*....|....*...
gi 18543225 310 QLAELKPP-SQAKGKRQR 326
Cdd:TIGR02168 401 EIERLEARlERLEDRRER 418
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
59-267 |
3.41e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 59 LELLEALATKNERenatIQELRDKVAQLESEKLE-KAEFRRRFDKELELIEEQWRSETNELVDLVSSLQDENKRLVKQTQ 137
Cdd:COG4913 251 IELLEPIRELAER----YAAARERLAELEYLRAAlRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 138 DLQSSSAQSSGlgasltesiismtnhelhsalsdtQVLQRLKEQIykqrdelKHRERELQDKYSELEHLNIQAERLKASE 217
Cdd:COG4913 327 ELEAQIRGNGG------------------------DRLEQLEREI-------ERLERELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 18543225 218 RDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLG--LAEKENE 267
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRreLRELEAE 427
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
75-315 |
4.94e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 45.80 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 75 TIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQWRSETnELVDLVSSLQDENKRLVKQTQDLQSSSAQSSGLGASLT 154
Cdd:PRK02224 469 TIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED-RIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 155 ESIISMTNHElhsalsdtQVLQRLKEQIYKQRDELKHRERELQDKYSELEHLN----IQAERLKASERDTRRRHKLmqAQ 230
Cdd:PRK02224 548 ELEAEAEEKR--------EAAAEAEEEAEEAREEVAELNSKLAELKERIESLErirtLLAAIADAEDEIERLREKR--EA 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 231 VKTLCEERADFLAQLQDQSREinqlrkrlgLAEKENEDLVasyDDGQNDPNRPRY----TTRELKELISERDELLTTIDT 306
Cdd:PRK02224 618 LAELNDERRERLAEKRERKRE---------LEAEFDEARI---EEAREDKERAEEyleqVEEKLDELREERDDLQAEIGA 685
|
....*....
gi 18543225 307 LNEQLAELK 315
Cdd:PRK02224 686 VENELEELE 694
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
164-315 |
1.00e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 164 ELHSALSDTQVLQRLKEQIYKQRDELKHRERELQDKYSE-----LEHLNIQAERLKASERDTRRRHKLMQAQVKTLCEER 238
Cdd:COG4913 296 ELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPL 375
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18543225 239 ADFLAQLQDQSREINQLRKRLGLAEKENEDLVASYDDGQNDpnrpryTTRELKELISERDELLTTIDTLNEQLAELK 315
Cdd:COG4913 376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD------LRRELRELEAEIASLERRKSNIPARLLALR 446
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
76-315 |
1.42e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 76 IQELRDKVAQLESEKLEKAEfrrrfdKELELIEEqwrsETNELVDLVSSLQDENKRLvkqtQDLQSSSAQssglgasLTE 155
Cdd:PRK03918 505 LKELEEKLKKYNLEELEKKA------EEYEKLKE----KLIKLKGEIKSLKKELEKL----EELKKKLAE-------LEK 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 156 SIismtnHELHSALSDtqVLQRLKEQIYKQRDELKHRERELQDKYSELEhlniqaeRLKASERDTRRRHKlmqaQVKTLC 235
Cdd:PRK03918 564 KL-----DELEEELAE--LLKELEELGFESVEELEERLKELEPFYNEYL-------ELKDAEKELEREEK----ELKKLE 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 236 EERADFLAQLQDQSREINQLRKRLglaekenEDLVASYDDGQNDPNRPRYT---------TRELKELISERDELLTTIDT 306
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKEL-------EELEKKYSEEEYEELREEYLelsrelaglRAELEELEKRREEIKKTLEK 698
|
....*....
gi 18543225 307 LNEQLAELK 315
Cdd:PRK03918 699 LKEELEERE 707
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
56-231 |
2.23e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 56 INTLELLEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDKELELIE--EQWRSETNELVDLVSSLQDENKR-- 131
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERle 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 132 -LVKQTQDLQSSSAQSSGLGASLTESIISMTNHELHSALSDTQVLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQA 210
Cdd:COG4717 150 eLEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180
....*....|....*....|.
gi 18543225 211 ERLKASERDTRRRHKLMQAQV 231
Cdd:COG4717 230 EQLENELEAAALEERLKEARL 250
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
219-314 |
2.31e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 219 DTRRRHKLMQAQVKTL---CEERADFLAQLQDQSREINQLRKRLGLAE---KENEDLVASYDDGQNDPNRPRYTTRELKE 292
Cdd:PRK11281 46 DALNKQKLLEAEDKLVqqdLEQTLALLDKIDRQKEETEQLKQQLAQAPaklRQAQAELEALKDDNDEETRETLSTLSLRQ 125
|
90 100
....*....|....*....|..
gi 18543225 293 LISERDELLTTIDTLNEQLAEL 314
Cdd:PRK11281 126 LESRLAQTLDQLQNAQNDLAEY 147
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
63-315 |
2.32e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.47 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 63 EALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQWRSETNELVDLV----------SSLQDENKRL 132
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQkelkskekelKKLNEEKKEL 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 133 VKQTQDLQSSSAQSSglgasLTESIISMTNHELHSALSDtqvlqrLKEQIYKQRDELKHR--ERELQDKYSELEHLNIQA 210
Cdd:TIGR04523 509 EEKVKDLTKKISSLK-----EKIEKLESEKKEKESKISD------LEDELNKDDFELKKEnlEKEIDEKNKEIEELKQTQ 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 211 ERLKASERDtrrrhklMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDLVASYDDGQNDPNrpryttrEL 290
Cdd:TIGR04523 578 KSLKKKQEE-------KQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKN-------KL 643
|
250 260
....*....|....*....|....*.
gi 18543225 291 KELISE-RDELLTTIDTLNEQLAELK 315
Cdd:TIGR04523 644 KQEVKQiKETIKEIRNKWPEIIKKIK 669
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
28-271 |
3.06e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.50 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 28 LASDIGKEYERIMD--RFGTDAVSGLMPKIINTLELLEALATKNERENATIQELRDkvAQLESEKLEkaEFRRRFDKELE 105
Cdd:TIGR00606 540 LTKDKMDKDEQIRKikSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAK--LNKELASLE--QNKNHINNELE 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 106 LIEEQWRSETNELVDLVSSlQDENKRLVKQTQDLQSSSAQSSGLGA--SLTESIISMTNHELHSALSDTQVLQRLKEQIY 183
Cdd:TIGR00606 616 SKEEQLSSYEDKLFDVCGS-QDEESDLERLKEEIEKSSKQRAMLAGatAVYSQFITQLTDENQSCCPVCQRVFQTEAELQ 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 184 KQRDELKHRERELQDKYSELEHLNIQAERlkasERD-----TRRRHKLMQAQVKTLCEERadflAQLQDQSREINQLRKR 258
Cdd:TIGR00606 695 EFISDLQSKLRLAPDKLKSTESELKKKEK----RRDemlglAPGRQSIIDLKEKEIPELR----NKLQKVNRDIQRLKND 766
|
250
....*....|...
gi 18543225 259 LGLAEKENEDLVA 271
Cdd:TIGR00606 767 IEEQETLLGTIMP 779
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
77-232 |
4.38e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 77 QELRDKVAQLESEKLEKAEFRRRFDKELELIEeQWRSETNELVDLVSSLQDENKRLVKQTQDLQsssAQSSGLGASLTES 156
Cdd:TIGR02169 364 EELEDLRAELEEVDKEFAETRDELKDYREKLE-KLKREINELKRELDRLQEELQRLSEELADLN---AAIAGIEAKINEL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 157 IISMTNHELHSALSDTQ------VLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASERDTRRRHKLMQAQ 230
Cdd:TIGR02169 440 EEEKEDKALEIKKQEWKleqlaaDLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKAS 519
|
..
gi 18543225 231 VK 232
Cdd:TIGR02169 520 IQ 521
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
33-314 |
5.72e-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: 42.41 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 33 GKEY-ERIMDRFgTDAVSGLMPKIINTLELLEalaTKNERENATIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQW 111
Cdd:pfam15921 72 GKEHiERVLEEY-SHQVKDLQRRLNESNELHE---KQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 112 RSETNELV-------DLV--SSLQDENKR--------LVKQTQDLQSSSAQSSGLGASLTESIISMTNHELHSALS---- 170
Cdd:pfam15921 148 QNTVHELEaakclkeDMLedSNTQIEQLRkmmlshegVLQEIRSILVDFEEASGKKIYEHDSMSTMHFRSLGSAISkilr 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 171 --DTQVlQRLKEQIYKQRDELKHRERELQDKYSEL-------------EHlNIQAERLKASERDTRRRHKLMQAQVKTLC 235
Cdd:pfam15921 228 elDTEI-SYLKGRIFPVEDQLEALKSESQNKIELLlqqhqdrieqlisEH-EVEITGLTEKASSARSQANSIQSQLEIIQ 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 236 EE----RADFLAQLQDQSREINQLRKRLGLAEKENEDLVASYDdgqndpNRPRYTTRELKELISERDELLTTIDTLNEQL 311
Cdd:pfam15921 306 EQarnqNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELE------KQLVLANSELTEARTERDQFSQESGNLDDQL 379
|
...
gi 18543225 312 AEL 314
Cdd:pfam15921 380 QKL 382
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
175-315 |
6.24e-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: 41.67 E-value: 6.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 175 LQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREI-N 253
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELaE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18543225 254 QLRKRLGLAEKENEDLVASYDDGQNDPNRPRYT--------------TRELKELISERDELLTTIDTLNEQLAELK 315
Cdd:COG4942 109 LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLkylaparreqaeelRADLAELAALRAELEAERAELEALLAELE 184
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
175-315 |
9.87e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 175 LQRLKEQIyKQRDELKHRERELQDKYSELEHLNIQAERLKASERDTRRRHKLM--QAQVKTLCEERADFLAQLQDQSREI 252
Cdd:COG4717 70 LKELKELE-EELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLekLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18543225 253 NQLRKRLGL---AEKENEDLVASYDDGQNDPNR-----PRYTTRELKELISERDELLTTIDTLNEQLAELK 315
Cdd:COG4717 149 EELEERLEElreLEEELEELEAELAELQEELEElleqlSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
74-318 |
9.98e-04 |
|
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: 41.86 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 74 ATIQELRDKVAQLEsEKLEKAE-FRRRFDKELELIEEqwrsetneLVDLVSSLQ--DENKRLVKQTQDLQSSSAQSSGLG 150
Cdd:COG3096 448 AKEQQATEEVLELE-QKLSVADaARRQFEKAYELVCK--------IAGEVERSQawQTARELLRRYRSQQALAQRLQQLR 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 151 ASLtesiismtnHELHSALSDTQVLQRLKEQIYKQRDELKHRERELQDKYSEL----EHLNIQAERLKASERDTRRRHKL 226
Cdd:COG3096 519 AQL---------AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELeaqlEELEEQAAEAVEQRSELRQQLEQ 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 227 MQAQVKTLcEERADFLAQLQDQsreINQLRKRLGlaekenedlvASYDDGQNDPNRPRYTTRELKELISERDELLTTIDT 306
Cdd:COG3096 590 LRARIKEL-AARAPAWLAAQDA---LERLREQSG----------EALADSQEVTAAMQQLLEREREATVERDELAARKQA 655
|
250
....*....|..
gi 18543225 307 LNEQLAELKPPS 318
Cdd:COG3096 656 LESQIERLSQPG 667
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
58-269 |
1.07e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 41.63 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 58 TLELLEALATKNERENAT--IQELRDKVAQLEseklEKAEFRrrfDKELELIEEQWRSETNELVDLVSSLQDENKRLVKQ 135
Cdd:pfam05483 243 SLLLIQITEKENKMKDLTflLEESRDKANQLE----EKTKLQ---DENLKELIEKKDHLTKELEDIKMSLQRSMSTQKAL 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 136 TQDLQSSSAQSSGLG----ASLTESIISMTNH-----ELHSALSDTQVLQRLKEQ-IYKQRDELKHRERELQDKYSELEH 205
Cdd:pfam05483 316 EEDLQIATKTICQLTeekeAQMEELNKAKAAHsfvvtEFEATTCSLEELLRTEQQrLEKNEDQLKIITMELQKKSSELEE 395
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18543225 206 LNiqaeRLKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDL 269
Cdd:pfam05483 396 MT----KFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDL 455
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
13-274 |
1.44e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 13 VLDAIDDIGVVDVYDLASDIgkEYERIMDrfgtdaVSGLMPKIINTLELLEALATKNErenaTIQELRDKVAQLESEKLE 92
Cdd:PRK05771 21 VLEALHELGVVHIEDLKEEL--SNERLRK------LRSLLTKLSEALDKLRSYLPKLN----PLREEKKKVSVKSLEELI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 93 KAEfrrrfDKELELIEEqwrsETNELVDLVSSLQDENKRLVKQTQDLQ---------------SSSAQSSGL----GASL 153
Cdd:PRK05771 89 KDV-----EEELEKIEK----EIKELEEEISELENEIKELEQEIERLEpwgnfdldlslllgfKYVSVFVGTvpedKLEE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 154 TESIISMTNHELHSAL--SDTQVLQRLKEQIYKQRDELKhrerelqdkyselehlNIQAERLKASErdtrrrhklmqaqV 231
Cdd:PRK05771 160 LKLESDVENVEYISTDkgYVYVVVVVLKELSDEVEEELK----------------KLGFERLELEE-------------E 210
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 18543225 232 KTLCEERADFLAQLQDQSREINQLRKRLG-LAEKENEDLVASYD 274
Cdd:PRK05771 211 GTPSELIREIKEELEEIEKERESLLEELKeLAKKYLEELLALYE 254
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
52-274 |
1.66e-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: 39.91 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 52 MPKIINTLELLEALATKNERENATIQELRDKVAQLESEklekaefRRRFDKELELIEEQWRSETNELVDLVSSLQDENKR 131
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKELPAELAELEDE-------LAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 132 LVKQTQDLQSSSaqssglgasltesiismTNHELHSalsdtqvLQRLKEQIYKQRDELKHRERELQDkyselehlniQAE 211
Cdd:COG1579 75 IKKYEEQLGNVR-----------------NNKEYEA-------LQKEIESLKRRISDLEDEILELME----------RIE 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18543225 212 RLKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRlgLAEKENEDLVASYD 274
Cdd:COG1579 121 ELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE--LAAKIPPELLALYE 181
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
55-315 |
1.68e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 55 IINTLELLEALATKNERENATIQELRDKVAQLESEKLEKaefrrrfDKELELIEEQWRSETNELVDLVSSLQdENKRLVK 134
Cdd:TIGR04523 147 IKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNI-------QKNIDKIKNKLLKLELLLSNLKKKIQ-KNKSLES 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 135 QTQDLQSSSAQssglgasLTESIIsmtnhELHSALSD-TQVLQRLKEQIYKQRDELKHRERELQDKYSELEHLN------ 207
Cdd:TIGR04523 219 QISELKKQNNQ-------LKDNIE-----KKQQEINEkTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNkkikel 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 208 ------IQAERLKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDlvaSYDDGQNDPN 281
Cdd:TIGR04523 287 ekqlnqLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTN---SESENSEKQR 363
|
250 260 270
....*....|....*....|....*....|....
gi 18543225 282 RPRYTTRELKELISERDELLTTIDTLNEQLAELK 315
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLE 397
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
34-272 |
1.68e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 40.81 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 34 KEYERIMDRFgtdavsglmPKIinTLELLEALATKNE-----RENATIQELRDKVAQLESEKLEKAEfrrrfdkelELIE 108
Cdd:PRK10929 68 KQYQQVIDNF---------PKL--SAELRQQLNNERDeprsvPPNMSTDALEQEILQVSSQLLEKSR---------QAQQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 109 EQWRS-ETNELVDLVSSLQDENKRLVKQ-TQDLQSSSAQSSGLG-ASLT----ESII--SMTNhELHSA-LS--DTQVLQ 176
Cdd:PRK10929 128 EQDRArEISDSLSQLPQQQTEARRQLNEiERRLQTLGTPNTPLAqAQLTalqaESAAlkALVD-ELELAqLSanNRQELA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 177 RLKEQIYKQRDElkHRERELQDKYSeleHLNIQaeRLKASERDTRRRHKLMQaQVKTLCEERADFLAQLQDQSREINQLR 256
Cdd:PRK10929 207 RLRSELAKKRSQ--QLDAYLQALRN---QLNSQ--RQREAERALESTELLAE-QSGDLPKSIVAQFKINRELSQALNQQA 278
|
250
....*....|....*.
gi 18543225 257 KRLglaekeneDLVAS 272
Cdd:PRK10929 279 QRM--------DLIAS 286
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
59-299 |
2.62e-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: 40.16 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 59 LELLEALATKNEREnatIQELRDKVAQLESEKL--------------EKAEFRRRF---DKELELIEEQWRSETNELVDL 121
Cdd:pfam01576 14 LQKVKERQQKAESE---LKELEKKHQQLCEEKNalqeqlqaetelcaEAEEMRARLaarKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 122 VSSLQDENKRLVKQTQDLQSSSAQSSGLGASLTESIISmTNHELHSALSDTQVLQRLKEQIYKQRDELKHRERELQDKYS 201
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVT-TEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 202 ELEHLNIQAERLKAS--------ERDTRRRHKLMQAQVKT---LCEERADFLAQLQDQSREINQLRKRLGLAEKENEDLV 270
Cdd:pfam01576 170 EEEEKAKSLSKLKNKheamisdlEERLKKEEKGRQELEKAkrkLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249
|
250 260
....*....|....*....|....*....
gi 18543225 271 ASYDDGQNDPNRPRYTTRELKELISERDE 299
Cdd:pfam01576 250 ARLEEETAQKNNALKKIRELEAQISELQE 278
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
77-315 |
2.67e-03 |
|
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: 40.06 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 77 QELRDKVAQLESEK----LEKAEFRRRFDkELELIEEQ---WRSETNELVDLVSSLQDENKRLVKQTQDLQSSSAQssgL 149
Cdd:pfam05622 17 HELDQQVSLLQEEKnslqQENKKLQERLD-QLESGDDSgtpGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEE---L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 150 GASLTEsiISMTNHELHSAlsdTQVLQRLKEQIykqrDELkhreRELQDKYSELEhLNIQAERLKASE-RDTRRrhklmq 228
Cdd:pfam05622 93 EKEVLE--LQHRNEELTSL---AEEAQALKDEM----DIL----RESSDKVKKLE-ATVETYKKKLEDlGDLRR------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 229 aQVKTLCEERADFL---AQLQDQSREINQLRKRLGLAEKENEDLVASYDDGQNDPNRPRYTTRELKE----LISERDELL 301
Cdd:pfam05622 153 -QVKLLEERNAEYMqrtLQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEkleaLQKEKERLI 231
|
250
....*....|....
gi 18543225 302 TTIDTLNEQLAELK 315
Cdd:pfam05622 232 IERDTLRETNEELR 245
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
52-315 |
2.69e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 52 MPKIINTLELLEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFdKELELIEEQWRSETNELVDLVSSLQDENKR 131
Cdd:PRK03918 147 REKVVRQILGLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELI-KEKEKELEEVLREINEISSELPELREELEK 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 132 LVKQTQDLQSssaqssglgaslTESIISMTNHELHSALSDTQVLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAE 211
Cdd:PRK03918 226 LEKEVKELEE------------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAE 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 212 R------LKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDL---VASYDD------- 275
Cdd:PRK03918 294 EyiklseFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELeerHELYEEakakkee 373
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 18543225 276 -----GQNDPNRPRYTTRELKELISERDELLTTIDTLNEQLAELK 315
Cdd:PRK03918 374 lerlkKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK 418
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
185-326 |
2.95e-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: 39.75 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 185 QRDELKHRERELQDKYSELEHLNIQAERLKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEK 264
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 265 ENED--------LVASYDDGQN----------DPNRPRYTTRELKELISERDELLTTIDTLNEQLAELKPPSQAKGKRQR 326
Cdd:COG4942 98 ELEAqkeelaelLRALYRLGRQpplalllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
57-315 |
3.02e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 57 NTLELLEALATKNERENATIQ-ELRDKVAQLESEKLEKAEFRRRFDK------ELELIEEQWRSETNELVDLVSSLQDEN 129
Cdd:TIGR04523 342 EQISQLKKELTNSESENSEKQrELEEKQNEIEKLKKENQSYKQEIKNlesqinDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 130 KRLVKQTQDLQSSSAQSSGLGASLTESI----ISMTNHELHSALSDTQvLQRLKEQIYKQRDELKHRERELQDKYSELEH 205
Cdd:TIGR04523 422 ELLEKEIERLKETIIKNNSEIKDLTNQDsvkeLIIKNLDNTRESLETQ-LKVLSRSINKIKQNLEQKQKELKSKEKELKK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 206 LNIQAERLKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQSREINQLRKRL--GLAEKE--------------NEDL 269
Cdd:TIGR04523 501 LNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEideknkeieelkqtQKSL 580
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 18543225 270 VASYDDGQNDPNRpryTTRELKELISERDELLTTIDTLNEQLAELK 315
Cdd:TIGR04523 581 KKKQEEKQELIDQ---KEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
118-267 |
3.41e-03 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 38.95 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 118 LVDLVSSLQDENKRLVKQTQDLQSSSAQSSGLGASLTESIISMT--NHELHSALSDTQvlQRLKEqIYKQRDELKHRERE 195
Cdd:pfam17078 8 LHDQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKFLENLASLKheNDNLSSMLNRKE--RRLKD-LEDQLSELKNSYEE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18543225 196 LQDKYSELEHlniQAERLKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDqsrEINQLRKRLGLAEKENE 267
Cdd:pfam17078 85 LTESNKQLKK---RLENSSASETTLEAELERLQIQYDALVDSQNEYKDHYQQ---EINTLQESLEDLKLENE 150
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
66-269 |
3.53e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 66 ATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDK-----------ELELIEEQWRSETNELVDLVSSLQDENKRLVK 134
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakkaeekkkadELKKAEELKKAEEKKKAEEAKKAEEDKNMALR 1581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 135 QTQDLQSSSAQSSGLGASLTESIISMTNHELHSALSDTQVLQRLK--EQIYKQRDELKHRERELQDKYSEL----EHLNI 208
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAEELkkaeEENKI 1661
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18543225 209 QAERL-KASERDTRRRHKLMQAQVKTlcEERADFLAQLQDQSREINQLRKRLGLAEKENEDL 269
Cdd:PTZ00121 1662 KAAEEaKKAEEDKKKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
60-259 |
3.55e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.90 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 60 ELLEALATKNERENATIQELRDKVAQLESeklEKAEFRRRFDKELELIEEQWrsetnELVDlVSSLQDENKRLVKQTQDL 139
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEA---ELDALQERREALQRLAEYSW-----DEID-VASAEREIAELEAELERL 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 140 QSSSAQSSGLGASLtesiismtnHELHSALSDT-QVLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASER 218
Cdd:COG4913 681 DASSDDLAALEEQL---------EELEAELEELeEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 18543225 219 DTRRRHKLMQAQVKTLceeRADFLAQLQDQSREINQLRKRL 259
Cdd:COG4913 752 EERFAAALGDAVEREL---RENLEERIDALRARLNRAEEEL 789
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
175-305 |
3.82e-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: 38.75 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 175 LQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKA---SERDTRRRHKLM------QAQVKTLCEERADFLAQL 245
Cdd:COG1579 40 LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgNVRNNKEYEALQkeieslKRRISDLEDEILELMERI 119
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 246 QDQSREINQLRKRLGLAEKENEDLVASYDDGQNDpnrpryTTRELKELISERDELLTTID 305
Cdd:COG1579 120 EELEEELAELEAELAELEAELEEKKAELDEELAE------LEAELEELEAEREELAAKIP 173
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
77-301 |
3.82e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 77 QELRDKVAQLESEKLEKAEFRRRFDKELELIEEQwRSETNELVDLVSSLQDENKRLVKQTQDLQSSSAQSSGLGASLTES 156
Cdd:PRK02224 202 KDLHERLNGLESELAELDEEIERYEEQREQARET-RDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 157 I------ISMTNHELHSALSDTQVLQRLKEQIYKQRDELKHRERELQDKYSE----LEHLNIQAERLKASERDTRRRHKL 226
Cdd:PRK02224 281 VrdlrerLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEcrvaAQAHNEEAESLREDADDLEERAEE 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 227 MQAQVKTL-------CEERADFLAQLQDQSREINQLRKR-------LGLAEKENEDLVASYDDGQNDPNRPRYTTRELKE 292
Cdd:PRK02224 361 LREEAAELeseleeaREAVEDRREEIEELEEEIEELRERfgdapvdLGNAEDFLEELREERDELREREAELEATLRTARE 440
|
....*....
gi 18543225 293 LISERDELL 301
Cdd:PRK02224 441 RVEEAEALL 449
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
60-328 |
4.10e-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: 39.77 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 60 ELLEALATKNERENATIQELRDKVAQLESEKLEKAEFRRRFDKELELIEEQWRSETNELVDLVSSLQD-------ENKRL 132
Cdd:pfam01576 331 ELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQakqdsehKRKKL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 133 VKQTQDLQSSSAQSSGLGASLTESIISMTNH--------------------ELHSALSDTQVLQRLKEQIYKQRDELKHR 192
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSKLQSElesvssllneaegkniklskDVSSLESQLQDTQELLQEETRQKLNLSTR 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 193 ERELQDKYSELEhlniqaERLKASERDTRRRHKlmqaQVKTLCEERADFLAQLQDQSREINQLRKRLGLAEKENEDLVAS 272
Cdd:pfam01576 491 LRQLEDERNSLQ------EQLEEEEEAKRNVER----QLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQ 560
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 18543225 273 YDDGQNDPNRPRYTTRELKElisERDELLTTIDTLNEQLAELKppsqakgKRQRHF 328
Cdd:pfam01576 561 LEEKAAAYDKLEKTKNRLQQ---ELDDLLVDLDHQRQLVSNLE-------KKQKKF 606
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
76-272 |
4.39e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 39.23 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 76 IQELRDKVAQLESEKLEKaefrrrFDKELELIEE---QWRSETNELVDLVSSLQDENKRLVKQTQ---DLQSSSAQSSGL 149
Cdd:PHA02562 204 IEEQRKKNGENIARKQNK------YDELVEEAKTikaEIEELTDELLNLVMDIEDPSAALNKLNTaaaKIKSKIEQFQKV 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 150 GASLTE--------SIISMTNHELHSALSDTQVLQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASERDTR 221
Cdd:PHA02562 278 IKMYEKggvcptctQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLV 357
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 18543225 222 RRHKLMQAQVKTLCEERADF---LAQLQDQSREINQlrKRLGLAEKENEDLVAS 272
Cdd:PHA02562 358 DKAKKVKAAIEELQAEFVDNaeeLAKLQDELDKIVK--TKSELVKEKYHRGIVT 409
|
|
| LCD1 |
pfam09798 |
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. ... |
79-162 |
5.39e-03 |
|
DNA damage checkpoint protein; This is a family of proteins which regulate checkpoint kinases. In Schizosaccharomyces pombe this protein is called Rad26 and in Saccharomyces cerevisiae it is called LCD1.
Pssm-ID: 462906 Cd Length: 615 Bit Score: 39.22 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 79 LRDKVAQLESEKLEKAEFRRRFDKELELIEEQwrsETNELVDLVSSLQDENKRLVKQTQDLQSSSAQSSGLGASLTESII 158
Cdd:pfam09798 2 LRDKLELLQQEKEKELEKLKNSYEELKSSHEE---ELEKLKQEVQKLEDEKKFLLNELRSLSATSPASSQSHETDTDDSS 78
|
....
gi 18543225 159 SMTN 162
Cdd:pfam09798 79 SVSL 82
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
173-270 |
7.67e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 36.79 E-value: 7.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 173 QVLQRLKEQIYKQRDELKHRERELQDKYSELehlniQAERLKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQSRE- 251
Cdd:smart00935 18 AAQKQLEKEFKKRQAELEKLEKELQKLKEKL-----QKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEe 92
|
90 100
....*....|....*....|....
gi 18543225 252 INQLRKRLG-----LAEKENEDLV 270
Cdd:smart00935 93 LQKILDKINkaikeVAKKKGYDLV 116
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
76-269 |
7.74e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.60 E-value: 7.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 76 IQELRDKVAQLESEKLEKAEfrrRFDKELELIEEQWRSetnelvdlvssLQDENKRLVKQTQDLQSSSAQSSGLGASLTE 155
Cdd:COG4717 48 LERLEKEADELFKPQGRKPE---LNLKELKELEEELKE-----------AEEKEEEYAELQEELEELEEELEELEAELEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 156 SIISMTNHE-LHSALSDTQVLQRLKEQIykqrDELKHRERELQDKYSELEHLNIQAERLKASERDTRRRHKLMQAQVKTL 234
Cdd:COG4717 114 LREELEKLEkLLQLLPLYQELEALEAEL----AELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLA 189
|
170 180 190
....*....|....*....|....*....|....*.
gi 18543225 235 CEER-ADFLAQLQDQSREINQLRKRLGLAEKENEDL 269
Cdd:COG4717 190 TEEElQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
175-315 |
8.15e-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: 37.60 E-value: 8.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 175 LQRLKEQIYKQRDELKHRERELQDKYSELEHLNIQAERLKASERDTRRRHKLMQAQVKTLCEERADFLAQLQDQS--REI 252
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEY 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18543225 253 NQLRKRLGLAEKENEDLvasyddgqndpnrprytTRELKELISERDELLTTIDTLNEQLAELK 315
Cdd:COG1579 92 EALQKEIESLKRRISDL-----------------EDEILELMERIEELEEELAELEAELAELE 137
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
77-315 |
8.38e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 38.51 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 77 QELRDKVAQLESEKLEKAEFR-RRFDKELELIE---EQWRSETNELVDLVSSLQDENKRLVKQTQDLQSSSAQSSGLGAS 152
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTpEKLEKELEELEkakEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 153 LTEsiismtNHELhsalsdtQVLQRLKEQIYKQRDELKhrerELQDKYSELEHLNIQAERLKASERDTRRRHKLMQaQVK 232
Cdd:PRK03918 445 LTE------EHRK-------ELLEEYTAELKRIEKELK----EIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLK 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18543225 233 TLCEERADF-LAQLQDQSREINQLRKRLGLAEKENEDLVASyddgqndpnrprytTRELKELISERDELLTTIDTLNEQL 311
Cdd:PRK03918 507 ELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGEIKSLKKE--------------LEKLEELKKKLAELEKKLDELEEEL 572
|
....
gi 18543225 312 AELK 315
Cdd:PRK03918 573 AELL 576
|
|
| |
