|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
975-1306 |
5.13e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 5.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 975 REAERQLAQ------RLRDRCEWQARQLG-LAR--------RELKKAIQGFDAlavstkhffgksERALAKEKELSIELA 1039
Cdd:COG1196 175 EEAERKLEAteenleRLEDILGELERQLEpLERqaekaeryRELKEELKELEA------------ELLLLKLRELEAELE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1040 NIRDEVAFNTAKCEKLQKEKETLERRFEEELRrlgwQQQAEVQELQERLQQQFQAESARLQAEHQDQLLRMRCQHQEQVE 1119
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1120 DITASHEAALLEMENNHTVAITILQDDHDHKVQELmsthefekKELEENFEKLRLTLQDQVDTLTFQSQSLRDRARRFEE 1199
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEEL--------EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1200 ALRKTTEEQLEIalapyQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVE----KNIILEERIQVLQQQNEDLKARI 1275
Cdd:COG1196 391 ALRAAAELAAQL-----EELEEAEEALLERLERLEEELEELEEALAELEEEEEeeeeALEEAAEEEAELEEEEEALLELL 465
|
330 340 350
....*....|....*....|....*....|.
gi 1327848537 1276 DQNTVVTRQLSEENANLQEYVEKETQEKKRL 1306
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARLLLL 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
973-1313 |
6.89e-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: 60.46 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 973 QAREAERQLaQRLRDRCEWQARQLGLARRELKKAIQGFDALAVSTKHFFGKSERALAKEKELSIELANIRDEVAFNTAKC 1052
Cdd:TIGR02168 692 KIAELEKAL-AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERL 770
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1053 EKLQKEKETLERRFEEELRRLgwQQQAEVQELQERLQQQFQAESARLQAEHQDQLLRM-RCQHQ-----EQVEDITASHE 1126
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQI--EQLKEELKALREALDELRAELTLLNEEAANLRERLeSLERRiaateRRLEDLEEQIE 848
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1127 AALLEMENNhTVAITILQDDHDHKVQELMStHEFEKKELEENFEKLRLTLQDQVDTLtfqsQSLRDRARRFEEALRKTTE 1206
Cdd:TIGR02168 849 ELSEDIESL-AAEIEELEELIEELESELEA-LLNERASLEEALALLRSELEELSEEL----RELESKRSELRRELEELRE 922
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1207 EQleialapyQHLEEDMQSLKQvlEMKNQQIHLQEKKIIELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVT---- 1282
Cdd:TIGR02168 923 KL--------AQLELRLEGLEV--RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNlaai 992
|
330 340 350
....*....|....*....|....*....|....
gi 1327848537 1283 ---RQLSEENANLQEYVEKETQEKKRLSRTNEEL 1313
Cdd:TIGR02168 993 eeyEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1022-1313 |
3.18e-08 |
|
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: 58.53 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1022 GKSERALAKEKELSIELANIRDEVAFNTAKCEKLQKE-KETLERRFEEELRRLGWQQQAEvqeLQERLQQQFQAESARLQ 1100
Cdd:TIGR02168 663 GGSAKTNSSILERRREIEELEEKIEELEEKIAELEKAlAELRKELEELEEELEQLRKELE---ELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1101 AEHQdQLLRMRCQHQEQVEDITASHEAALLEMENNhtvaitilqddhdhkvqelmsthEFEKKELEENfeklRLTLQDQV 1180
Cdd:TIGR02168 740 AEVE-QLEERIAQLSKELTELEAEIEELEERLEEA-----------------------EEELAEAEAE----IEELEAQI 791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1181 DTLTFQSQSLRDRARRFEEALRKTTEEQLEIALApYQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVEKniiLEER 1260
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLRER-LESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE---LEEL 867
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1327848537 1261 IQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1313
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
972-1307 |
9.01e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 972 LQAREAERqlAQRLRDrcEWQARQLGLARRELKKAIQGFDALAVSTKHFFGKSERALAKEKELSIELANIRDEVAFNTAK 1051
Cdd:TIGR02168 207 RQAEKAER--YKELKA--ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1052 CEKLQKEketlerrfeeelrrlgWQQQAEVQELQERLQQQFQAESARLQ---AEHQDQLLRMRcQHQEQVEDITASHEAA 1128
Cdd:TIGR02168 283 IEELQKE----------------LYALANEISRLEQQKQILRERLANLErqlEELEAQLEELE-SKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1129 LLEMENNHTVaitiLQDDHD--HKVQELMSTHEFEKKELEENFEKLRLTLQDQVDTLTFQSQSLRDRARRFEEALRKTTE 1206
Cdd:TIGR02168 346 LEELKEELES----LEAELEelEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1207 EQLEIALAPyqhLEEDMQSLKQVLEMKNQQIhlqEKKIIELEKLVEKNIILEERIQVLQQQNEDLK---ARIDQNTVVTR 1283
Cdd:TIGR02168 422 EIEELLKKL---EEAELKELQAELEELEEEL---EELQEELERLEEALEELREELEEAEQALDAAErelAQLQARLDSLE 495
|
330 340
....*....|....*....|....
gi 1327848537 1284 QLSEENANLQEYVEKETQEKKRLS 1307
Cdd:TIGR02168 496 RLQENLEGFSEGVKALLKNQSGLS 519
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1164-1318 |
7.81e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.79 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1164 ELEENFEKLR---------LTLQDQVDTLTFQSQSLRDRARRFE----EALRKTTEEQLEIALAPYQHLEEDMQSLKQVL 1230
Cdd:COG1196 197 ELERQLEPLErqaekaeryRELKEELKELEAELLLLKLRELEAEleelEAELEELEAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1231 EMKNQQIHLQEKKIIELEKLVEKniiLEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTN 1310
Cdd:COG1196 277 EELELELEEAQAEEYELLAELAR---LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL 353
|
....*...
gi 1327848537 1311 EELLWKLQ 1318
Cdd:COG1196 354 EEAEAELA 361
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1153-1319 |
1.74e-06 |
|
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: 52.72 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1153 ELMSTHEFE----KKELEENFEKLRLTL------QDQVDTLTFQSQSLRDRARRFEEALRKTTEEQLEIalapyqhlEED 1222
Cdd:TIGR04523 117 EQKNKLEVElnklEKQKKENKKNIDKFLteikkkEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNI--------QKN 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1223 MQSLKQ----------VLEMKNQQIHLQEKKIIELEKlveKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANL 1292
Cdd:TIGR04523 189 IDKIKNkllklelllsNLKKKIQKNKSLESQISELKK---QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKI 265
|
170 180
....*....|....*....|....*..
gi 1327848537 1293 QEYVEKETQEKKRLSRTNEELLWKLQT 1319
Cdd:TIGR04523 266 KKQLSEKQKELEQNNKKIKELEKQLNQ 292
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1022-1319 |
1.84e-06 |
|
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: 52.67 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1022 GKSERALAKEKElsiELANIRDEVA---FNTAKCEKLQKEKETLERRFEEELRRLGWQQQAEVQELQERLQQQFQAESAR 1098
Cdd:pfam02463 142 GKIEIIAMMKPE---RRLEIEEEAAgsrLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEK 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1099 LQAEHQDQLLRMRCQHQEQVEDITASheaaLLEMENNHTVAITILQDDHDHKVQELMSTHEFEKKElEENFEKLRLTLQD 1178
Cdd:pfam02463 219 LELEEEYLLYLDYLKLNEERIDLLQE----LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKE-KKLQEEELKLLAK 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1179 QvdtLTFQSQSLRDRARRFEEALRKTTEEQLEIALAP--YQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVEKNII 1256
Cdd:pfam02463 294 E---EEELKSELLKLERRKVDDEEKLKESEKEKKKAEkeLKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ 370
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327848537 1257 LEERIQVLQQQN-EDLKARIDQNtvvtrqlsEENANLQEYVEKETQEKKRLSRTNEELLWKLQT 1319
Cdd:pfam02463 371 LEEELLAKKKLEsERLSSAAKLK--------EEELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1162-1313 |
3.77e-06 |
|
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: 51.56 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1162 KKELEENFEKLrltlqDQVDTLTFQSQSLRDRARRFEEaLRKTTEEQLEIALAPYQHLEEDMQSLKQVLEMKNQQIHLQE 1241
Cdd:TIGR04523 373 EKLKKENQSYK-----QEIKNLESQINDLESKIQNQEK-LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLT 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327848537 1242 KKIIELEKLVEKniiLEERIQVLQQQNEDLKARIDQNtvvtRQLSEENAnlQEYVEKE------TQEKKRLSRTNEEL 1313
Cdd:TIGR04523 447 NQDSVKELIIKN---LDNTRESLETQLKVLSRSINKI----KQNLEQKQ--KELKSKEkelkklNEEKKELEEKVKDL 515
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1164-1324 |
6.05e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1164 ELEENFEKLR------LTLQDQVDTLtfqsQSLRDRARRFEEALRKTTEEQLEIALAPYQHLEEDMQSLKQVLEmknqqi 1237
Cdd:COG4913 229 ALVEHFDDLErahealEDAREQIELL----EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELE------ 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1238 HLQEkkiiELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTR-QLSEENANLqeyvEKETQEKKRLSRTNEELLWK 1316
Cdd:COG4913 299 ELRA----ELARLEAELERLEARLDALREELDELEAQIRGNGGDRLeQLEREIERL----ERELEERERRRARLEALLAA 370
|
....*...
gi 1327848537 1317 LQTGDPTS 1324
Cdd:COG4913 371 LGLPLPAS 378
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
971-1297 |
7.63e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.71 E-value: 7.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 971 DLQAREAERQLAQRLRDRCEWQARQLGLARRELKKAIQGFDAlavstkhffgKSERALAKEKELSIELANIRDEVAFNTA 1050
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL----------ELEEAQAEEYELLAELARLEQDIARLEE 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1051 KCEKLQKEKEtlerrfeeelrrlgwQQQAEvqelqerlqqqfQAESARLQAEHQDQLLRMrcqhQEQVEDITASHEAALL 1130
Cdd:COG1196 310 RRRELEERLE---------------ELEEE------------LAELEEELEELEEELEEL----EEELEEAEEELEEAEA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1131 EMENNHTVAITILQDDHdhkvqelmsthefEKKELEENFEKLRLTLQDQVDTLTFQSQSLRDRARRFEEALRKTTEEQLE 1210
Cdd:COG1196 359 ELAEAEEALLEAEAELA-------------EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1211 IALAPYQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVEkniiLEERIQVLQQQNEDLKARIDQNTVVTRQLSEENA 1290
Cdd:COG1196 426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE----LLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
|
....*..
gi 1327848537 1291 NLQEYVE 1297
Cdd:COG1196 502 DYEGFLE 508
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
1207-1318 |
1.22e-05 |
|
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: 46.45 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1207 EQLEIALAPYQHLEEDMQSLKQvlemKNQQIHLQEKKIIELEKLVEKNIILEEriQVLQQQNEDLKARIDQNTVVTRQLS 1286
Cdd:pfam09744 36 ELLESLASRNQEHNVELEELRE----DNEQLETQYEREKALRKRAEEELEEIE--DQWEQETKDLLSQVESLEEENRRLE 109
|
90 100 110
....*....|....*....|....*....|....*
gi 1327848537 1287 EENANLQEyvEKETQEKKRLSRTNE---ELLWKLQ 1318
Cdd:pfam09744 110 ADHVSRLE--EKEAELKKEYSKLHEretEVLRKLK 142
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1097-1267 |
1.36e-05 |
|
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: 48.86 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1097 ARLQAEhqdqllRM----RCQHQEQVEDITASHeaallemennhtvaITILQDDHDH--KVQELMSTHEFEKKELEENFE 1170
Cdd:smart00787 126 ARLEAK------KMwyewRMKLLEGLKEGLDEN--------------LEGLKEDYKLlmKELELLNSIKPKLRDRKDALE 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1171 KLRLTLQDQVDTLTFQSQSLRDRARrfeEALRKTtEEQLEIALAPYQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKL 1250
Cdd:smart00787 186 EELRQLKQLEDELEDCDPTELDRAK---EKLKKL-LQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKK 261
|
170 180
....*....|....*....|....*
gi 1327848537 1251 VEKN--------IILEERIQVLQQQ 1267
Cdd:smart00787 262 LEQCrgftfkeiEKLKEQLKLLQSL 286
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1161-1313 |
1.38e-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: 49.67 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1161 EKKELEENFEKLRLT-LQDQVDTLTFQSQSLRDRARRFEEALRKTTE--EQLEIALAP----YQHLEEDMQSLKQVLEMK 1233
Cdd:TIGR02168 221 ELRELELALLVLRLEeLREELEELQEELKEAEEELEELTAELQELEEklEELRLEVSEleeeIEELQKELYALANEISRL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1234 NQQI-HLQEKkiieLEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEE 1312
Cdd:TIGR02168 301 EQQKqILRER----LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
.
gi 1327848537 1313 L 1313
Cdd:TIGR02168 377 L 377
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
997-1318 |
1.41e-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: 49.68 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 997 GLARRELKKAIQGFDALAVSTKHFFGKSERALAKEKELSIELANIRDEVafntakcEKLQKEKEtlerrfeeelrrlgwq 1076
Cdd:TIGR02169 152 PVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQL-------ERLRRERE---------------- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1077 qQAEvqelqerlqqQFQAESARLQAEHQDQLLRMRCQHQEQVEDITASHEAALLEMENnhtvaITILQDDHDHKVQELMS 1156
Cdd:TIGR02169 209 -KAE----------RYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK-----LTEEISELEKRLEEIEQ 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1157 THEFEKKELEENFEKLRLTLQDQVDTLTFQSQSLRDRARRFEEALRKTtEEQLEIALAPYQHLEEDMQSLkqvlemknqq 1236
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA-EERLAKLEAEIDKLLAEIEEL---------- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1237 ihlqEKKIIELEKLVEKniiLEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWK 1316
Cdd:TIGR02169 342 ----EREIEEERKRRDK---LTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
..
gi 1327848537 1317 LQ 1318
Cdd:TIGR02169 415 LQ 416
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1161-1295 |
1.98e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1161 EKKELEENFEKLRL---TLQDQVDTLTFQSQsLRDRARRFEEALRKTTE-----EQLEIALAPYQHLEEDMQSLKQVLEM 1232
Cdd:COG4717 96 ELEELEEELEELEAeleELREELEKLEKLLQ-LLPLYQELEALEAELAElperlEELEERLEELRELEEELEELEAELAE 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327848537 1233 KNQQIHLQEKK------------IIELEKLVEKNIILEERIQVLQQQNEDLKARIDQnTVVTRQLSEENANLQEY 1295
Cdd:COG4717 175 LQEELEELLEQlslateeelqdlAEELEELQQRLAELEEELEEAQEELEELEEELEQ-LENELEAAALEERLKEA 248
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1103-1313 |
3.01e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 48.63 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1103 HQDQLLRMRCQHQEQVEDITASHEAA------------LLEMENNHTVA-ITILQD---DHDHK-------VQELMSTH- 1158
Cdd:pfam01576 343 HEAQLQEMRQKHTQALEELTEQLEQAkrnkanlekakqALESENAELQAeLRTLQQakqDSEHKrkklegqLQELQARLs 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1159 --EFEKKELEENFEKLrltlQDQVDTLTFQSQSLRDRARRFEEALrktteEQLEIALAPYQHL--EEDMQSLK---QVLE 1231
Cdd:pfam01576 423 esERQRAELAEKLSKL----QSELESVSSLLNEAEGKNIKLSKDV-----SSLESQLQDTQELlqEETRQKLNlstRLRQ 493
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1232 MKNQQIHLQEkkiiELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQ-------EKK 1304
Cdd:pfam01576 494 LEDERNSLQE----QLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQqleekaaAYD 569
|
....*....
gi 1327848537 1305 RLSRTNEEL 1313
Cdd:pfam01576 570 KLEKTKNRL 578
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1093-1310 |
4.27e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1093 QAESARLQAEHQD--QLLRMRCQHQEQVEDITASHEAALLEMENNhTVAITILQDDHDHKVQElmsthEFEK---KELEE 1167
Cdd:PRK11281 55 EAEDKLVQQDLEQtlALLDKIDRQKEETEQLKQQLAQAPAKLRQA-QAELEALKDDNDEETRE-----TLSTlslRQLES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1168 NFEKLRLTLQD-QVDTLTFQSQ--SLRDRARRF------------------------EEALRKTTEEQLEIALA------ 1214
Cdd:PRK11281 129 RLAQTLDQLQNaQNDLAEYNSQlvSLQTQPERAqaalyansqrlqqirnllkggkvgGKALRPSQRVLLQAEQAllnaqn 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1215 PYQHLE----EDMQSLKQV-LEMKNQQIHLQEKKIIELEKLV-EKNIILEERiQVLQQQNEDLKARIDQNTVVTRQLsEE 1288
Cdd:PRK11281 209 DLQRKSlegnTQLQDLLQKqRDYLTARIQRLEHQLQLLQEAInSKRLTLSEK-TVQEAQSQDEAARIQANPLVAQEL-EI 286
|
250 260
....*....|....*....|..
gi 1327848537 1289 NANLQEYVEKETQEKKRLSRTN 1310
Cdd:PRK11281 287 NLQLSQRLLKATEKLNTLTQQN 308
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1155-1314 |
4.30e-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: 48.12 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1155 MSTHEFEKKELEENFEKlRLTLQDQVDTLTFQSQSLRDRARRFEEALRKTTEEQLEIA--LAPYQHLEEDMQSLKQV-LE 1231
Cdd:TIGR00606 202 VQEHQMELKYLKQYKEK-ACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEhnLSKIMKLDNEIKALKSRkKQ 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1232 MKNQQIHLQEKkiieleklvekniileeRIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNE 1311
Cdd:TIGR00606 281 MEKDNSELELK-----------------MEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKT 343
|
...
gi 1327848537 1312 ELL 1314
Cdd:TIGR00606 344 ELL 346
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1175-1310 |
4.48e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1175 TLQDQVDTLTFQSQSLRDRARRFEEALRKTTEEQleialapyQHLEEDMQSLKQVLEMKNQQIHLQEKKII--------- 1245
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSEL--------EQLEEELEELNEQLQAAQAELAQAQEELEslqeeaeel 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327848537 1246 --ELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTN 1310
Cdd:COG4372 114 qeELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
971-1277 |
4.73e-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: 48.14 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 971 DLQAREAERQLAQRLRDRCEWQARQLGLARRELKKAIQGFDALAVSTKHFFGKSERALAKEKElsiELANIRDEVAFNTA 1050
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKS---ELKELEARIEELEE 772
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1051 KCEKLQKEKETLERRFEEELRRLGWQQQAEVQELQERLQQQFQAESARLQAEHQD-QLLRMRCQH-QEQVEDITASHEAA 1128
Cdd:TIGR02169 773 DLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEkEYLEKEIQElQEQRIDLKEQIKSI 852
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1129 LLEMENNHTVAITILQ--DDHDHKVQELMSTHEFEKKELEENFEKLRlTLQDQVDTLTFQSQSLRDRARRFEEALRKTTE 1206
Cdd:TIGR02169 853 EKEIENLNGKKEELEEelEELEAALRDLESRLGDLKKERDELEAQLR-ELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1207 EQLEIALAPYQHLEE-----DMQSLKQVLEMKNQQIHLQE----KKIIELEKLVEKNIILEERIQVLQQQNEDLKARIDQ 1277
Cdd:TIGR02169 932 ELSEIEDPKGEDEEIpeeelSLEDVQAELQRVEEEIRALEpvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1118-1316 |
5.11e-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: 47.79 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1118 VEDITASHEAALLEMENNHTVAITILQDDHDhKVQELMSTHefeKKELEENFEKLRLTL------QDQVDTLTFQSQSLR 1191
Cdd:pfam05483 192 IEKMILAFEELRVQAENARLEMHFKLKEDHE-KIQHLEEEY---KKEINDKEKQVSLLLiqitekENKMKDLTFLLEESR 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1192 DRARRFEEA-------LRKTTEEQ-------------LEIALAPYQHLEEDMQ----SLKQVLEMKNQQIHLQEKK---- 1243
Cdd:pfam05483 268 DKANQLEEKtklqdenLKELIEKKdhltkeledikmsLQRSMSTQKALEEDLQiatkTICQLTEEKEAQMEELNKAkaah 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1244 ---IIELEKLVeknIILEERIQVLQQQnedLKARIDQNTVVTRQLSEENANLQEYV------EKETQEKKRLSRTNEELL 1314
Cdd:pfam05483 348 sfvVTEFEATT---CSLEELLRTEQQR---LEKNEDQLKIITMELQKKSSELEEMTkfknnkEVELEELKKILAEDEKLL 421
|
..
gi 1327848537 1315 WK 1316
Cdd:pfam05483 422 DE 423
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1159-1314 |
5.31e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1159 EFEKKELEENFEKLRL------TLQDQVDTLTFQSQSLRDRARRFEEALRKTTEEQLEIALApYQHLEEDMQSLKQVLEM 1232
Cdd:COG1196 221 ELKELEAELLLLKLREleaeleELEAELEELEAELEELEAELAELEAELEELRLELEELELE-LEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1233 KNQQIHLQEKKIIELEKLVEKniiLEERIQVLQQQNEDLKARIDQntvVTRQLSEENANLQEYVEKETQEKKRLSRTNEE 1312
Cdd:COG1196 300 LEQDIARLEERRRELEERLEE---LEEELAELEEELEELEEELEE---LEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
..
gi 1327848537 1313 LL 1314
Cdd:COG1196 374 LA 375
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1219-1313 |
7.91e-05 |
|
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: 47.32 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1219 LEEDMQSLKQV---LEMKNQQIHLQ-EKKIIELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQE 1294
Cdd:TIGR04523 340 LNEQISQLKKEltnSESENSEKQRElEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ 419
|
90
....*....|....*....
gi 1327848537 1295 YVEKETQEKKRLSRTNEEL 1313
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKN 438
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1159-1314 |
9.09e-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: 46.97 E-value: 9.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1159 EFEKKELEENFEKL------RLTLQDQVDTLTFQSQSLRDRARRFEEALRKTTEEQLEIALA------PYQHLEEDMQSL 1226
Cdd:TIGR02168 235 EELREELEELQEELkeaeeeLEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEisrleqQKQILRERLANL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1227 KQVLEMKNQQIHLQEKKIIELEKLVEKniiLEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEyvEKETQEKKRL 1306
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAE---LEEKLEELKEELESLEAELEELEAELEELESRLEELEE--QLETLRSKVA 389
|
....*...
gi 1327848537 1307 SRTNEELL 1314
Cdd:TIGR02168 390 QLELQIAS 397
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
995-1330 |
1.08e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 995 QLGLARRELKKAIQGFDAlavsTKHFFGKSERALA------KEKELSIELAN-----IRDEVAFNTAKCEKLQKEKETLE 1063
Cdd:pfam15921 469 QLESTKEMLRKVVEELTA----KKMTLESSERTVSdltaslQEKERAIEATNaeitkLRSRVDLKLQELQHLKNEGDHLR 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1064 RRfeeelrrlgwqqQAEvqelqerlqqqfqAESARLQAEHQDQLLRMRCQHQEQVEDITASH---------EAALLEMEN 1134
Cdd:pfam15921 545 NV------------QTE-------------CEALKLQMAEKDKVIEILRQQIENMTQLVGQHgrtagamqvEKAQLEKEI 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1135 N----HTVAITILQDDHDHKVQEL---MSTHEFEK-KELEENFEKLRL----------------TLQDQVDTLTFQSQSL 1190
Cdd:pfam15921 600 NdrrlELQEFKILKDKKDAKIRELearVSDLELEKvKLVNAGSERLRAvkdikqerdqllnevkTSRNELNSLSEDYEVL 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1191 RDRARRFEEALRKTTEE---QLEIALAPYQHLEEDMQSL--------KQVLEMKNQ------QIHLQEKKIIELEKLV-- 1251
Cdd:pfam15921 680 KRNFRNKSEEMETTTNKlkmQLKSAQSELEQTRNTLKSMegsdghamKVAMGMQKQitakrgQIDALQSKIQFLEEAMtn 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1252 ---EKNIILEER--------------------IQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSR 1308
Cdd:pfam15921 760 ankEKHFLKEEKnklsqelstvateknkmageLEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKL 839
|
410 420
....*....|....*....|..
gi 1327848537 1309 TNEELLWKLQTGDPTSPIKLSP 1330
Cdd:pfam15921 840 QHTLDVKELQGPGYTSNSSMKP 861
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
995-1314 |
1.10e-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: 46.98 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 995 QLGLARRELKKAIQgFDALAVSTKHFFG----KSERALAKEKE-LSIELANIRDEVAFNTAKCEKLQKE---KETLERRF 1066
Cdd:TIGR02169 199 QLERLRREREKAER-YQALLKEKREYEGyellKEKEALERQKEaIERQLASLEEELEKLTEEISELEKRleeIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1067 EEELRRLGWQQQAEVQELQERlqqqFQAESARLQAEHQDQLLRMRcQHQEQVEDITASHEAALLEMENNHTvAITILQDD 1146
Cdd:TIGR02169 278 NKKIKDLGEEEQLRVKEKIGE----LEAEIASLERSIAEKERELE-DAEERLAKLEAEIDKLLAEIEELER-EIEEERKR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1147 HDhKVQElmsthefEKKELEENFEKLRLTLQdQVDTltfQSQSLRDRARRFEEALRKTTEEQLEIALAPYQHLEEDMQSL 1226
Cdd:TIGR02169 352 RD-KLTE-------EYAELKEELEDLRAELE-EVDK---EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLS 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1227 KQVLEMKNqQIHLQEKKIIELEKLVEKNII----LEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQ-EYVEKETQ 1301
Cdd:TIGR02169 420 EELADLNA-AIAGIEAKINELEEEKEDKALeikkQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQrELAEAEAQ 498
|
330
....*....|....*...
gi 1327848537 1302 -----EKKRLSRTNEELL 1314
Cdd:TIGR02169 499 araseERVRGGRAVEEVL 516
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1100-1319 |
1.70e-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: 46.21 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1100 QAEHQDQLLRMRcqhqEQVEDITASHEAALLEMEN--NHTVAITILQDDHDHKVQELMSTHEFEKKELE---ENFEKLRL 1174
Cdd:TIGR02169 669 SRSEPAELQRLR----ERLEGLKRELSSLQSELRRieNRLDELSQELSDASRKIGEIEKEIEQLEQEEEklkERLEELEE 744
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1175 TLQDQVDTLTFQSQSLRDRARRFEEALRKTTEEQLEIAlAPYQHL-EEDMQSLKQVLEMKNQQIHLQEKKIIELE----K 1249
Cdd:TIGR02169 745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN-DLEARLsHSRIPEIQAELSKLEEEVSRIEARLREIEqklnR 823
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1250 LVEKNIILEERIQVLQQQNEDLKARIDQN---------------------TVVTRQLSEENANLQEYVEKETQEKKRLSR 1308
Cdd:TIGR02169 824 LTLEKEYLEKEIQELQEQRIDLKEQIKSIekeienlngkkeeleeeleelEAALRDLESRLGDLKKERDELEAQLRELER 903
|
250
....*....|.
gi 1327848537 1309 TNEELLWKLQT 1319
Cdd:TIGR02169 904 KIEELEAQIEK 914
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1120-1292 |
1.72e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 44.13 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1120 DITASHEAALLEMENNHTvAITilqddhdHKVQELMSTHEFEKKELEENFEKLRLTLQDqvdtLTFQSQSLRD---RARR 1196
Cdd:pfam13851 1 ELMKNHEKAFNEIKNYYN-DIT-------RNNLELIKSLKEEIAELKKKEERNEKLMSE----IQQENKRLTEplqKAQE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1197 FEEALRKTTEEQ------LEIALAPYQHLEEDMQSLK---QVLEMKNQQIHL--------QEKKIIEL-EKLVEKNIILE 1258
Cdd:pfam13851 69 EVEELRKQLENYekdkqsLKNLKARLKVLEKELKDLKwehEVLEQRFEKVERerdelydkFEAAIQDVqQKTGLKNLLLE 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 1327848537 1259 ERIQVLQqqnEDLKARidqntvvTRQLSE--ENANL 1292
Cdd:pfam13851 149 KKLQALG---ETLEKK-------EAQLNEvlAAANL 174
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
977-1314 |
1.82e-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: 46.21 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 977 AERQLAQRLRDRCEWQARQLGLARRELKKAIQGFDALAVSTKHFFGKSERALAKEKELSIELANIRDEVAFNTAKCEKLQ 1056
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1057 KEKETLERRFeeelrrlgwQQQAEVQELQERLQQQFQAESARLQAEHQDQLLRMRCQHQEQVEDITASHEAALLEME--- 1133
Cdd:TIGR02169 751 QEIENVKSEL---------KELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEqkl 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1134 NNHTVAITILQDDHDHKVQELMSTHEfEKKELEENFEKLRLTL----------QDQVDTLTFQSQSLRDRARRFEEALRK 1203
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKE-QIKSIEKEIENLNGKKeeleeeleelEAALRDLESRLGDLKKERDELEAQLRE 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1204 TTEEQLEIALApYQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTR 1283
Cdd:TIGR02169 901 LERKIEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
|
330 340 350
....*....|....*....|....*....|.
gi 1327848537 1284 QLSEENANLQEYVEKetqeKKRLSRTNEELL 1314
Cdd:TIGR02169 980 EYEEVLKRLDELKEK----RAKLEEERKAIL 1006
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1076-1313 |
2.03e-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: 45.78 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1076 QQQAEVQELQERLQQQFQAESARLQAEHQDqLLRMRCQHQEQVEDITasHEAALLEME-NNHTVAITILQ---DDHDHKV 1151
Cdd:TIGR04523 401 QNQEKLNQQKDEQIKKLQQEKELLEKEIER-LKETIIKNNSEIKDLT--NQDSVKELIiKNLDNTRESLEtqlKVLSRSI 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1152 QELMSTHEFEKKELEENFEKLrLTLQDQVDTLTFQSQSLRDRARRFEEALRKTTEEQLEIALAPYQhLEEDMQSLKQVLE 1231
Cdd:TIGR04523 478 NKIKQNLEQKQKELKSKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD-LEDELNKDDFELK 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1232 MKNQQIHLQE--KKIIEL----EKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKR 1305
Cdd:TIGR04523 556 KENLEKEIDEknKEIEELkqtqKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKN 635
|
....*...
gi 1327848537 1306 LSRTNEEL 1313
Cdd:TIGR04523 636 IKSKKNKL 643
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
516-974 |
2.58e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 516 STPAPLLHPETTVNSSHHPTPPG--SSSQELGvfSGDTGSPSVASPPTdggqvlnTSPKVPDRTTcssgipkPPTHPKDT 593
Cdd:PHA03247 2513 SRLAPAILPDEPVGEPVHPRMLTwiRGLEELA--SDDAGDPPPPLPPA-------APPAAPDRSV-------PPPRPAPR 2576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 594 PSSQEAREKletekmeeraEAKPILMPKPkhVRPKIITYIRRNPQALSQgdaslvPVGLPYAPPTCGMPLPQEEKAASRD 673
Cdd:PHA03247 2577 PSEPAVTSR----------ARRPDAPPQS--ARPRAPVDDRGDPRGPAP------PSPLPPDTHAPDPPPPSPSPAANEP 2638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 674 LQPSAnmyeKLKPDLQKPRVFPSGLMVS-------------------GIKPPAHHFSQMSEKFLQEVADHPGKEEFCSPP 734
Cdd:PHA03247 2639 DPHPP----PTVPPPERPRDDPAPGRVSrprrarrlgraaqassppqRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHA 2714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 735 YTHYEVPPTFYRSAMLLKPQLGLGAMSRlPSTKSRILIASQRSSASaihPPGSLTTAASFYGSDPSDLKKASNSNAAKAS 814
Cdd:PHA03247 2715 LVSATPLPPGPAAARQASPALPAAPAPP-AVPAGPATPGGPARPAR---PPTTAGPPAPAPPAAPAAGPPRRLTRPAVAS 2790
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 815 LPKSGLRPPGYSRLPAAKLAAFGFVRSSSISAVPSSQSLDSVQPEQSRPVTRSTFGNEEQAPLKQALPSKD-TPKGAGRA 893
Cdd:PHA03247 2791 LSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDvRRRPPSRS 2870
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 894 APASSSNATTPRRSLLPAPK-STSTPAGAKKELQKDPEaKKPAVSSPKRTASAATKPHSPGYPKQRTSAPRNEFPPKPDL 972
Cdd:PHA03247 2871 PAAKPAAPARPPVRRLARPAvSRSTESFALPPDQPERP-PQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDP 2949
|
..
gi 1327848537 973 QA 974
Cdd:PHA03247 2950 AG 2951
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1162-1313 |
3.89e-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: 45.05 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1162 KKELEENFEKLRLTLQ--DQVDTLTF----QSQSLRDRARRFEEALRKTTEE---QLEIALAPYQHLEEDMQSLKQVLEM 1232
Cdd:TIGR02168 171 KERRKETERKLERTREnlDRLEDILNelerQLKSLERQAEKAERYKELKAELrelELALLVLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1233 KNQQIHLQEKKIIELE-KLVEKNII---LEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQ-EYVEKETQ---EKK 1304
Cdd:TIGR02168 251 AEEELEELTAELQELEeKLEELRLEvseLEEEIEELQKELYALANEISRLEQQKQILRERLANLErQLEELEAQleeLES 330
|
....*....
gi 1327848537 1305 RLSRTNEEL 1313
Cdd:TIGR02168 331 KLDELAEEL 339
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1102-1299 |
4.75e-04 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 43.11 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1102 EHQDQLLRMRCQHQEQVEDITASHEAALLEMENNHTVAItilqdDHDHKVQELMST---HEFEKKELEENFEKLRLTLQD 1178
Cdd:pfam15665 11 EHEAEIQALKEAHEEEIQQILAETREKILQYKSKIGEEL-----DLKRRIQTLEESleqHERMKRQALTEFEQYKRRVEE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1179 Q--------VDTLTFQSQSLRDRARRFEEALRKTTEEQLEIALAPYQHLEE-DMQSLKQVLEMKNQQIHLQEKKIIELEK 1249
Cdd:pfam15665 86 RelkaeaehRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEElRAKHRQEIQELLTTQRAQSASSLAEQEK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1250 LVEKniiLEERIQVLQQQNEDLKAridQNTVVTRQLSEENANLQEYVEKE 1299
Cdd:pfam15665 166 LEEL---HKAELESLRKEVEDLRK---EKKKLAEEYEQKLSKAQAFYERE 209
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1095-1320 |
4.87e-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: 44.83 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1095 ESARLQAEHQDQLLRmRCQHQEQVEDItaSHEAALLEMENNhTVAITILQDDHDHKvqELMStHEFEKKELEENFEKLRL 1174
Cdd:pfam12128 214 PKSRLNRQQVEHWIR-DIQAIAGIMKI--RPEFTKLQQEFN-TLESAELRLSHLHF--GYKS-DETLIASRQEERQETSA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1175 TLQDQVDTLTFQSQSLRDRARRFEEALR---KTTEEQLEIALAPY-QHLEEDMQSLKQVLEMKNQ---QIHLQEKkiiEL 1247
Cdd:pfam12128 287 ELNQLLRTLDDQWKEKRDELNGELSAADaavAKDRSELEALEDQHgAFLDADIETAAADQEQLPSwqsELENLEE---RL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1248 EKLVEKNIILEE----RIQVLQQQNEDLKARIDQNT-----VVTRQLSEENANLQ--EYVEKETQEKKRLSRTNEELLWK 1316
Cdd:pfam12128 364 KALTGKHQDVTAkynrRRSKIKEQNNRDIAGIKDKLakireARDRQLAVAEDDLQalESELREQLEAGKLEFNEEEYRLK 443
|
....
gi 1327848537 1317 LQTG 1320
Cdd:pfam12128 444 SRLG 447
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
973-1306 |
4.94e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.72 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 973 QAREAERQLAQRLRDRCEWQARQLGLARRELKKAIQGFDALAVSTKHFFGKSERALA----KEKELSIEL-ANIR--DEV 1045
Cdd:pfam15921 328 QLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdlhkREKELSLEKeQNKRlwDRD 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1046 AFNTAKCEKLQKEKETLerrfeeelrrlgwqqqaevqelqerlqqqfQAESARLQAehqdqLLR-MRCQHQEQVEditas 1124
Cdd:pfam15921 408 TGNSITIDHLRRELDDR------------------------------NMEVQRLEA-----LLKaMKSECQGQME----- 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1125 HEAALLEMENNHTVAITILqddhdhkVQELMSTHEFEKKELEENFEKlRLTLQDQVDTLTFQSQSLRDRARRFEEALRKT 1204
Cdd:pfam15921 448 RQMAAIQGKNESLEKVSSL-------TAQLESTKEMLRKVVEELTAK-KMTLESSERTVSDLTASLQEKERAIEATNAEI 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1205 TE--EQLEIALAPYQHLEEDMQSLKQVlEMKNQQIHLQekkiielekLVEKNIILEeriqVLQQQNEDLKARIDQNTVVT 1282
Cdd:pfam15921 520 TKlrSRVDLKLQELQHLKNEGDHLRNV-QTECEALKLQ---------MAEKDKVIE----ILRQQIENMTQLVGQHGRTA 585
|
330 340
....*....|....*....|....
gi 1327848537 1283 RQLSEENANLQEYVEKETQEKKRL 1306
Cdd:pfam15921 586 GAMQVEKAQLEKEINDRRLELQEF 609
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1094-1309 |
6.25e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 44.36 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1094 AESAR--LQAEHQDQLLRMRCQHQEQVEDITASHEAALLEMENNH---TVAITILQDDHDHKVQELmSTHEFEKKELEEN 1168
Cdd:pfam07111 127 AEMVRknLEEGSQRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAeglEKSLNSLETKRAGEAKQL-AEAQKEAELLRKQ 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1169 FEKLRLTLQDQVdTLTfqsQSLRDRA--RRFEEALRKTTEEQLEIALAPYQHLEEDMQSLKQVLEMKNQQIH-------L 1239
Cdd:pfam07111 206 LSKTQEELEAQV-TLV---ESLRKYVgeQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQslthmlaL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1240 QEKkiiELEKLVEKNIILE---------------ERIQVLQQQnedLKARIDQNTVVTRQLSEENANLQEYVEKETQEKK 1304
Cdd:pfam07111 282 QEE---ELTRKIQPSDSLEpefpkkcrsllnrwrEKVFALMVQ---LKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQA 355
|
....*
gi 1327848537 1305 RLSRT 1309
Cdd:pfam07111 356 ILQRA 360
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
973-1228 |
6.40e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 973 QAREAERQLAQrLRdrcewQARQLGLARRELKKAIQGFDALAVSTKHFFGKSERALAKEkelsiELANIRDEVAFNTAKC 1052
Cdd:COG4913 243 ALEDAREQIEL-LE-----PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA-----ELEELRAELARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1053 EKLQKEKEtlerrfeeelrrlgwQQQAEVQelqerlqqqfQAESARLQAEHQ--DQLLRMRCQHQEQVEDITASHEaall 1130
Cdd:COG4913 312 ERLEARLD---------------ALREELD----------ELEAQIRGNGGDrlEQLEREIERLERELEERERRRA---- 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1131 emennhtvaitilqddhdhKVQELMSTHEFEKKELEENFEKLRLTLQDQVDTLTFQSQSLRDRARRFEEALRKTTEEqle 1210
Cdd:COG4913 363 -------------------RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE--- 420
|
250
....*....|....*...
gi 1327848537 1211 ialapYQHLEEDMQSLKQ 1228
Cdd:COG4913 421 -----LRELEAEIASLER 433
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
625-977 |
7.57e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 44.16 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 625 VRPKIITYIRrNPQALSQGDAS-----LVPVGLPYA-----PPTCGMPLPQEEKAASRDLQPSAnmyeklKPDLQKPRVf 694
Cdd:PHA03247 2529 VHPRMLTWIR-GLEELASDDAGdppppLPPAAPPAApdrsvPPPRPAPRPSEPAVTSRARRPDA------PPQSARPRA- 2600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 695 PSGLMVSGIKPPAHHfsqmsekflqevadhpgkeefCSPPYTHYEVPPTFYRSAMLLKPQLGlGAMSRLPSTKSRILIAS 774
Cdd:PHA03247 2601 PVDDRGDPRGPAPPS---------------------PLPPDTHAPDPPPPSPSPAANEPDPH-PPPTVPPPERPRDDPAP 2658
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 775 QRSSASAihppgslttaasfygsdpsdlKKASNSNAAKASLPKSGLRPPGySRLPAAKLAAFGFVRSSSISAVPSSQSLD 854
Cdd:PHA03247 2659 GRVSRPR---------------------RARRLGRAAQASSPPQRPRRRA-ARPTVGSLTSLADPPPPPPTPEPAPHALV 2716
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 855 SVQPeqSRPVTRSTFGNEEQAPLKQ---------ALPSKDTPKG-----AGRAAPASSSN-ATTPRRSLLPAPKSTSTPA 919
Cdd:PHA03247 2717 SATP--LPPGPAAARQASPALPAAPappavpagpATPGGPARPArppttAGPPAPAPPAApAAGPPRRLTRPAVASLSES 2794
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1327848537 920 GAKKELQKDPEAKKPAVSSPKRTASAATKPhSPGYPKQRTSAPRNEFPPKPDLQAREA 977
Cdd:PHA03247 2795 RESLPSPWDPADPPAAVLAPAAALPPAASP-AGPLPPPTSAQPTAPPPPPGPPPPSLP 2851
|
|
| BAR_SNX |
cd07596 |
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ... |
1129-1314 |
9.51e-04 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153280 [Multi-domain] Cd Length: 218 Bit Score: 42.34 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1129 LLEMENNHTVAITILQDdHDHKVQELMSTHEfekkELEENFEKLRLTLQDQVDTLtfqSQSLRDRARRFEE---ALRKTT 1205
Cdd:cd07596 13 ILKLEEQLKKLSKQAQR-LVKRRRELGSALG----EFGKALIKLAKCEEEVGGEL---GEALSKLGKAAEElssLSEAQA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1206 EEQLEIALAPYQHLEEDMQSLKQVLEMKNQ-QIHLQ------EKKIIELEKLVEKNIILEERIQVLQQQNEDLKARIDQ- 1277
Cdd:cd07596 85 NQELVKLLEPLKEYLRYCQAVKETLDDRADaLLTLQslkkdlASKKAQLEKLKAAPGIKPAKVEELEEELEEAESALEEa 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1327848537 1278 ----NTVVTRqLSEE------------NANLQEYVEKETQEKKRLSRTNEELL 1314
Cdd:cd07596 165 rkryEEISER-LKEElkrfheerardlKAALKEFARLQVQYAEKIAEAWESLL 216
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
1116-1313 |
9.87e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 9.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1116 EQVEDITASHEAALLEMEN----NHTVAITILQDDHDHkVQELMsTHEFE-KKELEENFEKLRLTL---QDQVDTL---- 1183
Cdd:PRK04778 256 KEIQDLKEQIDENLALLEEldldEAEEKNEEIQERIDQ-LYDIL-EREVKaRKYVEKNSDTLPDFLehaKEQNKELkeei 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1184 TFQSQSLR------DRARRFEEALRKTTEEQLEIAL------APYQHLEED-MQSLKQVLEMKNQQIHLQEkkiiELEKL 1250
Cdd:PRK04778 334 DRVKQSYTlneselESVRQLEKQLESLEKQYDEITEriaeqeIAYSELQEElEEILKQLEEIEKEQEKLSE----MLQGL 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327848537 1251 VEKNIILEERIQVLQQQNEDLKaridqntvvtRQLseENANL----QEYVEKETQEKKRLSRTNEEL 1313
Cdd:PRK04778 410 RKDELEAREKLERYRNKLHEIK----------RYL--EKSNLpglpEDYLEMFFEVSDEIEALAEEL 464
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
972-1321 |
1.12e-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: 43.56 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 972 LQAREAERQ------LAQRLRDRCEWQARQLGLARRELKKAIQGFDALAVSTKHFFGKSERALAKEKELsielaniRDEV 1045
Cdd:pfam05483 247 IQITEKENKmkdltfLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKAL-------EEDL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1046 AFNTAKCEKLQKEKETLErrfeeelrrlgwQQQAEVQELQERLQQQFQAESARLQaehqdQLLRMRCQHQEQVEDitash 1125
Cdd:pfam05483 320 QIATKTICQLTEEKEAQM------------EELNKAKAAHSFVVTEFEATTCSLE-----ELLRTEQQRLEKNED----- 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1126 EAALLEME----NNHTVAITILQDDHDHKVQELMSTHEFEKKELEEN--FEKLRLTLQDQVDTLTFQSQSlrdrarrfee 1199
Cdd:pfam05483 378 QLKIITMElqkkSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKkqFEKIAEELKGKEQELIFLLQA---------- 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1200 alRKTTEEQLEIALAPYQHLEEdmQSLKQVLEMKNqqihlqekkiiELEKLVEKNIILEERIQVLQQQNEDLKARIDQNT 1279
Cdd:pfam05483 448 --REKEIHDLEIQLTAIKTSEE--HYLKEVEDLKT-----------ELEKEKLKNIELTAHCDKLLLENKELTQEASDMT 512
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1327848537 1280 VVTRQLSEENAN-----------LQEYVEKETQEKKRLSRTNEELlwkLQTGD 1321
Cdd:pfam05483 513 LELKKHQEDIINckkqeermlkqIENLEEKEMNLRDELESVREEF---IQKGD 562
|
|
| ZapB |
pfam06005 |
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ... |
1247-1318 |
1.18e-03 |
|
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.
Pssm-ID: 428718 [Multi-domain] Cd Length: 71 Bit Score: 38.79 E-value: 1.18e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327848537 1247 LEKLVEKNIILEERIQVLQQQNEDLKARidqntvvTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQ 1318
Cdd:pfam06005 6 LEQLETKIQAAVDTIALLQMENEELKEE-------NEELKEEANELEEENQQLKQERNQWQERIRGLLGKLD 70
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1050-1313 |
1.31e-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: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1050 AKCEKLQKEKETLERRFEEELRRLGWQQQaeVQELQERLQQQFQAEsARLQAEHQDQLLRMRCQHQEqVEDITASHEAAl 1129
Cdd:pfam01576 9 AKEEELQKVKERQQKAESELKELEKKHQQ--LCEEKNALQEQLQAE-TELCAEAEEMRARLAARKQE-LEEILHELESR- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1130 LEMENNHTVAITILQDDHDHKVQELMSTHE----------FEKKELEENFEKLR---LTLQDQVDTLTFQSQSLRDRARR 1196
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDLEEQLDeeeaarqklqLEKVTTEAKIKKLEediLLLEDQNSKLSKERKLLEERISE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1197 FEEALrkTTEEQLEIALAPYQHLEEDMQSLKQVLEMKnqqihlQEKKIIELEKLVEKniiLEERIQVLQQQNEDLKARID 1276
Cdd:pfam01576 164 FTSNL--AEEEEKAKSLSKLKNKHEAMISDLEERLKK------EEKGRQELEKAKRK---LEGESTDLQEQIAELQAQIA 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 1327848537 1277 QNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1313
Cdd:pfam01576 233 ELRAQLAKKEEELQAALARLEEETAQKNNALKKIREL 269
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1023-1294 |
1.39e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1023 KSERALAKEKELSIELANIRDEVAFNTAKCEKLQKEKETLerrfeeelrrlgwQQQAEVQELQERLQQQFQAESARLQAE 1102
Cdd:PRK02224 193 KAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQA-------------RETRDEADEVLEEHEERREELETLEAE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1103 HQD------QLLRMRCQHQEQVEDITASHEAalLEMENNHTVAITILQDDHDHKVQELMSTHEFEKKELEENFEKLRLTL 1176
Cdd:PRK02224 260 IEDlretiaETEREREELAEEVRDLRERLEE--LEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1177 QDqvdtLTFQSQSLRDRARRFEEALRKTTEEQLEialapyqhLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKLVEKNII 1256
Cdd:PRK02224 338 QA----HNEEAESLREDADDLEERAEELREEAAE--------LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1327848537 1257 ----LEERIQVLQQQNEDLKARIDQNTVVTRQLS---EENANLQE 1294
Cdd:PRK02224 406 dlgnAEDFLEELREERDELREREAELEATLRTARervEEAEALLE 450
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
553-1060 |
1.45e-03 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 43.22 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 553 SPSVASPPTDGG--------QVLNTSPKVpdrTTCSSGIPKPPTHPKDTPSSqearekLETEKMEERAEAKPIlMPKPKH 624
Cdd:pfam03154 145 SPSIPSPQDNESdsdssaqqQILQTQPPV---LQAQSGAASPPSPPPPGTTQ------AATAGPTPSAPSVPP-QGSPAT 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 625 VRPKIITYIRRNPQALSQGDASLVPVGLPYA-PPTCGMPLPQEEKAASRDLQPSANMYEKLKPDLQKPRVFPSGLMVSGI 703
Cdd:pfam03154 215 SQPPNQTQSTAAPHTLIQQTPTLHPQRLPSPhPPLQPMTQPPPPSQVSPQPLPQPSLHGQMPPMPHSLQTGPSHMQHPVP 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 704 KPPAHHFSQMSEKFL----QEVADHPGKEEFCSPPYTHYEVPPTFYRSAMLLKPQLGLGAMSRLPSTKSRILIASQrssa 779
Cdd:pfam03154 295 PQPFPLTPQSSQSQVppgpSPAAPGQSQQRIHTPPSQSQLQSQQPPREQPLPPAPLSMPHIKPPPTTPIPQLPNPQ---- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 780 SAIHPPgslttaasfYGSDPSDLKKASNSNAAKASLPKSGL---RPPGYSRLPAAKLAAFGFVRSSSISAVPSSQSLDSV 856
Cdd:pfam03154 371 SHKHPP---------HLSGPSPFQMNSNLPPPPALKPLSSLsthHPPSAHPPPLQLMPQSQQLPPPPAQPPVLTQSQSLP 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 857 QPEQSRPVTRSTFGNEEQAPLKQA--LPSKDTPKGAGRAAPASSSNATTPRRSLLPAPKSTSTPagakkeLQKDPEAKKP 934
Cdd:pfam03154 442 PPAASHPPTSGLHQVPSQSPFPQHpfVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGP------VPAAVSCPLP 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 935 AVSSPKRTASAATKPHSPGyPKQRTSAPRNEFPPKPDLQAREAerqlaqrlrdrcewqarqlglarRELKKAIQGFDALA 1014
Cdd:pfam03154 516 PVQIKEEALDEAEEPESPP-PPPRSPSPEPTVVNTPSHASQSA-----------------------RFYKHLDRGYNSCA 571
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1327848537 1015 VSTKHFFGKSERALAKEKELSIELANIRDEVAFNTAKCEKLQKEKE 1060
Cdd:pfam03154 572 RTDLYFMPLAGSKLAKKREEALEKAKREAEQKAREEKEREKEKEKE 617
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1164-1313 |
1.56e-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: 42.75 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1164 ELEENFEKLRLTlQDQVDTLTFQSQSLRDRArrfeEALRKTTEE--QLEIALAPYQHLEEDMQSLK-QV--LEMKNQqIH 1238
Cdd:pfam05622 91 ELEKEVLELQHR-NEELTSLAEEAQALKDEM----DILRESSDKvkKLEATVETYKKKLEDLGDLRrQVklLEERNA-EY 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1239 LQEKkiIELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLS-------RTNE 1311
Cdd:pfam05622 165 MQRT--LQLEEELKKANALRGQLETYKRQVQELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIierdtlrETNE 242
|
..
gi 1327848537 1312 EL 1313
Cdd:pfam05622 243 EL 244
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1094-1312 |
1.73e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 42.80 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1094 AESARLQAEHQDQLLRMR----------CQHQEQVEDITASHEAALLEME---NNHTV--------AITILQDDHDHKVQ 1152
Cdd:pfam17380 337 AEQERMAMERERELERIRqeerkrelerIRQEEIAMEISRMRELERLQMErqqKNERVrqeleaarKVKILEEERQRKIQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1153 ELMSTHEFEKKELEENFEKLRLTLQDQvdtltfqsqslrdRARRFEEALRKTTEEQLEIALAPYQHLEEDMQSLKQVLEM 1232
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQREVRRLEEE-------------RAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1233 KNQQ-IHLQEKKIIELEKLVEKNIILEE--RIQVLQQQNEDLKA--------RIDQNTVVTRQLSEENANLQEYVEKETQ 1301
Cdd:pfam17380 484 RDRKrAEEQRRKILEKELEERKQAMIEEerKRKLLEKEMEERQKaiyeeerrREAEEERRKQQEMEERRRIQEQMRKATE 563
|
250
....*....|.
gi 1327848537 1302 EKKRLSRTNEE 1312
Cdd:pfam17380 564 ERSRLEAMERE 574
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
309-677 |
1.82e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 309 PRNEEGLTSAQAQGPGCHEERSMSPVERQELLEKAYREATSQGNSSHRQlGVRRGSSLEEMTGVSAGVEGSQQATPTLSA 388
Cdd:PHA03247 2633 PAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQ-RPRRRAARPTVGSLTSLADPPPPPPTPEPA 2711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 389 APAGEAGTRL-TGKMSAGVGRMARETASGQTAPDVGQAAPVRRDPTESVPSEvsgeerrlgSGNSGSTKllASGPSAGGS 467
Cdd:PHA03247 2712 PHALVSATPLpPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTT---------AGPPAPAP--PAAPAAGPP 2780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 468 RTDTSGLLSPRGSNLEARKGKEMVAEnrnllenAAQTDNTPAGVDSAFSTPAPLLHPETTVNSSHHPTPPGSSSQELGVF 547
Cdd:PHA03247 2781 RRLTRPAVASLSESRESLPSPWDPAD-------PPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG 2853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 548 SG-DTGSPSVASPPTDGGQVLNTSPKVPDRTTCSSGIPKPPTHPKDTPSSQEAREKLETEKMEERAEAKPILMPKPKhvr 626
Cdd:PHA03247 2854 GSvAPGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ--- 2930
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1327848537 627 PKIITYIRRNPQALSQGDASLVPVGLPYAPPTCGMPLPQEEKAASRDLQPS 677
Cdd:PHA03247 2931 PPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQ 2981
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1093-1313 |
1.90e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1093 QAESARLQAEHQDQLLRMRCQHQEQVEDITASHEAALLEMENnHTVAITILQDDHdHKVQELMSTHEFEKKELEENFEKL 1172
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA-LERRIAALARRI-RALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1173 RLTLQDQVDTLtfqsqslrdrARRFEEALRKTTEEQLEIALAP--YQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEKL 1250
Cdd:COG4942 96 RAELEAQKEEL----------AELLRALYRLGRQPPLALLLSPedFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327848537 1251 VEKNIILEERIQVL----QQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1313
Cdd:COG4942 166 RAELEAERAELEALlaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1154-1314 |
2.47e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1154 LMSTHEFEKKELEENFEKLRLTLQDQVDTLTFQSQSLRDRARRFEEAL--RKTTEEQLEIALAPYQHLEEDMQSLKQVle 1231
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQeeLEELEEELEELEAELEELREELEKLEKL-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1232 mknqqihlqekkiIELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNE 1311
Cdd:COG4717 125 -------------LQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE 191
|
...
gi 1327848537 1312 ELL 1314
Cdd:COG4717 192 EEL 194
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1161-1308 |
2.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1161 EKKELEENFEKLRlTLQDQVDTLTFQSQSLRDRARRFEEALrKTTEEQLEIALAPYQHLEEDMQSLKQVLEMKNQQIHLQ 1240
Cdd:COG4372 71 ARSELEQLEEELE-ELNEQLQAAQAELAQAQEELESLQEEA-EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1327848537 1241 EKKIIELEKLVEKniiLEERIQVLQQQNEDLKARiDQNTVVTRQLSEENANLQEYVEKETQEKKRLSR 1308
Cdd:COG4372 149 EEELKELEEQLES---LQEELAALEQELQALSEA-EAEQALDELLKEANRNAEKEEELAEAEKLIESL 212
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1126-1308 |
2.69e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1126 EAALLEMENNHTVAITILQDdhdhKVQELMSTHEFEKKELEENFEKLRLTLQDQVDTLTFQSQSLRDRarrfeealrktt 1205
Cdd:PRK12704 45 EEAKKEAEAIKKEALLEAKE----EIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKR------------ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1206 eeqleialapyqhlEEDMQSLKQVLEMKNQQIhlqEKKIIELEKLVEKNIILEERIQVLQQqnEDLKARIDQNtvVTRQL 1285
Cdd:PRK12704 109 --------------EEELEKKEKELEQKQQEL---EKKEEELEELIEEQLQELERISGLTA--EEAKEILLEK--VEEEA 167
|
170 180
....*....|....*....|....
gi 1327848537 1286 SEENANL-QEYVEKETQEKKRLSR 1308
Cdd:PRK12704 168 RHEAAVLiKEIEEEAKEEADKKAK 191
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1170-1313 |
2.77e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1170 EKLRLTLQDQVDTLTFQSQSLRDRARRFEEALRKTTEE--QLEIALAPYQHLEEDMQS-LKQVleMKNQQIHLQEKkiiE 1246
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEikRLELEIEEVEARIKKYEEqLGNV--RNNKEYEALQK---E 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327848537 1247 LEKLVEKNIILEERIQVLQQQNEDLKARIDQntvVTRQLSEENANLQeyvEKETQEKKRLSRTNEEL 1313
Cdd:COG1579 98 IESLKRRISDLEDEILELMERIEELEEELAE---LEAELAELEAELE---EKKAELDEELAELEAEL 158
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1113-1308 |
3.69e-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: 41.65 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1113 QHQEQVEDITASHEAALLEMENNHTVAITILQDDHDHKVQELMSTHEFEKKELE------ENFEKLRLTLQ--DQVDTLT 1184
Cdd:pfam05557 13 QLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEaeealrEQAELNRLKKKylEALNKKL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1185 FQSQSLRDRARRFEEALRKTTEE---QLEIALAPYQHLEEDMQSLKQVLEMKNQQIHLQEKKIIELEK----LVEKNIIL 1257
Cdd:pfam05557 93 NEKESQLADAREVISCLKNELSElrrQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKqqssLAEAEQRI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1327848537 1258 EERIQVLQQQNED---LK------ARIDQNTVVTRQLSEENANLQEYVE-----KETQE--KKRLSR 1308
Cdd:pfam05557 173 KELEFEIQSQEQDseiVKnskselARIPELEKELERLREHNKHLNENIEnklllKEEVEdlKRKLER 239
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1093-1266 |
4.44e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1093 QAESARLQAEHQDQLLRmrcQHQEQVEDITASHEAALLEMEN--NHTVAITILQDDHDHKVQelMSTHEFEKKELEENFE 1170
Cdd:COG4717 75 ELEEELKEAEEKEEEYA---ELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQE--LEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1171 KLR---LTLQDQVDTLTFQSQSLRDRARRFEEALRKT---TEEQLEIALAPYQHLEEDMQSLKQVLEMKNQQIHLQEKKI 1244
Cdd:COG4717 150 ELEerlEELRELEEELEELEAELAELQEELEELLEQLslaTEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180
....*....|....*....|..
gi 1327848537 1245 IELEKLVEkNIILEERIQVLQQ 1266
Cdd:COG4717 230 EQLENELE-AAALEERLKEARL 250
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1116-1322 |
5.73e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.04 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1116 EQVEDITASHEAALLEMENNHTVaITILQDDHDHKVQEL--MSTHEFEKKELEENFEKLRLTLQDQVDTLTFQSQSLRDR 1193
Cdd:PRK01156 204 KQIADDEKSHSITLKEIERLSIE-YNNAMDDYNNLKSALneLSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERH 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1194 ARRFEEALRKTTEEQLEialapYQHLEEDMQSLKQVLEMKNQQI---HLQEKKIIELEKLVEKNIILEERIQVLQQQNED 1270
Cdd:PRK01156 283 MKIINDPVYKNRNYIND-----YFKYKNDIENKKQILSNIDAEInkyHAIIKKLSVLQKDYNDYIKKKSRYDDLNNQILE 357
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1327848537 1271 LKARIDQNTVVTRQLSeenaNLQEYVEKETQEKKRLSRTNEELLwKLQTGDP 1322
Cdd:PRK01156 358 LEGYEMDYNSYLKSIE----SLKKKIEEYSKNIERMSAFISEIL-KIQEIDP 404
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1159-1317 |
8.31e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1159 EFEKKELEEnfeKLRlTLQDQVDTLTFQSQSLRDRARRFEEaLRKTTEEQLEIAlAPYQHLEEDMQSLKQVLEMKNQQIH 1238
Cdd:PRK03918 251 EGSKRKLEE---KIR-ELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLS-EFYEEYLDELREIEKRLSRLEEEIN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1239 LQEKKIIELEKLVEKNIILEERIQVLQQQNEDLKAR------IDQNTVVTRQLSEENANLQ-EYVEKETQEKKRLSRTNE 1311
Cdd:PRK03918 325 GIEERIKELEEKEERLEELKKKLKELEKRLEELEERhelyeeAKAKKEELERLKKRLTGLTpEKLEKELEELEKAKEEIE 404
|
....*.
gi 1327848537 1312 ELLWKL 1317
Cdd:PRK03918 405 EEISKI 410
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1101-1313 |
8.38e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 8.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1101 AEHQDQLLRMRCQHQEQVEDITASHEAALLEMEnnhtvaITILQDDHDhKVQELMSTHEFEKKELEENFEKLRltlqDQV 1180
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVEAEDR------IERLEERRE-DLEELIAERRETIEEKRERAEELR----ERA 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1181 DTLTFQSQSLRDRARRFEEALRKTTEE-------------------QLEIALAPYQHLEEDMQSL----KQVLEMKNQQI 1237
Cdd:PRK02224 547 AELEAEAEEKREAAAEAEEEAEEAREEvaelnsklaelkeriesleRIRTLLAAIADAEDEIERLrekrEALAELNDERR 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327848537 1238 -HLQEK--KIIELEKLVEkniilEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEEL 1313
Cdd:PRK02224 627 eRLAEKreRKRELEAEFD-----EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERR 700
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1099-1303 |
8.67e-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: 40.72 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1099 LQAEHQDQLLRMRcQHQEQVEDITASHEAALlemennHTVAITILQDDHDHKvqeLMSTHEFEKKELEENFEKLRlTLQD 1178
Cdd:TIGR00618 619 RKLQPEQDLQDVR-LHLQQCSQELALKLTAL------HALQLTLTQERVREH---ALSIRVLPKELLASRQLALQ-KMQS 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1179 QVDTLTF------QSQSLRDRARRFEEALRKTTEEQLEIALAPYQHLEEDMQSLKQVL-EMKNQQIHLQEKKIIELEKLV 1251
Cdd:TIGR00618 688 EKEQLTYwkemlaQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLkELMHQARTVLKARTEAHFNNN 767
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1327848537 1252 EKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEK 1303
Cdd:TIGR00618 768 EEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIL 819
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1163-1320 |
9.24e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.89 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1163 KELEENFEKLR--LTLQDQVDTLTFQSQSLRDRARRFEEALRKTTEEqleialapYQHLEEDMQSLKQvlemknqqihlq 1240
Cdd:COG1340 143 KELEKELEKAKkaLEKNEKLKELRAELKELRKEAEEIHKKIKELAEE--------AQELHEEMIELYK------------ 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327848537 1241 ekkiiELEKLVEKNIILEERIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVE--KETQEKKRLSRTNEELLWKLQ 1318
Cdd:COG1340 203 -----EADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRalKREKEKEELEEKAEEIFEKLK 277
|
..
gi 1327848537 1319 TG 1320
Cdd:COG1340 278 KG 279
|
|
| |
