|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-264 |
2.24e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 15 AETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTelktklhEEKMKELQAVREAL 94
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-------LEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 95 LRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALtm 174
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE-- 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 175 viQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLLDE-KDARRFQLKIAELSAIIRKLEDRNALLSEERNELLKRLR 253
Cdd:COG1196 410 --EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAaEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
|
250
....*....|.
gi 1907184534 254 EAESQYKPLLD 264
Cdd:COG1196 488 EAAARLLLLLE 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
7-335 |
1.41e-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: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 7 GSRAKGDKAETLAALQAANE--ELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHavlvtELKTKLHEEKM 84
Cdd:TIGR02168 659 GVITGGSAKTNSSILERRREieELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-----ELSRQISALRK 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 85 KELQAVREALLRQHEAELLRVikikdnENQRLQALLNTLRDGApdkvktvllcEAKEEAKKGFEVEKVKMQQEISELKGA 164
Cdd:TIGR02168 734 DLARLEAEVEQLEERIAQLSK------ELTELEAEIEELEERL----------EEAEEELAEAEAEIEELEAQIEQLKEE 797
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 165 KKQVEEALT---MVIQADKIKAAEIRSVYhlhqEEITRIKKECEREIRRLLDEKdaRRFQLKIAELSAIIRKLEDRNALL 241
Cdd:TIGR02168 798 LKALREALDelrAELTLLNEEAANLRERL----ESLERRIAATERRLEDLEEQI--EELSEDIESLAAEIEELEELIEEL 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 242 SEERNELLKRLREAESQYKPLLDKNkrltrknEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRrpsslndLDQSQDERE 321
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSEL-------EELSEELRELESKRSELRRELEELREKLAQLE-------LRLEGLEVR 937
|
330
....*....|....
gi 1907184534 322 IDFLKLQIVEQQNL 335
Cdd:TIGR02168 938 IDNLQERLSEEYSL 951
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
11-288 |
1.33e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 57.39 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 11 KGDKAETLAALQAANEELRAKLTDIQI-ELQQEKSKVSKVEREKSQELKQVREHEQRKHavlvteLKTKLHEEKMKELQA 89
Cdd:TIGR02169 767 IEELEEDLHKLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIEQKLNRLT------LEKEYLEKEIQELQE 840
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 90 VREALlrqheaellrviKIKDNENQRLQALLNTlrdgapDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKKQVE 169
Cdd:TIGR02169 841 QRIDL------------KEQIKSIEKEIENLNG------KKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 170 EA---LTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLLDEKDARRFQLKIAELSAIIRKLEDRNALLSEERN 246
Cdd:TIGR02169 903 RKieeLEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYE 982
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907184534 247 ELLKRLREaesqykpLLDKNKRLTRKNEDLSHTLRRIESKLK 288
Cdd:TIGR02169 983 EVLKRLDE-------LKEKRAKLEEERKAILERIEEYEKKKR 1017
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
16-310 |
2.57e-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: 56.60 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 16 ETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKsQELKQVREHEQRKHAVLVTELktkLHEEKMKELQAVREALL 95
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK-QILRERLANLERQLEELEAQL---EELESKLDELAEELAEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 96 RQHEAELLrvikikdNENQRLQALLNTLRdgapdkvktvllcEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTMV 175
Cdd:TIGR02168 343 EEKLEELK-------EELESLEAELEELE-------------AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 176 IQADKIKAAEIRSVYHLHQEeitrikkecEREIRRLLDEKDARRFQLKIAELSAIIRKLEDRNALLSEERNELLKRLREA 255
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQE---------IEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907184534 256 ESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRRPSSL 310
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
16-336 |
3.21e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 16 ETLAALQAANEELRAKLTDIQIELQQEKSKVSKvEREKSQELKQVREHEQRKHAVLVTELKTklhEEKMKELQAVREALL 95
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEE-LRLELEELELELEEAQAEEYELLAELAR---LEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 96 RQHEAELLRVIKIKDNENQRLQALLNTLRdgapdkvktvllcEAKEEAKKgfevekvkmqqeisELKGAKKQVEEALTMV 175
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELE-------------EELEEAEE--------------ELEEAEAELAEAEEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 176 IQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLLDEKDARRFQLKIAELSAIIRKLEDRNALLSEERNELLKRLREA 255
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 256 ESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAgiirrpSSLNDLDQSQDEREIDFLKLQIVEQQNL 335
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL------LLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
.
gi 1907184534 336 I 336
Cdd:COG1196 522 L 522
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
17-261 |
3.59e-08 |
|
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: 55.16 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 17 TLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRkhaVLVTELKTKLHEEKMKELqavrEALLR 96
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR---IAALARRIRALEQELAAL----EAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 97 QHEAELLRVIKIKDNENQRLQALLNTL-RDGAPDKVKTVLLCEAKEEAkkgfevekVKMQQEISELKGAKKQVEEALTMV 175
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDA--------VRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 176 IQADKIKAAEIRSvyhlHQEEITRIKKECEREIRRLLDEKDARrfQLKIAELSAIIRKLEDRNALLSEERNELLKRLREA 255
Cdd:COG4942 159 LAELAALRAELEA----ERAELEALLAELEEERAALEALKAER--QKLLARLEKELAELAAELAELQQEAEELEALIARL 232
|
....*.
gi 1907184534 256 ESQYKP 261
Cdd:COG4942 233 EAEAAA 238
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-348 |
5.58e-08 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 55.53 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 3 KKGAGSRAKGDKAETLAALQAANEELRAKLTDIQielQQEKSKVSKVEREKSQELKQVREhEQRKhavlVTELKTKLHEE 82
Cdd:PTZ00121 1424 KKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK---KAEEAKKKAEEAKKADEAKKKAE-EAKK----ADEAKKKAEEA 1495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 83 KmKELQAVREALLRQHEAELLRvikiKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELK 162
Cdd:PTZ00121 1496 K-KKADEAKKAAEAKKKADEAK----KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 163 GAKKQVEEALTMVIQADKIKAAEIRSVYHLHQEEIT----RIKKECEREIR----RLLDEKDARRFQLKIAELSAI---- 230
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKmkaeEAKKAEEAKIKaeelKKAEEEKKKVEQLKKKEAEEKkkae 1650
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 231 -IRKLEDRNALLSEErnelLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRRPSS 309
Cdd:PTZ00121 1651 eLKKAEEENKIKAAE----EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
330 340 350
....*....|....*....|....*....|....*....
gi 1907184534 310 LNDLDQSQDEREIDFLKLQIVEQQnlIDELSKVSMQHFR 348
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAK--KDEEEKKKIAHLK 1763
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
336-455 |
1.31e-07 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 52.94 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 336 IDELSKVSMQHFRAVLSCVRR-------SHAPCCPVPSGATPPTAlcPPEPRPLLPCAlrSHAPYCPvPSGATT--PTAL 406
Cdd:PHA02682 55 VKEAGRYYQSRLKANSACMQRpsgqsplAPSPACAAPAPACPACA--PAAPAPAVTCP--APAPACP-PATAPTcpPPAV 129
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907184534 407 CPPEPRPllpcalrghAPCCPVHSLK------LPSPDSLCPSRavPLLTAHSLLP 455
Cdd:PHA02682 130 CPAPARP---------APACPPSTRQcppappLPTPKPAPAAK--PIFLHNQLPP 173
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
26-288 |
1.46e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.91 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 26 EELRAKLTDIQ---IELQQEKSKVSKVEREKSQELKQVREHEQRKHAvlvTELKTKLHEEKMKELQAVREAL--LRQHEA 100
Cdd:PRK03918 217 PELREELEKLEkevKELEELKEEIEELEKELESLEGSKRKLEEKIRE---LEERIEELKKEIEELEEKVKELkeLKEKAE 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 101 ELLRVIKIKDNENQRLQAL---LNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTMVIQ 177
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIekrLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 178 ADKIKAAE-IRSVYHLHQ--EEITRIKKECEREIRRLLDEKdaRRFQLKIAELSAIIRKLED--------RNALLSEERN 246
Cdd:PRK03918 374 LERLKKRLtGLTPEKLEKelEELEKAKEEIEEEISKITARI--GELKKEIKELKKAIEELKKakgkcpvcGRELTEEHRK 451
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907184534 247 ELLKRLREaesQYKPLLDKNKRLTRKNEDLSHTLRRIESKLK 288
Cdd:PRK03918 452 ELLEEYTA---ELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
7-321 |
7.34e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 7 GSRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREkSQELKQVREHEQRKHAVLVTELKT-KLHEEKMK 85
Cdd:TIGR02169 658 GSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENR-LDELSQELSDASRKIGEIEKEIEQlEQEEEKLK 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 86 ELQAVREALLRQHEAELLRVI-KIKDNEN--QRLQALLNTLRDgAPDKVKTVLLCEAKEEAKKgfevEKVKMQQEISELK 162
Cdd:TIGR02169 737 ERLEELEEDLSSLEQEIENVKsELKELEAriEELEEDLHKLEE-ALNDLEARLSHSRIPEIQA----ELSKLEEEVSRIE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 163 GAKKQVEEALTMVIQADKIKAAEIRSVYHLhQEEITRIKKECEREIRrlLDEKDARRFQLKIAELSAIIRKLEDRNALLS 242
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQ-RIDLKEQIKSIEKEIE--NLNGKKEELEEELEELEAALRDLESRLGDLK 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 243 EERNELLKRLREAESQYkplldknKRLTRKNEDLSHTLRRIESKLKFVTQENIEM-RQRAGIIRRPSSLNDLDQSQDERE 321
Cdd:TIGR02169 889 KERDELEAQLRELERKI-------EELEAQIEKKRKRLSELKAKLEALEEELSEIeDPKGEDEEIPEEELSLEDVQAELQ 961
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
48-339 |
1.27e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 48 KVEREKS-QELKQVREHEQRKHAVLvTELKTKLHE--------EKMKELQAvrEALLRQHEAELLRvIKIKDNENQRLQA 118
Cdd:COG1196 171 KERKEEAeRKLEATEENLERLEDIL-GELERQLEPlerqaekaERYRELKE--ELKELEAELLLLK-LRELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 119 LLNTLRDGAPDKVKTVLLCEAKEEAKKgfeVEKVKMQQEISELKGAKKQVEEALTMVIQADKIKAAEIRSVyhlhQEEIT 198
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELR---LELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL----EERLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 199 RIKKECEREIRRLLDEKDarrfqlKIAELSAIIRKLEDRNALLSEERNELLKRLREAESQYKPLLDKNKRLTRKNEDLSH 278
Cdd:COG1196 320 ELEEELAELEEELEELEE------ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907184534 279 TLRRIESKLKFVTQENIEMRQRagIIRRPSSLNDLDQSQDEREIDFLKLQIVEQQNLIDEL 339
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLER--LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
6-357 |
1.56e-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: 50.74 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 6 AGSRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKSkvSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMK 85
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELK--LKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 86 ELQAVREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAK 165
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 166 KQVEEALTmVIQADKIKAAEIRSVYHLH-----QEEITRIKKECEREIRRLLDEKDARRFQLKIAELSAIIRKLEDRNAL 240
Cdd:pfam02463 321 KEKKKAEK-ELKKEKEEIEELEKELKELeikreAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 241 LSEERNELLKRLREAESQykpLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAgiirrpSSLNDLDQSQDER 320
Cdd:pfam02463 400 KSEEEKEAQLLLELARQL---EDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQE------LKLLKDELELKKS 470
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907184534 321 EIDFLKLQIVEQQNLIDELSKVSMQHFRAVLSCVRRS 357
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
25-347 |
1.81e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.82 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 25 NEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMKELQAVREAlLRQHEAELLR 104
Cdd:TIGR01612 691 NTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINKDLNKILED-FKNKEKELSN 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 105 VIKIKDNENQRL---QALLNTLRDGAPDKVKTVLLCEakEEAKKGFE----------VEKVKMQQEISELKGAKKQVEEA 171
Cdd:TIGR01612 770 KINDYAKEKDELnkyKSKISEIKNHYNDQINIDNIKD--EDAKQNYDkskeyiktisIKEDEIFKIINEMKFMKDDFLNK 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 172 LTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREirrlldekdarrfQLKIAElsaiiRKLEDRNALLSEERNELLKR 251
Cdd:TIGR01612 848 VDKFINFENNCKEKIDSEHEQFAELTNKIKAEISDD-------------KLNDYE-----KKFNDSKSLINEINKSIEEE 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 252 LREAESQYKplLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRRPSS---LNDLDQSQDEREIDFLKLQ 328
Cdd:TIGR01612 910 YQNINTLKK--VDEYIKICENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKdkfDNTLIDKINELDKAFKDAS 987
|
330
....*....|....*....
gi 1907184534 329 IVEQQNLIDELskvsMQHF 347
Cdd:TIGR01612 988 LNDYEAKNNEL----IKYF 1002
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
11-295 |
2.02e-06 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 50.31 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 11 KGDKAETLAALQAAN----EELRAKLTDIQI-ELQQEKSKVSkverEKSQELKQVREHEQrkhavLVTELKTKLHEEKMK 85
Cdd:PRK05771 15 KSYKDEVLEALHELGvvhiEDLKEELSNERLrKLRSLLTKLS----EALDKLRSYLPKLN-----PLREEKKKVSVKSLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 86 ELQAVREALLRQHEAELLRVI-KIK--DNENQRLQALLNTLrdgapDKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELK 162
Cdd:PRK05771 86 ELIKDVEEELEKIEKEIKELEeEISelENEIKELEQEIERL-----EPWGNFDLDLSLLLGFKYVSVFVGTVPEDKLEEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 163 GAKKQVEEALTmviqadkIKAAEIRSVYhlhqeeITRIKKECEREIRRLLDEKDARRFQLK-IAELSAIIRKLEDRNALL 241
Cdd:PRK05771 161 KLESDVENVEY-------ISTDKGYVYV------VVVVLKELSDEVEEELKKLGFERLELEeEGTPSELIREIKEELEEI 227
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1907184534 242 SEERNELLKRLREAESQYKPLLDKNKrltrknEDLSHTLRRIESKLKFVTQENI 295
Cdd:PRK05771 228 EKERESLLEELKELAKKYLEELLALY------EYLEIELERAEALSKFLKTDKT 275
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1-306 |
2.71e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 1 MSKKGAGSRAKGDKAETLAALQAANEELR-AKLTDIQIELQQEKSKVSKVEREKSQELK---QVREHEQRKHAvlvtELK 76
Cdd:PTZ00121 1488 AKKKAEEAKKKADEAKKAAEAKKKADEAKkAEEAKKADEAKKAEEAKKADEAKKAEEKKkadELKKAEELKKA----EEK 1563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 77 TKLHEEKMKE---LQAVREA-LLRQHEAELLRVIKIKDNENQRLQAllNTLRDGAPDKVKTVLLCEAkEEAKKGFEVEKV 152
Cdd:PTZ00121 1564 KKAEEAKKAEedkNMALRKAeEAKKAEEARIEEVMKLYEEEKKMKA--EEAKKAEEAKIKAEELKKA-EEEKKKVEQLKK 1640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 153 KMQQEISELKGAKKQVEEaltmviqaDKIKAAEIRsvyhlHQEEITRIKKEcerEIRRLLDEKDARRFQLKIAELSAiiR 232
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEE--------NKIKAAEEA-----KKAEEDKKKAE---EAKKAEEDEKKAAEALKKEAEEA--K 1702
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907184534 233 KLEDRNALLSEERNElLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRR 306
Cdd:PTZ00121 1703 KAEELKKKEAEEKKK-AEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-264 |
7.66e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 7.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 3 KKGAGSRAKGDKAETLAALQAANEELRAKLTDIQIELQ--QEKSKVSKVERE---------KSQELKQVREHEQRKHAVL 71
Cdd:PTZ00121 1521 AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKkaEEKKKAEEAKKAeedknmalrKAEEAKKAEEARIEEVMKL 1600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 72 VTELKTKLHEEKMKELQAVREA-LLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVE 150
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEAKIKAeELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEA 1680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 151 KVKMQQEISELKGAKKQVEEA-----LTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRL----LDEKDARRF- 220
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAkkaeeLKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeeakKDEEEKKKIa 1760
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1907184534 221 QLKIAELSAIIRKLEDRNALLSEE-RNELLKRLREAESQYKPLLD 264
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEElDEEDEKRRMEVDKKIKDIFD 1805
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
4-293 |
9.18e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.19 E-value: 9.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 4 KGAGSRAKGDKAETLAALQAANEELRaKLTDIQIELQQEKSKVSKVEREKSQElKQVREHEQRKhavlVTELKTKLHEEK 83
Cdd:pfam15921 436 KAMKSECQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEMLRKVVEELTAK-KMTLESSERT----VSDLTASLQEKE 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 84 mkelqavreallRQHEAELLRVIKIKDNENQRLQALLNTLRDGapdkvktvllcEAKEEAKKGFEVEKVKMQQEISELKG 163
Cdd:pfam15921 510 ------------RAIEATNAEITKLRSRVDLKLQELQHLKNEG-----------DHLRNVQTECEALKLQMAEKDKVIEI 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 164 AKKQVEEALTMVIQADKIKAAEIRSVYHLhQEEITRIKKECErEIRRLLDEKDArrfqlKIAELSAIIRKLEDRNALL-- 241
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEKAQL-EKEINDRRLELQ-EFKILKDKKDA-----KIRELEARVSDLELEKVKLvn 639
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907184534 242 ------------SEERNELLKRLREAESQYKPLLDKNKRLTR----KNEDLSHTLRRIESKLKFVTQE 293
Cdd:pfam15921 640 agserlravkdiKQERDQLLNEVKTSRNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQLKSAQSE 707
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3-243 |
1.78e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 3 KKGAGSRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKskvsKVEREKSQELKQVREHEQRKHAVLVTELKTKlhEE 82
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL----AELEEELEELEEELEELEEELEEAEEELEEA--EA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 83 KMKELQAVREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDgapdkvktvllCEAKEEAKKGFEVEKVKMQQEISELK 162
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-----------LEELEEAEEALLERLERLEEELEELE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 163 GAKKQVEEALTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLLDEKDARRFQLKIAELSAIIRKLEDRNALLS 242
Cdd:COG1196 428 EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFL 507
|
.
gi 1907184534 243 E 243
Cdd:COG1196 508 E 508
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
13-255 |
2.47e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 13 DKAETLAALQAANEELRAKLTDIQiELQQEKSKVSKVERE-KSQELKQVREHEQRKHAVLVTELKTklHEEKMKELQAVR 91
Cdd:COG4913 249 EQIELLEPIRELAERYAAARERLA-ELEYLRAALRLWFAQrRLELLEAELEELRAELARLEAELER--LEARLDALREEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 92 EALLRQheaellrvikIKDNENQRLQALLNTLRDgapdkvktvllceakeeakkgfevekvkMQQEISELKGAKKQVEEA 171
Cdd:COG4913 326 DELEAQ----------IRGNGGDRLEQLEREIER----------------------------LERELEERERRRARLEAL 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 172 LTMV---IQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLLDEKdaRRFQLKIAELSAIIRKLEDRNALLSEERNEL 248
Cdd:COG4913 368 LAALglpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL--RDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
....*..
gi 1907184534 249 LKRLREA 255
Cdd:COG4913 446 RDALAEA 452
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
11-328 |
2.60e-05 |
|
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: 46.66 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 11 KGDKAETLAALQAANEELRAKLTDIQiELQQEkskvSKVEREKSQELKQVREHEQRKHAVLvtelktKLHEEKMKEL--- 87
Cdd:pfam05557 110 KNELSELRRQIQRAELELQSTNSELE-ELQER----LDLLKAKASEAEQLRQNLEKQQSSL------AEAEQRIKELefe 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 88 ---QAVREALLRQHEAELLRVIKIkDNENQRLQALLNTLRDGAPDKVktvLLCEAKEEAKKGFEVEKvKMQQEISELKGA 164
Cdd:pfam05557 179 iqsQEQDSEIVKNSKSELARIPEL-EKELERLREHNKHLNENIENKL---LLKEEVEDLKRKLEREE-KYREEAATLELE 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 165 KKQVEEALTMVIQADKIKAAEIRS-------VYHLHQEEITRIK---------KECEREIRRLLDEKDARRFQL-----K 223
Cdd:pfam05557 254 KEKLEQELQSWVKLAQDTGLNLRSpedlsrrIEQLQQREIVLKEenssltssaRQLEKARRELEQELAQYLKKIedlnkK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 224 IAELSAIIRKLEDRNALLSEERNeLLKRLREAesqykplLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGI 303
Cdd:pfam05557 334 LKRHKALVRRLQRRVLLLTKERD-GYRAILES-------YDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSV 405
|
330 340
....*....|....*....|....*
gi 1907184534 304 IRRPSSLNDLDQSQDEREIDFLKLQ 328
Cdd:pfam05557 406 AEEELGGYKQQAQTLERELQALRQQ 430
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
25-341 |
2.70e-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: 46.55 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 25 NEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMKelqavrealLRQHEAELLR 104
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKK---------LEEIQNQISQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 105 VIKIKDNENQRLQALLNTLRDGAPDKVKtvllcEAKEEAKKGFEVEKVKMQ-----QEISELKGAKKQVEEALTMVIQAD 179
Cdd:TIGR04523 333 NNKIISQLNEQISQLKKELTNSESENSE-----KQRELEEKQNEIEKLKKEnqsykQEIKNLESQINDLESKIQNQEKLN 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 180 KIKAAEIRSV---YHLHQEEITRIKKECER---EIRRLLDEKDARR------------FQLKIAELSAIIRK----LEDR 237
Cdd:TIGR04523 408 QQKDEQIKKLqqeKELLEKEIERLKETIIKnnsEIKDLTNQDSVKEliiknldntresLETQLKVLSRSINKikqnLEQK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 238 NALLSEERNELLK---RLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQragiirrpsslnDLD 314
Cdd:TIGR04523 488 QKELKSKEKELKKlneEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF------------ELK 555
|
330 340
....*....|....*....|....*..
gi 1907184534 315 QSQDEREIDFLKLQIVEQQNLIDELSK 341
Cdd:TIGR04523 556 KENLEKEIDEKNKEIEELKQTQKSLKK 582
|
|
| PHA02682 |
PHA02682 |
ORF080 virion core protein; Provisional |
336-446 |
3.66e-05 |
|
ORF080 virion core protein; Provisional
Pssm-ID: 177464 [Multi-domain] Cd Length: 280 Bit Score: 45.24 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 336 IDELSKVSMQHFRAVLSCVRRSHAPCCPVPSGATP--PTALCPPePRPLLPcalrSHAPYCPVPsgattptALCPPEPRP 413
Cdd:PHA02682 47 VDPLDKYSVKEAGRYYQSRLKANSACMQRPSGQSPlaPSPACAA-PAPACP----ACAPAAPAP-------AVTCPAPAP 114
|
90 100 110
....*....|....*....|....*....|...
gi 1907184534 414 LLPCALrghAPCCPvhslklpsPDSLCPSRAVP 446
Cdd:PHA02682 115 ACPPAT---APTCP--------PPAVCPAPARP 136
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
35-293 |
4.08e-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: 46.17 E-value: 4.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 35 IQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAvLVTELK-----TKLHEEKMKELQAVREALLRQHEAELLRVIK-- 107
Cdd:TIGR04523 361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQIND-LESKIQnqeklNQQKDEQIKKLQQEKELLEKEIERLKETIIKnn 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 108 --IKDNENQRLQ-----ALLNTLRDGAPDKVKTVLLCEAKEEAK-KGFEVEKVKMQQEISELKGAKKQVEEALTMVIQad 179
Cdd:TIGR04523 440 seIKDLTNQDSVkeliiKNLDNTRESLETQLKVLSRSINKIKQNlEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK-- 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 180 kiKAAEIRSvyhlHQEEITRIKKECEREIRRLLDEKDARRFQLKIAELSAIIRKL--------EDRNALLSE-------- 243
Cdd:TIGR04523 518 --KISSLKE----KIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKnkeieelkQTQKSLKKKqeekqeli 591
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1907184534 244 -----ERNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQE 293
Cdd:TIGR04523 592 dqkekEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQE 646
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
14-296 |
4.36e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 14 KAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEReksqELKQVREHEQRkhavlVTELKTKLhEEKMKELQAVREa 93
Cdd:PRK03918 291 KAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEE----RIKELEEKEER-----LEELKKKL-KELEKRLEELEE- 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 94 llrqhEAELLRVIKIKDNENQRLQALLNTLrdgAPDKVKTVLlcEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALt 173
Cdd:PRK03918 360 -----RHELYEEAKAKKEELERLKKRLTGL---TPEKLEKEL--EELEKAKEEIEEEISKITARIGELKKEIKELKKAI- 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 174 mviqadkikaaeirsvyhlhqEEITRIKKECEReIRRLLDEKDARRFqlkIAELSAIIRKLEDRNALLSEERNELLKRLR 253
Cdd:PRK03918 429 ---------------------EELKKAKGKCPV-CGRELTEEHRKEL---LEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1907184534 254 EAESqykpLLDKNKRLtRKNEDLSHTLRRIESKLKFVTQENIE 296
Cdd:PRK03918 484 ELEK----VLKKESEL-IKLKELAEQLKELEEKLKKYNLEELE 521
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
39-339 |
7.93e-05 |
|
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: 45.11 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 39 LQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHE-EKMKELQAVREALLRqheAELLRVIKIKDNENQRLQ 117
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEaEKARQAEMDRQAAIY---AEQERMAMERERELERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 118 allntlRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEI------SELKGAKKQ--VEEALTMVIQADKIKAAEIRSV 189
Cdd:pfam17380 355 ------QEERKRELERIRQEEIAMEISRMRELERLQMERQQknervrQELEAARKVkiLEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 190 Y-HLHQEEITRIKKECEREIRRLLDEKDARRFQLKIAELSAIIRKL--------EDRNALLSEERNELLKRLREAESQyK 260
Cdd:pfam17380 429 QeEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRkklelekeKRDRKRAEEQRRKILEKELEERKQ-A 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 261 PLLDKNKR--LTRKNEDLSHTL----RRIESKLKFVTQENIEMRQR--AGIIRRPSSLNDLDQSQDEREidfLKLQIVEQ 332
Cdd:pfam17380 508 MIEEERKRklLEKEMEERQKAIyeeeRRREAEEERRKQQEMEERRRiqEQMRKATEERSRLEAMERERE---MMRQIVES 584
|
....*..
gi 1907184534 333 QNLIDEL 339
Cdd:pfam17380 585 EKARAEY 591
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
15-341 |
8.39e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.31 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 15 AETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMKELQAVREAL 94
Cdd:COG1196 420 EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 95 LRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVL-----------LCEAKEEAKKGFEVEK------------ 151
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALeaalaaalqniVVEDDEVAAAAIEYLKaakagratflpl 579
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 152 VKMQQEISELKGAKKQVEEALTMVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLL----DEKDARRFQLKIAEL 227
Cdd:COG1196 580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVtlagRLREVTLEGEGGSAG 659
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 228 SAIIRKLEDRNALLSEERNELLKRLREAESQYkpLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRRP 307
Cdd:COG1196 660 GSLTGGSRRELLAALLEAEAELEELAERLAEE--ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
330 340 350
....*....|....*....|....*....|....*..
gi 1907184534 308 SSLNDLDQSQDEREIDFLKLQIV---EQQNLIDELSK 341
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPdleELERELERLER 774
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
23-301 |
1.21e-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: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 23 AANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVrEHEQRKHAVLVTELKTKlhEEKMKELQAVREALLRQHEAEL 102
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGEL-EKASREETFARTALKNA--RLDLRRLFDEKQSEKDKKNKAL 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 103 LRVIKIKDNENQRLQALLNTLRDGAPDkvktvllceAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTmviqadkik 182
Cdd:pfam12128 674 AERKDSANERLNSLEAQLKQLDKKHQA---------WLEEQKEQKREARTEKQAYWQVVEGALDAQLALLK--------- 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 183 aAEIRSVYHLHQEEITRIKKECEREIRRL-LDEKDARRFQLKIAELSAIIRKLE-DRNALLSEERnellkRLREAESQYK 260
Cdd:pfam12128 736 -AAIAARRSGAKAELKALETWYKRDLASLgVDPDVIAKLKREIRTLERKIERIAvRRQEVLRYFD-----WYQETWLQRR 809
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1907184534 261 PLLDKNKRLT-RKNEDLSHTLRRIESKLKFVTQeNIEMRQRA 301
Cdd:pfam12128 810 PRLATQLSNIeRAISELQQQLARLIADTKLRRA-KLEMERKA 850
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
9-260 |
1.57e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.27 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 9 RAKGDKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQ--ELKQVREHEQRKHAVLVTELKTKLHEEKMKE 86
Cdd:TIGR00606 829 QEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQigTNLQRRQQFEEQLVELSTEVQSLIREIKDAK 908
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 87 LQAV-REALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKV---KTVL--LCEAKEEAKKGFEVEKVKMQQEISE 160
Cdd:TIGR00606 909 EQDSpLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymKDIEnkIQDGKDDYLKQKETELNTVNAQLEE 988
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 161 LKGAKKQVEEALTMVIQAdkIKAAEIRSvyHLHQEEITRIKKECE-REIRRLLDEKDARRFQLKIAELSAIIRKLEDRNA 239
Cdd:TIGR00606 989 CEKHQEKINEDMRLMRQD--IDTQKIQE--RWLQDNLTLRKRENElKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENID 1064
|
250 260
....*....|....*....|.
gi 1907184534 240 LLSEERNELLKRLREAESQYK 260
Cdd:TIGR00606 1065 LIKRNHVLALGRQKGYEKEIK 1085
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
21-294 |
3.88e-04 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 43.17 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 21 LQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVrEHEQRKHAVLVTELKTkLHEEKMKELQAVREALLRQHEA 100
Cdd:pfam05483 497 LLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQI-ENLEEKEMNLRDELES-VREEFIQKGDEVKCKLDKSEEN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 101 ELLRVIKIKDNENQR--LQALLNTLRDGAPDKVKTV--LLCEAKEEAKKG------FEVEKVKMQQEISELKGAKKQVEE 170
Cdd:pfam05483 575 ARSIEYEVLKKEKQMkiLENKCNNLKKQIENKNKNIeeLHQENKALKKKGsaenkqLNAYEIKVNKLELELASAKQKFEE 654
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 171 ALTMVIQADKIKAAEIRSVYhlhqEEITRIKKECEREIRrlLDEKDARRFQLKIAELSAIIRKLEDRNALLSEERNE--- 247
Cdd:pfam05483 655 IIDNYQKEIEDKKISEEKLL----EEVEKAKAIADEAVK--LQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSelg 728
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1907184534 248 LLKRLREAESQYKPLLD------KNKRLTRKNEdlSHTLRRIESKLKFVTQEN 294
Cdd:pfam05483 729 LYKNKEQEQSSAKAALEielsniKAELLSLKKQ--LEIEKEEKEKLKMEAKEN 779
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
26-341 |
4.62e-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: 42.70 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 26 EELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHavlvtELKTKLHEeKMKELQAVREALLRQHEaeLLRV 105
Cdd:TIGR04523 134 KENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELN-----LLEKEKLN-IQKNIDKIKNKLLKLEL--LLSN 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 106 IKIKDNENQRLQALLNTLRDGAPDKVKTV-LLCEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTMVIQADKI--- 181
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIeKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKike 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 182 KAAEIRSVyhlhQEEITRIKKECEREIRRLLD------EKDARRFQLKIAELSAIIRKLEDRNALLSEERN-------EL 248
Cdd:TIGR04523 286 LEKQLNQL----KSEISDLNNQKEQDWNKELKselknqEKKLEEIQNQISQNNKIISQLNEQISQLKKELTnsesensEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 249 LKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQRAGIIRrpsslndLDQSQDEREIDFLKLQ 328
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQ-------QEKELLEKEIERLKET 434
|
330
....*....|...
gi 1907184534 329 IVEQQNLIDELSK 341
Cdd:TIGR04523 435 IIKNNSEIKDLTN 447
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-321 |
5.54e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 3 KKGAGSRAKGDKAETLAALQAANE----ELRAKLTDIQIELQQEKSKVSKV---EREKSQELKQVREHEQRK-HAVLVTE 74
Cdd:PTZ00121 1335 KKKAEEAKKAAEAAKAEAEAAADEaeaaEEKAEAAEKKKEEAKKKADAAKKkaeEKKKADEAKKKAEEDKKKaDELKKAA 1414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 75 LKTKLHEEKMKELQAVREALLRQHEAELLRV---IKIKDNENQRLQallnTLRDGAPDKVKTVLLCEAKEEAKKGFEVEK 151
Cdd:PTZ00121 1415 AAKKKADEAKKKAEEKKKADEAKKKAEEAKKadeAKKKAEEAKKAE----EAKKKAEEAKKADEAKKKAEEAKKADEAKK 1490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 152 -----VKMQQEISELKGAKKQVEEALTmviQADKIKAAEIRSVYHLHQEEITRIKKECER--EIRRLLDEKDARrfQLKI 224
Cdd:PTZ00121 1491 kaeeaKKKADEAKKAAEAKKKADEAKK---AEEAKKADEAKKAEEAKKADEAKKAEEKKKadELKKAEELKKAE--EKKK 1565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 225 AELSAiiRKLEDRNALL---SEERNELLKRLREAESQYKPLLDKNKRLTRKNEDL---SHTLRRIESKLKFVTQ---ENI 295
Cdd:PTZ00121 1566 AEEAK--KAEEDKNMALrkaEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikAEELKKAEEEKKKVEQlkkKEA 1643
|
330 340
....*....|....*....|....*.
gi 1907184534 296 EMRQRAGIIRRPSSLNDLDQSQDERE 321
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEEAKK 1669
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
3-349 |
6.81e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 3 KKGAGSRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEE 82
Cdd:PTZ00121 1290 KKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 83 KMKELQAVREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEkvKMQQEISELK 162
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAK--KKAEEAKKAD 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 163 GAKKQVEEALTMviQADKIKAAEIRSVYHLhqeeitriKKECEREIRRLLDEKDARRFQLKIAELSAIIRKLEDRNALLS 242
Cdd:PTZ00121 1448 EAKKKAEEAKKA--EEAKKKAEEAKKADEA--------KKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 243 EERNELLKRLREAESQYKPLLDKNKRLTRKNEDL--SHTLRRIESKLKfVTQENIEMRQRAGIIRRPSslnDLDQSQDER 320
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKADELkkAEELKKAEEKKK-AEEAKKAEEDKNMALRKAE---EAKKAEEAR 1593
|
330 340
....*....|....*....|....*....
gi 1907184534 321 EIDFLKLQIVEQQNLIDELSKVSMQHFRA 349
Cdd:PTZ00121 1594 IEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
22-185 |
9.01e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 41.33 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 22 QAANEELRAKLTDIQIELQQEKsKVSKVEREKSQELKQVREHEQRKHAVlvtelktklheekmkelQAVREALLRQHEAE 101
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQK-QAAEQERLKQLEKERLAAQEQKKQAE-----------------EAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 102 llrvikikdnENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVEKVKMQQEiselkGAKKQVEEALTMVIQADKI 181
Cdd:PRK09510 136 ----------EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAA-----EAKKKAEAEAAAKAAAEAK 200
|
....
gi 1907184534 182 KAAE 185
Cdd:PRK09510 201 KKAE 204
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
348-463 |
9.30e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 41.85 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 348 RAVLSCVRRSHAPCCPVPSGATPPTALCPPEPRPLLPCALRSHAPYCP-------VPSGATTPTALCPPEPRPLLPCALR 420
Cdd:PHA03247 2689 RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPaapappaVPAGPATPGGPARPARPPTTAGPPA 2768
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1907184534 421 GHAPCCPVHSlklpspdslcPSRAVPLLTAHSLLPYLLSTPHP 463
Cdd:PHA03247 2769 PAPPAAPAAG----------PPRRLTRPAVASLSESRESLPSP 2801
|
|
| FapA |
pfam03961 |
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta ... |
81-183 |
1.01e-03 |
|
Flagellar Assembly Protein A beta solenoid domain; This entry represents the C-terminal beta solenoid domain of FapA and its homologs. Members of this family include FapA (flagellar assembly protein A) found in Vibrio vulnificus. The synthesis of flagella allows bacteria to respond to chemotaxis by facilitating motility. Studies examining the role of FapA show that the loss or delocalization of FapA results in a complete failure of the flagellar biosynthesis and motility in response to glucose mediated chemotaxis. The polar localization of FapA is required for flagellar synthesis, and dephosphorylated EIIAGlc (Glucose-permease IIA component) inhibited the polar localization of FapA through direct interaction. This entry shows similarity to pfam03775 suggesting a similar functional role.
Pssm-ID: 461111 [Multi-domain] Cd Length: 272 Bit Score: 40.75 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 81 EEKMKELQAVREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKtvllCEAKEEAKKgFEVEKVKMQQEISE 160
Cdd:pfam03961 140 GTKTEIEVGVDFPELKEKLEELEKELEELEEELEKLKKRLKKLPKKARGQLP----PEKREQLEK-LLETKNKLSEELEE 214
|
90 100
....*....|....*....|...
gi 1907184534 161 LKGAKKQVEEALTMVIQADKIKA 183
Cdd:pfam03961 215 LEEELKELKEELESLLGEGKISV 237
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
154-288 |
1.34e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 154 MQQEISELKGAKKQVEEAltmviqADKIKA-AEIRSVYHLHQEEITRIkKECEREIRRLLDEKDARRFQL---KIAELSA 229
Cdd:COG4913 230 LVEHFDDLERAHEALEDA------REQIELlEPIRELAERYAAARERL-AELEYLRAALRLWFAQRRLELleaELEELRA 302
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 230 IIRKLEDRNALLSEERNELLKRLREAESQYKPL-LDKNKRLTRKNEDLSHTLRRIESKLK 288
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRA 362
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
21-265 |
1.38e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.16 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 21 LQAANEELRAKLTDIQIELQQEKSKVSKVEreksQELKQVREheqrKHAVLVTELKTKLHEEKMKELQAVREALLRQHEA 100
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAE----AALEEFRQ----KNGLVDLSEEAKLLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 101 ELLRVikikdnenQRLQALLNTLRDGAPDKVKTVLLceakeeakkgfevekVKMQQEISELKGAKKQVEEALTmvIQADK 180
Cdd:COG3206 238 AEARL--------AALRAQLGSGPDALPELLQSPVI---------------QQLRAQLAELEAELAELSARYT--PNHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 181 IKAAeirsvyhlhQEEITRIKKECEREIRRLLDEKDARRFQLK--IAELSAIIRKLEDRNALLSEERNELLKRLREAE-- 256
Cdd:COG3206 293 VIAL---------RAQIAALRAQLQQEAQRILASLEAELEALQarEASLQAQLAQLEARLAELPELEAELRRLEREVEva 363
|
250
....*....|
gi 1907184534 257 -SQYKPLLDK 265
Cdd:COG3206 364 rELYESLLQR 373
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
146-283 |
1.39e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.92 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 146 GFEVEKVKMQQEISELKG-AKKQVEEAltmVIQADKIKAAEIRSVyhlhQEEITRIKKECEREIRRlldekdaRRFQLKI 224
Cdd:PRK12704 21 GYFVRKKIAEAKIKEAEEeAKRILEEA---KKEAEAIKKEALLEA----KEEIHKLRNEFEKELRE-------RRNELQK 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907184534 225 AELSAIIRK--LEDRNALLSEERNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRI 283
Cdd:PRK12704 87 LEKRLLQKEenLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERI 147
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
143-288 |
1.60e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.00 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 143 AKKGFEVEKVKmqqeISELKGakKQVEEALTMVIQADKIKAAEIRSVYHLHQE-EITRIKKEC---EREIRRLLDEKdaR 218
Cdd:COG2433 359 VPPDVDRDEVK----ARVIRG--LSIEEALEELIEKELPEEEPEAEREKEHEErELTEEEEEIrrlEEQVERLEAEV--E 430
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907184534 219 RFQLKIAELSAIIRKLEDRNALLSEERNELLKRLREAESqykplLDK-NKRLTRKNEDLSHTLRRIESKLK 288
Cdd:COG2433 431 ELEAELEEKDERIERLERELSEARSEERREIRKDREISR-----LDReIERLERELEEERERIEELKRKLE 496
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1-260 |
2.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 1 MSKKGAGSRAKGDKAETLAAL------QAANEELRAKLTDIQIELQQEKSKVSKVEREKsQELKQVREHEQRKHAVLVTE 74
Cdd:COG4913 582 QVKGNGTRHEKDDRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQRLAEYSWDE 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 75 LKTKLHEEKMKELQAVREALlrqheaellrvikikDNENQRLQALlntlrdgapdkvktvllceakEEAKKGFEVEKVKM 154
Cdd:COG4913 661 IDVASAEREIAELEAELERL---------------DASSDDLAAL---------------------EEQLEELEAELEEL 704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 155 QQEISELKGAKKQVEEALtmviqadkikaAEIRSVYHLHQEEITRIKKECEREIRRLLDEkdaRRFQLKIAELSAIIRK- 233
Cdd:COG4913 705 EEELDELKGEIGRLEKEL-----------EQAEEELDELQDRLEAAEDLARLELRALLEE---RFAAALGDAVERELREn 770
|
250 260
....*....|....*....|....*..
gi 1907184534 234 LEDRNALLSEERNELLKRLREAESQYK 260
Cdd:COG4913 771 LEERIDALRARLNRAEEELERAMRAFN 797
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
57-292 |
2.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 57 LKQVREHEQRKHAVLVTELKTKLHEEKMKELQA---VREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKT 133
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAalgLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 134 VLLCEAKEEAKKGFEvEKVKMQQEISELKGAKKQVEEALT-----MVIQADKIKAAEIRSVYHLHQEEItrikKECEREI 208
Cdd:COG4717 374 ALLAEAGVEDEEELR-AALEQAEEYQELKEELEELEEQLEellgeLEELLEALDEEELEEELEELEEEL----EELEEEL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 209 RRLLDEkdarrfqlkIAELSAIIRKLEDRNAL--LSEERNELLKRLREAESQY------KPLLDKNKRLTRKnEDLSHTL 280
Cdd:COG4717 449 EELREE---------LAELEAELEQLEEDGELaeLLQELEELKAELRELAEEWaalklaLELLEEAREEYRE-ERLPPVL 518
|
250
....*....|..
gi 1907184534 281 RRIESKLKFVTQ 292
Cdd:COG4717 519 ERASEYFSRLTD 530
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
11-162 |
2.49e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 39.87 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 11 KGDKAETLAALQAANEELRAKLtdiqieLQQEKskvsKVEREKSQELKQVREHEQRkhavlvtelktkLHEEKMKELQAV 90
Cdd:cd16269 188 QADQALTEKEKEIEAERAKAEA------AEQER----KLLEEQQRELEQKLEDQER------------SYEEHLRQLKEK 245
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907184534 91 REALLRQHEAELLRVIKIKDNENQRLQallntlrdgapdkvktvllceakeeaKKGFEVEKVKMQQEISELK 162
Cdd:cd16269 246 MEEERENLLKEQERALESKLKEQEALL--------------------------EEGFKEQAELLQEEIRSLK 291
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
8-177 |
2.50e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 8 SRAKGDKAETLAA--LQAANEELRAKLTDIQIELQQE----KSKVSKVEREKSQELKQVREHEQRKHAVLvtELKTKLHE 81
Cdd:PRK12704 29 AEAKIKEAEEEAKriLEEAKKEAEAIKKEALLEAKEEihklRNEFEKELRERRNELQKLEKRLLQKEENL--DRKLELLE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 82 EKMKELQAVREALLRQHE-AELLR--VIKIKDNENQRLQALLNTLRDGApdkvKTVLLCEAKEEAKKgfevEKVKMQQEI 158
Cdd:PRK12704 107 KREEELEKKEKELEQKQQeLEKKEeeLEELIEEQLQELERISGLTAEEA----KEILLEKVEEEARH----EAAVLIKEI 178
|
170 180
....*....|....*....|.
gi 1907184534 159 SEL--KGAKKQVEEALTMVIQ 177
Cdd:PRK12704 179 EEEakEEADKKAKEILAQAIQ 199
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
13-288 |
3.76e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 13 DKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEREK--SQELKQVREHEQRK------HAVLVTELKTKLHEEKM 84
Cdd:COG4717 196 DLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELeaAALEERLKEARLLLliaaalLALLGLGGSLLSLILTI 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 85 KELQAVREALL--------------RQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEVE 150
Cdd:COG4717 276 AGVLFLVLGLLallflllarekaslGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 151 KVKMQQEIsELKGAKKQVEEALTMViQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLLDEKDARRFQLKIAELSAI 230
Cdd:COG4717 356 AEELEEEL-QLEELEQEIAALLAEA-GVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEE 433
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1907184534 231 IRKLEDRNALLSEERNELLKRLREAESQYKpLLDKNKRLTRKNEDLSHTLRRIESKLK 288
Cdd:COG4717 434 LEELEEELEELEEELEELREELAELEAELE-QLEEDGELAELLQELEELKAELRELAE 490
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
138-272 |
3.83e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 38.75 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 138 EAKEEAKKGFEVEKVKMQQEISELKGAKKQVEEALTMV---IQADKIKAAEIRSV--YHLHQEEITRIKKE---CEREIR 209
Cdd:COG1579 34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVearIKKYEEQLGNVRNNkeYEALQKEIESLKRRisdLEDEIL 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907184534 210 RLLDEKDARRfqlkiAELSAIIRKLEDRNALLSEERNELLKRLREAESQYKPLLDKNKRLTRK 272
Cdd:COG1579 114 ELMERIEELE-----EELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
13-217 |
4.29e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.43 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 13 DKAETLAALQAANEELRAKLTDIQIELQQEKSKVSKVEreksQELKQVREHEQrkhavlvtELKTKLhEEKMKELQAVRE 92
Cdd:COG3883 20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQ----AELEALQAEID--------KLQAEI-AEAEAEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 93 ALlrqheAELLRVIKIKDNENQRLQALL---------------NTLRDGAPDKVKTVL-LCEAKEEAKKGFEVEKVKMQQ 156
Cdd:COG3883 87 EL-----GERARALYRSGGSVSYLDVLLgsesfsdfldrlsalSKIADADADLLEELKaDKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907184534 157 EISELKGAKKQVEEALTmVIQADKIKAAEIRSVYHLHQEEITRIKKECEREIRRLLDEKDA 217
Cdd:COG3883 162 LKAELEAAKAELEAQQA-EQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
141-342 |
4.64e-03 |
|
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: 39.67 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 141 EEAKKGFEVEKVKMQQEISELKGAKKQVEEALTMviQADKIKAAEIRSVYHLHQEEITRI-KKECEREIRRLLDEKDARR 219
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKAERY--QALLKEKREYEGYELLKEKEALERqKEAIERQLASLEEELEKLT 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 220 FQL--KIAELSAIIRKLEDRNA----LLSEERNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLKFV--T 291
Cdd:TIGR02169 258 EEIseLEKRLEEIEQLLEELNKkikdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLlaE 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1907184534 292 QENIEMRQRAGIIRRPSSLNDLDQSQDEREIDFLKLQIVEQQN--LIDELSKV 342
Cdd:TIGR02169 338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFaeTRDELKDY 390
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
84-300 |
5.72e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 84 MKELQAVREALLRQHE-AELLRVIKIKDNENQRLQALLNTLRDgapdkVKTVLLCEAKEEAKKGFEVEKVKMQQEISELK 162
Cdd:COG4913 234 FDDLERAHEALEDAREqIELLEPIRELAERYAAARERLAELEY-----LRAALRLWFAQRRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 163 GAKKQVEEALTmviQADkikaAEIRSVYHLHQEEITRIKKECEREIRRLLDEKDAR-----RFQLKIA-----------E 226
Cdd:COG4913 309 AELERLEARLD---ALR----EELDELEAQIRGNGGDRLEQLEREIERLERELEERerrraRLEALLAalglplpasaeE 381
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907184534 227 LSAIIRKLEDRNALLSEERNELLKRLREAESQYkplldknKRLTRKNEDLSHTLRRIESKLKFVTQENIEMRQR 300
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAAL-------RDLRRELRELEAEIASLERRKSNIPARLLALRDA 448
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
26-288 |
6.08e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 39.12 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 26 EELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVRE--HEQRKHAVLVT----ELKTKLHEEKMKELQAVREalLRQHE 99
Cdd:pfam15964 399 EELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEaqKQLASQEMDVTkvcgEMRYQLNQTKMKKDEAEKE--HREYR 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 100 AELLRVIKIKDNENQRL--------QALLNTLRDGAPDKVKTVLLCEAKEEAKKGFEV---EKVKMQQEISELKGAK--- 165
Cdd:pfam15964 477 TKTGRQLEIKDQEIEKLglelseskQRLEQAQQDAARAREECLKLTELLGESEHQLHLtrlEKESIQQSFSNEAKAQalq 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 166 -KQVEEALT-----MVIQADKiKAAEIRSVYHLHQEEITRIKKECEREIRRLldEKDARRFQLKIAELSAIIR------- 232
Cdd:pfam15964 557 aQQREQELTqkmqqMEAQHDK-TVNEQYSLLTSQNTFIAKLKEECCTLAKKL--EEITQKSRSEVEQLSQEKEylqdrle 633
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 233 KLEDRNALLSEE--------------RNELLKRLREAESQYKPLLDKNKRLTRKNEDLSHTLRRIESKLK 288
Cdd:pfam15964 634 KLQKRNEELEEQcvqhgrmhermkqrLRQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQVP 703
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
24-276 |
6.15e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.35 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 24 ANEELRAKLTDIQIELQQEKSKVSKVEREKSQELKQVRE-----HEQRKHAVLVTELKTKLHEEKMKELQAVREALLRQH 98
Cdd:PTZ00121 1220 AEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEearmaHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAE 1299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 99 EAELLRVIKIKDNENQRLQALLNTLRDGapdKVKTVLLCEAKEEAKKGFEVEKVKMQQEISELKGAKKQVEealtmviqA 178
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEA---KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAE--------A 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 179 DKIKAAEIRSVYHLHQEEITRIKKECEREIRRLLDEKDARRFQLKIAElsaiiRKLEDRNALLSEERNELLKRLREAESQ 258
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAA-----KKKADEAKKKAEEKKKADEAKKKAEEA 1443
|
250
....*....|....*....
gi 1907184534 259 YKP-LLDKNKRLTRKNEDL 276
Cdd:PTZ00121 1444 KKAdEAKKKAEEAKKAEEA 1462
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
16-341 |
6.20e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 16 ETLAALQAANEELRAKLT--DIQIELQQEKSKVSKVEREKSQELKQVREHEQRKHAVLVTELKTKLHEEKMKELQAVREA 93
Cdd:COG4717 102 EELEELEAELEELREELEklEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 94 LLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVllcEAKEEAKKGFEVEKV--KMQQEISELK--------- 162
Cdd:COG4717 182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEEL---EELEEELEQLENELEaaALEERLKEARlllliaaal 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 163 -----------GAKKQVEEALTMVI-----------------QADKIKAAEIRSVYHLHQEEITRIKKECE--------- 205
Cdd:COG4717 259 lallglggsllSLILTIAGVLFLVLgllallflllarekaslGKEAEELQALPALEELEEEELEELLAALGlppdlspee 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 206 --------REIRRLLDEKDARRFQLKIAELSAIIRKL------EDRNALLS-----EERNELLKRLREAESQYKPLLDKN 266
Cdd:COG4717 339 llelldriEELQELLREAEELEEELQLEELEQEIAALlaeagvEDEEELRAaleqaEEYQELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907184534 267 KRLTRKN--EDLSHTLRRIESKLKFVTQENIEMRQRAGIIRrpsslNDLDQSQDEREIDFLKLQIVEQQNLIDELSK 341
Cdd:COG4717 419 EELLEALdeEELEEELEELEEELEELEEELEELREELAELE-----AELEQLEEDGELAELLQELEELKAELRELAE 490
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
8-171 |
7.20e-03 |
|
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: 38.88 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 8 SRAKGDKAETLAALQAANEELRAKLTDIQIELQQEKskvskVEREKSQELKQVREHEQRKhavLVTELKTklHEEKMKEL 87
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALL-----NERASLEEALALLRSELEE---LSEELRE--LESKRSEL 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 88 QAVREALLRQHEAELLRVIKIKDNENQRLQALLNTLRDGAPDKVKTVLLCEAKEEAKKGF-------------------- 147
Cdd:TIGR02168 914 RRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRlkrlenkikelgpvnlaaie 993
|
170 180
....*....|....*....|....*....
gi 1907184534 148 EVEKVK-----MQQEISELKGAKKQVEEA 171
Cdd:TIGR02168 994 EYEELKerydfLTAQKEDLTEAKETLEEA 1022
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
355-461 |
9.36e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 38.77 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907184534 355 RRSHAPCCPvPSGATPPTALCPPEPRPLLPCALRSHAPYCPVPSGATTPTALCPPEPRPLLPCALRGHAPCCPVHSLKLP 434
Cdd:PHA03247 2665 RRARRLGRA-AQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPA 2743
|
90 100
....*....|....*....|....*..
gi 1907184534 435 SPDslcpSRAVPLLTAHSLLPYLLSTP 461
Cdd:PHA03247 2744 VPA----GPATPGGPARPARPPTTAGP 2766
|
|
| |
