|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
341-588 |
6.89e-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: 56.22 E-value: 6.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 341 EFEQKLASTEKEVLQLNEflkQRLSLFSEEKKKLEEKLKTRDRyISSLKKKCQKESEQNKEKQRRIETLEKYL----ADL 416
Cdd:TIGR02168 236 ELREELEELQEELKEAEE---ELEELTAELQELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKqilrERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 417 PTLDDVQSQ-SLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcLEDGIRL 495
Cdd:TIGR02168 312 ANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET-LRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 496 PMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMM-----EELEKKERNVQRLTKAL 570
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqEELERLEEALEELREEL 470
|
250
....*....|....*...
gi 767942809 571 LENQRQTDETCSLLDQGQ 588
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQ 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
398-596 |
8.58e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 8.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 398 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTT 477
Cdd:COG1196 219 KEELKELEAELLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 478 VQSLQQKVERCLEDGIRLPmLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELE 557
Cdd:COG1196 297 LARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190
....*....|....*....|....*....|....*....
gi 767942809 558 KKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSRQQ 596
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
341-561 |
8.54e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 8.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 341 EFEQKLASTEKEVLQLNEfLKQRLSlfseekkKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLD 420
Cdd:PRK03918 218 ELREELEKLEKEVKELEE-LKEEIE-------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 421 DVQSQSLQL-----QILEEKNkNLQEALIDTEKKLEEIKKQCQDKETqlicQKKKEKELVTTVQSLQQKVERcLEDGIRL 495
Cdd:PRK03918 290 EKAEEYIKLsefyeEYLDELR-EIEKRLSRLEEEINGIEERIKELEE----KEERLEELKKKLKELEKRLEE-LEERHEL 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767942809 496 pMLDAKQLQNENDNLRQQ--NETASKI------IDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKER 561
Cdd:PRK03918 364 -YEEAKAKKEELERLKKRltGLTPEKLekeleeLEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
338-604 |
9.28e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.16 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 338 QQGEFEQKLASTEKEVLQLN---EFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLA 414
Cdd:COG1196 247 ELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 415 DLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEikkqcqdketqlicQKKKEKELVTTVQSLQQKVERCLEDGIR 494
Cdd:COG1196 327 EL--EEELEELEEELEELEEELEEAEEELEEAEAELAE--------------AEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 495 LpMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQ 574
Cdd:COG1196 391 A-LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270
....*....|....*....|....*....|
gi 767942809 575 RQTDETCSLLDQGQEPDQSRQQTVLSKRPL 604
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
398-596 |
1.09e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 398 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLicqKKKEKELVTT 477
Cdd:COG3883 17 QIQAKQKELSELQAELEAA--QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 478 VQSLQQkvercleDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDrmilEIQSMQGKLSKEKLTTQKMMEELE 557
Cdd:COG3883 92 ARALYR-------SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELE 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 767942809 558 KKERNVQRLTKALlenQRQTDETCSLLDQGQEPDQSRQQ 596
Cdd:COG3883 161 ALKAELEAAKAEL---EAQQAEQEALLAQLSAEEAAAEA 196
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
341-579 |
1.62e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 341 EFEQKLASTEKEV---LQLNEFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLp 417
Cdd:TIGR02168 688 ELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL- 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 418 tLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEdgirlpm 497
Cdd:TIGR02168 767 -EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER------- 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 498 lDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQT 577
Cdd:TIGR02168 839 -RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
..
gi 767942809 578 DE 579
Cdd:TIGR02168 918 EE 919
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
440-602 |
1.80e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.45 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 440 QEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcLEDGIRLPMLDAKQLQNENDNLRQQNETASK 519
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 520 IIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKA---LLENQRQTDETCSLLDQGQEPDQSRQQ 596
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERAELE 177
|
....*.
gi 767942809 597 TVLSKR 602
Cdd:COG4942 178 ALLAEL 183
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
253-563 |
2.79e-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: 44.29 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 253 QDFSKWESMLKIKEGLLRQKEIVIDRQKQQITHLHERIRDNELRAqHAMLGHYVNCEDSYVASLQPQYENtslQTPFSEE 332
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL-HKLEEALNDLEARLSHSRIPEIQA---ELSKLEE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 333 SVShsqqgEFEQKLASTEKE---VLQLNEFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETL 409
Cdd:TIGR02169 806 EVS-----RIEARLREIEQKlnrLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 410 EKYLADlptlddvqsqslqlqiLEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCL 489
Cdd:TIGR02169 881 ESRLGD----------------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767942809 490 EDGIRLPMLD--AKQLQNENDNLRQQNETASKIIDSQQDEIDRMiLEIQSMQGKLSKEKLTTQKMMEELEKKERNV 563
Cdd:TIGR02169 945 EIPEEELSLEdvQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
385-579 |
3.04e-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: 44.24 E-value: 3.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 385 ISSLKKKCQKESEQNKEKQRRIETLEKYLADLptldDVQSQSLQLQILEEKN--KNLQEALIDTEKKLEEIKKQCQDKET 462
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELL----EKEIERLKETIIKNNSeiKDLTNQDSVKELIIKNLDNTRESLET 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 463 QLicqKKKEKELVTTVQSLQQKVERCLEDGIRLPMLDA--KQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQG 540
Cdd:TIGR04523 469 QL---KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEekKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767942809 541 KLSKEK--LTTQKMMEELEKKERNVQRL---TKALLENQRQTDE 579
Cdd:TIGR04523 546 ELNKDDfeLKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQE 589
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
414-602 |
7.90e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 414 ADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcledgi 493
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 494 rlpmldakqlqnenDNLRQQNETASKIIDSQQDEIDRMILEIQsmqgKLSKEKLttqKMMEELEKKERNVQRLTKALLEN 573
Cdd:COG1579 78 --------------YEEQLGNVRNNKEYEALQKEIESLKRRIS----DLEDEIL---ELMERIEELEEELAELEAELAEL 136
|
170 180
....*....|....*....|....*....
gi 767942809 574 QRQTDETCSLLDQGQEPDQSRQQTVLSKR 602
Cdd:COG1579 137 EAELEEKKAELDEELAELEAELEELEAER 165
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
337-699 |
1.04e-03 |
|
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: 42.65 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 337 SQQGEFEQKLASTEKEVLQLNEFLKqRLSLFSEEKKKLEEKLKTRDRYIS------SLKKKCQKESEQNKEKQR---RIE 407
Cdd:pfam02463 139 VQGGKIEIIAMMKPERRLEIEEEAA-GSRLKRKKKEALKKLIEETENLAEliidleELKLQELKLKEQAKKALEyyqLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 408 TLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEaLIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVER 487
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE-EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 488 CLEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLT 567
Cdd:pfam02463 297 ELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 568 KALLENQRQTDETCSLLDQGQEPDQSRQQTVLSKRPLFDLTVIDQLFKEMSCCLFDLKALCSILNQRAQGKE--PNLSLL 645
Cdd:pfam02463 377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEekEELEKQ 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 767942809 646 LGIRSMNCSAEETENDHSTETLTKKLSDVCQLRRDIDELRT-TISDRYAQDMGDN 699
Cdd:pfam02463 457 ELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEErSQKESKARSGLKV 511
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
385-580 |
1.10e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 385 ISSLKKKCQKESEQNKEKQRRIETLEKYLADlptlddvqsqslqlqiLEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL 464
Cdd:TIGR04523 126 LNKLEKQKKENKKNIDKFLTEIKKKEKELEK----------------LNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 465 ICQKKKEKELVTTVQSLQQKVERcledgirlpmldAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSK 544
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQK------------NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
170 180 190
....*....|....*....|....*....|....*...
gi 767942809 545 EKLTTQKMMEELEKKERNVQRLTKAL--LENQRQTDET 580
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIkeLEKQLNQLKS 295
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
262-570 |
1.19e-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: 42.35 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 262 LKIKEGLLRQKEIVIDRQKQQITHLHERIRD-----NELRAQHAMLGHYVNCEDSYVASLQPQYENTS--LQTPFSEESV 334
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQlrkelEELSRQISALRKDLARLEAEVEQLEERIAQLSkeLTELEAEIEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 335 SHSQQGEFEQKLASTEKEVLQLNEFLKQ---RLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEK 411
Cdd:TIGR02168 766 LEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 412 YLADLptlddvqsqSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVercled 491
Cdd:TIGR02168 846 QIEEL---------SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR------ 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 492 girlpmldaKQLQNENDNLRQQNETAskiidsqQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKK--------ERNV 563
Cdd:TIGR02168 911 ---------SELRRELEELREKLAQL-------ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKieddeeeaRRRL 974
|
....*..
gi 767942809 564 QRLTKAL 570
Cdd:TIGR02168 975 KRLENKI 981
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
368-594 |
1.41e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 368 SEEKKKLeeklktrdryisslKKKCQKESEQNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTE 447
Cdd:COG4942 19 ADAAAEA--------------EAELEQLQQEIAELEKELAALKKEEKAL--LKQLAALERRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 448 KKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQ--------KVERCLEDGIRLPMLDA--KQLQNENDNLRQQNETA 517
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllSPEDFLDAVRRLQYLKYlaPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 518 SKI---IDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSR 594
Cdd:COG4942 163 AALraeLEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
382-548 |
1.62e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 382 DRYISSLKKKCQKESEQnKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKE 461
Cdd:COG4717 88 EEYAELQEELEELEEEL-EELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 462 TQLICQKKKEKELVTTVQSLQQKVERCLEDGIRlpmlDAKQLQNENDNLRQQNETASKIIDSQQDEIDRM--ILEIQSMQ 539
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAE----ELEELQQRLAELEEELEEAQEELEELEEELEQLenELEAAALE 242
|
....*....
gi 767942809 540 GKLSKEKLT 548
Cdd:COG4717 243 ERLKEARLL 251
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
262-578 |
1.65e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 262 LKIKEGLLRQKEIviDRQKQQITHLHERIRDNELRAQHAMLGhyvncedsyVASLQPQYENTSLQtpFSEESVSHSQQGE 341
Cdd:COG1196 222 LKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAE---------LAELEAELEELRLE--LEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 342 FEQKLASTEKEVLQLNEFLKQRLSLFSEEKKKLEEKlktrdryISSLKKKCQKESEQNKEKQRRIETLEKYLADLptldd 421
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAEEELEEA----- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 422 vqsqSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEDGIRLpmldAK 501
Cdd:COG1196 357 ----EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL----EE 428
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767942809 502 QLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLtKALLENQRQTD 578
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYE 504
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
341-572 |
2.96e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 341 EFEQKLASTEKEVLQLNEFLKqRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKES-EQNKEKQRRIETLEKYLADLPTL 419
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLEL 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 420 DDVQSqslQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLicqkkKEKELVTTVQSLQQKVERCLEDGIRLPMLD 499
Cdd:PRK03918 608 KDAEK---ELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL-----EELEKKYSEEEYEELREEYLELSRELAGLR 679
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767942809 500 AKQLQNEndNLRQQNETASKIIDSQQDEIDRMILEIQSMqgklskeklttQKMMEELEKKERNVQRLtKALLE 572
Cdd:PRK03918 680 AELEELE--KRREEIKKTLEKLKEELEEREKAKKELEKL-----------EKALERVEELREKVKKY-KALLK 738
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
385-596 |
2.98e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.77 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 385 ISSLKKKCQKeseqNKEKQRRIETLEKYLADLPtlDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL 464
Cdd:TIGR04523 203 LSNLKKKIQK----NKSLESQISELKKQNNQLK--DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 465 ICQKKKEKELVTTVQSLQQKVERC---LEDGIrlpmldAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGK 541
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLnnqKEQDW------NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767942809 542 LSKEKLTTQKMMEELEKKERNVQRLTKallENQRQTDETCSLLDQGQEPDQSRQQ 596
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKK---ENQSYKQEIKNLESQINDLESKIQN 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
383-576 |
3.82e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.43 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 383 RYISSLKKKCQKESEQNKEKQRRIETLEKyladlpTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKEt 462
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEE------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 463 qlicqkKKEKELvttvQSLQQKVERCLEDGirlpmldaKQLQNENDNLRQQNETASKIiDSQQDEIDRMILEIQSMQ--- 539
Cdd:PRK03918 280 ------EKVKEL----KELKEKAEEYIKLS--------EFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEerl 340
|
170 180 190
....*....|....*....|....*....|....*..
gi 767942809 540 GKLSKEKLTTQKMMEELEKKERNVQRLtKALLENQRQ 576
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEA-KAKKEELER 376
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
385-487 |
4.56e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 39.14 E-value: 4.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 385 ISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL 464
Cdd:COG1579 54 LEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL 133
|
90 100
....*....|....*....|...
gi 767942809 465 icqKKKEKELVTTVQSLQQKVER 487
Cdd:COG1579 134 ---AELEAELEEKKAELDEELAE 153
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
427-579 |
6.72e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 39.81 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 427 LQLQILEEKNKNLQEaliDTEKkLEEIKKQCQDKETQlicQKKKEKELvttvQSLQQKVERCLEDGIRLpmldAKQLQNE 506
Cdd:PRK00409 499 LPENIIEEAKKLIGE---DKEK-LNELIASLEELERE---LEQKAEEA----EALLKEAEKLKEELEEK----KEKLQEE 563
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767942809 507 NDNLRQ-QNETASKIIDSQQDEIDRMILEIQSMQgKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDE 579
Cdd:PRK00409 564 EDKLLEeAEKEAQQAIKEAKKEADEIIKELRQLQ-KGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
414-602 |
6.83e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 39.89 E-value: 6.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 414 ADLPTLDDVQSQSLQLQ---ILEEKNKNLQEALIDT----------EKKLEEIKKQCQDKETQLicqKKKEKELVTTVQS 480
Cdd:PRK11281 33 GDLPTEADVQAQLDALNkqkLLEAEDKLVQQDLEQTlalldkidrqKEETEQLKQQLAQAPAKL---RQAQAELEALKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 481 LQQKVERCLEDgIRLPMLDAK------QLQNENDNLrqqNETASKIIDSQ------QDEIDRMILEIQSMQ-----GKLS 543
Cdd:PRK11281 110 NDEETRETLST-LSLRQLESRlaqtldQLQNAQNDL---AEYNSQLVSLQtqperaQAALYANSQRLQQIRnllkgGKVG 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767942809 544 KEKLT-TQKMMEELEKKERNVQ-RLTKALLEN--------QRQTDETCSLLDQGQEPDQSRQQTVLSKR 602
Cdd:PRK11281 186 GKALRpSQRVLLQAEQALLNAQnDLQRKSLEGntqlqdllQKQRDYLTARIQRLEHQLQLLQEAINSKR 254
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
386-594 |
9.13e-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: 39.34 E-value: 9.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 386 SSLKKKCQKESEQNKEKQRRIETLEKYLADlptlddvQSQSLQLQIleEKNKNLQEALIDTEKKLEEIKKQCQDKETQLI 465
Cdd:pfam05557 37 SALKRQLDRESDRNQELQKRIRLLEKREAE-------AEEALREQA--ELNRLKKKYLEALNKKLNEKESQLADAREVIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 466 CQKKKEKELVT-------TVQSLQQKVERCLEdgiRLPMLDAKQLQNEndNLRQQNETASKIIDSQQDEIDRMILEIQSM 538
Cdd:pfam05557 108 CLKNELSELRRqiqraelELQSTNSELEELQE---RLDLLKAKASEAE--QLRQNLEKQQSSLAEAEQRIKELEFEIQSQ 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767942809 539 qgklSKEKLTTQKMMEELE---KKERNVQRLtKALLENQRQTDETCSLLDQGQEPDQSR 594
Cdd:pfam05557 183 ----EQDSEIVKNSKSELAripELEKELERL-REHNKHLNENIENKLLLKEEVEDLKRK 236
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
381-539 |
9.34e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 39.24 E-value: 9.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 381 RDRYISSLKK---KCQKESEQNKEKQRRIETLEKYLADLPTLD--------DVQSQSLQLQILEEKNKNLQEALIdteKK 449
Cdd:pfam05667 358 IKKLESSIKQveeELEELKEQNEELEKQYKVKKKTLDLLPDAEeniaklqaLVDASAQRLVELAGQWEKHRVPLI---EE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942809 450 LEEIKKQCQDKETQliCQKKKEKelvttVQSLQQKVERCLEDgIRLPMLDAKQLQNENDNLRQQ---NETASKI------ 520
Cdd:pfam05667 435 YRALKEAKSNKEDE--SQRKLEE-----IKELREKIKEVAEE-AKQKEELYKQLVAEYERLPKDvsrSAYTRRIleivkn 506
|
170
....*....|....*....
gi 767942809 521 IDSQQDEIDRMILEIQSMQ 539
Cdd:pfam05667 507 IKKQKEEITKILSDTKSLQ 525
|
|
|