|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
446-693 |
1.31e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 446 EFEQKLASTEKEVLQLNEflkQRLSLFSEEKKKLEEKLKTRDRyISSLKKKCQKESEQNKEKQRRIETLEKYL----ADL 521
Cdd:TIGR02168 236 ELREELEELQEELKEAEE---ELEELTAELQELEEKLEELRLE-VSELEEEIEELQKELYALANEISRLEQQKqilrERL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 522 PTLDDVQSQ-SLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcLEDGIRL 600
Cdd:TIGR02168 312 ANLERQLEElEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET-LRSKVAQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 601 PMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMM-----EELEKKERNVQRLTKAL 675
Cdd:TIGR02168 391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEEleelqEELERLEEALEELREEL 470
|
250
....*....|....*...
gi 1034650193 676 LENQRQTDETCSLLDQGQ 693
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQ 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
503-701 |
2.80e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 503 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTT 582
Cdd:COG1196 219 KEELKELEAELLLLKLREL--EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 583 VQSLQQKVERCLEDGIRLPmLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELE 662
Cdd:COG1196 297 LARLEQDIARLEERRRELE-ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190
....*....|....*....|....*....|....*....
gi 1034650193 663 KKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSRQQ 701
Cdd:COG1196 376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
446-666 |
4.51e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 4.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 446 EFEQKLASTEKEVLQLNEfLKQRLSlfseekkKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLD 525
Cdd:PRK03918 218 ELREELEKLEKEVKELEE-LKEEIE-------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELK 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 526 DVQSQSLQL-----QILEEKNkNLQEALIDTEKKLEEIKKQCQDKETqlicQKKKEKELVTTVQSLQQKVERcLEDGIRL 600
Cdd:PRK03918 290 EKAEEYIKLsefyeEYLDELR-EIEKRLSRLEEEINGIEERIKELEE----KEERLEELKKKLKELEKRLEE-LEERHEL 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034650193 601 pMLDAKQLQNENDNLRQQ--NETASKI------IDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKER 666
Cdd:PRK03918 364 -YEEAKAKKEELERLKKRltGLTPEKLekeleeLEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKG 436
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
443-709 |
2.86e-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: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 443 QQGEFEQKLASTEKEVLQLN---EFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLA 519
Cdd:COG1196 247 ELEELEAELEELEAELAELEaelEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 520 DLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEikkqcqdketqlicQKKKEKELVTTVQSLQQKVERCLEDGIR 599
Cdd:COG1196 327 EL--EEELEELEEELEELEEELEEAEEELEEAEAELAE--------------AEEALLEAEAELAEAEEELEELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 600 LpMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQ 679
Cdd:COG1196 391 A-LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
250 260 270
....*....|....*....|....*....|
gi 1034650193 680 RQTDETCSLLDQGQEPDQSRQQTVLSKRPL 709
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
503-701 |
3.38e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 503 QNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLicqKKKEKELVTT 582
Cdd:COG3883 17 QIQAKQKELSELQAELEAA--QAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 583 VQSLQQkvercleDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDrmilEIQSMQGKLSKEKLTTQKMMEELE 662
Cdd:COG3883 92 ARALYR-------SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELE 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 1034650193 663 KKERNVQRLTKALlenQRQTDETCSLLDQGQEPDQSRQQ 701
Cdd:COG3883 161 ALKAELEAAKAEL---EAQQAEQEALLAQLSAEEAAAEA 196
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
446-677 |
4.69e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 50.44 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 446 EFEQKLASTEKEV---LQLNEFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLp 522
Cdd:TIGR02168 688 ELEEKIAELEKALaelRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL- 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 523 tLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEdgirlpm 602
Cdd:TIGR02168 767 -EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER------- 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 603 lDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQ-------SMQGKLSKEKLTTQKMMEELEKKERNVQRLTKAL 675
Cdd:TIGR02168 839 -RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallneraSLEEALALLRSELEELSEELRELESKRSELRREL 917
|
..
gi 1034650193 676 LE 677
Cdd:TIGR02168 918 EE 919
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
545-707 |
6.35e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 545 QEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcLEDGIRLPMLDAKQLQNENDNLRQQNETASK 624
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 625 IIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKA---LLENQRQTDETCSLLDQGQEPDQSRQQ 701
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArreQAEELRADLAELAALRAELEAERAELE 177
|
....*.
gi 1034650193 702 TVLSKR 707
Cdd:COG4942 178 ALLAEL 183
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
490-684 |
2.10e-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: 48.09 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 490 ISSLKKKCQKESEQNKEKQRRIETLEKYLADLptldDVQSQSLQLQILEEKN--KNLQEALIDTEKKLEEIKKQCQDKET 567
Cdd:TIGR04523 393 INDLESKIQNQEKLNQQKDEQIKKLQQEKELL----EKEIERLKETIIKNNSeiKDLTNQDSVKELIIKNLDNTRESLET 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 568 QLicqKKKEKELVTTVQSLQQKVERCLEDGIRLPMLDA--KQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQG 645
Cdd:TIGR04523 469 QL---KVLSRSINKIKQNLEQKQKELKSKEKELKKLNEekKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLED 545
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1034650193 646 KLSKEK--LTTQKMMEELEKKERNVQRL---TKALLENQRQTDE 684
Cdd:TIGR04523 546 ELNKDDfeLKKENLEKEIDEKNKEIEELkqtQKSLKKKQEEKQE 589
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
358-668 |
4.02e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 358 QDFSKWESMLKIKEGLLRQKEIVIDRQKQQITHLHERIRDNELRAqHAMLGHYVNCEDSYVASLQPQYENtslQTPFSEE 437
Cdd:TIGR02169 730 QEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDL-HKLEEALNDLEARLSHSRIPEIQA---ELSKLEE 805
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 438 SVShsqqgEFEQKLASTEKE---VLQLNEFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETL 514
Cdd:TIGR02169 806 EVS-----RIEARLREIEQKlnrLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 515 EKYLADlptlddvqsqslqlqiLEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCL 594
Cdd:TIGR02169 881 ESRLGD----------------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034650193 595 EDGIRLPMLD--AKQLQNENDNLRQQNETASKIIDSQQDEIDRMiLEIQSMQGKLSKEKLTTQKMMEELEKKERNV 668
Cdd:TIGR02169 945 EIPEEELSLEdvQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
442-804 |
4.82e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 47.27 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 442 SQQGEFEQKLASTEKEVLQLNEFLKqRLSLFSEEKKKLEEKLKTRDRYIS------SLKKKCQKESEQNKEKQR---RIE 512
Cdd:pfam02463 139 VQGGKIEIIAMMKPERRLEIEEEAA-GSRLKRKKKEALKKLIEETENLAEliidleELKLQELKLKEQAKKALEyyqLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 513 TLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEaLIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVER 592
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQELLRDEQE-EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 593 CLEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLT 672
Cdd:pfam02463 297 ELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 673 KALLENQRQTDETCSLLDQGQEPDQSRQQTVLSKRPLFDLTVIDQLFKEMSCCLFDLKALCSILNQRAQGKE--PNLSLL 750
Cdd:pfam02463 377 AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEekEELEKQ 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034650193 751 LGIRSMNCSAEETEND--HSTETLTKKLSDVCQLRRDIDELRTTiSDRYAQDMGDN 804
Cdd:pfam02463 457 ELKLLKDELELKKSEDllKETQLVKLQEQLELLLSRQKLEERSQ-KESKARSGLKV 511
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
519-707 |
8.34e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 519 ADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERcledgi 598
Cdd:COG1579 4 EDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 599 rlpmldakqlqnenDNLRQQNETASKIIDSQQDEIDRMILEIQsmqgKLSKEKLttqKMMEELEKKERNVQRLTKALLEN 678
Cdd:COG1579 78 --------------YEEQLGNVRNNKEYEALQKEIESLKRRIS----DLEDEIL---ELMERIEELEEELAELEAELAEL 136
|
170 180
....*....|....*....|....*....
gi 1034650193 679 QRQTDETCSLLDQGQEPDQSRQQTVLSKR 707
Cdd:COG1579 137 EAELEEKKAELDEELAELEAELEELEAER 165
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
490-685 |
1.13e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.78 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 490 ISSLKKKCQKESEQNKEKQRRIETLEKYLADlptlddvqsqslqlqiLEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL 569
Cdd:TIGR04523 126 LNKLEKQKKENKKNIDKFLTEIKKKEKELEK----------------LNNKYNDLKKQKEELENELNLLEKEKLNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 570 ICQKKKEKELVTTVQSLQQKVERcledgirlpmldAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSK 649
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLKKKIQK------------NKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQ 257
|
170 180 190
....*....|....*....|....*....|....*...
gi 1034650193 650 EKLTTQKMMEELEKKERNVQRLTKAL--LENQRQTDET 685
Cdd:TIGR04523 258 LKDEQNKIKKQLSEKQKELEQNNKKIkeLEKQLNQLKS 295
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
367-675 |
1.65e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 45.43 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 367 LKIKEGLLRQKEIVIDRQKQQITHLHERIRD------------NELRAQHAMLGHYVNCEDSYVASLQpqYENTSLQtpf 434
Cdd:TIGR02168 686 IEELEEKIAELEKALAELRKELEELEEELEQlrkeleelsrqiSALRKDLARLEAEVEQLEERIAQLS--KELTELE--- 760
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 435 SEESVSHSQQGEFEQKLASTEKEVLQLNEFLKQ---RLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRI 511
Cdd:TIGR02168 761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 512 ETLEKYLADLptlddvqsqSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVe 591
Cdd:TIGR02168 841 EDLEEQIEEL---------SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR- 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 592 rcledgirlpmldaKQLQNENDNLRQQNETAskiidsqQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKK------- 664
Cdd:TIGR02168 911 --------------SELRRELEELREKLAQL-------ELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKieddeee 969
|
330
....*....|..
gi 1034650193 665 -ERNVQRLTKAL 675
Cdd:TIGR02168 970 aRRRLKRLENKI 981
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
490-701 |
2.20e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 45.01 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 490 ISSLKKKCQKeseqNKEKQRRIETLEKYLADLPtlDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL 569
Cdd:TIGR04523 203 LSNLKKKIQK----NKSLESQISELKKQNNQLK--DNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 570 ICQKKKEKELVTTVQSLQQKVERcledgirlpmLDAKQLQNENDNLR---QQNETASKIIDSQQDEIDRMILEIQSMQGK 646
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISD----------LNNQKEQDWNKELKselKNQEKKLEEIQNQISQNNKIISQLNEQISQ 346
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034650193 647 LSKEK----LTTQKMMEELEKKERNVQRLTKallENQRQTDETCSLLDQGQEPDQSRQQ 701
Cdd:TIGR04523 347 LKKELtnseSENSEKQRELEEKQNEIEKLKK---ENQSYKQEIKNLESQINDLESKIQN 402
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
446-677 |
2.62e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 446 EFEQKLASTEKEVLQLNEFLKqRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKES-EQNKEKQRRIETLEKYLADLPTL 524
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLEL 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 525 DDVQSqslQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLicqkkKEKELVTTVQSLQQKVERCLEDGIRLPMLD 604
Cdd:PRK03918 608 KDAEK---ELEREEKELKKLEEELDKAFEELAETEKRLEELRKEL-----EELEKKYSEEEYEELREEYLELSRELAGLR 679
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034650193 605 AKQLQNEndNLRQQNETASKIIDSQQDEIDRMILEIqsmqgklskEKLttQKMMEELEKKERNVQRLtKALLE 677
Cdd:PRK03918 680 AELEELE--KRREEIKKTLEKLKEELEEREKAKKEL---------EKL--EKALERVEELREKVKKY-KALLK 738
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
488-681 |
2.67e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 488 RYISSLKKKCQKESEQNKEKQRRIETLEKyladlpTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKEt 567
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEE------LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELE- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 568 qlicqkKKEKELvttvQSLQQKVERCLEDGirlpmldaKQLQNENDNLRQQNETASKIiDSQQDEIDRMILEIQSMQ--- 644
Cdd:PRK03918 280 ------EKVKEL----KELKEKAEEYIKLS--------EFYEEYLDELREIEKRLSRL-EEEINGIEERIKELEEKEerl 340
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034650193 645 GKLSKEKLTTQKMMEELEKKERNVQRLtKALLENQRQ 681
Cdd:PRK03918 341 EELKKKLKELEKRLEELEERHELYEEA-KAKKEELER 376
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
487-653 |
3.08e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 487 DRYISSLKKKCQKESEQnKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKE 566
Cdd:COG4717 88 EEYAELQEELEELEEEL-EELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 567 TQLICQKKKEKELVTTVQSLQQKVERCLEDGIRlpmlDAKQLQNENDNLRQQNETASKIIDSQQDEIDRM--ILEIQSMQ 644
Cdd:COG4717 167 ELEAELAELQEELEELLEQLSLATEEELQDLAE----ELEELQQRLAELEEELEEAQEELEELEEELEQLenELEAAALE 242
|
....*....
gi 1034650193 645 GKLSKEKLT 653
Cdd:COG4717 243 ERLKEARLL 251
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
473-699 |
3.39e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 473 SEEKKKLeeklktrdryisslKKKCQKESEQNKEKQRRIETLEKYLADLptLDDVQSQSLQLQILEEKNKNLQEALIDTE 552
Cdd:COG4942 19 ADAAAEA--------------EAELEQLQQEIAELEKELAALKKEEKAL--LKQLAALERRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 553 KKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQ--------KVERCLEDGIRLPMLDA--KQLQNENDNLRQQNETA 622
Cdd:COG4942 83 AELAELEKEIAELRAELEAQKEELAELLRALYRLGRqpplalllSPEDFLDAVRRLQYLKYlaPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 623 SKI---IDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDETCSLLDQGQEPDQSR 699
Cdd:COG4942 163 AALraeLEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
367-683 |
3.92e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.16 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 367 LKIKEGLLRQKEIviDRQKQQITHLHERIRDNELRAQHAMLGhyvncedsyVASLQPQYENTSLQtpFSEESVSHSQQGE 446
Cdd:COG1196 222 LKELEAELLLLKL--RELEAELEELEAELEELEAELEELEAE---------LAELEAELEELRLE--LEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 447 FEQKLASTEKEVLQLNEFLKQRLSLFSEEKKKLEEKlktrdryISSLKKKCQKESEQNKEKQRRIETLEKYLADLptldd 526
Cdd:COG1196 289 EEYELLAELARLEQDIARLEERRRELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAEEELEEA----- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 527 vqsqSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEDGIRLpmldAK 606
Cdd:COG1196 357 ----EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL----EE 428
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034650193 607 QLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLtKALLENQRQTD 683
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARL-LLLLEAEADYE 504
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
491-699 |
6.45e-04 |
|
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: 43.19 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 491 SSLKKKCQKESEQNKEKQRRIETLEKYLADlptlddvQSQSLQLQIleEKNKNLQEALIDTEKKLEEIKKQCQDKETQLI 570
Cdd:pfam05557 37 SALKRQLDRESDRNQELQKRIRLLEKREAE-------AEEALREQA--ELNRLKKKYLEALNKKLNEKESQLADAREVIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 571 CQKKKEKELVT-------TVQSLQQKVERCLEdgiRLPMLDAKqLQNENDnLRQQNETASKIIDSQQDEIDRMILEIQSM 643
Cdd:pfam05557 108 CLKNELSELRRqiqraelELQSTNSELEELQE---RLDLLKAK-ASEAEQ-LRQNLEKQQSSLAEAEQRIKELEFEIQSQ 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034650193 644 qgklSKEKLTTQKMMEELE---KKERNVQRLtKALLENQRQTDETCSLLDQGQEPDQSR 699
Cdd:pfam05557 183 ----EQDSEIVKNSKSELAripELEKELERL-REHNKHLNENIENKLLLKEEVEDLKRK 236
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
490-592 |
1.07e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 490 ISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQL 569
Cdd:COG1579 54 LEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAEL 133
|
90 100
....*....|....*....|...
gi 1034650193 570 icqKKKEKELVTTVQSLQQKVER 592
Cdd:COG1579 134 ---AELEAELEEKKAELDEELAE 153
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
486-644 |
2.36e-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: 41.55 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 486 RDRYISSLKK---KCQKESEQNKEKQRRIETLEKYLADLPTLD--------DVQSQSLQLQILEEKNKNLQEALIdteKK 554
Cdd:pfam05667 358 IKKLESSIKQveeELEELKEQNEELEKQYKVKKKTLDLLPDAEeniaklqaLVDASAQRLVELAGQWEKHRVPLI---EE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 555 LEEIKKQCQDKETQliCQKKKEKelvttVQSLQQKVERCLEDgIRLPMLDAKQLQNENDNLRQQ---NETASKI------ 625
Cdd:pfam05667 435 YRALKEAKSNKEDE--SQRKLEE-----IKELREKIKEVAEE-AKQKEELYKQLVAEYERLPKDvsrSAYTRRIleivkn 506
|
170
....*....|....*....
gi 1034650193 626 IDSQQDEIDRMILEIQSMQ 644
Cdd:pfam05667 507 IKKQKEEITKILSDTKSLQ 525
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
447-694 |
2.50e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 447 FEQKLASTEKEVLQLNEFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQ-KESEQNKEKQRRIETLEKYLADLPTlD 525
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQlAAAEAEQELEESKRETETGIQNLTA-E 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 526 DVQSQSLQLQILEEKNKNLQEalIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEDGIRLPMLDA 605
Cdd:COG5185 345 IEQGQESLTENLEAIKEEIEN--IVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQI 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 606 KQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQS-----MQGKLSKEKLTTQKMMEELEKK----ERNVQRLTKALL 676
Cdd:COG5185 423 EELQRQIEQATSSNEEVSKLLNELISELNKVMREADEesqsrLEEAYDEINRSVRSKKEDLNEEltqiESRVSTLKATLE 502
|
250 260
....*....|....*....|..
gi 1034650193 677 EN----QRQTDETCSLLDQGQE 694
Cdd:COG5185 503 KLraklERQLEGVRSKLDQVAE 524
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
503-651 |
2.78e-03 |
|
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.
Pssm-ID: 464776 [Multi-domain] Cd Length: 193 Bit Score: 39.89 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 503 QNKEKQRRIETLEKYLADLPTLddVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLicqKKKEK----- 577
Cdd:pfam15619 40 LQKRQEKALGKYEGTESELPQL--IARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQL---KRLEKlsedk 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 578 ------ELVTTVQSLQQKVERCLEDGIRLpmldAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLsKEK 651
Cdd:pfam15619 115 nlaereELQKKLEQLEAKLEDKDEKIQDL----ERKLELENKSFRRQLAAEKKKHKEAQEEVKILQEEIERLQQKL-KEK 189
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
485-673 |
2.86e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 39.66 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 485 TRDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQI---LEEKNKNLQEaLIDTEKKLEEIKKQ 561
Cdd:pfam05010 19 EKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIqkvLEEKDQALAD-LNSVEKSFSDLFKR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 562 CQDKETQLICQKKKEKELVTTVQSLQQKVERcleDGIRLPMLDAKQLQNendnLRQQNETASKIIDSQQDEIdrmileiQ 641
Cdd:pfam05010 98 YEKQKEVISGYKKNEESLKKCAQDYLARIKK---EEQRYQALKAHAEEK----LDQANEEIAQVRSKAKAET-------A 163
|
170 180 190
....*....|....*....|....*....|..
gi 1034650193 642 SMQGKLSKEKLTTQKMMEELEKKERNVQRLTK 673
Cdd:pfam05010 164 ALQASLRKEQMKVQSLERQLEQKTKENEELTK 195
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
499-684 |
3.11e-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: 41.21 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 499 KESEQNKEKQRRIETLEKYLADLptLDDVQSQslqlqilEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKE 578
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSL--QSELRRI-------ENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 579 LVTTVQSLQQK---VERCLEDGI-RLPMLDAK--QLQNENDNL-----RQQNETASKIIDSQQDEIDRMILEIQSMQGKL 647
Cdd:TIGR02169 742 LEEDLSSLEQEienVKSELKELEaRIEELEEDlhKLEEALNDLearlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKL 821
|
170 180 190
....*....|....*....|....*....|....*..
gi 1034650193 648 SKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDE 684
Cdd:TIGR02169 822 NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
442-684 |
3.22e-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: 40.52 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 442 SQQGEFEQKLASTEKEVLQLNEFLKQRlslfSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKEKQRRIETLEKyladl 521
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 522 ptlddvqsqslQLQILEEKNKNLQEALidtEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEDGIRLp 601
Cdd:COG4942 91 -----------EIAELRAELEAQKEEL---AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 602 MLDAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEI---QSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLEN 678
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKaerQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
....*.
gi 1034650193 679 QRQTDE 684
Cdd:COG4942 236 AAAAAE 241
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
532-684 |
3.29e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 532 LQLQILEEKNKNLQEaliDTEKkLEEIKKQCQDKETQlicQKKKEKELvttvQSLQQKVERCLEDGIRLpmldAKQLQNE 611
Cdd:PRK00409 499 LPENIIEEAKKLIGE---DKEK-LNELIASLEELERE---LEQKAEEA----EALLKEAEKLKEELEEK----KEKLQEE 563
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034650193 612 NDNLRQ-QNETASKIIDSQQDEIDRMILEIQSMQgKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDE 684
Cdd:PRK00409 564 EDKLLEeAEKEAQQAIKEAKKEADEIIKELRQLQ-KGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
291-686 |
3.41e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.86 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 291 VPIQPSVRTQMWLTEQLRTNplegrnTEDSYSLAPWQQQQIEDFRQGSETPMQVLTgssrqsyspgyqdfsKWESMLKIK 370
Cdd:pfam05483 303 MSLQRSMSTQKALEEDLQIA------TKTICQLTEEKEAQMEELNKAKAAHSFVVT---------------EFEATTCSL 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 371 EGLLRQKEIVIDRQKQQIthlheRIRDNELRAQHAMLGHYVNCEDSYVASLQpqyentSLQTPFSEESVSHSQQGEFE-- 448
Cdd:pfam05483 362 EELLRTEQQRLEKNEDQL-----KIITMELQKKSSELEEMTKFKNNKEVELE------ELKKILAEDEKLLDEKKQFEki 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 449 -QKLASTEKEVLQLNEFLKQRLSLFSEEKKKLEEKLKTRDRYISSLKKKCQKESEQNKE------------KQRRIETLE 515
Cdd:pfam05483 431 aEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEltahcdklllenKELTQEASD 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 516 KYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLe 595
Cdd:pfam05483 511 MTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQM- 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 596 dgirlpmldaKQLQNENDNLRQQNETASKIIDSQQDE---------------------IDRMILEIQSMQGKLSK----- 649
Cdd:pfam05483 590 ----------KILENKCNNLKKQIENKNKNIEELHQEnkalkkkgsaenkqlnayeikVNKLELELASAKQKFEEiidny 659
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1034650193 650 ------EKLTTQKMMEELEKKERNVQRLTKAllenQRQTDETC 686
Cdd:pfam05483 660 qkeiedKKISEEKLLEEVEKAKAIADEAVKL----QKEIDKRC 698
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
604-691 |
3.97e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 604 DAKQLQNENDNLRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTT-----QKMMEELEKKERNVQRLTKALLE- 677
Cdd:smart00935 5 DVQKILQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKDAATLseaarEKKEKELQKKVQEFQRKQQKLQQd 84
|
90
....*....|....*
gi 1034650193 678 -NQRQTDETCSLLDQ 691
Cdd:smart00935 85 lQKRQQEELQKILDK 99
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
519-707 |
4.05e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 40.67 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 519 ADLPTLDDVQSQSLQLQ---ILEEKNKNLQEALIDT----------EKKLEEIKKQCQDKETQLicqKKKEKELVTTVQS 585
Cdd:PRK11281 33 GDLPTEADVQAQLDALNkqkLLEAEDKLVQQDLEQTlalldkidrqKEETEQLKQQLAQAPAKL---RQAQAELEALKDD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 586 LQQKVERCLEDgIRLPMLDAK------QLQNENDNLrqqNETASKIIDSQ------QDEIDRMILEIQSMQ-----GKLS 648
Cdd:PRK11281 110 NDEETRETLST-LSLRQLESRlaqtldQLQNAQNDL---AEYNSQLVSLQtqperaQAALYANSQRLQQIRnllkgGKVG 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034650193 649 KEKLT-TQKMMEELEKKERNVQ-RLTKALLEN--------QRQTDETCSLLDQGQEPDQSRQQTVLSKR 707
Cdd:PRK11281 186 GKALRpSQRVLLQAEQALLNAQnDLQRKSLEGntqlqdllQKQRDYLTARIQRLEHQLQLLQEAINSKR 254
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
535-689 |
4.81e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 40.46 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 535 QILEEKNKNLQEALIDTEKKLEEIkkQCQDKETQLICQKKKEKELVTTVQSLQQKVERCLEdgiRLPMLDAKQlqNENDN 614
Cdd:PRK12705 30 RLAKEAERILQEAQKEAEEKLEAA--LLEAKELLLRERNQQRQEARREREELQREEERLVQ---KEEQLDARA--EKLDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 615 LRQQNETASKIIDSQQDEID------RMILE--------------IQSMQGKLSKEKLTTQKMMEE---LEKKERNVQRL 671
Cdd:PRK12705 103 LENQLEEREKALSARELELEelekqlDNELYrvagltpeqarkllLKLLDAELEEEKAQRVKKIEEeadLEAERKAQNIL 182
|
170
....*....|....*...
gi 1034650193 672 TKALlenQRQTDETCSLL 689
Cdd:PRK12705 183 AQAM---QRIASETASDL 197
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
499-738 |
5.62e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.34 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 499 KESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEeknknlqealiDTEKKLEEIKKQCQDKETQLICQKKKEKE 578
Cdd:TIGR00618 186 FAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLE-----------KELKHLREALQQTQQSHAYLTQKREAQEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 579 LVTTVQSLQQKVERCLEDGIRLPMLdakQLQNENDNLRQQNE---TASKIIDSQQDEIDRMILEIQSMQGKLSKE---KL 652
Cdd:TIGR00618 255 QLKKQQLLKQLRARIEELRAQEAVL---EETQERINRARKAAplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLlmkRA 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 653 TTQKMMEELEKKERNVQRLTKALLENQRQTDETCSLLdqgqepDQSRQQTVLSKRplfdltvIDQLFKEMSCCLFDLKAL 732
Cdd:TIGR00618 332 AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR------EISCQQHTLTQH-------IHTLQQQKTTLTQKLQSL 398
|
....*.
gi 1034650193 733 CSILNQ 738
Cdd:TIGR00618 399 CKELDI 404
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
486-665 |
5.84e-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: 40.44 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 486 RDRYISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLddvqsqslqlqiLEEKNKNLQEAlidtEKKLEEIKKQCQDK 565
Cdd:TIGR02169 221 REYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEE------------ISELEKRLEEI----EQLLEELNKKIKDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 566 ETQLICQKKKEkelvttVQSLQQKVERClEDGIRLPMLDAKQLQNEndnlRQQNETaskiidsqqdEIDRMILEIQSMQG 645
Cdd:TIGR02169 285 GEEEQLRVKEK------IGELEAEIASL-ERSIAEKERELEDAEER----LAKLEA----------EIDKLLAEIEELER 343
|
170 180
....*....|....*....|
gi 1034650193 646 KLSKEKLTTQKMMEELEKKE 665
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELK 363
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
624-691 |
6.12e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 38.28 E-value: 6.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034650193 624 KIIDSQQDEIDRMILEIQSMQGKLSKEKLTT-----QKMMEELEKKERNVQRLTKALLE--NQRQTDETCSLLDQ 691
Cdd:COG2825 50 KEFKKRQAELQKLEKELQALQEKLQKEAATLseeerQKKERELQKKQQELQRKQQEAQQdlQKRQQELLQPILEK 124
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
492-665 |
6.59e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.76 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 492 SLKKKcqKESEQNKEKQRRIETLEKyladlptldDVQSQSLQLQILEEKNKNLQEALidtEKKLEEIKKqcqdKETQLic 571
Cdd:PRK12704 53 AIKKE--ALLEAKEEIHKLRNEFEK---------ELRERRNELQKLEKRLLQKEENL---DRKLELLEK----REEEL-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 572 qKKKEKELVTTVQSLQQKVERCledgirlpmldaKQLQNEndnlrqQNETASKIIDSQQDEIDRMILEiqSMQGKLSKEK 651
Cdd:PRK12704 113 -EKKEKELEQKQQELEKKEEEL------------EELIEE------QLQELERISGLTAEEAKEILLE--KVEEEARHEA 171
|
170
....*....|....
gi 1034650193 652 LTTQKMMEELEKKE 665
Cdd:PRK12704 172 AVLIKEIEEEAKEE 185
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
490-684 |
7.20e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 7.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 490 ISSLKKKCQKESEQNKEKQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNK---------------NLQEALIDTEKK 554
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKkynleelekkaeeyeKLKEKLIKLKGE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 555 LEEIKKQCQDKETQlicqKKKEKELVTTVQSLQQKVERCLEDGIRLPMLDAKQLQNENDNLRQQNETASKIIDSQQdeid 634
Cdd:PRK03918 541 IKSLKKELEKLEEL----KKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEK---- 612
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1034650193 635 rmilEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKALLENQRQTDE 684
Cdd:PRK03918 613 ----ELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
|
| Spc42p |
pfam11544 |
Spindle pole body component Spc42p; Spc42p is a 42-kD component of the S.cerevisiae spindle ... |
615-674 |
7.91e-03 |
|
Spindle pole body component Spc42p; Spc42p is a 42-kD component of the S.cerevisiae spindle body that localizes to the electron dense central region of the SPB.Spc42p is a phosphoprotein which forms a polymeric layer at the periphery of the SPB central plaque. This functions during SPB duplication and also facilitates the attachment of the SPB to the nuclear membrane.
Pssm-ID: 402925 Cd Length: 72 Bit Score: 35.88 E-value: 7.91e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 615 LRQQNETASKIIDSQQDEIDRMILEIQSMQGKLSKEKLTTQKMMEELEKKERNVQRLTKA 674
Cdd:pfam11544 3 LIKQNKELQNKLDEKQEEIDRLNVLVGSLRAKLIKYTELNKKLEDELQQSERSSSSGNSR 62
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
427-596 |
8.23e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 427 NTSLQTPFSEESVSHSQQGEFEQKLASTEKEVLQLNEFLKQRLSLFseekkkLEEKLKTRDRYISSLKKKcqkesEQNKE 506
Cdd:COG4717 331 PPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL------AEAGVEDEEELRAALEQA-----EEYQE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034650193 507 KQRRIETLEKYLADLPTLDDVQSQSLQLQILEEKNKNLQEALIDTEKKLEEIKKQCQDKETQLicqkkKEKELVTTVQSL 586
Cdd:COG4717 400 LKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAEL-----EQLEEDGELAEL 474
|
170
....*....|
gi 1034650193 587 QQKVERCLED 596
Cdd:COG4717 475 LQELEELKAE 484
|
|
| |
