|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
364-581 |
1.58e-11 |
|
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: 67.77 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 364 LKEKELLIDKQRKHISQLEQKVRE--SELQVHSALLGRpapfgdvCLLRLQELQRENTFLRAQFAQKTEALS---REKID 438
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEElqKELYALANEISR-------LEQQKQILRERLANLERQLEELEAQLEeleSKLDE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 439 LEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEE---RVKGRDKHINNLKKK---CQKESEQNREKQQRIETLERYLAD 512
Cdd:TIGR02168 335 LAEELAELEEKLEELKEELESLEAELEELEAELEElesRLEELEEQLETLRSKvaqLELQIASLNNEIERLEARLERLED 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825701 513 LPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDK 581
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERE 483
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
309-647 |
8.45e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.34 E-value: 8.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 309 ELSTCRQQLELIRLQMEQMQLQngaichhpaafapslpilepaqwISILNSNEHLLKEKELLIDKQRKHisqLEQKVRES 388
Cdd:COG1196 261 ELAELEAELEELRLELEELELE-----------------------LEEAQAEEYELLAELARLEQDIAR---LEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 389 ELQvhsallgrpapfgdvcLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEV 468
Cdd:COG1196 315 EER----------------LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 469 KKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESLLE 548
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE--ALEEAAEEEAELEE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 549 ETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGegpEVEMESWQKQYDSLQKVTEDVQAVTEDCGEAATEDG 628
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL---EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVE 533
|
330
....*....|....*....
gi 1622825701 629 SVALTSTEPRAGSGSRRRN 647
Cdd:COG1196 534 AAYEAALEAALAAALQNIV 552
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
374-570 |
5.16e-10 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 61.37 E-value: 5.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 374 QRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLL--RLQELQRENTFLRAQFA-----QKTEALSREKIDLEKKLSAS 446
Cdd:pfam15905 92 QDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLekQLLELTRVNELLKAKFSedgtqKKMSSLSMELMKLRNKLEAK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 447 EVEVQLIRESLKVALQ------KHS-EEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDH 519
Cdd:pfam15905 172 MKEVMAKQEGMEGKLQvtqknlEHSkGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEEL 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622825701 520 QKQsqqlKDSELKS--TELQEKVTELESLLEETQAICRDRETQLESLRQREAE 570
Cdd:pfam15905 252 LKE----KNDEIESlkQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEE 300
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
305-615 |
7.55e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 305 EQSCELSTCRQQLELIRLQMEQMQLQNGAICHHPAAFAPSLPILEP--AQWISILNSNEHLLKEKELLIDKQRKHISQLE 382
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeiENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 383 QKVRESelqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSrekiDLEKKLSASEVEVQLIRESLKVALQ 462
Cdd:TIGR02169 786 ARLSHS---------------------RIPEIQAELSKLEEEVSRIEARLR----EIEQKLNRLTLEKEYLEKEIQELQE 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 463 KHSEevkkQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptledhqkqSQQLKDSELKSTELQEKVTE 542
Cdd:TIGR02169 841 QRID----LKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDL---------KKERDELEAQLRELERKIEE 907
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622825701 543 LESLLEETQAICRDRETQLESLRQREAEFSSAghslqdKQSVEETSGEGPEVEmeswqKQYDSLQKVTEDVQA 615
Cdd:TIGR02169 908 LEAQIEKKRKRLSELKAKLEALEEELSEIEDP------KGEDEEIPEEELSLE-----DVQAELQRVEEEIRA 969
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
352-614 |
1.91e-08 |
|
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: 57.72 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 352 QWISILNSNEHL---LKEKELLIDKQRKHISQLEQKVRE--SELQVhsallgrpapfgdvclLRLQELQRENTFLRAQFA 426
Cdd:TIGR04523 254 QLNQLKDEQNKIkkqLSEKQKELEQNNKKIKELEKQLNQlkSEISD----------------LNNQKEQDWNKELKSELK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 427 QKTEalsrEKIDLEKKLSASEvevQLIREsLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 506
Cdd:TIGR04523 318 NQEK----KLEEIQNQISQNN---KIISQ-LNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 507 ERYLADLPTLEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQaicrDRETQLESLRQREAEFSSAGHSLQDKQSV 584
Cdd:TIGR04523 390 ESQINDLESKIQNQEKLNQQKDEQIKKlqQEKELLEKEIERLKETII----KNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
250 260 270
....*....|....*....|....*....|
gi 1622825701 585 EETsgegpevEMESWQKQYDSLQKVTEDVQ 614
Cdd:TIGR04523 466 LET-------QLKVLSRSINKIKQNLEQKQ 488
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
419-626 |
3.29e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.99 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 419 TFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSE---EVKKQEERVKGRDKHINNLKKKCQKESEQ 495
Cdd:TIGR02168 662 TGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEEleeELEQLRKELEELSRQISALRKDLARLEAE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 496 NREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAG 575
Cdd:TIGR02168 742 VEQLEERIAQLSKELTEL--EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622825701 576 HSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGEAATE 626
Cdd:TIGR02168 820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEE 870
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
361-565 |
5.07e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 5.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 361 EHLLKEKELLIDKQRKHISQLEQKVRESElqvhsallgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSRekidLE 440
Cdd:PRK03918 258 EEKIRELEERIEELKKEIEELEEKVKELK--------------------ELKEKAEEYIKLSEFYEEYLDELRE----IE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 441 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKcQKESEQNREKQQRIETLERYLADLPTledhQ 520
Cdd:PRK03918 314 KRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTP----E 387
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622825701 521 KQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLR 565
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
410-607 |
1.23e-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: 55.07 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 410 RLQELQREntflRAQfAQKTEALSREKIDLEKKLSASEVE--------VQLIRESLKVALQKHSEEVKKQEERVKGRDKH 481
Cdd:TIGR02169 199 QLERLRRE----REK-AERYQALLKEKREYEGYELLKEKEalerqkeaIERQLASLEEELEKLTEEISELEKRLEEIEQL 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 482 INNLKKKCQK--ESEQNREKQQ------RIETLERYLADLPT-LEDHQKQSQQLkDSELKST-----ELQEKVTELESLL 547
Cdd:TIGR02169 274 LEELNKKIKDlgEEEQLRVKEKigeleaEIASLERSIAEKEReLEDAEERLAKL-EAEIDKLlaeieELEREIEEERKRR 352
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 548 EETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQ 607
Cdd:TIGR02169 353 DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
360-583 |
3.94e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 360 NEHLLKEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLRLQELQRENTflRAQFAQKTEALSREKIDL 439
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE--VEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 440 EKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT- 515
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAeaeIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERr 839
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622825701 516 LEDHQKQSQQLKDSELKST----ELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQS 583
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAaeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
304-571 |
6.51e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 304 REQSCELSTCRQQLELIRLQMEQMQLQNGAICHHPAAFAPSLPILEP--AQWISILNSNEHLLKEKELLIDKQRKHISQL 381
Cdd:TIGR02168 694 AELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAevEQLEERIAQLSKELTELEAEIEELEERLEEA 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 382 EQKVRESElqVHSALLGRpapfgdvcllRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIrESLKVAL 461
Cdd:TIGR02168 774 EEELAEAE--AEIEELEA----------QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRI-AATERRL 840
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 462 QKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSElkstelqEKVT 541
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL--RSELEELSEELRELE-------SKRS 911
|
250 260 270
....*....|....*....|....*....|
gi 1622825701 542 ELESLLEETQAICRDRETQLESLRQREAEF 571
Cdd:TIGR02168 912 ELRRELEELREKLAQLELRLEGLEVRIDNL 941
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
293-612 |
7.58e-07 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.52 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 293 VWQPSPDTWHPREQSCELSTCRQQLEL-IRLQMEQMQLQNGAICHHPAAFAPSLPILEPAQWISILNSNEHLLKEKELL- 370
Cdd:pfam10174 57 VLKEQYRVTQEENQHLQLTIQALQDELrAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKELFLLr 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 371 ---------IDKQRKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLR---------------LQELQRENTFLR---- 422
Cdd:pfam10174 137 ktleemelrIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERTRriaeaemqlghlevlLDQKEKENIHLReelh 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 423 -----AQFAQKTEALSR------EKI-DLEKKLSASEVEVQLIRESLKVALQKHSEEVkKQEERVKGRDKHINN----LK 486
Cdd:pfam10174 217 rrnqlQPDPAKTKALQTviemkdTKIsSLERNIRDLEDEVQMLKTNGLLHTEDREEEI-KQMEVYKSHSKFMKNkidqLK 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 487 KKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSqqLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQ 566
Cdd:pfam10174 296 QELSKKESELLALQTKLETLTNQNSDCKQHIEVLKES--LTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLTE 373
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1622825701 567 REAEFSSAGHSLQDKQSVEETsgegpevEMESWQKQYDSLQKVTED 612
Cdd:pfam10174 374 EKSTLAGEIRDLKDMLDVKER-------KINVLQKKIENLQEQLRD 412
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
361-589 |
9.97e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 9.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 361 EHLLKEKELLIDKQ-------RKHISQLEQKVRESELQVHsallgrpapfgdvcllRLQELQREntflRAQFAQKTEALS 433
Cdd:COG4717 49 ERLEKEADELFKPQgrkpelnLKELKELEEELKEAEEKEE----------------EYAELQEE----LEELEEELEELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 434 REKIDLEKKLSASEVEVQLIRESLKV-ALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLAd 512
Cdd:COG4717 109 AELEELREELEKLEKLLQLLPLYQELeALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLS- 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825701 513 lptledhQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrdretQLESLRQREAEFSSAGHSLQDKQSVEETSG 589
Cdd:COG4717 188 -------LATEEELQDLAEELEELQQRLAELEEELEEAQE-------ELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
405-597 |
1.01e-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: 52.37 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 405 DVCLLRLQELQREntflRAQFAQKTEALSREKIDLEKKLSASEVEVQLIR----------ESLKVALQKHSEEVKKQEER 474
Cdd:TIGR02168 228 ALLVLRLEELREE----LEELQEELKEAEEELEELTAELQELEEKLEELRlevseleeeiEELQKELYALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 475 VKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL-----PTLEDHQKQSQQLK-------DSELKSTELQEKVTE 542
Cdd:TIGR02168 304 KQILRERLANLERQLEELEAQLEELESKLDELAEELAELeekleELKEELESLEAELEeleaeleELESRLEELEEQLET 383
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622825701 543 LES----------LLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEME 597
Cdd:TIGR02168 384 LRSkvaqlelqiaSLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEE 448
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
361-567 |
1.22e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.84 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 361 EHLLKEKELLID-----KQRKHISQLEQKVRESELQVHsALLGRPAPFGDV--CLLRLQELQRENTFLRAQFAQKTEALS 433
Cdd:COG4913 215 EYMLEEPDTFEAadalvEHFDDLERAHEALEDAREQIE-LLEPIRELAERYaaARERLAELEYLRAALRLWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 434 REKID-LEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDkhINNLKKKCQKESEQNREKQQRIETLERYLAD 512
Cdd:COG4913 294 EAELEeLRAELARLEAELERLEARLD-ALREELDELEAQIRGNGGDR--LEQLEREIERLERELEERERRRARLEALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622825701 513 L--------PTLEDHQKQSQQLKDS-ELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 567
Cdd:COG4913 371 LglplpasaEEFAALRAEAAALLEAlEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
410-580 |
1.51e-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: 50.92 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 410 RLQELQRENTFLRAQFAQ---KTEALSREKIDLEKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHIN 483
Cdd:COG4942 28 ELEQLQQEIAELEKELAAlkkEEKALLKQLAALERRIAALARRIRALEQELAALeaeLAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 484 NLKKKCQKESEQ-------------------------NREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKstELQE 538
Cdd:COG4942 108 ELLRALYRLGRQpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLA--ELEE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622825701 539 KVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQD 580
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
373-623 |
1.69e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 51.33 E-value: 1.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 373 KQRKHISQLeQKVRESELQVHSAllgrpapfgdvcllRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQL 452
Cdd:pfam01576 324 KREQEVTEL-KKALEEETRSHEA--------------QLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 453 IRESLKVALQKHSEevkkQEERVKGRDKHINNLKKKCqkeSEQNREKQQRIETLERYLADLPTLedhqkqSQQLKDSELK 532
Cdd:pfam01576 389 LQAELRTLQQAKQD----SEHKRKKLEGQLQELQARL---SESERQRAELAEKLSKLQSELESV------SSLLNEAEGK 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 533 STELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTED 612
Cdd:pfam01576 456 NIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEE 535
|
250
....*....|.
gi 1622825701 613 VQAVTEDCGEA 623
Cdd:pfam01576 536 DAGTLEALEEG 546
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
410-626 |
1.90e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 410 RLQELQREntflrAQFAQKTEALSREKIDLEKKLSASEVE-VQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 488
Cdd:COG1196 201 QLEPLERQ-----AEKAERYRELKEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 489 CQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrDRETQLESLRQRE 568
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARL--EQDIARLEERRRELEERLEELEEELAELEEELEELEE---ELEELEEELEEAE 350
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622825701 569 AEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGEAATE 626
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
411-583 |
1.96e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 411 LQELQRENTFLRAQFAQKTEALS--REKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKK 488
Cdd:TIGR04523 182 KLNIQKNIDKIKNKLLKLELLLSnlKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 489 CQKESEQNREKQQRIET-------LERYLADLPT-LEDHQKQSQQLKDSELKS--TELQEKVTELESLLEETQAICRDRE 558
Cdd:TIGR04523 262 QNKIKKQLSEKQKELEQnnkkikeLEKQLNQLKSeISDLNNQKEQDWNKELKSelKNQEKKLEEIQNQISQNNKIISQLN 341
|
170 180
....*....|....*....|....*....
gi 1622825701 559 TQLESLRQ----REAEFSSAGHSLQDKQS 583
Cdd:TIGR04523 342 EQISQLKKeltnSESENSEKQRELEEKQN 370
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
361-582 |
2.28e-06 |
|
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: 51.22 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 361 EHLLKEKELLIDKQRK---HISQLEQKVRESELQVHSALLgrpapfgdvcllRLQELQRENTFLRAQFA----------Q 427
Cdd:TIGR02169 684 EGLKRELSSLQSELRRienRLDELSQELSDASRKIGEIEK------------EIEQLEQEEEKLKERLEeleedlssleQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 428 KTEALSREKIDLEKKLSASE---VEVQLIRESLKVAL--------QKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQN 496
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEedlHKLEEALNDLEARLshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 497 REKqqrIETLERYLADLptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGH 576
Cdd:TIGR02169 832 EKE---IQELQEQRIDL---------KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLR 899
|
....*.
gi 1622825701 577 SLQDKQ 582
Cdd:TIGR02169 900 ELERKI 905
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
498-626 |
2.87e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.81 E-value: 2.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 498 EKQQRIETLERYLADLPT----LEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSS 573
Cdd:PRK02224 472 EDRERVEELEAELEDLEEeveeVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEA 551
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 574 AGHSLQDK-QSVEETSGEGPEVEMESWQKQ------YDSLQKVtEDVQAVTEDCGEAATE 626
Cdd:PRK02224 552 EAEEKREAaAEAEEEAEEAREEVAELNSKLaelkerIESLERI-RTLLAAIADAEDEIER 610
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
317-591 |
3.47e-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: 50.50 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 317 LELIRLQMEQMQLQNGAicHHPAAFAPslpILEPAQWISILNSNEHLLKEKELLIDKQRKHISQLEQKVRESELQ----- 391
Cdd:pfam15921 564 IEILRQQIENMTQLVGQ--HGRTAGAM---QVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklv 638
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 392 ---------VHSALLGRPAPFGDV--CLLRLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVA 460
Cdd:pfam15921 639 nagserlraVKDIKQERDQLLNEVktSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 461 LQKHSEEVK---KQEERVKGRDKHINNLKKKCQKESE----QNREKQQRIETLERYLADLPTL-EDHQKQSQQLKDSELK 532
Cdd:pfam15921 719 EGSDGHAMKvamGMQKQITAKRGQIDALQSKIQFLEEamtnANKEKHFLKEEKNKLSQELSTVaTEKNKMAGELEVLRSQ 798
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622825701 533 STELQEKVTELESLLEETQ---AICRD---RETQlESLRQReaefssaghsLQDKQSVEETSGEG 591
Cdd:pfam15921 799 ERRLKEKVANMEVALDKASlqfAECQDiiqRQEQ-ESVRLK----------LQHTLDVKELQGPG 852
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
361-572 |
3.53e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 3.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 361 EHLLKEKELLIDKQRKHISQLEQKVRESELQVhSALLGRpapfgdvcLLRLQELqrentflraqfAQKTEALSREKIDLE 440
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREEL-EKLEKE--------VKELEEL-----------KEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 441 KKLSASEVEVQLIRESLKvALQKHSEEVKKQEERV---KGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADL-PTL 516
Cdd:PRK03918 252 GSKRKLEEKIRELEERIE-ELKKEIEELEEKVKELkelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIeERI 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622825701 517 EDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAIcRDRETQLESLRQREAEFS 572
Cdd:PRK03918 331 KELEEKEERLEELKKKLKELEKRLEELEERHELYEEA-KAKKEELERLKKRLTGLT 385
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
427-614 |
3.98e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 427 QKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 506
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 507 ERYLADLPTLEDHQKQSQQLKdsELKStELQEKVTELESLLEetqaicrDRETQLESLRQREAEFSSaghslqDKQSVEE 586
Cdd:PRK03918 279 EEKVKELKELKEKAEEYIKLS--EFYE-EYLDELREIEKRLS-------RLEEEINGIEERIKELEE------KEERLEE 342
|
170 180 190
....*....|....*....|....*....|...
gi 1622825701 587 TSGEGPEV-----EMESWQKQYDSLQKVTEDVQ 614
Cdd:PRK03918 343 LKKKLKELekrleELEERHELYEEAKAKKEELE 375
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
427-586 |
8.15e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.27 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 427 QKTEALSREKIDLEKKLSASEVEvqliRESLKvalqkhsEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETL 506
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETERE----REELA-------EEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 507 ERYLADL-PTLEDHQKQSQQL-----------KDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR----EAE 570
Cdd:PRK02224 320 EDRDEELrDRLEECRVAAQAHneeaeslredaDDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEieelRER 399
|
170
....*....|....*.
gi 1622825701 571 FSSAGHSLQDKQSVEE 586
Cdd:PRK02224 400 FGDAPVDLGNAEDFLE 415
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
410-622 |
8.90e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 48.74 E-value: 8.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 410 RLQELQRE-NTFLRAQFAQKT-------------EALSREKIDLEKKlsaseveVQLIRESLKVALQKHSEEVKKQEERV 475
Cdd:pfam07888 35 RLEECLQErAELLQAQEAANRqrekekerykrdrEQWERQRRELESR-------VAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 476 KGRDKhinnLKKKCQKESEQNREKQQRIETLERYL-----------ADLPTLEDHQKQS-QQLKDSELKSTELQEKvtel 543
Cdd:pfam07888 108 ASSEE----LSEEKDALLAQRAAHEARIRELEEDIktltqrvlereTELERMKERAKKAgAQRKEEEAERKQLQAK---- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 544 eslLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEE---TSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDC 620
Cdd:pfam07888 180 ---LQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTqklTTAHRKEAENEALLEELRSLQERLNASERKVEGL 256
|
..
gi 1622825701 621 GE 622
Cdd:pfam07888 257 GE 258
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
410-564 |
1.25e-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: 47.23 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 410 RLQELQRENTFLRAQFAQKTEALSrekiDLEKKLSASEVEVQLIRESLKVaLQKHSEEVKKQEErVKGRDKHINNLKKKC 489
Cdd:COG1579 32 ELAELEDELAALEARLEAAKTELE----DLEKEIKRLELEIEEVEARIKK-YEEQLGNVRNNKE-YEALQKEIESLKRRI 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622825701 490 QKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDselKSTELQEKVTELESLLEETQAicrDRETQLESL 564
Cdd:COG1579 106 SDLEDEILELMERIEELEEELAEL--EAELAELEAELEE---KKAELDEELAELEAELEELEA---EREELAAKI 172
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
408-570 |
1.54e-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: 46.84 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 408 LLRLQELQREntflRAQFAQKTEALSREKIDLEKKLSASEVEVqlirESLKVALQKHSEEVKKQEERVKGRDKHINNLKK 487
Cdd:COG1579 9 LLDLQELDSE----LDRLEHRLKELPAELAELEDELAALEARL----EAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 488 KcQKESEQNRE---KQQRIETLERYLADLptlEDHQKQSQQLKDselkstELQEKVTELESLLEETQA----ICRDRETQ 560
Cdd:COG1579 81 Q-LGNVRNNKEyeaLQKEIESLKRRISDL---EDEILELMERIE------ELEEELAELEAELAELEAeleeKKAELDEE 150
|
170
....*....|
gi 1622825701 561 LESLRQREAE 570
Cdd:COG1579 151 LAELEAELEE 160
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
426-616 |
1.84e-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: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 426 AQKTEALSREKIDLEKKLSASEVEVQLI---RESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQR 502
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALkkeEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 503 IETLERYLADLptLEDHQKQSQQLKDSELKStelQEKVTELESLLEETQAICRDRETQLESLRQREAEfssaghsLQDKQ 582
Cdd:COG4942 99 LEAQKEELAEL--LRALYRLGRQPPLALLLS---PEDFLDAVRRLQYLKYLAPARREQAEELRADLAE-------LAALR 166
|
170 180 190
....*....|....*....|....*....|....
gi 1622825701 583 SVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAV 616
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKL 200
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
408-612 |
1.88e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 408 LLRLQELQRENTFLRAQFAQKTEalsrEKIDLEKKLSASEVEVQLIRESLKVA---LQKHSEEVKKQEERVKGRDKHINN 484
Cdd:COG4372 37 LFELDKLQEELEQLREELEQARE----ELEQLEEELEQARSELEQLEEELEELneqLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 485 LKKKCQKESEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicRDRETQLESL 564
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAEL--QSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDEL 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1622825701 565 RqREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTED 612
Cdd:COG4372 189 L-KEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLAL 235
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
408-626 |
2.88e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 47.64 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 408 LLRLQELQRENTFLR-AQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGR-------- 478
Cdd:COG3096 428 LCGLPDLTPENAEDYlAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYE-LVCKIAGEVERSQAWQTARellrryrs 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 479 DKHI----NNLKKKcQKESEQNREKQQRIETLeryLADLptledHQKQSQQLKDSELKSTELQEKVTELESLLEEtQAIC 554
Cdd:COG3096 507 QQALaqrlQQLRAQ-LAELEQRLRQQQNAERL---LEEF-----CQRIGQQLDAAEELEELLAELEAQLEELEEQ-AAEA 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 555 RDR----ETQLESLRQREAEFSS---AGHSLQDK-QSVEETSGEgpevemeswqkQYDSLQKVTEDVQAVTEDCGEAATE 626
Cdd:COG3096 577 VEQrselRQQLEQLRARIKELAArapAWLAAQDAlERLREQSGE-----------ALADSQEVTAAMQQLLEREREATVE 645
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
410-618 |
4.63e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.06 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 410 RLQELQRENTFLRAQFAQKTEAlsREKIDLEKKLSasevEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINN--LKK 487
Cdd:PTZ00121 1183 KAEEVRKAEELRKAEDARKAEA--ARKAEEERKAE----EARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNeeIRK 1256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 488 KCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSE--------LKSTELQEKVTELESLLEETQAICRDRET 559
Cdd:PTZ00121 1257 FEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEekkkadeaKKKAEEAKKADEAKKKAEEAKKKADAAKK 1336
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825701 560 QLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTE 618
Cdd:PTZ00121 1337 KAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADE 1395
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
420-615 |
5.27e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.30 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 420 FLRAQFAqktEALSREKIDLEK----KLSASEVEVQLIRESLKVALQKHsEEVKKQEERVKGRDKHINNLKKkcqkeseQ 495
Cdd:COG4717 42 FIRAMLL---ERLEKEADELFKpqgrKPELNLKELKELEEELKEAEEKE-EEYAELQEELEELEEELEELEA-------E 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 496 NREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEEtqaiCRDRETQLESLRQREAEfSSAG 575
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE----LEELEAELAELQEELEE-LLEQ 185
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1622825701 576 HSLQDKQSVEETSGegpevEMESWQKQYDSLQKVTEDVQA 615
Cdd:COG4717 186 LSLATEEELQDLAE-----ELEELQQRLAELEEELEEAQE 220
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
411-546 |
5.95e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.78 E-value: 5.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 411 LQELQRENTFLRAQFAQkteaLSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ 490
Cdd:smart00787 153 LEGLKEDYKLLMKELEL----LNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLE 228
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 491 KESEQNREKQQRIETL----ERYLADLPTLEDHQKQSQQLKDSELKstELQEKVTELESL 546
Cdd:smart00787 229 ELEEELQELESKIEDLtnkkSELNTEIAEAEKKLEQCRGFTFKEIE--KLKEQLKLLQSL 286
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
365-563 |
6.30e-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: 45.91 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 365 KEKELL--IDKQRKHISQLEQKVRESELQVhsALLGRpapfgdvcllRLQELQRENTFLRAQFAQKTEALSREKIDLEKK 442
Cdd:COG4942 49 EEKALLkqLAALERRIAALARRIRALEQEL--AALEA----------ELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 443 LSASEVEVQLIRESLKVA------LQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLptL 516
Cdd:COG4942 117 GRQPPLALLLSPEDFLDAvrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL--K 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1622825701 517 EDHQKQSQQLKDSELKS----TELQEKVTELESLLEETQAICRDRETQLES 563
Cdd:COG4942 195 AERQKLLARLEKELAELaaelAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
406-596 |
8.54e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 8.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 406 VCLLRLQELQREN-----TFLRAQFAQKTEALsREKIDLE----KKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVK 476
Cdd:pfam05483 242 VSLLLIQITEKENkmkdlTFLLEESRDKANQL-EEKTKLQdenlKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQ 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 477 GRDKHINNL--KKKCQKEsEQNREKQQRIETLERYLADLPTLEDHQKQSQQ-LKDSE----LKSTELQEKVTELESLLEE 549
Cdd:pfam05483 321 IATKTICQLteEKEAQME-ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQrLEKNEdqlkIITMELQKKSSELEEMTKF 399
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622825701 550 TQaicrDRETQLESLRQREAEFSSAghsLQDKQSVEETSGE--GPEVEM 596
Cdd:pfam05483 400 KN----NKEVELEELKKILAEDEKL---LDEKKQFEKIAEElkGKEQEL 441
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
357-611 |
8.92e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 45.87 E-value: 8.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 357 LNSNEHLLKEKELLIDKQRKHISQLE---QKVR---ESELQVHSALLGRPAPFGDVCLLrLQELQRENTFLRAQFAQKTE 430
Cdd:pfam05483 101 LKQKENKLQENRKIIEAQRKAIQELQfenEKVSlklEEEIQENKDLIKENNATRHLCNL-LKETCARSAEKTKKYEYERE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 431 ALSREKIDL----EKKLSASE---VEVQLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKCQKESEQNREKQQRI 503
Cdd:pfam05483 180 ETRQVYMDLnnniEKMILAFEelrVQAENARLEMHFKLKEDHEKIQHLEEEYK---KEINDKEKQVSLLLIQITEKENKM 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 504 ETLERYLADLPTLEDHQKQSQQLKDSELK-STELQEKVT-ELESL-------------LEE-----TQAICR---DRETQ 560
Cdd:pfam05483 257 KDLTFLLEESRDKANQLEEKTKLQDENLKeLIEKKDHLTkELEDIkmslqrsmstqkaLEEdlqiaTKTICQlteEKEAQ 336
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622825701 561 LESLRQREA-------EFSSAGHSLQ-----DKQSVEETSGEGPEVEMEsWQKQYDSLQKVTE 611
Cdd:pfam05483 337 MEELNKAKAahsfvvtEFEATTCSLEellrtEQQRLEKNEDQLKIITME-LQKKSSELEEMTK 398
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
357-549 |
8.94e-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: 45.78 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 357 LNSNEHLLKEKEL--LIDKQRKHISQLEQ-----KVRESELQvhsallgrpapfgdvclLRLQELQRENTFLRAQFAQKT 429
Cdd:TIGR04523 547 LNKDDFELKKENLekEIDEKNKEIEELKQtqkslKKKQEEKQ-----------------ELIDQKEKEKKDLIKEIEEKE 609
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 430 -----------------EALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhINNLKKKCQKE 492
Cdd:TIGR04523 610 kkisslekelekakkenEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD-IIELMKDWLKE 688
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825701 493 SEQNREKqqRIETLERYlADLPTLEDHQKQSQQlkdsELKstELQEKVTELESLLEE 549
Cdd:TIGR04523 689 LSLHYKK--YITRMIRI-KDLPKLEEKYKEIEK----ELK--KLDEFSKELENIIKN 736
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
410-678 |
9.38e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 410 RLQELQRENTFLRAQFA---QKTEALSREKIDLEKKLSASEVEVQLIRESLKVAlqkhSEEVKKQEERVKGRdkhINNLK 486
Cdd:COG3883 24 ELSELQAELEAAQAELDalqAELEELNEEYNELQAELEALQAEIDKLQAEIAEA----EAEIEERREELGER---ARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 487 KKCQKESE--------------QNREKQQRI-----ETLERYLADLPTLEDHQKQ-SQQLKDSELKSTELQEKVTELESL 546
Cdd:COG3883 97 RSGGSVSYldvllgsesfsdflDRLSALSKIadadaDLLEELKADKAELEAKKAElEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 547 LEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGEAATE 626
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAG 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1622825701 627 DGSVALTSTEPRAGSGSRRRNKPGPERGGPTKGFSPAAAAHSREGAFSAKPG 678
Cdd:COG3883 257 AAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSG 308
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
361-653 |
9.52e-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: 45.88 E-value: 9.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 361 EHLLKEKE-LLIDKQRKHISQLEQKVRESELQVHSALLgrpAPFGDVCLLRLQELQRentflraqfaQKTEALSREKIDL 439
Cdd:pfam17380 299 ERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQAAIY---AEQERMAMERERELER----------IRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 440 EKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKgrdkhinnlKKKCQKESEQNREKQQRIEtleryladlptLEDH 519
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR---------KVKILEEERQRKIQQQKVE-----------MEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 520 QKQSQQLKDSELKSTElQEKVTELESLLEETQaicrDRETQLESLRQREAEFSSAGHSL----QDKQSVEETSGEGPEVE 595
Cdd:pfam17380 426 RAEQEEARQREVRRLE-EERAREMERVRLEEQ----ERQQQVERLRQQEEERKRKKLELekekRDRKRAEEQRRKILEKE 500
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1622825701 596 MESWQKQYDSLQKVTEDVQAVTEDCGEAATEDgsvaltsTEPRAGSGSRRRNKPGPER 653
Cdd:pfam17380 501 LEERKQAMIEEERKRKLLEKEMEERQKAIYEE-------ERRREAEEERRKQQEMEER 551
|
|
| Yuri_gagarin |
pfam15934 |
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis. |
465-590 |
1.09e-04 |
|
Yuri gagarin; The yuri gagarin protein found in Drosophila, it plays roles in spermatogenesis.
Pssm-ID: 318204 [Multi-domain] Cd Length: 234 Bit Score: 44.18 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 465 SEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDhqkQSQQLKDSELKSTELQEKVTELE 544
Cdd:pfam15934 92 SENNRLKEEIHDLKQKNCVQARVVRKMGLELKGQEEQRVELCDKYESLLGSFEE---QCQELKRANRRVQSLQTRLSQVE 168
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1622825701 545 SLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGE 590
Cdd:pfam15934 169 KLQEELRTERKILREEVIALKEKDAKSNGRERALQDQLKCCQTEIE 214
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
430-566 |
1.43e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 45.23 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 430 EALSREKidlEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKkkcqkesEQNREKQQRIETLERY 509
Cdd:COG2433 380 EALEELI---EKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE-------AELEEKDERIERLERE 449
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825701 510 LADLptleDHQKQSQQLKDSELKSteLQEKVTELESLLEETQAICRDRETQLESLRQ 566
Cdd:COG2433 450 LSEA----RSEERREIRKDREISR--LDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
410-614 |
1.62e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.59 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 410 RLQELQREntflraqfAQKTEALSREKidlEKKLSASEVEVQLirESLKVALQKH---SEEVKKQEERVKGRDKHINNLK 486
Cdd:cd00176 1 KLQQFLRD--------ADELEAWLSEK---EELLSSTDYGDDL--ESVEALLKKHealEAELAAHEERVEALNELGEQLI 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 487 KKCQKESEQNREKQQRIETLERYLADL-----PTLEDHQKQSQQL------------KDSELKSTELQEKVTELESLLEE 549
Cdd:cd00176 68 EEGHPDAEEIQERLEELNQRWEELRELaeerrQRLEEALDLQQFFrdaddleqwleeKEAALASEDLGKDLESVEELLKK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622825701 550 TQAICRD---RETQLESLRQREAEFSSAGHSLQDKQSveetsgegpEVEMESWQKQYDSLQKVTEDVQ 614
Cdd:cd00176 148 HKELEEEleaHEPRLKSLNELAEELLEEGHPDADEEI---------EEKLEELNERWEELLELAEERQ 206
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
434-564 |
1.88e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 434 REKIDLEKKLSASEVEVQLIRESLKVAlqkhseEVKKQEERVKGRDKhINNLKKKCQKESEQNREK--------QQRIET 505
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLEAKEE-IHKLRNEFEKELRERRNElqklekrlLQKEEN 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825701 506 LERYLADLptledhQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrDRETQLESL 564
Cdd:PRK12704 98 LDRKLELL------EKREEELEKKEKELEQKQQELEKKEEELEELIE---EQLQELERI 147
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
412-567 |
3.34e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.20 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 412 QELQRENTFLRAQFAQKT---EALSREKIDLEKKLSASEVEVQLIRESLKVAlQKHSEEVKKQEERVKGRDKHINNLKKk 488
Cdd:pfam13851 29 KSLKEEIAELKKKEERNEklmSEIQQENKRLTEPLQKAQEEVEELRKQLENY-EKDKQSLKNLKARLKVLEKELKDLKW- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 489 cqkeseQNREKQQRIETLERylaDLPTLEDHQKQSQQ--LKDSELKSTELQEKVTELESLLEEtqaicrdRETQLESLRQ 566
Cdd:pfam13851 107 ------EHEVLEQRFEKVER---ERDELYDKFEAAIQdvQQKTGLKNLLLEKKLQALGETLEK-------KEAQLNEVLA 170
|
.
gi 1622825701 567 R 567
Cdd:pfam13851 171 A 171
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
421-623 |
3.75e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 421 LRAQFAQKTEALSREKI-DLEKKLSASEVEVQLI----------RESLKVALQKHSEevKKQE-ERVKGRDKHINNLKKK 488
Cdd:PRK02224 192 LKAQIEEKEEKDLHERLnGLESELAELDEEIERYeeqreqaretRDEADEVLEEHEE--RREElETLEAEIEDLRETIAE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 489 CQKE----SEQNREKQQRIETLERYLADLptLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESL 564
Cdd:PRK02224 270 TEREreelAEEVRDLRERLEELEEERDDL--LAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESL 347
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825701 565 RQREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGEA 623
Cdd:PRK02224 348 REDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
355-570 |
4.01e-04 |
|
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: 43.41 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 355 SILNSNEHLLKEKELLIDKQRKHISQLEQKVRESE--------LQVHSALLGRPAPFGDVC---------LLRLQE--LQ 415
Cdd:COG5185 268 EKLGENAESSKRLNENANNLIKQFENTKEKIAEYTksidikkaTESLEEQLAAAEAEQELEeskretetgIQNLTAeiEQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 416 RENTFLRAQFAQKTEALS----REKIDLEKKLSASEVEVQLIRESL---KVALQKHSEEVKKQEERVKGR-DKHINNLKK 487
Cdd:COG5185 348 GQESLTENLEAIKEEIENivgeVELSKSSEELDSFKDTIESTKESLdeiPQNQRGYAQEILATLEDTLKAaDRQIEELQR 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 488 KCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQ-QLKDSELKST------ELQEKVTELES----LLEETQAICRD 556
Cdd:COG5185 428 QIEQATSSNEEVSKLLNELISELNKVMREADEESQSRlEEAYDEINRSvrskkeDLNEELTQIESrvstLKATLEKLRAK 507
|
250
....*....|....
gi 1622825701 557 RETQLESLRQREAE 570
Cdd:COG5185 508 LERQLEGVRSKLDQ 521
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
446-627 |
4.34e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.77 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 446 SEVEVQLirESLK----VALQ----KHSEEVKKQEERVKgrdkHINNLKKKCQKESEQNREKQQRIETLErylADLPTLE 517
Cdd:COG1196 196 GELERQL--EPLErqaeKAERyrelKEELKELEAELLLL----KLRELEAELEELEAELEELEAELEELE---AELAELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 518 -DHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEfssaghsLQDKQSVEETSGEGPEVEM 596
Cdd:COG1196 267 aELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE-------LEEELAELEEELEELEEEL 339
|
170 180 190
....*....|....*....|....*....|.
gi 1622825701 597 ESWQKQYDSLQKVTEDVQAVTEDCGEAATED 627
Cdd:COG1196 340 EELEEELEEAEEELEEAEAELAEAEEALLEA 370
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
410-618 |
4.36e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 410 RLQELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKhinnlKKKC 489
Cdd:PTZ00121 1243 KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEE-----AKKA 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 490 QKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAicrdretqlESLRQREA 569
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA---------DAAKKKAE 1388
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1622825701 570 EFSSAGHSlqdKQSVEETSGEGPEV-EMESWQKQYDSLQKVTEDVQAVTE 618
Cdd:PTZ00121 1389 EKKKADEA---KKKAEEDKKKADELkKAAAAKKKADEAKKKAEEKKKADE 1435
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
413-636 |
4.87e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 413 ELQRENTFLRAQFAQKTEALSREKIDLEKKLSASEVEVQLIREslKVALQKHSEEVKKQEERVKGRDKhinnLKKKCQK- 491
Cdd:PTZ00121 1370 EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKK--AAAAKKKADEAKKKAEEKKKADE----AKKKAEEa 1443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 492 ----ESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKdselKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 567
Cdd:PTZ00121 1444 kkadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAK----KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAE 1519
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825701 568 EAEFSSAGHSLQDKQSVEETSgEGPEVEMESWQKQYDSLQKvTEDVQAVTEdcGEAATEDGSVALTSTE 636
Cdd:PTZ00121 1520 EAKKADEAKKAEEAKKADEAK-KAEEKKKADELKKAEELKK-AEEKKKAEE--AKKAEEDKNMALRKAE 1584
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
365-626 |
6.81e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.11 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 365 KEKELLIDKQRKHISQLEQKVRESELQVHSALLGRPAPfgDVCLLRLQELQRENTFLRAQFAQKTEALSREKIDLE---K 441
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADA--EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAEslrE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 442 KLSASEVEVQLIRE---SLKVALQKHSEEVKKQEERVKGRDKHINNLKK----------KCQKESEQNREK----QQRIE 504
Cdd:PRK02224 350 DADDLEERAEELREeaaELESELEEAREAVEDRREEIEELEEEIEELRErfgdapvdlgNAEDFLEELREErdelREREA 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 505 TLErylADLPTLEDHQKQSQQL-------------KDSELKST--ELQEKVTELESLL---EETQAICRDRETQLESLRQ 566
Cdd:PRK02224 430 ELE---ATLRTARERVEEAEALleagkcpecgqpvEGSPHVETieEDRERVEELEAELedlEEEVEEVEERLERAEDLVE 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 567 REAEFSsaghSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGEAATE 626
Cdd:PRK02224 507 AEDRIE----RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
354-549 |
7.55e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 7.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 354 ISILNSNehlLKEKELLIDKQRKhisqLEQKVRESELQVhSALLGRPAPFGDVCL----LRLQELQR-ENTFLRAQFAQK 428
Cdd:PRK03918 541 IKSLKKE---LEKLEELKKKLAE----LEKKLDELEEEL-AELLKELEELGFESVeeleERLKELEPfYNEYLELKDAEK 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 429 -----TEALSREKIDLEK---KLSASEVEVQLIRESLKVALQKHSEE---------------VKKQEERVKGRDKHINNL 485
Cdd:PRK03918 613 elereEKELKKLEEELDKafeELAETEKRLEELRKELEELEKKYSEEeyeelreeylelsreLAGLRAELEELEKRREEI 692
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825701 486 KK---KCQKESEQNREKQQRIETLERYLADLptledhqkqsqqlkdselksTELQEKVTELESLLEE 549
Cdd:PRK03918 693 KKtleKLKEELEEREKAKKELEKLEKALERV--------------------EELREKVKKYKALLKE 739
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
428-567 |
8.50e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 8.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 428 KTEALSREKidlEKKLSASEvEVQLIRESLKVALQKHSEEVKKQEERVKgrdKHINNLKKKcqkeSEQNREKQQRIETLE 507
Cdd:PRK12704 48 KKEAEAIKK---EALLEAKE-EIHKLRNEFEKELRERRNELQKLEKRLL---QKEENLDRK----LELLEKREEELEKKE 116
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622825701 508 ryladlptledhQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRD--RETQLESLRQR 567
Cdd:PRK12704 117 ------------KELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLEKVEEE 166
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
355-567 |
9.74e-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: 42.31 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 355 SILNSNEHLLKEKELL---IDKQRKHISQLEQKVRESELQvhsallgrpapfgdvcllrLQELQRENTFLRAQFAQKTEA 431
Cdd:TIGR04523 381 SYKQEIKNLESQINDLeskIQNQEKLNQQKDEQIKKLQQE-------------------KELLEKEIERLKETIIKNNSE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 432 LSrekiDLEKKLSAsevevqliresLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLA 511
Cdd:TIGR04523 442 IK----DLTNQDSV-----------KELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622825701 512 DLptledhqkqSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQR 567
Cdd:TIGR04523 507 EL---------EEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFE 553
|
|
| HAP1_N |
pfam04849 |
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ... |
410-567 |
1.18e-03 |
|
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.
Pssm-ID: 461455 [Multi-domain] Cd Length: 309 Bit Score: 41.55 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 410 RLQELQRENTFLRAQFAQkteaLSREKIDLEKKlsasevEVQLIR---ESLKVA----------LQKHSEEVKKQEERVK 476
Cdd:pfam04849 172 KLRGLEEENLKLRSEASH----LKTETDTYEEK------EQQLMSdcvEQLSEAnqqmaelseeLARKMEENLRQQEEIT 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 477 GRDKHINNLKKKCQKESEQNREKQQRIETleryladlptledhQKQSQQLKDSELKstELQEKVTELESLLEETQaicrd 556
Cdd:pfam04849 242 SLLAQIVDLQHKCKELGIENEELQQHLQA--------------SKEAQRQLTSELQ--ELQDRYAECLGMLHEAQ----- 300
|
170
....*....|.
gi 1622825701 557 reTQLESLRQR 567
Cdd:pfam04849 301 --EELKELRKK 309
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
375-609 |
1.33e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 375 RKHISQLEQKVRESElqvhsallgrpapfgdvclLRLQELQRENTFL-----RAQFAQKTEALSREKIDLEKKLSASEVE 449
Cdd:COG3206 181 EEQLPELRKELEEAE-------------------AALEEFRQKNGLVdlseeAKLLLQQLSELESQLAEARAELAEAEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 450 VQLIRESLKVALQKHSEEVkkqeervkgRDKHINNLKkkcqkeSEQNREKQQRIETLERYLADLPTLedhqkqsqqlkds 529
Cdd:COG3206 242 LAALRAQLGSGPDALPELL---------QSPVIQQLR------AQLAELEAELAELSARYTPNHPDV------------- 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 530 elksTELQEKVTELESLL-EETQAICRDRETQLESLRQREAEFSSaghSLQD-KQSVEETSGEgpEVEMESWQKQYDSLQ 607
Cdd:COG3206 294 ----IALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQA---QLAQlEARLAELPEL--EAELRRLEREVEVAR 364
|
..
gi 1622825701 608 KV 609
Cdd:COG3206 365 EL 366
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
375-586 |
1.67e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.56 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 375 RKHISQLEQKVRESELQVHSALLGRPAPFGDVCLLR--LQELQRENTFLRAQFAqkTEALSREKIDLEKK-LSASEVEVQ 451
Cdd:PRK02224 250 REELETLEAEIEDLRETIAETEREREELAEEVRDLRerLEELEEERDDLLAEAG--LDDADAEAVEARREeLEDRDEELR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 452 LIRESLKVALQKHSEEVKKQEERVKGRDkhinnlkkkcqkesEQNREKQQRIETLERYLADlpTLEDHQKQSQQLKDSEL 531
Cdd:PRK02224 328 DRLEECRVAAQAHNEEAESLREDADDLE--------------ERAEELREEAAELESELEE--AREAVEDRREEIEELEE 391
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622825701 532 KSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDkqSVEE 586
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARE--RVEE 444
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
408-569 |
1.73e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 408 LLRLQELQRENTFLRAQFAQKTEALSREKID-----LEKKLSASEVEVQLIRESLKVALQKHSEEVKKQEE-RVKGRDKH 481
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEellaaLGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQE 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 482 INNLKKKCQKESE-----------QNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEET 550
Cdd:COG4717 372 IAALLAEAGVEDEeelraaleqaeEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEEL 451
|
170
....*....|....*....
gi 1622825701 551 QAICRDRETQLESLRQREA 569
Cdd:COG4717 452 REELAELEAELEQLEEDGE 470
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
422-641 |
1.74e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 41.24 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 422 RAQFAQKTEALSREKIDLEKKLSASEVEvqlirESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQ------KESEQ 495
Cdd:pfam03528 132 RAQWNQYRESAEREIADLRRRLSEGQEE-----ENLEDEMKKAQEDAEKLRSVVMPMEKEIAALKAKLTeaedkiKELEA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 496 NR----------EKQQRIEtLERYLADLPTledhQKQSQQlKDSELKSTELQEKVTELE------SLLEETQAICRDRET 559
Cdd:pfam03528 207 SKmkelnhyleaEKSCRTD-LEMYVAVLNT----QKSVLQ-EDAEKLRKELHEVCHLLEqerqqhNQLKHTWQKANDQFL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 560 QLESLRQREAE-FSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGEAATEDgSVALTSTEPR 638
Cdd:pfam03528 281 ESQRLLMRDMQrMESVLTSEQLRQVEEIKKKDQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVET-SAPLSNVEEQ 359
|
...
gi 1622825701 639 AGS 641
Cdd:pfam03528 360 INS 362
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
361-572 |
1.77e-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: 41.54 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 361 EHLLKEKEL-----LIDKQRKHISQLEQKVRESELQVhsallgrpapfgdvcllrlQELQRentfLRAQFAQKTEALSRE 435
Cdd:TIGR04523 420 EKELLEKEIerlkeTIIKNNSEIKDLTNQDSVKELII-------------------KNLDN----TRESLETQLKVLSRS 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 436 KIDLEKKLSASEVEVqlirESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERYLadlpt 515
Cdd:TIGR04523 477 INKIKQNLEQKQKEL----KSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDEL----- 547
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1622825701 516 ledhQKQSQQLKDSELKsTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFS 572
Cdd:TIGR04523 548 ----NKDDFELKKENLE-KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKK 599
|
|
| Lebercilin |
pfam15619 |
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ... |
410-570 |
2.64e-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: 39.50 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 410 RLQELQRENTFLRAQFAQKTEALsrekidleKKLSASEVEVQLIreslkvaLQKHSEEV--------------KKQEERV 475
Cdd:pfam15619 26 KLEELRKENRLLKRLQKRQEKAL--------GKYEGTESELPQL-------IARHNEEVrvlrerlrrlqekeRDLERKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 476 KGRDKHINNLKKKCQKESEQNREKQ-QRIETLERYLADLPT-LEDHQKQSQQL-KDSELKSTELQEKVTELESLLEETQA 552
Cdd:pfam15619 91 KEKEAELLRLRDQLKRLEKLSEDKNlAEREELQKKLEQLEAkLEDKDEKIQDLeRKLELENKSFRRQLAAEKKKHKEAQE 170
|
170
....*....|....*...
gi 1622825701 553 ICRDRETQLESLRQREAE 570
Cdd:pfam15619 171 EVKILQEEIERLQQKLKE 188
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
408-648 |
2.97e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 408 LLRLQELQRENTFLRAQFAQKTEALSREkidlEKKLSASEV----EVQLIRESLKVALQKHSEE-----VKKQEERVKGR 478
Cdd:PTZ00121 1515 AKKAEEAKKADEAKKAEEAKKADEAKKA----EEKKKADELkkaeELKKAEEKKKAEEAKKAEEdknmaLRKAEEAKKAE 1590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 479 DKHINNLKKKCQKESEQNREKQQRIETLERYLADLPTLEDHQKQSQQLKDSE------------------LKSTELQEKV 540
Cdd:PTZ00121 1591 EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEaeekkkaeelkkaeeenkIKAAEEAKKA 1670
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 541 TELESLLEETQAICRDRETQLESLRqREAEFSSAGHSLQDKQSVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDC 620
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEALK-KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA 1749
|
250 260
....*....|....*....|....*...
gi 1622825701 621 GEAATEDGSVALTSTEPRAGSGSRRRNK 648
Cdd:PTZ00121 1750 KKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
408-586 |
3.42e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 408 LLRLQELQREntflRAQFAQKTEALSREKIDLEKKLS----ASEVEVQLIRESLKVALQKHSEeVKKQEERVKGRDKHIN 483
Cdd:PRK03918 548 LEKLEELKKK----LAELEKKLDELEEELAELLKELEelgfESVEELEERLKELEPFYNEYLE-LKDAEKELEREEKELK 622
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 484 NLKKKCQKESEQNREKQQRIETLERYLADLPTL---EDHQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQ 560
Cdd:PRK03918 623 KLEEELDKAFEELAETEKRLEELRKELEELEKKyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
170 180
....*....|....*....|....*.
gi 1622825701 561 LESLRQREAEFSSAGHSLQDKQSVEE 586
Cdd:PRK03918 703 LEEREKAKKELEKLEKALERVEELRE 728
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
365-567 |
3.90e-03 |
|
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: 40.80 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 365 KEKELLIDKQRKHISQLEQKVreSELQVHSALLGrpapfgdvcllrlqelqrENTFLRAQFAQKTEALSREKIDLEKKLS 444
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKT--NELKSEKLQIG------------------TNLQRRQQFEEQLVELSTEVQSLIREIK 905
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 445 ASEVEVQLIRESLKVALQKHSEEVKKQEERVKGRDKHINNLKKKC-----------------------QKESEQNR---- 497
Cdd:TIGR00606 906 DAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVknihgymkdienkiqdgkddylkQKETELNTvnaq 985
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622825701 498 --EKQQRIETLERYLADLPTLEDHQKQSQQLKDSELKSTELQEKVTELESLLEE-TQAICRDRETQLESLRQR 567
Cdd:TIGR00606 986 leECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQhLKEMGQMQVLQMKQEHQK 1058
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
339-570 |
4.77e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.62 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 339 AAFAPSLPILEPAQWISilnsnehllkeKELlidkqRKHISQLEQKVRESELQVhsaLLGRPAPF-------GDVCLLRL 411
Cdd:smart00787 56 VAGYCTVPLLELYQFSC-----------KEL-----KKYISEGRDLFKEIEEET---LINNPPLFkeyfsasPDVKLLMD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 412 QELQRENTFLRAQfAQKTEALSREKI--DLEKKLsasEVEVQLIRESLKVaLQKHSEEVKkqEERVKGRDKHiNNLKKKC 489
Cdd:smart00787 117 KQFQLVKTFARLE-AKKMWYEWRMKLleGLKEGL---DENLEGLKEDYKL-LMKELELLN--SIKPKLRDRK-DALEEEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 490 QKESEQNREKQQRIET-LERYLADLptledhQKQSQQLKDSELKSTELQEKVTELESLLEETQAICRDRETQLESLRQRE 568
Cdd:smart00787 189 RQLKQLEDELEDCDPTeLDRAKEKL------KKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKL 262
|
..
gi 1622825701 569 AE 570
Cdd:smart00787 263 EQ 264
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
418-528 |
6.67e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 39.19 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 418 NTFLRaQFAQKTEALSREKIDLEKKLSASEVEVQLIR---ESLKVALQKHSEEVKKQEERVKGRDK----HINNLKKKCQ 490
Cdd:pfam02841 175 EEVLQ-EFLQSKEAVEEAILQTDQALTAKEKAIEAERakaEAAEAEQELLREKQKEEEQMMEAQERsyqeHVKQLIEKME 253
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1622825701 491 KESEQNREKQQRI--ETLERYLADLptLEDHQKQSQQLKD 528
Cdd:pfam02841 254 AEREQLLAEQERMleHKLQEQEELL--KEGFKTEAESLQK 291
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
370-613 |
7.12e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 39.81 E-value: 7.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 370 LIDKQRKHISQLEQKVRESELQV----HSALLGRPAPFGDVCLLRL----------------QELQRENTFLRAqFAQKT 429
Cdd:pfam10174 234 VIEMKDTKISSLERNIRDLEDEVqmlkTNGLLHTEDREEEIKQMEVykshskfmknkidqlkQELSKKESELLA-LQTKL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 430 EAL------SREKID-LEKKLSASE-------VEVQLIR---ESLKVALQKHSEEVK-KQEER---------------VK 476
Cdd:pfam10174 313 ETLtnqnsdCKQHIEvLKESLTAKEqraailqTEVDALRlrlEEKESFLNKKTKQLQdLTEEKstlageirdlkdmldVK 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 477 grDKHINNLKKKCQKESEQNREKQQRIETLERYLADLPT---------------LEDHQKQSQQLKdsELKSTELQEKVT 541
Cdd:pfam10174 393 --ERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTdssntdtalttleeaLSEKERIIERLK--EQREREDRERLE 468
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622825701 542 ELESLLEETQaicrDRETQLESLRQREAEFSSAGHSLQDKQSVEETSGegpeVEMESWQKQYD-SLQKVTEDV 613
Cdd:pfam10174 469 ELESLKKENK----DLKEKVSALQPELTEKESSLIDLKEHASSLASSG----LKKDSKLKSLEiAVEQKKEEC 533
|
|
| Mrs2_Mfm1p-like |
cd12823 |
Saccharomyces cerevisiae inner mitochondrial membrane Mg2+ transporters Mfm1p and Mrs2p-like ... |
378-548 |
7.31e-03 |
|
Saccharomyces cerevisiae inner mitochondrial membrane Mg2+ transporters Mfm1p and Mrs2p-like family; A eukaryotic subfamily belonging to the Escherichia coli CorA-Salmonella typhimurium ZntB_like family (EcCorA_ZntB-like) family of the MIT superfamily of essential membrane proteins involved in transporting divalent cations (uptake or efflux) across membranes. This functionally diverse subfamily includes the inner mitochondrial membrane Mg2+ transporters Saccharomyces cerevisiae Mfm1p/Lpe10p, Mrs2p, and human MRS2/ MRS2L. It also includes a family of Arabidopsis thaliana proteins (AtMGTs) some of which are localized to distinct tissues, and not all of which can transport Mg2+. Structures of the intracellular domain of two EcCorA_ZntB-like family transporters: Vibrio parahaemolyticus and Salmonella typhimurium ZntB form funnel-shaped homopentamers, the tip of the funnel is formed from two C-terminal transmembrane (TM) helices from each monomer, and the large opening of the funnel from the N-terminal cytoplasmic domains. The GMN signature motif of the MIT superfamily occurs just after TM1, mutation within this motif is known to abolish Mg2+ transport through Salmonella typhimurium CorA, and Mrs2p. Natural variants such as GVN and GIN, as in some ZntB family proteins, may be associated with the transport of different divalent cations, such as zinc and cadmium. The functional diversity of MIT transporters may also be due to minor structural differences regulating gating, substrate selection, and transport.
Pssm-ID: 213357 Cd Length: 323 Bit Score: 39.15 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 378 ISQLEQKVRESELQVHSALLGRPAPFG----DVCLL-RLQELQRENTFLRAQFAQKTEALSREKI--------DLEKKLS 444
Cdd:cd12823 85 LEELQRRLASSNGSESESGGEDSLPFEfralEAALEeVCSHLEAELKRLEPEALPLLDELTDKIStsnlerllPLKRRLV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 445 ASEVEVQLIRESLkvalqkhsEEVKKQEERVKGRdkhinNL-KKKCQKESEQNREKQQRIETLErYLadlptLEDHQKQS 523
Cdd:cd12823 165 ELETRVQKVRDAL--------EELLDDDEDMADM-----YLtDKAAGPERLESSRKEDDHEEVE-ML-----LEAYLQQV 225
|
170 180
....*....|....*....|....*
gi 1622825701 524 QQLKDselKSTELQEKVTELESLLE 548
Cdd:cd12823 226 DELLN---KLEELREYIDDTEELIN 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
466-626 |
8.60e-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: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 466 EEVKKQEERVKGRDKHINNLKKKCQKESEQ-------NREKQQ--------RIETLERYL----ADLPTLEDHQKQSQQL 526
Cdd:TIGR02169 180 EEVEENIERLDLIIDEKRQQLERLRREREKaeryqalLKEKREyegyellkEKEALERQKeaieRQLASLEEELEKLTEE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 527 KD-----------------------SELKSTELQEKVTELESLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQS 583
Cdd:TIGR02169 260 ISelekrleeieqlleelnkkikdlGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1622825701 584 VEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGEAATE 626
Cdd:TIGR02169 340 ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
|
| CENP-Q |
pfam13094 |
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles ... |
430-566 |
9.40e-03 |
|
CENP-Q, a CENPA-CAD centromere complex subunit; CENP-Q is one of the components that assembles onto the CENPA-nucleosome distal (CAD) centromere. The centromere, which is the basic element of chromosome inheritance, is epigenetically determined in mammals. CENP-A, the centromere-specific histone H3 variant, assembles an array of nucleosomes and it is this that seems to be the prime candidate for specifying centromere identity. CENPA nucleosomes directly recruit a proximal CENPA-nucleosome-associated complex (NAC) comprised of CENP-M, CENP-N and CENP-T, CENP-U(50), CENP-C and CENP-H. Assembly of the CENPA NAC at centromeres is dependent on CENP-M, CENP-N and CENP-T. Additionally, there are seven other subunits which make up the CENPA-nucleosome distal (CAD) centromere, CENP-K, CENP-L, CENP-O, CENP-P, CENP-Q, CENP-R and CENP-S, also assembling on the CENP-A NAC. Fta7 is the equivalent component of the fission yeast Sim4 complex.
Pssm-ID: 432970 [Multi-domain] Cd Length: 159 Bit Score: 37.27 E-value: 9.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 430 EALSREKIDLEKKLSASEVEVQLIReslkvalqkhsEEVKKQEERVKGRDKHINNLKKKCQKESEQNREKQQRIETLERY 509
Cdd:pfam13094 22 EKLLDRNKALEAQLSAELHSLELLE-----------EEIEKEEALLESDEEYLEELEKNAKAEARERKEKLKKEHPLLQE 90
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90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1622825701 510 L--ADLPTLEDHQKQSQQLKDSELKSTELQEkvtELESLLEETQAicrdretQLESLRQ 566
Cdd:pfam13094 91 DdsGVLSLPELSSDLGLGDTDFSLFDPTLDE---ELLPLLEQLQK-------HLESMQG 139
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| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
435-678 |
9.46e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 435 EKIDLEKKLSASEVEVQLIRESLKvALQKHSEEVKKQEERVKGRdkhINNLKKKCQKESEQNREKQQRIETLERYLADLp 514
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELD-ALQAELEELNEEYNELQAE---LEALQAEIDKLQAEIAEAEAEIEERREELGER- 91
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 515 tLEDHQKQSQQLKDSE--LKSTELQEKVTELE----------SLLEETQAICRDRETQLESLRQREAEFSSAGHSLQDKQ 582
Cdd:COG3883 92 -ARALYRSGGSVSYLDvlLGSESFSDFLDRLSalskiadadaDLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 583 SVEETSGEGPEVEMESWQKQYDSLQKVTEDVQAVTEDCGEAATEDGSVALTSTEPRAGSGSRRRNKPGPERGGPTKGFSP 662
Cdd:COG3883 171 AELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
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250
....*....|....*.
gi 1622825701 663 AAAAHSREGAFSAKPG 678
Cdd:COG3883 251 AAGAAGAAAGSAGAAG 266
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| mukB |
PRK04863 |
chromosome partition protein MukB; |
423-618 |
9.90e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.17 E-value: 9.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 423 AQFAQKTEALSREKIDLEKKLSAS-------EVEVQLIR------------ESLKVALQKHSEEvKKQEERVKGRDKHIN 483
Cdd:PRK04863 445 EEFQAKEQEATEELLSLEQKLSVAqaahsqfEQAYQLVRkiagevsrseawDVARELLRRLREQ-RHLAEQLQQLRMRLS 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622825701 484 NLkkkcqkesEQNREKQQRietLERYLADLptledHQKQSQQLKDSElkstelqekvtELESLLEETQAICRDRETQLES 563
Cdd:PRK04863 524 EL--------EQRLRQQQR---AERLLAEF-----CKRLGKNLDDED-----------ELEQLQEELEARLESLSESVSE 576
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622825701 564 LRQREAEFSsagHSLQD-KQSVEETSGEGPEvemesWQKQYDSLQKVTE-------DVQAVTE 618
Cdd:PRK04863 577 ARERRMALR---QQLEQlQARIQRLAARAPA-----WLAAQDALARLREqsgeefeDSQDVTE 631
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