|
Name |
Accession |
Description |
Interval |
E-value |
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
366-701 |
5.05e-11 |
|
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: 66.20 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 366 KESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTE-EYSKECLKEF--KKII 442
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKnKLLKLELLLSnlKKKI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 443 SKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKTQSDMAIVNNENNRMSIEM-----EAMKTNILLIQDEKEM 517
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLsekqkELEQNNKKIKELEKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 518 LEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQT 597
Cdd:TIGR04523 291 NQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 598 YQSTAE---ENFLQEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQILKEELKKHSQENIKFENSISRLTEDKI 674
Cdd:TIGR04523 371 EIEKLKkenQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
330 340
....*....|....*....|....*..
gi 1034639233 675 LLENYVRSIENERDTLEFEMRHLQREY 701
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSI 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
337-657 |
3.39e-10 |
|
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: 63.92 E-value: 3.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 337 IISENEKtsKVNSVTEQCVAKIQY--LQNYLKEsVQIQKKVMELESenlnLKSKMKPLIFTTQSLIQKVETYEKQLKNLV 414
Cdd:TIGR02168 194 ILNELER--QLKSLERQAEKAERYkeLKAELRE-LELALLVLRLEE----LREELEELQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 415 EEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQGQ-----------NKTLEEKNIQLSLEKQQMMEALDQLKSKEHKT 483
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerlanlERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 484 QSDMAIVNNENNRMS---IEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELK--ESQLEIIQlkekERLAKTEQE 558
Cdd:TIGR02168 347 EELKEELESLEAELEeleAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIErlEARLERLE----DRRERLQQE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 559 TLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQtyqsTAEENFLQEIKNAKSEASIYKNSLSEIGKECEMLSKMV 638
Cdd:TIGR02168 423 IEELLKKLEEAELKELQAELEELEEELEELQEELERLE----EALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
330
....*....|....*....
gi 1034639233 639 METKTDNQILKEELKKHSQ 657
Cdd:TIGR02168 499 ENLEGFSEGVKALLKNQSG 517
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
357-726 |
2.08e-09 |
|
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: 61.28 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 357 KIQYL-QNYLKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVetyekqlkNLVEEKSTIQSK-LSKTEEYSKEC 434
Cdd:pfam05483 223 KIQHLeEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKA--------NQLEEKTKLQDEnLKELIEKKDHL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 435 LKEFKKIISKYNVLQGQNKTLEE------KNI-QLSLEKQQMMEALDQLKskehkTQSDMAIVNNENNRMSIEmEAMKTN 507
Cdd:pfam05483 295 TKELEDIKMSLQRSMSTQKALEEdlqiatKTIcQLTEEKEAQMEELNKAK-----AAHSFVVTEFEATTCSLE-ELLRTE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 508 ILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAkTEQETLLQIIETVKDEKLNLETTLQESTAARQI 587
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIL-AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 588 MEREIENIQ---TYQSTAEENFLQEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQILKEELKKHSQENIKFEN 664
Cdd:pfam05483 448 REKEIHDLEiqlTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKK 527
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034639233 665 SISRLTEDKILLENYVRSIENERDTLEFEMRHLQREYLSLSDKicNQHNDPSKTTYISRREK 726
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK--SEENARSIEYEVLKKEK 587
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
342-697 |
1.99e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 342 EKTSKVNSVTEQCVAKIQYLQNYLKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNL-------- 413
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelk 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 414 -VEEKSTIQSKLSKTEEYSKECLKEFKKIISKY----NVLQGQNKTLEEKNI---QLSLEKQQMMEALDQLKSKEHKTQS 485
Cdd:PRK03918 287 eLKEKAEEYIKLSEFYEEYLDELREIEKRLSRLeeeiNGIEERIKELEEKEErleELKKKLKELEKRLEELEERHELYEE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 486 DMAIVNNENN----RMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKT-----E 556
Cdd:PRK03918 367 AKAKKEELERlkkrLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVcgrelT 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 557 QETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQS-----TAEENFLQEIKNAKSEASIY-KNSLSEIGKE 630
Cdd:PRK03918 447 EEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeselIKLKELAEQLKELEEKLKKYnLEELEKKAEE 526
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034639233 631 CEMLSKMVMETKTDNQILKEELKKhsqenikfensISRLTEDKILLENYVRSIENERDTLEFEMRHL 697
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEK-----------LEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
365-604 |
2.72e-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: 54.30 E-value: 2.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 365 LKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKS--------TIQSKLSKTEEYSKECLK 436
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSIAEKER 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 437 EFK-------KIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKTQSDMAIVNNENNRMSIEMEAMKTNIL 509
Cdd:TIGR02169 316 ELEdaeerlaKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 510 LIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEK------------ERLAKTEQ--ETLLQIIETVKDEKLNLE 575
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineleeekedkaLEIKKQEWklEQLAADLSKYEQELYDLK 475
|
250 260
....*....|....*....|....*....
gi 1034639233 576 TTLQESTAARQIMEREIENIQTYQSTAEE 604
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
392-604 |
4.41e-07 |
|
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: 52.84 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 392 LIFTTQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMME 471
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 472 ALDQLKSKEHKTQSDMAIVNNENNRMSIE-------------------------MEAMKTNILLIQDEKEMLEKKTHQLL 526
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639233 527 KEKSSLGNELKESQLEIIQLKEkerlAKTEQETLLQIIETvkdEKLNLETTLQESTAARQIMEREIENIQTYQSTAEE 604
Cdd:COG4942 171 AERAELEALLAELEEERAALEA----LKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
356-704 |
5.04e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 356 AKIQYLQNYLKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVE-----------------EKS 418
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeeieelekeleslegSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 419 TIQSKLSKTEEYSKECLKEFKKIISKYNVLQgQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKTQSDMAIVN---NENN 495
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEeriKELE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 496 RMSIEMEAMKTNILLIQDEKEMLEKKtHQLLKEKSSLGNEL-----KESQLEIIQLKEKERLAKTEQETLLQIIETVKDE 570
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELerlkkRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 571 KLNLETTLQESTAA---------------RQIMEREIENIQTYQSTAEENFLQEIKNAKSEASIYKNSLSEIGKECEMLS 635
Cdd:PRK03918 414 IGELKKEIKELKKAieelkkakgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 636 KMVMETKTDNQI--LKEELKKHSQEN---------------IKFENSISRLTED---KILLENYVRSIENERDTLEFEMR 695
Cdd:PRK03918 494 ELIKLKELAEQLkeLEEKLKKYNLEElekkaeeyeklkeklIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELA 573
|
....*....
gi 1034639233 696 HLQREYLSL 704
Cdd:PRK03918 574 ELLKELEEL 582
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
500-708 |
5.41e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.40 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 500 EMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQ 579
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 580 ESTAARQIMEREIENIQTYQSTAEEnflqEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQILKEELKKHSQEN 659
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEE----ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034639233 660 IKFENSISRLTEDKILLENYVRSIENERDTLEFEMRHLQREYLSLSDKI 708
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
496-708 |
7.94e-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: 52.76 E-value: 7.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 496 RMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLE 575
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 576 TTLQESTAARQIMEREIENIQT-----YQSTAEEnFLQEIKNAKSEASIYKNSLSEIGKECE-----------MLSKMVM 639
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEalndlEARLSHS-RIPEIQAELSKLEEEVSRIEARLREIEqklnrltlekeYLEKEIQ 836
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639233 640 ETKTDNQILKEELKKHSQE----NIKFENSISRLTEDKILLENYVRS---IENERDTLEFEMRHLQREYLSLSDKI 708
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEienlNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQI 912
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
361-708 |
1.77e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 361 LQNYLKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTEeysKECLKEFKK 440
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ---KELEQNNKK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 441 IISKYNVLQGQNKTLEEKNIQLslEKQQMMEALDQLKSKEHK-TQSDMAIVNNENNrmsiemeamktnILLIQDEKEMLE 519
Cdd:TIGR04523 283 IKELEKQLNQLKSEISDLNNQK--EQDWNKELKSELKNQEKKlEEIQNQISQNNKI------------ISQLNEQISQLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 520 KKTHQLLKEKSSLGNELKESQLEIIQLKEkerlaktEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQ 599
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKK-------ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 600 STAEENFL----------QEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQILKEELKKHSQENIKFENSISRL 669
Cdd:TIGR04523 422 ELLEKEIErlketiiknnSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
330 340 350
....*....|....*....|....*....|....*....
gi 1034639233 670 TEDKILLENYVRSIENERDTLEFEMRHLQREYLSLSDKI 708
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
225-616 |
4.15e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 4.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 225 KEENLDgNLNEDIKSKRISELEALVKKLLPFRETVSKFHVHFCRKCKKLsKSEMHRGKKN----EKNNKEIPITGKNITD 300
Cdd:PRK03918 370 KKEELE-RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL-KKEIKELKKAieelKKAKGKCPVCGRELTE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 301 LKFHSRVPRYT--LSFLDQTKHEMKDKERQ--PFLVKQGSIISENEKTSKVNSVTEQCVAKIQYLQNYLKESVQ------ 370
Cdd:PRK03918 448 EHRKELLEEYTaeLKRIEKELKEIEEKERKlrKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEkkaeey 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 371 --IQKKVMELESENLNLKSKMKPLifttQSLIQKVETYEKQLKNLVEEKSTIQSKLS----KTEEYSKECLKEFKKIISK 444
Cdd:PRK03918 528 ekLKEKLIKLKGEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKELEelgfESVEELEERLKELEPFYNE 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 445 YNVLQGQNKTLEEKniqlslekqqmMEALDQLKSKEHKTQSDMAIVNNENNRMSIEMEAMKTNilLIQDEKEMLEKKTHQ 524
Cdd:PRK03918 604 YLELKDAEKELERE-----------EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK--YSEEEYEELREEYLE 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 525 LLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETllqiIETVKDEKLNLETtlqestaARQIMEREIENIQTYQSTAEE 604
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEE----REKAKKELEKLEK-------ALERVEELREKVKKYKALLKE 739
|
410
....*....|..
gi 1034639233 605 NFLQEIKNAKSE 616
Cdd:PRK03918 740 RALSKVGEIASE 751
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
407-623 |
5.49e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.44 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 407 EKQLKNLVEEKSTIQSKLSKTEEyskeclkEFKKIISKYNVLQGQNKTLEEkniqlslEKQQMMEALDQLKSKEHKTQSD 486
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEALQA-------EIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 487 M------------------AIVNNEN--------NRMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKsslgNELKESQ 540
Cdd:COG3883 88 LgeraralyrsggsvsyldVLLGSESfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKL----AELEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 541 LEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEENFLQEIKNAKSEASIY 620
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
...
gi 1034639233 621 KNS 623
Cdd:COG3883 244 ASA 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
404-671 |
7.22e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 404 ETYEKQLKNLVEEKSTIQSKLSKTEEYSKECLKEFKKI--ISKYNVLQGQNKTLEEKNIQLSLEK-QQMMEALDQLKSKE 480
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKL 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 481 HKTQSDMAIVNNENNRMsiemEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNE-LKESQLEIIQL----KEKERLAKT 555
Cdd:PRK03918 535 IKLKGEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELepfyNEYLELKDA 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 556 EQEtllqiIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEENFLQE-IKNAKSEASIYKNSLSEIGKECEML 634
Cdd:PRK03918 611 EKE-----LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEeYEELREEYLELSRELAGLRAELEEL 685
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1034639233 635 SKMVMETKTDNQILKEEL---KKHSQENIKFENSISRLTE 671
Cdd:PRK03918 686 EKRREEIKKTLEKLKEELeerEKAKKELEKLEKALERVEE 725
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
404-708 |
1.90e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 404 ETYEKQLKNLVEEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKT 483
Cdd:pfam02463 211 EYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 484 QSDMAIVNNENNRMSIEMEAMKTNIL-LIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQ 562
Cdd:pfam02463 291 LAKEEEELKSELLKLERRKVDDEEKLkESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 563 IIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEENFLQEIKNAKSEASIYKNSLSEIGKECEMLSkmvmETK 642
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ----GKL 446
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639233 643 TDNQILKEELKKHSQENIKFENSISRLTEDKILLENYVRSIENERDTLEFEMRHLQREYLSLSDKI 708
Cdd:pfam02463 447 TEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
91-706 |
3.47e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.42 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 91 PSQIHSEDTLTLR--TSTDNLSSNIIIHPSENSdILKNynnfyrflpTAPPNVMSQAD-----TVILDKSKITVPFL-KH 162
Cdd:pfam15921 5 PCESNNEDLLSSSgiTSNRGSSSPFFVSSIRGT-IIEN---------TSSTGTFTQIPifpkyEVELDSPRKIIAYPgKE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 163 GFCENLDDICHSIKQMKEELQKSHD-----------GEVALTNELQTLQTD----PDVHRNGKYDMSPIHQDKMNFIKEE 227
Cdd:pfam15921 75 HIERVLEEYSHQVKDLQRRLNESNElhekqkfylrqSVIDLQTKLQEMQMErdamADIRRRESQSQEDLRNQLQNTVHEL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 228 NLDGNLNEDIKSKRISELEALVKKLLPFR---ETVSKFHVHFCRKCKKL-----SKSEMHRGKKNEKNNKEIPITGKNIT 299
Cdd:pfam15921 155 EAAKCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKiyehdSMSTMHFRSLGSAISKILRELDTEIS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 300 DLK---FHSRVPRYTLSFLDQTKHEM-----KDKERQPFLVKQGSIISENEKTSKVNSVTEQCVAKIQYLQNYLK-ESVQ 370
Cdd:pfam15921 235 YLKgriFPVEDQLEALKSESQNKIELllqqhQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARnQNSM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 371 IQKKVMELESENLNLKSKMKPLIFTTQSLIQKVEtyekqlKNLVEEKSTIQSKLSKTEEYSKEC----------LKEFKK 440
Cdd:pfam15921 315 YMRQLSDLESTVSQLRSELREAKRMYEDKIEELE------KQLVLANSELTEARTERDQFSQESgnlddqlqklLADLHK 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 441 IISKYNVLQGQNKTLEEKNIQLS--------------LEKQQMMEALDQLKSK-EHKTQSDMAIVNNENNrmsiEMEAMK 505
Cdd:pfam15921 389 REKELSLEKEQNKRLWDRDTGNSitidhlrrelddrnMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNE----SLEKVS 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 506 TNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETL----------LQIIETVKDEKLNLE 575
Cdd:pfam15921 465 SLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEItklrsrvdlkLQELQHLKNEGDHLR 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 576 TTLQESTAARQIMEREIENIQTYQstaeenflQEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQILKEELKKH 655
Cdd:pfam15921 545 NVQTECEALKLQMAEKDKVIEILR--------QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKK 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639233 656 SQENIKFENSISRLTEDKILLEN-------YVRSIENERDTLEFEMRHLQREYLSLSD 706
Cdd:pfam15921 617 DAKIRELEARVSDLELEKVKLVNagserlrAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
397-617 |
8.87e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 397 QSLIQKVETYEKQLKNLVEEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQL 476
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 477 KSKEHKTQSDMAIVNNENNRMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEK------- 549
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQleeleea 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639233 550 -----ERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEENFLQEIKNAKSEA 617
Cdd:COG1196 409 eeallERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
370-627 |
9.68e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 370 QIQKKVMELESENLNLKSKMKPLifttQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQ 449
Cdd:COG4372 53 ELEQAREELEQLEEELEQARSEL----EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 450 GQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKTQSDMAIVNNENNRMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEK 529
Cdd:COG4372 129 QQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 530 SSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEENFLQE 609
Cdd:COG4372 209 IESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEAL 288
|
250
....*....|....*...
gi 1034639233 610 IKNAKSEASIYKNSLSEI 627
Cdd:COG4372 289 EEAALELKLLALLLNLAA 306
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
316-592 |
1.08e-04 |
|
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: 45.66 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 316 DQTKHEMKDKERQpflvkqgsiISENEKTSKVNSVTEQCVAKIQYLQNYLKESVQIQKKVMELESENLNLKSKMKplift 395
Cdd:pfam07888 95 KHEELEEKYKELS---------ASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK----- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 396 tQSLIQKVETYEkqlknlveEKSTIQSKLSKTEEYSKECLKEFkkiiskynvlQGQNKTLEEKNIQLslekQQMMEALDQ 475
Cdd:pfam07888 161 -KAGAQRKEEEA--------ERKQLQAKLQQTEEELRSLSKEF----------QELRNSLAQRDTQV----LQLQDTITT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 476 LKSKEhktqsdmaivnNENNRMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGN-------ELKESQLEIIQL-- 546
Cdd:pfam07888 218 LTQKL-----------TTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAqrdrtqaELHQARLQAAQLtl 286
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034639233 547 ----------KEKERLAKtEQETLLQIIETVKD--EKLN-----LETTLQESTAARQIMEREI 592
Cdd:pfam07888 287 qladaslalrEGRARWAQ-ERETLQQSAEADKDriEKLSaelqrLEERLQEERMEREKLEVEL 348
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
341-700 |
1.45e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 341 NEKTSKVNSVTEQcVAKIQYLQNYLKESVQIQKKVMELESENLNLKSKMKPLifTTQSLIQKVETYEKQLKNLVEEKSTI 420
Cdd:PRK03918 334 EEKEERLEELKKK-LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 421 QSKLSKTEEYSKE---CLKEFKKIISKYNVLQGQNKTLEEKNI--QLSLEKQQMMEALDQLKSKEHKTQSDMAIVNNENN 495
Cdd:PRK03918 411 TARIGELKKEIKElkkAIEELKKAKGKCPVCGRELTEEHRKELleEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 496 RMSiEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQL----EIIQLK---EKERLAKTEQETLLQIIETVK 568
Cdd:PRK03918 491 KES-ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIklkgEIKSLKkelEKLEELKKKLAELEKKLDELE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 569 DEKLNLETTLQE-STAARQIMEREIENIQTYQstaeeNFLQEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQI 647
Cdd:PRK03918 570 EELAELLKELEElGFESVEELEERLKELEPFY-----NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639233 648 LKEEL----KKHSQENIK-FENSISRLTEDKILLENYVRSIENERDTLEFEMRHLQRE 700
Cdd:PRK03918 645 LRKELeeleKKYSEEEYEeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
409-686 |
1.55e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 409 QLKNLVEEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQGQNKTLEEK------NIQLSLEKQQMMEAL-DQLKSKEH 481
Cdd:PLN02939 129 QLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRlsetdaRIKLAAQEKIHVEILeEQLEKLRN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 482 KTQSDMAIVNNENNRMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLL 561
Cdd:PLN02939 209 ELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 562 QI----IETVKDEKLNLETTLQesTAARQImEREIENIQTYQSTaeENFLQEIKNAKSEASIYKNSLSEIgkecEMLSKM 637
Cdd:PLN02939 289 KLsplqYDCWWEKVENLQDLLD--RATNQV-EKAALVLDQNQDL--RDKVDKLEASLKEANVSKFSSYKV----ELLQQK 359
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1034639233 638 VMETKTDNQILKEELKKH---SQENIK-FENSISRLTED--KILLENYVRSIENE 686
Cdd:PLN02939 360 LKLLEERLQASDHEIHSYiqlYQESIKeFQDTLSKLKEEskKRSLEHPADDMPSE 414
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
333-710 |
2.02e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 333 KQGSIISENEKTSKVNSVTEQCVAKIQYLQnylkesvqiqKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKN 412
Cdd:pfam15921 449 QMAAIQGKNESLEKVSSLTAQLESTKEMLR----------KVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 413 LVEEKSTIQSKLSKTEEYSKEClKEFKKIISKYNVLQGQnktLEEKNIQLSLEKQQMmEALDQLKSKEHKT----QSDMA 488
Cdd:pfam15921 519 ITKLRSRVDLKLQELQHLKNEG-DHLRNVQTECEALKLQ---MAEKDKVIEILRQQI-ENMTQLVGQHGRTagamQVEKA 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 489 IVNNENNRMSIEMEAMKtnilLIQDEKEM----LEKKTHQLLKEKSSLGNELKESQLEIIQLKEkerlaktEQETLLQII 564
Cdd:pfam15921 594 QLEKEINDRRLELQEFK----ILKDKKDAkireLEARVSDLELEKVKLVNAGSERLRAVKDIKQ-------ERDQLLNEV 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 565 ETVKDEKLNLettlqesTAARQIMEREIENIQTYQSTAEENFLQEIKNAKSEASIYKNSLSE------------IGKECE 632
Cdd:pfam15921 663 KTSRNELNSL-------SEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdghamkvaMGMQKQ 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 633 MLSK--MVMETKTDNQILKEELKKHSQENikfensiSRLTEDKILLENYVRSIENERDTLEFEMRHLQREYLSLSDKICN 710
Cdd:pfam15921 736 ITAKrgQIDALQSKIQFLEEAMTNANKEK-------HFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAN 808
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
351-705 |
2.16e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.76 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 351 TEQCVAKIQYLQNYLKESVQIQKKVMELESE--NLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTE 428
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 429 EYSKEC------------------LKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKTQSD---- 486
Cdd:COG4717 167 ELEAELaelqeeleelleqlslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlk 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 487 ---------------MAIVNNENNRMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKE--- 548
Cdd:COG4717 247 earlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEElla 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 549 ----KERLAKTEQETLLQIIETVKDEKLNLETtlQESTAARQIMEREIENI-QTYQSTAEENF------LQEIKNAKSEA 617
Cdd:COG4717 327 alglPPDLSPEELLELLDRIEELQELLREAEE--LEEELQLEELEQEIAALlAEAGVEDEEELraaleqAEEYQELKEEL 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 618 SIYKNSLSEIGKECEMLSKMVMETKTDNQI---------LKEELKKHSQENIKFENSISRLTEDKILLEnyvrsIENERD 688
Cdd:COG4717 405 EELEEQLEELLGELEELLEALDEEELEEELeeleeeleeLEEELEELREELAELEAELEQLEEDGELAE-----LLQELE 479
|
410
....*....|....*..
gi 1034639233 689 TLEFEMRHLQREYLSLS 705
Cdd:COG4717 480 ELKAELRELAEEWAALK 496
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
365-614 |
4.58e-04 |
|
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: 43.26 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 365 LKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTEEYskeclkefKKIISK 444
Cdd:pfam15905 86 VQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQ--------KKMSSL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 445 YNVLQGQNKTLEEKNiQLSLEKQQMMEALDQLKSKeHKTQSDMAIVNNENNRMSIEMEamktnillIQDEKEMLEKKTHQ 524
Cdd:pfam15905 158 SMELMKLRNKLEAKM-KEVMAKQEGMEGKLQVTQK-NLEHSKGKVAQLEEKLVSTEKE--------KIEEKSETEKLLEY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 525 lLKEKSSLGNELKESQLEIIQLKEkerLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEE 604
Cdd:pfam15905 228 -ITELSCVSEQVEKYKLDIAQLEE---LLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQ 303
|
250
....*....|
gi 1034639233 605 NFLQEIKNAK 614
Cdd:pfam15905 304 TLNAELEELK 313
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
465-708 |
6.44e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.52 E-value: 6.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 465 EKQQMMEALDQLKSKEHKTQSDMAIVNNENNRMSIEME-AMKTNIL----------LIQDEKEMLEKKTHQLLKEKSSLG 533
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkAERYQALlkekreyegyELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 534 NELKESQLEIIQL-KEKERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEENFLQ---E 609
Cdd:TIGR02169 251 EELEKLTEEISELeKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKleaE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 610 IKNAKSEASIYKNSLSEIGKECEMLSKMVMETK--------------TDNQILKEELK-------KHSQENIKFENSISR 668
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeledlraeleevdKEFAETRDELKdyrekleKLKREINELKRELDR 410
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1034639233 669 LTEDKILLENYVRSIENERDTLEFEMRHLQREYLSLSDKI 708
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
511-700 |
9.13e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 511 IQDEKEmlEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMER 590
Cdd:COG1196 218 LKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 591 EIENIQtyqstAEENFLQE-IKNAKSEASIYKNSLSEIGKECEMLSKmvmETKTDNQILKEELKKHSQENIKFENSISRL 669
Cdd:COG1196 296 ELARLE-----QDIARLEErRRELEERLEELEEELAELEEELEELEE---ELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190
....*....|....*....|....*....|.
gi 1034639233 670 TEDKILLENYVRSIENERDTLEFEMRHLQRE 700
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
334-577 |
1.03e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.74 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 334 QGSIISENEKTSKVNSVTEQCVAKIQYLQ----NYLKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQ 409
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 410 LKNLVEEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSK----EHKTQS 485
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrselRRELEE 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 486 DMAIVNNENNRM------------------SIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGN----------ELK 537
Cdd:TIGR02168 920 LREKLAQLELRLeglevridnlqerlseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPvnlaaieeyeELK 999
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1034639233 538 ESQLEIiqLKEKERLAKTEqETLLQIIetvkdEKLNLETT 577
Cdd:TIGR02168 1000 ERYDFL--TAQKEDLTEAK-ETLEEAI-----EEIDREAR 1031
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
417-652 |
1.48e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 417 KSTIQS--KLSKTEEYSKECLKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHktqsdmaivnnen 494
Cdd:COG4717 36 KSTLLAfiRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEE------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 495 nrmsiEMEAMKTNILLIQDEKEMLEK--KTHQLLKEKSSLGNELKESQLEIIQLKEKERlaktEQETLLQIIETVKDEKL 572
Cdd:COG4717 103 -----ELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLE----ELRELEEELEELEAELA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 573 NLETTLQEstAARQIMEREIENIQTYQSTAEEnFLQEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQILKEEL 652
Cdd:COG4717 174 ELQEELEE--LLEQLSLATEEELQDLAEELEE-LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
524-705 |
1.48e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 41.28 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 524 QLLKEKSSLGNELKESQLEIIQLK-EKERLAKTEQETLLQIIETVKDeklnLETTLQESTAARQIMEREIENIQtyqsta 602
Cdd:pfam09787 51 ELRQERDLLREEIQKLRGQIQQLRtELQELEAQQQEEAESSREQLQE----LEEQLATERSARREAEAELERLQ------ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 603 eenflQEIKNAKSEASIYKNSLSEIGKECEmlskmVMETKTDNQILKEELKKHSQEniKFENSISRLTEDKILLENYVRS 682
Cdd:pfam09787 121 -----EELRYLEEELRRSKATLQSRIKDRE-----AEIEKLRNQLTSKSQSSSSQS--ELENRLHQLTETLIQKQTMLEA 188
|
170 180
....*....|....*....|...
gi 1034639233 683 IENERDTLEFEMRHLQREYLSLS 705
Cdd:pfam09787 189 LSTEKNSLVLQLERMEQQIKELQ 211
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
340-614 |
2.21e-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: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 340 ENEKTSKVNSVTEQCVAKIQYLQNYLKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNlveekst 419
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK------- 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 420 IQSKLSKTEeyskeclKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKTQSDMAIVNNENNRMSI 499
Cdd:TIGR04523 480 IKQNLEQKQ-------KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 500 EM--EAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETT 577
Cdd:TIGR04523 553 ELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSI 632
|
250 260 270
....*....|....*....|....*....|....*..
gi 1034639233 578 LQESTAARQIMEREIENIQTYQSTAEENFLQEIKNAK 614
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIK 669
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
506-708 |
3.32e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 506 TNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQESTAAR 585
Cdd:TIGR02168 670 SSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 586 QIMEREIEN----IQTYQSTAEENFL-------------QEIKNAKSEASIYKNSLSEIGKE--------------CEML 634
Cdd:TIGR02168 750 AQLSKELTEleaeIEELEERLEEAEEelaeaeaeieeleAQIEQLKEELKALREALDELRAEltllneeaanlrerLESL 829
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034639233 635 SKMVMETKTDNQILKEELKKHSQENIKFENSISRLTEDKILLENYVRSIENERDTLEFEMRHLQREYLSLSDKI 708
Cdd:TIGR02168 830 ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL 903
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
436-700 |
4.97e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 436 KEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKS--KEHKTQSDmaivnnennrmsiEMEAMKTNILLIQD 513
Cdd:PRK02224 199 KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEvlEEHEERRE-------------ELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 514 EKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQES----TAARQIME 589
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECrvaaQAHNEEAE 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 590 REIENIQTYQSTAEE------NFLQEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDnqilKEELKKHSQEnikFE 663
Cdd:PRK02224 346 SLREDADDLEERAEElreeaaELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD----LGNAEDFLEE---LR 418
|
250 260 270
....*....|....*....|....*....|....*..
gi 1034639233 664 NSISRLTEDKILLENyvrSIENERDTLEfEMRHLQRE 700
Cdd:PRK02224 419 EERDELREREAELEA---TLRTARERVE-EAEALLEA 451
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
371-630 |
5.71e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 40.44 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 371 IQKKVMELESENLNLKSKMkplifttQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQG 450
Cdd:TIGR02169 693 LQSELRRIENRLDELSQEL-------SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEA 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 451 QNKTLEEK--NIQLSLEKQQMMEALDQLKSKEHKTQSdmaiVNNENNRMSIEMEAMKTNILLIQDEKEMLEkkthqllKE 528
Cdd:TIGR02169 766 RIEELEEDlhKLEEALNDLEARLSHSRIPEIQAELSK----LEEEVSRIEARLREIEQKLNRLTLEKEYLE-------KE 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 529 KSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEENFLQ 608
Cdd:TIGR02169 835 IQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
250 260
....*....|....*....|....*
gi 1034639233 609 EIKNA---KSEASIYKNSLSEIGKE 630
Cdd:TIGR02169 915 KRKRLselKAKLEALEEELSEIEDP 939
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
341-701 |
5.77e-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: 40.42 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 341 NEKTSKVNSVTEQCVAKIQYLQNYLKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKSTI 420
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETL 773
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 421 QSKLSKTEEYSKECLKEfkkiISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKTQSDmaivnNENNRMSIE 500
Cdd:TIGR00606 774 LGTIMPEEESAKVCLTD----VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ-----HELDTVVSK 844
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 501 MEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQleiiQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQE 580
Cdd:TIGR00606 845 IELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQ----QFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEK 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 581 STAAR------------------QIMEREIENIQTYQSTAeENFLQE-----IKNAKSEASIYKNSLSEIGKECEMLSK- 636
Cdd:TIGR00606 921 DQQEKeelissketsnkkaqdkvNDIKEKVKNIHGYMKDI-ENKIQDgkddyLKQKETELNTVNAQLEECEKHQEKINEd 999
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034639233 637 -MVMETKTDNQILKEELKKHSQENIKFENSISRLTE-----DKILLENYVRSIENERDTLEFEMRHLQREY 701
Cdd:TIGR00606 1000 mRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEelkqhLKEMGQMQVLQMKQEHQKLEENIDLIKRNH 1070
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
453-594 |
5.92e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 453 KTLEEKNIQLSLEKQqmmEALDQLKSKEHKTQSDMaivNNENNRMSIEMEAMKTNIlliQDEKEMLEKKTHQLLKEKSSL 532
Cdd:PRK12704 42 RILEEAKKEAEAIKK---EALLEAKEEIHKLRNEF---EKELRERRNELQKLEKRL---LQKEENLDRKLELLEKREEEL 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034639233 533 GNELK--ESQLEIIQLKEKE--RLAKTEQETLLQIIETVKDE--KLNLETTLQESTAARQIMEREIEN 594
Cdd:PRK12704 113 EKKEKelEQKQQELEKKEEEleELIEEQLQELERISGLTAEEakEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
355-698 |
8.29e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 39.77 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 355 VAKIQYLQNYLKEsvqIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTEEyskec 434
Cdd:pfam01576 67 AARKQELEEILHE---LESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEE----- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 435 lkefkkiiskyNVLqgqnkTLEEKNIQLSLEKQQMMEAL----DQLKSKEHKTQSdMAIVNNENNRMSIEMEAMktnilL 510
Cdd:pfam01576 139 -----------DIL-----LLEDQNSKLSKERKLLEERIseftSNLAEEEEKAKS-LSKLKNKHEAMISDLEER-----L 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 511 IQDEK--EMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKerLAKTEQEtlLQiietvkdeklNLETTLQESTAARQIM 588
Cdd:pfam01576 197 KKEEKgrQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQ--LAKKEEE--LQ----------AALARLEEETAQKNNA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 589 EREIENIQTYQSTAEENFLQEiKNAKSEASIYKNSLSE-------------------------IGKECEMLSK-MVMETK 642
Cdd:pfam01576 263 LKKIRELEAQISELQEDLESE-RAARNKAEKQRRDLGEelealkteledtldttaaqqelrskREQEVTELKKaLEEETR 341
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034639233 643 TDNQILKEELKKHSQENIKFENSISRLTEDKILLENYVRSIENERDTLEFEMRHLQ 698
Cdd:pfam01576 342 SHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQ 397
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
465-694 |
8.86e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 465 EKQQMMEALDQL-KSKEHKTQSDMAivnnennRMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEI 543
Cdd:PRK02224 150 DRQDMIDDLLQLgKLEEYRERASDA-------RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEI 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 544 IQLKEKERLAKTEQETLLQIIETVKDEKLNLETtlqestaarqiMEREIENIQTYQSTAE---ENFLQEIKNAKSEASIY 620
Cdd:PRK02224 223 ERYEEQREQARETRDEADEVLEEHEERREELET-----------LEAEIEDLRETIAETErerEELAEEVRDLRERLEEL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034639233 621 KNSLSEIGKEC-------EMLSKMVMETKTDNQILKEELKKHSQENIKFENSISRLTEDKILLENYVRSIENERDTLEFE 693
Cdd:PRK02224 292 EEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE 371
|
.
gi 1034639233 694 M 694
Cdd:PRK02224 372 L 372
|
|
| |
