|
Name |
Accession |
Description |
Interval |
E-value |
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
436-771 |
2.81e-10 |
|
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: 63.89 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 436 KESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTE-EYSKECLKEF--KKII 512
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKnKLLKLELLLSnlKKKI 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 513 SKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKTQSDMAIVNNENNRMSIEM-----EAMKTNILLIQDEKEM 587
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLsekqkELEQNNKKIKELEKQL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 588 LEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQT 667
Cdd:TIGR04523 291 NQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 668 YQSTAE---ENFLQEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQILKEELKKHSQENIKFENSISRLTEDKI 744
Cdd:TIGR04523 371 EIEKLKkenQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
330 340
....*....|....*....|....*..
gi 22749515 745 LLENYVRSIENERDTLEFEMRHLQREY 771
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLKVLSRSI 477
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
407-727 |
2.03e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.61 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 407 IISENEKtsKVNSVTEQCVAKIQY--LQNYLKEsVQIQKKVMELESenlnLKSKMKPLIFTTQSLIQKVETYEKQLKNLV 484
Cdd:TIGR02168 194 ILNELER--QLKSLERQAEKAERYkeLKAELRE-LELALLVLRLEE----LREELEELQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 485 EEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQGQ-----------NKTLEEKNIQLSLEKQQMMEALDQLKSKEHKT 553
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQkqilrerlanlERQLEELEAQLEELESKLDELAEELAELEEKL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 554 QSDMAIVNNENNRMS---IEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELK--ESQLEIIQlkekERLAKTEQE 628
Cdd:TIGR02168 347 EELKEELESLEAELEeleAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIErlEARLERLE----DRRERLQQE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 629 TLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQtyqsTAEENFLQEIKNAKSEASIYKNSLSEIGKECEMLSKMV 708
Cdd:TIGR02168 423 IEELLKKLEEAELKELQAELEELEEELEELQEELERLE----EALEELREELEEAEQALDAAERELAQLQARLDSLERLQ 498
|
330
....*....|....*....
gi 22749515 709 METKTDNQILKEELKKHSQ 727
Cdd:TIGR02168 499 ENLEGFSEGVKALLKNQSG 517
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
427-796 |
2.07e-08 |
|
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: 57.81 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 427 KIQYL-QNYLKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVetyekqlkNLVEEKSTIQSK-LSKTEEYSKEC 504
Cdd:pfam05483 223 KIQHLeEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKA--------NQLEEKTKLQDEnLKELIEKKDHL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 505 LKEFKKIISKYNVLQGQNKTLEE------KNI-QLSLEKQQMMEALDQLKskehkTQSDMAIVNNENNRMSIEmEAMKTN 577
Cdd:pfam05483 295 TKELEDIKMSLQRSMSTQKALEEdlqiatKTIcQLTEEKEAQMEELNKAK-----AAHSFVVTEFEATTCSLE-ELLRTE 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 578 ILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAkTEQETLLQIIETVKDEKLNLETTLQESTAARQI 657
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIL-AEDEKLLDEKKQFEKIAEELKGKEQELIFLLQA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 658 MEREIENIQ---TYQSTAEENFLQEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQILKEELKKHSQENIKFEN 734
Cdd:pfam05483 448 REKEIHDLEiqlTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKK 527
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22749515 735 SISRLTEDKILLENYVRSIENERDTLEFEMRHLQREYLSLSDKicNQHNDPSKTTYISRREK 796
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDK--SEENARSIEYEVLKKEK 587
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
412-767 |
2.11e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 412 EKTSKVNSVTEQCVAKIQYLQNYLKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNL-------- 483
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELeekvkelk 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 484 -VEEKSTIQSKLSKTEEYSKECLKEFKKIISKY----NVLQGQNKTLEEKNI---QLSLEKQQMMEALDQLKSKEHKTQS 555
Cdd:PRK03918 287 eLKEKAEEYIKLSEFYEEYLDELREIEKRLSRLeeeiNGIEERIKELEEKEErleELKKKLKELEKRLEELEERHELYEE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 556 DMAIVNNENN----RMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKT-----E 626
Cdd:PRK03918 367 AKAKKEELERlkkrLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVcgrelT 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 627 QETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQS-----TAEENFLQEIKNAKSEASIY-KNSLSEIGKE 700
Cdd:PRK03918 447 EEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeselIKLKELAEQLKELEEKLKKYnLEELEKKAEE 526
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22749515 701 CEMLSKMVMETKTDNQILKEELKKhsqenikfensISRLTEDKILLENYVRSIENERDTLEFEMRHL 767
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKELEK-----------LEELKKKLAELEKKLDELEEELAELLKELEEL 582
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
435-674 |
1.24e-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: 52.38 E-value: 1.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 435 LKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKS--------TIQSKLSKTEEYSKECLK 506
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSIAEKER 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 507 EFK-------KIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKTQSDMAIVNNENNRMSIEMEAMKTNIL 579
Cdd:TIGR02169 316 ELEdaeerlaKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 580 LIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEK------------ERLAKTEQ--ETLLQIIETVKDEKLNLE 645
Cdd:TIGR02169 396 KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKineleeekedkaLEIKKQEWklEQLAADLSKYEQELYDLK 475
|
250 260
....*....|....*....|....*....
gi 22749515 646 TTLQESTAARQIMEREIENIQTYQSTAEE 674
Cdd:TIGR02169 476 EEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
570-778 |
1.59e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.86 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 570 EMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQ 649
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 650 ESTAARQIMEREIENIQTYQSTAEEnflqEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQILKEELKKHSQEN 729
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEE----ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 22749515 730 IKFENSISRLTEDKILLENYVRSIENERDTLEFEMRHLQREYLSLSDKI 778
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
462-674 |
1.72e-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: 51.30 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 462 LIFTTQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMME 541
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 542 ALDQLKSKEHKTQSDMAIVNNENNRMSIE-------------------------MEAMKTNILLIQDEKEMLEKKTHQLL 596
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22749515 597 KEKSSLGNELKESQLEIIQLKEkerlAKTEQETLLQIIETvkdEKLNLETTLQESTAARQIMEREIENIQTYQSTAEE 674
Cdd:COG4942 171 AERAELEALLAELEEERAALEA----LKAERQKLLARLEK---ELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
566-778 |
3.91e-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: 50.84 E-value: 3.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 566 RMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLE 645
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 646 TTLQESTAARQIMEREIENIQT-----YQSTAEEnFLQEIKNAKSEASIYKNSLSEIGKECE-----------MLSKMVM 709
Cdd:TIGR02169 758 SELKELEARIEELEEDLHKLEEalndlEARLSHS-RIPEIQAELSKLEEEVSRIEARLREIEqklnrltlekeYLEKEIQ 836
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22749515 710 ETKTDNQILKEELKKHSQE----NIKFENSISRLTEDKILLENYVRS---IENERDTLEFEMRHLQREYLSLSDKI 778
Cdd:TIGR02169 837 ELQEQRIDLKEQIKSIEKEienlNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQI 912
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
426-774 |
5.80e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 426 AKIQYLQNYLKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVE-----------------EKS 488
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElkeeieelekeleslegSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 489 TIQSKLSKTEEYSKECLKEFKKIISKYNVLQgQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKTQSDMAIVN---NENN 565
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEeriKELE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 566 RMSIEMEAMKTNILLIQDEKEMLEKKtHQLLKEKSSLGNEL-----KESQLEIIQLKEKERLAKTEQETLLQIIETVKDE 640
Cdd:PRK03918 335 EKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELerlkkRLTGLTPEKLEKELEELEKAKEEIEEEISKITAR 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 641 KLNLETTLQESTAA---------------RQIMEREIENIQTYQSTAEENFLQEIKNAKSEASIYKNSLSEIGKECEMLS 705
Cdd:PRK03918 414 IGELKKEIKELKKAieelkkakgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 706 KMVMETKTDNQI--LKEELKKHSQEN---------------IKFENSISRLTED---KILLENYVRSIENERDTLEFEMR 765
Cdd:PRK03918 494 ELIKLKELAEQLkeLEEKLKKYNLEElekkaeeyeklkeklIKLKGEIKSLKKElekLEELKKKLAELEKKLDELEEELA 573
|
....*....
gi 22749515 766 HLQREYLSL 774
Cdd:PRK03918 574 ELLKELEEL 582
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
431-778 |
1.08e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 431 LQNYLKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTEeysKECLKEFKK 510
Cdd:TIGR04523 206 LKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQ---KELEQNNKK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 511 IISKYNVLQGQNKTLEEKNIQLslEKQQMMEALDQLKSKEHK-TQSDMAIVNNENNrmsiemeamktnILLIQDEKEMLE 589
Cdd:TIGR04523 283 IKELEKQLNQLKSEISDLNNQK--EQDWNKELKSELKNQEKKlEEIQNQISQNNKI------------ISQLNEQISQLK 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 590 KKTHQLLKEKSSLGNELKESQLEIIQLKEkerlaktEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQ 669
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKK-------ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 670 STAEENFL----------QEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQILKEELKKHSQENIKFENSISRL 739
Cdd:TIGR04523 422 ELLEKEIErlketiiknnSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
330 340 350
....*....|....*....|....*....|....*....
gi 22749515 740 TEDKILLENYVRSIENERDTLEFEMRHLQREYLSLSDKI 778
Cdd:TIGR04523 502 NEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
477-693 |
5.03e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 477 EKQLKNLVEEKSTIQSKLSKTEEyskeclkEFKKIISKYNVLQGQNKTLEEkniqlslEKQQMMEALDQLKSKEHKTQSD 556
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEALQA-------EIDKLQAEIAEAEAEIEERREE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 557 M------------------AIVNNEN--------NRMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKsslgNELKESQ 610
Cdd:COG3883 88 LgeraralyrsggsvsyldVLLGSESfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKL----AELEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 611 LEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEENFLQEIKNAKSEASIY 690
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
...
gi 22749515 691 KNS 693
Cdd:COG3883 244 ASA 246
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
295-686 |
5.14e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 295 KEENLDgNLNEDIKSKRISELEALVKKLLPFRETVSKFHVHFCRKCKKLsKSEMHRGKKN----EKNNKEIPITGKNITD 370
Cdd:PRK03918 370 KKEELE-RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL-KKEIKELKKAieelKKAKGKCPVCGRELTE 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 371 LKFHSRVPRYT--LSFLDQTKHEMKDKERQ--PFLVKQGSIISENEKTSKVNSVTEQCVAKIQYLQNYLKESVQ------ 440
Cdd:PRK03918 448 EHRKELLEEYTaeLKRIEKELKEIEEKERKlrKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEkkaeey 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 441 --IQKKVMELESENLNLKSKMKPLifttQSLIQKVETYEKQLKNLVEEKSTIQSKLS----KTEEYSKECLKEFKKIISK 514
Cdd:PRK03918 528 ekLKEKLIKLKGEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKELEelgfESVEELEERLKELEPFYNE 603
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 515 YNVLQGQNKTLEEKniqlslekqqmMEALDQLKSKEHKTQSDMAIVNNENNRMSIEMEAMKTNilLIQDEKEMLEKKTHQ 594
Cdd:PRK03918 604 YLELKDAEKELERE-----------EKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK--YSEEEYEELREEYLE 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 595 LLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETllqiIETVKDEKLNLETtlqestaARQIMEREIENIQTYQSTAEE 674
Cdd:PRK03918 671 LSRELAGLRAELEELEKRREEIKKTLEKLKEELEE----REKAKKELEKLEK-------ALERVEELREKVKKYKALLKE 739
|
410
....*....|..
gi 22749515 675 NFLQEIKNAKSE 686
Cdd:PRK03918 740 RALSKVGEIASE 751
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
474-741 |
5.18e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 5.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 474 ETYEKQLKNLVEEKSTIQSKLSKTEEYSKECLKEFKKI--ISKYNVLQGQNKTLEEKNIQLSLEK-QQMMEALDQLKSKE 550
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKEseLIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKL 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 551 HKTQSDMAIVNNENNRMsiemEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNE-LKESQLEIIQL----KEKERLAKT 625
Cdd:PRK03918 535 IKLKGEIKSLKKELEKL----EELKKKLAELEKKLDELEEELAELLKELEELGFEsVEELEERLKELepfyNEYLELKDA 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 626 EQEtllqiIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEENFLQE-IKNAKSEASIYKNSLSEIGKECEML 704
Cdd:PRK03918 611 EKE-----LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEeYEELREEYLELSRELAGLRAELEEL 685
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 22749515 705 SKMVMETKTDNQILKEEL---KKHSQENIKFENSISRLTE 741
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 ... |
474-778 |
1.20e-04 |
|
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: 45.73 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 474 ETYEKQLKNLVEEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKT 553
Cdd:pfam02463 211 EYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 554 QSDMAIVNNENNRMSIEMEAMKTNIL-LIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQ 632
Cdd:pfam02463 291 LAKEEEELKSELLKLERRKVDDEEKLkESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQ 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 633 IIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEENFLQEIKNAKSEASIYKNSLSEIGKECEMLSkmvmETK 712
Cdd:pfam02463 371 LEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQ----GKL 446
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22749515 713 TDNQILKEELKKHSQENIKFENSISRLTEDKILLENYVRSIENERDTLEFEMRHLQREYLSLSDKI 778
Cdd:pfam02463 447 TEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVL 512
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
467-687 |
2.21e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.93 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 467 QSLIQKVETYEKQLKNLVEEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQL 546
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 547 KSKEHKTQSDMAIVNNENNRMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEK------- 619
Cdd:COG1196 329 EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQleeleea 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 22749515 620 -----ERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEENFLQEIKNAKSEA 687
Cdd:COG1196 409 eeallERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
479-756 |
2.69e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.89 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 479 QLKNLVEEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQGQNKTLEEK------NIQLSLEKQQMMEAL-DQLKSKEH 551
Cdd:PLN02939 129 QLEDLVGMIQNAEKNILLLNQARLQALEDLEKILTEKEALQGKINILEMRlsetdaRIKLAAQEKIHVEILeEQLEKLRN 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 552 KTQSDMAIVNNENNRMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLL 631
Cdd:PLN02939 209 ELLIRGATEGLCVHSLSKELDVLKEENMLLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLRELESKFIVAQEDVS 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 632 QI----IETVKDEKLNLETTLQesTAARQImEREIENIQTYQSTaeENFLQEIKNAKSEASIYKNSLSEIgkecEMLSKM 707
Cdd:PLN02939 289 KLsplqYDCWWEKVENLQDLLD--RATNQV-EKAALVLDQNQDL--RDKVDKLEASLKEANVSKFSSYKV----ELLQQK 359
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 22749515 708 VMETKTDNQILKEELKKH---SQENIK-FENSISRLTED--KILLENYVRSIENE 756
Cdd:PLN02939 360 LKLLEERLQASDHEIHSYiqlYQESIKeFQDTLSKLKEEskKRSLEHPADDMPSE 414
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
390-776 |
2.89e-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: 44.72 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 390 HEMKDKERQPFLVKQGSIISENEKTSKVNSVTEQCVAKIQYLQNYLK-ESVQIQKKVMELESENLNLKSKMKPLIFTTQS 468
Cdd:pfam15921 263 QQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARnQNSMYMRQLSDLESTVSQLRSELREAKRMYED 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 469 LIQKVEtyekqlKNLVEEKSTIQSKLSKTEEYSKEC----------LKEFKKIISKYNVLQGQNKTLEEKNIQLS----- 533
Cdd:pfam15921 343 KIEELE------KQLVLANSELTEARTERDQFSQESgnlddqlqklLADLHKREKELSLEKEQNKRLWDRDTGNSitidh 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 534 ---------LEKQQMMEALDQLKSK-EHKTQSDMAIVNNENNrmsiEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLG 603
Cdd:pfam15921 417 lrrelddrnMEVQRLEALLKAMKSEcQGQMERQMAAIQGKNE----SLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLE 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 604 NELKESQLEIIQLKEKERLAKTEQETL----------LQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQstae 673
Cdd:pfam15921 493 SSERTVSDLTASLQEKERAIEATNAEItklrsrvdlkLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILR---- 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 674 enflQEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQILKEELKKHSQENIKFENSISRLTEDKILLEN----- 748
Cdd:pfam15921 569 ----QQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNagser 644
|
410 420 430
....*....|....*....|....*....|
gi 22749515 749 --YVRSIENERDTLEFEMRHLQREYLSLSD 776
Cdd:pfam15921 645 lrAVKDIKQERDQLLNEVKTSRNELNSLSE 674
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
403-780 |
1.07e-03 |
|
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: 42.80 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 403 KQGSIISENEKTSKVNSVTEQCVAKIQYLQnylkesvqiqKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKN 482
Cdd:pfam15921 449 QMAAIQGKNESLEKVSSLTAQLESTKEMLR----------KVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAE 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 483 LVEEKSTIQSKLSKTEEYSKEClKEFKKIISKYNVLQGQnktLEEKNIQLSLEKQQMmEALDQLKSKEHKT----QSDMA 558
Cdd:pfam15921 519 ITKLRSRVDLKLQELQHLKNEG-DHLRNVQTECEALKLQ---MAEKDKVIEILRQQI-ENMTQLVGQHGRTagamQVEKA 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 559 IVNNENNRMSIEMEAMKtnilLIQDEKEM----LEKKTHQLLKEKSSLGNELKESQLEIIQLKEkerlaktEQETLLQII 634
Cdd:pfam15921 594 QLEKEINDRRLELQEFK----ILKDKKDAkireLEARVSDLELEKVKLVNAGSERLRAVKDIKQ-------ERDQLLNEV 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 635 ETVKDEKLNLettlqesTAARQIMEREIENIQTYQSTAEENFLQEIKNAKSEASIYKNSLSE------------IGKECE 702
Cdd:pfam15921 663 KTSRNELNSL-------SEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSmegsdghamkvaMGMQKQ 735
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 703 MLSK--MVMETKTDNQILKEELKKHSQENikfensiSRLTEDKILLENYVRSIENERDTLEFEMRHLQREYLSLSDKICN 780
Cdd:pfam15921 736 ITAKrgQIDALQSKIQFLEEAMTNANKEK-------HFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAN 808
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
436-697 |
1.14e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 436 KESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTEEYSKECLKEFKKIISKY 515
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKER 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 516 NVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKTQSDMAIVNNENNRMSIEMEAMKTNILLIQDEKEMLEKKTHQL 595
Cdd:COG4372 125 QDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 596 LKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEEN 675
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
250 260
....*....|....*....|..
gi 22749515 676 FLQEIKNAKSEASIYKNSLSEI 697
Cdd:COG4372 285 LEALEEAALELKLLALLLNLAA 306
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
411-770 |
1.40e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 411 NEKTSKVNSVTEQcVAKIQYLQNYLKESVQIQKKVMELESENLNLKSKMKPLifTTQSLIQKVETYEKQLKNLVEEKSTI 490
Cdd:PRK03918 334 EEKEERLEELKKK-LKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGL--TPEKLEKELEELEKAKEEIEEEISKI 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 491 QSKLSKTEEYSKE---CLKEFKKIISKYNVLQGQNKTLEEKNI--QLSLEKQQMMEALDQLKSKEHKTQSDMAIVNNENN 565
Cdd:PRK03918 411 TARIGELKKEIKElkkAIEELKKAKGKCPVCGRELTEEHRKELleEYTAELKRIEKELKEIEEKERKLRKELRELEKVLK 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 566 RMSiEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQL----EIIQLK---EKERLAKTEQETLLQIIETVK 638
Cdd:PRK03918 491 KES-ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIklkgEIKSLKkelEKLEELKKKLAELEKKLDELE 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 639 DEKLNLETTLQE-STAARQIMEREIENIQTYQstaeeNFLQEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQI 717
Cdd:PRK03918 570 EELAELLKELEElGFESVEELEERLKELEPFY-----NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEE 644
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 22749515 718 LKEEL----KKHSQENIK-FENSISRLTEDKILLENYVRSIENERDTLEFEMRHLQRE 770
Cdd:PRK03918 645 LRKELeeleKKYSEEEYEeLREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
435-662 |
1.45e-03 |
|
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: 42.19 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 435 LKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTEEYSKECLKEFkkiisk 514
Cdd:pfam07888 121 LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEF------ 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 515 ynvlQGQNKTLEEKNIQLslekQQMMEALDQLKSKEhktqsdmaivnNENNRMSIEMEAMKTNILLIQDEKEMLEKKTHQ 594
Cdd:pfam07888 195 ----QELRNSLAQRDTQV----LQLQDTITTLTQKL-----------TTAHRKEAENEALLEELRSLQERLNASERKVEG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 595 LLKEKSSLGN-------ELKESQLEIIQL------------KEKERLAKtEQETLLQIIETVKD--EKLN-----LETTL 648
Cdd:pfam07888 256 LGEELSSMAAqrdrtqaELHQARLQAAQLtlqladaslalrEGRARWAQ-ERETLQQSAEADKDriEKLSaelqrLEERL 334
|
250
....*....|....
gi 22749515 649 QESTAARQIMEREI 662
Cdd:pfam07888 335 QEERMEREKLEVEL 348
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
435-684 |
2.31e-03 |
|
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: 40.95 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 435 LKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTEEYskeclkefKKIISK 514
Cdd:pfam15905 86 VQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAKFSEDGTQ--------KKMSSL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 515 YNVLQGQNKTLEEKNiQLSLEKQQMMEALDQLKSKeHKTQSDMAIVNNENNRMSIEMEamktnillIQDEKEMLEKKTHQ 594
Cdd:pfam15905 158 SMELMKLRNKLEAKM-KEVMAKQEGMEGKLQVTQK-NLEHSKGKVAQLEEKLVSTEKE--------KIEEKSETEKLLEY 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 595 lLKEKSSLGNELKESQLEIIQLKEkerLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEE 674
Cdd:pfam15905 228 -ITELSCVSEQVEKYKLDIAQLEE---LLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQ 303
|
250
....*....|
gi 22749515 675 NFLQEIKNAK 684
Cdd:pfam15905 304 TLNAELEELK 313
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
581-770 |
2.64e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.46 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 581 IQDEKEmlEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMER 660
Cdd:COG1196 218 LKEELK--ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 661 EIENIQtyqstAEENFLQE-IKNAKSEASIYKNSLSEIGKECEMLSKmvmETKTDNQILKEELKKHSQENIKFENSISRL 739
Cdd:COG1196 296 ELARLE-----QDIARLEErRRELEERLEELEEELAELEEELEELEE---ELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
170 180 190
....*....|....*....|....*....|.
gi 22749515 740 TEDKILLENYVRSIENERDTLEFEMRHLQRE 770
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
421-775 |
2.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 421 TEQCVAKIQYLQNYLKESVQIQKKVMELESE--NLNLKSKMKPLIFTTQSLIQKVETYEKQLKNLVEEKSTIQSKLSKTE 498
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREEleKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 499 EYSKEC------------------LKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKTQSD---- 556
Cdd:COG4717 167 ELEAELaelqeeleelleqlslatEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEerlk 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 557 ---------------MAIVNNENNRMSIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKE--- 618
Cdd:COG4717 247 earlllliaaallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEElla 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 619 ----KERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREiENIQTYQSTAEENF------LQEIKNAKSEAS 688
Cdd:COG4717 327 alglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELraaleqAEEYQELKEELE 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 689 IYKNSLSEIGKECEMLSKMVMETKTDNQI---------LKEELKKHSQENIKFENSISRLTEDKILLEnyvrsIENERDT 759
Cdd:COG4717 406 ELEEQLEELLGELEELLEALDEEELEEELeeleeeleeLEEELEELREELAELEAELEQLEEDGELAE-----LLQELEE 480
|
410
....*....|....*.
gi 22749515 760 LEFEMRHLQREYLSLS 775
Cdd:COG4717 481 LKAELRELAEEWAALK 496
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
535-778 |
3.10e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.21 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 535 EKQQMMEALDQLKSKEHKTQSDMAIVNNENNRMSIEME-AMKTNIL----------LIQDEKEMLEKKTHQLLKEKSSLG 603
Cdd:TIGR02169 171 KKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREkAERYQALlkekreyegyELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 604 NELKESQLEIIQL-KEKERLAKTEQETLLQIIETVKDEKLNLETTLQESTAARQIMEREIENIQTYQSTAEENFLQ---E 679
Cdd:TIGR02169 251 EELEKLTEEISELeKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKleaE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 680 IKNAKSEASIYKNSLSEIGKECEMLSKMVMETK--------------TDNQILKEELK-------KHSQENIKFENSISR 738
Cdd:TIGR02169 331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKeeledlraeleevdKEFAETRDELKdyrekleKLKREINELKRELDR 410
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 22749515 739 LTEDKILLENYVRSIENERDTLEFEMRHLQREYLSLSDKI 778
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEI 450
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
404-640 |
4.28e-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: 40.81 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 404 QGSIISENEKTSKVNSVTEQCVAKIQYLQ----NYLKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQ 479
Cdd:TIGR02168 760 EAEIEELEERLEEAEEELAEAEAEIEELEaqieQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR 839
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 480 LKNLVEEKSTIQSKLSKTEEYSKECLKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSK----EHKTQS 555
Cdd:TIGR02168 840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKrselRRELEE 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 556 DMAIVNNENNRM------------------SIEMEAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGN----------ELK 607
Cdd:TIGR02168 920 LREKLAQLELRLeglevridnlqerlseeySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPvnlaaieeyeELK 999
|
250 260 270
....*....|....*....|....*....|...
gi 22749515 608 ESQLEIiqLKEKERLAKTEqETLLQIIETVKDE 640
Cdd:TIGR02168 1000 ERYDFL--TAQKEDLTEAK-ETLEEAIEEIDRE 1029
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
594-775 |
4.48e-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: 40.13 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 594 QLLKEKSSLGNELKESQLEIIQLK-EKERLAKTEQETLLQIIETVKDeklnLETTLQESTAARQIMEREIENIQtyqsta 672
Cdd:pfam09787 51 ELRQERDLLREEIQKLRGQIQQLRtELQELEAQQQEEAESSREQLQE----LEEQLATERSARREAEAELERLQ------ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 673 eenflQEIKNAKSEASIYKNSLSEIGKECEmlskmVMETKTDNQILKEELKKHSQEniKFENSISRLTEDKILLENYVRS 752
Cdd:pfam09787 121 -----EELRYLEEELRRSKATLQSRIKDRE-----AEIEKLRNQLTSKSQSSSSQS--ELENRLHQLTETLIQKQTMLEA 188
|
170 180
....*....|....*....|...
gi 22749515 753 IENERDTLEFEMRHLQREYLSLS 775
Cdd:pfam09787 189 LSTEKNSLVLQLERMEQQIKELQ 211
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
410-684 |
6.58e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 40.00 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 410 ENEKTSKVNSVTEQCVAKIQYLQNYLKESVQIQKKVMELESENLNLKSKMKPLIFTTQSLIQKVETYEKQLKNlveekst 489
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK------- 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 490 IQSKLSKTEeyskeclKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHKTQSDMAIVNNENNRMSI 569
Cdd:TIGR04523 480 IKQNLEQKQ-------KELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDF 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 570 EM--EAMKTNILLIQDEKEMLEKKTHQLLKEKSSLGNELKESQLEIIQLKEKERLAKTEQETLLQIIETVKDEKLNLETT 647
Cdd:TIGR04523 553 ELkkENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSI 632
|
250 260 270
....*....|....*....|....*....|....*..
gi 22749515 648 LQESTAARQIMEREIENIQTYQSTAEENFLQEIKNAK 684
Cdd:TIGR04523 633 IKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIK 669
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
487-722 |
9.15e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 9.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 487 KSTIQS--KLSKTEEYSKECLKEFKKIISKYNVLQGQNKTLEEKNIQLSLEKQQMMEALDQLKSKEHktqsdmaivnnen 564
Cdd:COG4717 36 KSTLLAfiRAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEE------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 565 nrmsiEMEAMKTNILLIQDEKEMLEK--KTHQLLKEKSSLGNELKESQLEIIQLKEKERlaktEQETLLQIIETVKDEKL 642
Cdd:COG4717 103 -----ELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEERLE----ELRELEEELEELEAELA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749515 643 NLETTLQEstAARQIMEREIENIQTYQSTAEEnFLQEIKNAKSEASIYKNSLSEIGKECEMLSKMVMETKTDNQILKEEL 722
Cdd:COG4717 174 ELQEELEE--LLEQLSLATEEELQDLAEELEE-LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARL 250
|
|
| |
