|
Name |
Accession |
Description |
Interval |
E-value |
| CCDC73 |
pfam15818 |
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ... |
27-1060 |
0e+00 |
|
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.
Pssm-ID: 464893 [Multi-domain] Cd Length: 1048 Bit Score: 1526.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 27 QLLDFRTSLLEALEELRMRRKAETQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAMGVLKNQLQMKMYALEEEK 106
Cdd:pfam15818 1 QLLDFKTSLLEALEELRMRREAETQYEEQIGKIIVETQELKWQKETLQNQKETLAKQHKEAMAVFKKQLQMKMCALEEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 107 GKYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYYAAITNQFGLVRENHVKL 186
Cdd:pfam15818 81 GKYQLATEIKEKEIEGLKETLKALQVSKYSLQKKVSEMEQKLQLHLLAKEDHHKQLNEIEKYYATITGQFGLVKENHGKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 187 EQNVQEAIQLNKRLSTLNEKQESEIHSLKKELKKAASELIKSKVTCQHKMEEESIDLIIKEQKYEELQERLNMELEVNKK 266
Cdd:pfam15818 161 EQNVQEAIQLNKRLSALNKKQESEICSLKKELKKVTSDLIKSKVTCQYKMGEENINLTIKEQKFQELQERLNMELELNKK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 267 INEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEKEHERALG 346
Cdd:pfam15818 241 INEEITHIQEEKQDIIISFQHMQQLLQQQTQANTEMEAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKALG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 347 TWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEEYKKFQNVPELNNENSdELTRKKSENIITQKYNSGP 426
Cdd:pfam15818 321 TWKKHVEELNGEINEIKNELSSLKETHIKLQEHYNKLCNQKKFEEDKKFQNVPEVNNENS-EMSTEKSENLIIQKYNSEQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 427 EIWGKNTKSFCLDTEYRE-EEKKDLPVGKT-AEDLQPFEISAKSEINTMVSQDRHQSGMSPHRVLCLDKNATDQEQTSDV 504
Cdd:pfam15818 400 EIREENTKSFCSDTEYREtEKKKGPPVEEIiIEDLQVLEKSFKNEIDTSVPQDKNQSEISLSKTLCTDKDLISQGQTLNV 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 505 TDSRKSVTVEVKDKLCLEKASGCSEFKSLNNFFLVVDESLETEMVRLEGTEGLGILHSggDIPLDTRSNKASSNGMSNEM 584
Cdd:pfam15818 480 TDFRKSVTTEIKDKLCLEKDNGCSEFKSPNNLFLVADQSIETEKIHLESTEGLGLHHA--DIHLETESNRSSFNGTLNEM 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 585 AHKRNFNTDGSESNPFKQQSKLLPADLENATEKEITNQDQTKAGLDSFLDIKLNLDPCKKHGLQDSSHVTLDVKHQKIKQ 664
Cdd:pfam15818 558 AHNTNHNKDVSENEPFKQQFRLLLCTQENATEKRITNSDQTKAGLDSSLDVKKNPVQCQKYSLQDSSNVSLDDKQCKIEQ 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 665 TVREESQCSTEP----RSCYQLASKAPQKPGGTIACAVVS--PLGPSASSDNKLTALKKSENSINTLPTAAKPAPSPAER 738
Cdd:pfam15818 638 LLNKKSECSTLPlkqtSSFQQLCNDTSEKPGLTIPCDTVVshPISPAAFSDNLKADLKNSDNNVNIMPMLVKPNSSPGKR 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 739 TTRTNTNDIQNSSLRNHLGASESSVSVSDFQVNQGDSHTSQAKGLKTVVSLTTSSEKQPPS------ESQITETPKSGLF 812
Cdd:pfam15818 718 TTRKNLDDMQSSQFKNCLGGLENGVTISHLQVNNENSHASQAKDLKTAVHPKTSTEIQFSSkesqidENQITEATKNDLF 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 813 SLVDVTGRQCMWLNNRDKTEALNGILSGGTCLEGQLEEAHLSPATPSADSVSTSARSAFDLPSPD-KPEKTPGYIKFVPP 891
Cdd:pfam15818 798 LLVNVNERQHTLLNNTEKTESLNDIVSGKIYSEGQLEESHSFHIKPSGDLVNRSGRSAFDLSTSDkKTEKTPVYLNFLDP 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 892 SPWPKVNQT--KTVGTATPSIPLFLKEKTVDLSGSRVTTPVTFCKNVVLDDTRKNIESDPTSNSRAADTVSNWSIHLDPK 969
Cdd:pfam15818 878 SPWSKVNQTegQTVSTSTSSIPLLLKEKPIGPSENTKIISVTLCKNVGVDDVRKDIGPDTTSISRVADTLNNSSIHPDPK 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 970 GQPREERNATAQTVYDSSFPTEHVKAEPLISTVQQSHSQTVKVTDSPDPLTFSPGNNDWQSLVMNRLTEIEKLLSLESDN 1049
Cdd:pfam15818 958 GEPSEERNATAKTFYDSSFPTEHVKTEPLKSTVLQSHFQTVKIKDSPDLLKSSPGEDDWQSLITNQITEIEKLLSLENDN 1037
|
1050
....*....|.
gi 148695785 1050 QPKRRKVEEML 1060
Cdd:pfam15818 1038 QPKKRKAEEML 1048
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
26-366 |
1.19e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 69.32 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 26 IQLLDFRTSLLEALEELRMRRKAETQYEEqiakiiLETQELKWQKEALQNQKEALiKQHKEAMGVLKNQLQMKMYALEEE 105
Cdd:TIGR02168 189 DRLEDILNELERQLKSLERQAEKAERYKE------LKAELRELELALLVLRLEEL-REELEELQEELKEAEEELEELTAE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 106 KGKYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYyaaitnqfglvrenhvk 185
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ----------------- 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 186 LEQNVQEAIQLNKRLSTLNEKQES---EIHSLKKELKKAASELikskvtcqHKMEEESIDLiikEQKYEELQERLNMELE 262
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEElkeELESLEAELEELEAEL--------EELESRLEEL---EEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 263 VNKKINEEITHIQEEKQDIiisfQHMQQLLQQETQAN----------------TEIDAELKVLRENNQTLERDNELQREK 326
Cdd:TIGR02168 394 QIASLNNEIERLEARLERL----EDRRERLQQEIEELlkkleeaelkelqaelEELEEELEELQEELERLEEALEELREE 469
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 148695785 327 VKENEEKFLSLEKEHERA---LGTWKKHVEELSGEMNGIKNEL 366
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALL 512
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
34-415 |
1.31e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 34 SLLEALEELRMRRKAETQYEEQIAKIILETQELKWQKEALqnqkealikqhkEAMGVLKNQLQMKMYALEEEKGKYK-LA 112
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY------------IKLSEFYEEYLDELREIEKRLSRLEeEI 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 113 TEIKE--KEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEdyhkQLNEIEKYYAAITnqfGLVRENHVKLEQNV 190
Cdd:PRK03918 324 NGIEEriKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA----KKEELERLKKRLT---GLTPEKLEKELEEL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 191 QEA-IQLNKRLSTLNEKQeSEIHSLKKELKKAASELIKSKVTCQHKMEEesidliIKEQKYEELQERLNMELevnKKINE 269
Cdd:PRK03918 397 EKAkEEIEEEISKITARI-GELKKEIKELKKAIEELKKAKGKCPVCGRE------LTEEHRKELLEEYTAEL---KRIEK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 270 EITHIQEEKQDIIISFQHMQQLLQQETqantEIDAELKVLRENNQTLERDNELQREKVKENEEKFlslekeheralgtwk 349
Cdd:PRK03918 467 ELKEIEEKERKLRKELRELEKVLKKES----ELIKLKELAEQLKELEEKLKKYNLEELEKKAEEY--------------- 527
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148695785 350 khvEELSGEMNGIKNELSSLRETHAKLQEHYNKLCE-----QKKTEEYKKFQN-VPELNNENSDELTRKKSE 415
Cdd:PRK03918 528 ---EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAElekklDELEEELAELLKeLEELGFESVEELEERLKE 596
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
37-418 |
1.46e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 68.94 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 37 EALEELRMRRKAETQYEEQIAKIILETQELKWQKEALQNQKEALiKQHKEAMGVLKNQLQmkmyalEEEKG----KYKLA 112
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEEL-KKAKGKCPVCGRELT------EEHRKelleEYTAE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 113 TEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKedyhkQLNEIEKYYAAItnqfglvreNHVKLEQNVQE 192
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-----QLKELEEKLKKY---------NLEELEKKAEE 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 193 AIQLNKRLSTLnekqESEIHSLKKELKKAAsELIKSKVTCQHKM---EEESIDLI--IKEQKYEELQErLNMELEVNKKI 267
Cdd:PRK03918 527 YEKLKEKLIKL----KGEIKSLKKELEKLE-ELKKKLAELEKKLdelEEELAELLkeLEELGFESVEE-LEERLKELEPF 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 268 NEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLErdnELQR----EKVKENEEKFLSLEKEHER 343
Cdd:PRK03918 601 YNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE---ELEKkyseEEYEELREEYLELSRELAG 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 344 A---LGTWKKHVEELS----------GEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEEYKKFQNVPELNNENSDELT 410
Cdd:PRK03918 678 LraeLEELEKRREEIKktleklkeelEEREKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFEELT 757
|
....*...
gi 148695785 411 RKKSENII 418
Cdd:PRK03918 758 EGKYSGVR 765
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
36-346 |
1.99e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 68.42 E-value: 1.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 36 LEALEelRMRRKAET----QYEEQIAKIILETQELKWQKEALQnQKEALIKQHKEAMGVLKNQLQmkmyALEEEKGKYKL 111
Cdd:COG1196 202 LEPLE--RQAEKAERyrelKEELKELEAELLLLKLRELEAELE-ELEAELEELEAELEELEAELA----ELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 112 ATEIKEKEIEGLKETLktlqvsqYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKyyaaitnqfglvrenhvKLEQNVQ 191
Cdd:COG1196 275 ELEELELELEEAQAEE-------YELLAELARLEQDIARLEERRRELEERLEELEE-----------------ELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 192 EAIQLNKRLSTLNEKQ---ESEIHSLKKELKKAASELIKSKVTCQHKMEEEsidliikEQKYEELQERLNMELEVNKKIN 268
Cdd:COG1196 331 ELEELEEELEELEEELeeaEEELEEAEAELAEAEEALLEAEAELAEAEEEL-------EELAEELLEALRAAAELAAQLE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 269 EEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQ---REKVKENEEKFLSLEKEHERAL 345
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEealLELLAELLEEAALLEAALAELL 483
|
.
gi 148695785 346 G 346
Cdd:COG1196 484 E 484
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
38-377 |
7.07e-11 |
|
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: 66.63 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 38 ALEELRmrrkaetQYEEQIAKIILETQELKWQKEALQNQKEALIKQHkeamgvlknqlqmkmyALEEEKGKYKL-----A 112
Cdd:TIGR02169 175 ALEELE-------EVEENIERLDLIIDEKRQQLERLRREREKAERYQ----------------ALLKEKREYEGyellkE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 113 TEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHlyhlAKEDYHKQLN-EIEKY----YAAITNQFGLVRENHVKLE 187
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLE----EIEQLLEELNkKIKDLgeeeQLRVKEKIGELEAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 188 QNVQEAIQLNKRLSTLNEKQESEIHSLKKELKKAASELIKSKVTCQHKMEEesidLIIKEQKYEELQERLNmELEVN--- 264
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEE----YAELKEELEDLRAELE-EVDKEfae 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 265 -----KKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEK 339
Cdd:TIGR02169 383 trdelKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAA 462
|
330 340 350
....*....|....*....|....*....|....*...
gi 148695785 340 EheraLGTWKKHVEELSGEMNGIKNELSSLRETHAKLQ 377
Cdd:TIGR02169 463 D----LSKYEQELYDLKEEYDRVEKELSKLQRELAEAE 496
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
27-384 |
3.00e-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: 64.69 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 27 QLLDFRTSLLEALEELRMRRKAETQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAMGVLKnQLQMKMYALEEEK 106
Cdd:TIGR02168 720 ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEEL 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 107 GKYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQkaHLYHLAKEdyHKQLNE-IEKYYAAITNQFGLVRENHVK 185
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEAANLRERLESLERRIAATER--RLEDLEEQ--IEELSEdIESLAAEIEELEELIEELESE 874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 186 LEQNVQEAIQLNKRLSTLNEKQESEIHSLKkELKKAASELIKSKVTCQHKMEEESIDLIIKEQKYEELQERLNMELEVNk 265
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELR-ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT- 952
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 266 kineeithiqeekqdiiisFQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEKEHE--- 342
Cdd:TIGR02168 953 -------------------LEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEdlt 1013
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 148695785 343 RALGTWKKHVEELSGEMngikneLSSLRETHAKLQEHYNKLC 384
Cdd:TIGR02168 1014 EAKETLEEAIEEIDREA------RERFKDTFDQVNENFQRVF 1049
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
114-381 |
4.32e-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: 64.31 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 114 EIKE--KEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYYAAITNQFGLVRENHVKLEQNVQ 191
Cdd:TIGR02168 678 EIEEleEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 192 EAIQ----LNKRLSTLNEK---QESEIHSLKKELKKAASEL--IKSKVTCQHK-MEEESIDLIIKEQKYEELQERLNMEL 261
Cdd:TIGR02168 758 ELEAeieeLEERLEEAEEElaeAEAEIEELEAQIEQLKEELkaLREALDELRAeLTLLNEEAANLRERLESLERRIAATE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 262 EVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEKEH 341
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 148695785 342 ERAlgtwKKHVEELSGEMNGIKNELSSLREthaKLQEHYN 381
Cdd:TIGR02168 918 EEL----REKLAQLELRLEGLEVRIDNLQE---RLSEEYS 950
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
137-415 |
1.19e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 137 LQKKVSEMEQKAHLyhLAKEDYHKQLNEIEKYYAAITNQfglVRENHVKLEQNVQEAIQLNKRLSTLNEK----QESEIH 212
Cdd:TIGR02169 216 LLKEKREYEGYELL--KEKEALERQKEAIERQLASLEEE---LEKLTEEISELEKRLEEIEQLLEELNKKikdlGEEEQL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 213 SLKKELKKAASELIKSKVTCQHKmEEESIDLIIKEQKYEELQERLNMELEvnkKINEEITHIQEEK---QDIIISFQHMQ 289
Cdd:TIGR02169 291 RVKEKIGELEAEIASLERSIAEK-ERELEDAEERLAKLEAEIDKLLAEIE---ELEREIEEERKRRdklTEEYAELKEEL 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 290 QLLQQETQantEIDAELKVLRennqtlERDNELQREKVKENEEKflsleKEHERALGTWKKHVEELSGEMNGIKNELSSL 369
Cdd:TIGR02169 367 EDLRAELE---EVDKEFAETR------DELKDYREKLEKLKREI-----NELKRELDRLQEELQRLSEELADLNAAIAGI 432
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 148695785 370 RETHAKLQEHYNKLCEQKKTEEYKKFQNVPELNNEnSDELTRKKSE 415
Cdd:TIGR02169 433 EAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY-EQELYDLKEE 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-348 |
4.39e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 4.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 27 QLLDFRTSLLEALEELRMRRKAETQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAMGVLKNQLQMKMyALEEEK 106
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR-ELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 107 GKYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYYAAITNQFGLVRENHVKL 186
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 187 EQNVQEAIQLNKRLSTLNEKQESEIHSLKKELKKAASELikskvtcqhkmEEESIDLIIKEQKYEELQERLNMELEVNKK 266
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE-----------EEEEEALEEAAEEEAELEEEEEALLELLAE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 267 INEEITHIQEEKQDIiisfqhMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEKEHERALG 346
Cdd:COG1196 468 LLEEAALLEAALAEL------LEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
..
gi 148695785 347 TW 348
Cdd:COG1196 542 AA 543
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
102-394 |
7.15e-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: 60.07 E-value: 7.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 102 LEEEKG--KYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEdYHKQLNEIEKYYAAitnqfGLV 179
Cdd:TIGR02168 161 FEEAAGisKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELELALLV-----LRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 180 RENHVKLEQNVQEAIQLNKRLSTLnEKQESEIHSLKKELKKAASELIKSKVTCQHKMEEESIDLIIKEQKYEELQERLNM 259
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEEL-TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 260 ELEVNKKINEEITHIQeekqdiiisfqhmQQLLQQETQANtEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEK 339
Cdd:TIGR02168 314 LERQLEELEAQLEELE-------------SKLDELAEELA-ELEEKLEELKEELESLEAELEELEAELEELESRLEELEE 379
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 148695785 340 EHERAlgtwKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEEYKK 394
Cdd:TIGR02168 380 QLETL----RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKL 430
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
205-391 |
9.83e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 9.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 205 EKQESEIHSLKKELKKAASELikskVTCQHKMEEESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIIS 284
Cdd:COG1196 242 EELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 285 FQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKN 364
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
170 180
....*....|....*....|....*..
gi 148695785 365 ELSSLRETHAKLQEHYNKLCEQKKTEE 391
Cdd:COG1196 398 LAAQLEELEEAEEALLERLERLEEELE 424
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
62-394 |
1.21e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 59.31 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 62 ETQELKWQKEALQNQKEALIKQHKEAMGVLkNQLQMKMYALEEEkgkyklaTEIKEKEIEGLKETLKTLQVSQYSLQKKV 141
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQSELRRIENRL-DELSQELSDASRK-------IGEIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 142 SEMEQ-----KAHLYHLAKE---------DYHKQLNEIEKYYA-----AITNQFGLVRENHVKLEQNVQEAIQLNKRLST 202
Cdd:TIGR02169 747 SSLEQeienvKSELKELEARieeleedlhKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIEQKLNRLTL 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 203 LNEKQESEIHSLKKELKKAASelikskvtcQHKMEEESIDLIIKeqKYEELQERL-NMELEVNkKINEEITHIQEEKQDI 281
Cdd:TIGR02169 827 EKEYLEKEIQELQEQRIDLKE---------QIKSIEKEIENLNG--KKEELEEELeELEAALR-DLESRLGDLKKERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 282 IisfQHMQQLLQQETQANTEIDAELKVLRENNQTLErdNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNG 361
Cdd:TIGR02169 895 E---AQLRELERKIEELEAQIEKKRKRLSELKAKLE--ALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRA 969
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 148695785 362 I--------------KNELSSLRETHAKLQEHYNKLceQKKTEEYKK 394
Cdd:TIGR02169 970 LepvnmlaiqeyeevLKRLDELKEKRAKLEEERKAI--LERIEEYEK 1014
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
123-415 |
1.28e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 123 LKETLKTLQVSQYSLQKKVSEMEQKahlyhLAKEDYHKQLNEIEKYYAAItnqfglvRENHVKLEQNVQEAIQLNKRLst 202
Cdd:COG1196 218 LKEELKELEAELLLLKLRELEAELE-----ELEAELEELEAELEELEAEL-------AELEAELEELRLELEELELEL-- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 203 lNEKQESEihslkKELKKAASELIKSKVTCQHKMEEESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQDII 282
Cdd:COG1196 284 -EEAQAEE-----YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 283 ISFQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNGI 362
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 148695785 363 KNELSSLRETHAKLQEHYNKLCEQKKTEEYKKFQNvpELNNENSDELTRKKSE 415
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEA--ALLEAALAELLEELAE 488
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
53-421 |
2.10e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 53 EEQIAKIILETQELKWQKEALQNQKEALIKQH---KEAMGVLKNQLQMKMYALEEEKGKYKLATEIkEKEIEGLKETLKT 129
Cdd:TIGR04523 151 EKELEKLNNKYNDLKKQKEELENELNLLEKEKlniQKNIDKIKNKLLKLELLLSNLKKKIQKNKSL-ESQISELKKQNNQ 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 130 LQVSQYSLQKKVSEMEQKAhlyhlakEDYHKQLNEIEKYYAAITNQfglVRENHVKLEQNVQEAIQLNKRLSTL------ 203
Cdd:TIGR04523 230 LKDNIEKKQQEINEKTTEI-------SNTQTQLNQLKDEQNKIKKQ---LSEKQKELEQNNKKIKELEKQLNQLkseisd 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 204 --NEKQESEIHSLKKELKKAASEL--IKSKVTCQHKM---EEESIDLIIKEQKY-----EELQERLNMELEVNKKINEEI 271
Cdd:TIGR04523 300 lnNQKEQDWNKELKSELKNQEKKLeeIQNQISQNNKIisqLNEQISQLKKELTNsesenSEKQRELEEKQNEIEKLKKEN 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 272 THIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLE----------KEH 341
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTnqdsvkeliiKNL 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 342 ERALGTWKKHVEELSGEMNGIKNELSSL-RETHAKLQEHyNKLCEQKKTEEykkfQNVPELNNENSDELTR-KKSENIIT 419
Cdd:TIGR04523 460 DNTRESLETQLKVLSRSINKIKQNLEQKqKELKSKEKEL-KKLNEEKKELE----EKVKDLTKKISSLKEKiEKLESEKK 534
|
..
gi 148695785 420 QK 421
Cdd:TIGR04523 535 EK 536
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
27-401 |
2.63e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 58.44 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 27 QLLDFRTSLLEALEELRMRRKAETQYE--EQIAKIILETQElKWQKEALQNQKEALIKQHKEAmgVLKNQLQMKM-YALE 103
Cdd:TIGR00618 393 QKLQSLCKELDILQREQATIDTRTSAFrdLQGQLAHAKKQQ-ELQQRYAELCAAAITCTAQCE--KLEKIHLQESaQSLK 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 104 EEKGKYKLATEIKEKEIEGLKETLKTLQVSQYS---LQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYyaaitnqfglvr 180
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEpcpLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTY------------ 537
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 181 ENHVKLEQNVQ-EAIQLNKRLSTLNEKQESEIHSLKK------ELKKAASELIKSKVTCQHKMEEESIDLIIKEQKYEEL 253
Cdd:TIGR00618 538 AQLETSEEDVYhQLTSERKQRASLKEQMQEIQQSFSIltqcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 254 QERLNMELEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQ----ANTEIDAELKVLRENNQTLERDNELQREKVKE 329
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRehalSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 148695785 330 NEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLC-EQKKTEEYKKFQNVPEL 401
Cdd:TIGR00618 698 MLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQArTVLKARTEAHFNNNEEV 770
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
91-420 |
8.21e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 91 LKNQLQmkmyALEEEKG---KYK-LATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIE 166
Cdd:COG1196 198 LERQLE----PLERQAEkaeRYReLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 167 KYYAAITNQFGLVREnhvKLEQNVQEAIQLNKRLSTLNEKQEsEIHSLKKELKKAASELIKSKVTCQHKMEEESIDLIIK 246
Cdd:COG1196 274 LELEELELELEEAQA---EEYELLAELARLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 247 EQKYEELQERLNMELEVNKKINEEITHIQEEKQDIiisfqhmQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREK 326
Cdd:COG1196 350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEEL-------AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 327 VKENEEKFLSLEKEHERAlgtwkkhveelsgemngiKNELSSLRETHAKLQEHYNKLCEQKKTEEYKKFQNVPELNNENS 406
Cdd:COG1196 423 LEELEEALAELEEEEEEE------------------EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE 484
|
330
....*....|....
gi 148695785 407 DELTRKKSENIITQ 420
Cdd:COG1196 485 ELAEAAARLLLLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
27-350 |
9.33e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.48 E-value: 9.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 27 QLLDFRTSLLEALEELRMRRKAETQYEEQIAKIILETQELKWQKEALQNQKEAlikqhkeamgvlknqLQMKMYALEEEK 106
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEE---------------AQAEEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 107 GKYklateikEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKyyaaitnqfglvrenhvKL 186
Cdd:COG1196 298 ARL-------EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE-----------------EL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 187 EQNVQEAIQLNKRLSTLNEKQESEIHSLKKELKKAASELIKskvtcQHKMEEESIDLIIKEQKYEELQERLNMELEVNKK 266
Cdd:COG1196 354 EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-----AAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 267 INEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEKEHERALG 346
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
|
....
gi 148695785 347 TWKK 350
Cdd:COG1196 509 GVKA 512
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
30-371 |
1.45e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.83 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 30 DFRTSLLEALEELRMRRKAETQYEEQIAKIILETQELKWQKEALQNQKEALIKQhkeamgvlKNQLQMKMYALEEEKGKY 109
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKE--------LEELSRQISALRKDLARL 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 110 KLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHlyhlAKEDyhkQLNEIEKYYAAITNQFGLVRENHVKLEQN 189
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA----EAEA---EIEELEAQIEQLKEELKALREALDELRAE 811
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 190 VQEaiqLNKRLSTLNEKQES---EIHSLKKELKKAASelikskvtcQHKMEEESIDLIIKEQkyEELQERLNmelevnkK 266
Cdd:TIGR02168 812 LTL---LNEEAANLRERLESlerRIAATERRLEDLEE---------QIEELSEDIESLAAEI--EELEELIE-------E 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 267 INEEITHIQEEKQDIiisFQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNE------LQREKVKENEEKFLS-LEK 339
Cdd:TIGR02168 871 LESELEALLNERASL---EEALALLRSELEELSEELRELESKRSELRRELEELREklaqleLRLEGLEVRIDNLQErLSE 947
|
330 340 350
....*....|....*....|....*....|..
gi 148695785 340 EHERALGTWKKHVEELSGEMNGIKNELSSLRE 371
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
62-350 |
1.68e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 55.52 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 62 ETQELKWQKEALQNQKEALIKQHKEAMGVLKNQLQMKMYALEEEKGKYKlateikekeieglketlktlqvsqySLQKKV 141
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQ-------------------------ELQKRI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 142 SEMEQKAHLyhlAKEDYHKQLNEIEKYYAAITNQFGLVRENHVKLEQNVQEAIQLNKRLSTLN---EKQESEIHSLKKEL 218
Cdd:pfam05557 58 RLLEKREAE---AEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRrqiQRAELELQSTNSEL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 219 KKAASelikskvtcQHKMEEESIDLIikEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIISfqhmqQLLQQETQA 298
Cdd:pfam05557 135 EELQE---------RLDLLKAKASEA--EQLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIV-----KNSKSELAR 198
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148695785 299 NTEIDAELKVLRENNQ---TLERDNELQREKVK------ENEEKF------LSLEKEH-ERALGTWKK 350
Cdd:pfam05557 199 IPELEKELERLREHNKhlnENIENKLLLKEEVEdlkrklEREEKYreeaatLELEKEKlEQELQSWVK 266
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
71-413 |
5.53e-07 |
|
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: 53.82 E-value: 5.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 71 EALQNQKEALIKQHKEAMGVLKnqlqmkMYALEEEKGKYKLATEIKEKEIEGLKETLKtlqvsqysLQKKVSEMEQKAHL 150
Cdd:pfam02463 145 EIIAMMKPERRLEIEEEAAGSR------LKRKKKEALKKLIEETENLAELIIDLEELK--------LQELKLKEQAKKAL 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 151 YHLAKEdyhKQLNEIEKYYAAITNQFGLVRENHV--KLEQNVQEAIQLNKRLSTLNEKQESEIHSLKKELKKAASELIKS 228
Cdd:pfam02463 211 EYYQLK---EKLELEEEYLLYLDYLKLNEERIDLlqELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 229 KVTCQHKMEEESIDLIIKEQKYEELQERLNMELEVNKKINEEIthiqEEKQDIIISFQHMQQLLQQETQANTEIDAELKV 308
Cdd:pfam02463 288 LKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKEL----KKEKEEIEELEKELKELEIKREAEEEEEEELEK 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 309 LRENNQTLERDNElqrEKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEhynKLCEQKK 388
Cdd:pfam02463 364 LQEKLEQLEEELL---AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELE---ILEEEEE 437
|
330 340
....*....|....*....|....*
gi 148695785 389 TEEYKKFQNVPELNNENSDELTRKK 413
Cdd:pfam02463 438 SIELKQGKLTEEKEELEKQELKLLK 462
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
36-383 |
9.80e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 9.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 36 LEALEELRMRRKAETQYEEQIAKIILETQELKWQKEALQNQKEALikqhKEAMGVLKNQLQMKMYALEEEKGKYKLATEI 115
Cdd:COG4717 70 LKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL----REELEKLEKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 116 KE-KEIEGLKETLKTLQVSQYSLQKKVSEMEQK-AHLYHLAKEDYHKQLNEIEKYYAAITNQFGLVREnhvKLEQNVQEA 193
Cdd:COG4717 146 ERlEELEERLEELRELEEELEELEAELAELQEElEELLEQLSLATEEELQDLAEELEELQQRLAELEE---ELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 194 IQLNKRLSTLNEKQESEihSLKKELKKA-----------------------------------------ASELIKSKVTC 232
Cdd:COG4717 223 EELEEELEQLENELEAA--ALEERLKEArlllliaaallallglggsllsliltiagvlflvlgllallFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 233 QHKMEEESIDLIIKEQKYEELQERLNmelEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTE-IDAELKVLRE 311
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLA---ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEeLEQEIAALLA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 312 NN---------QTLERDNELQ--REKVKENEEKFLSLEKEHERALGTWKKhvEELSGEMNGIKNELSSLRETHAKLQEHY 380
Cdd:COG4717 378 EAgvedeeelrAALEQAEEYQelKEELEELEEQLEELLGELEELLEALDE--EELEEELEELEEELEELEEELEELREEL 455
|
...
gi 148695785 381 NKL 383
Cdd:COG4717 456 AEL 458
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
50-370 |
1.04e-06 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 52.55 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 50 TQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAM----------GVLKNQLQMKMYALEEEKGKYKLATEikEKE 119
Cdd:pfam06160 96 DDIEEDIKQILEELDELLESEEKNREEVEELKDKYRELRktllanrfsyGPAIDELEKQLAEIEEEFSQFEELTE--SGD 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 120 IEGLKETLKTLQVSQYSLQKKVSEMEQkahLYHLAKEDYHKQLNEIEKYYAAITNQfglvrenHVKLEQNvqeaiQLNKR 199
Cdd:pfam06160 174 YLEAREVLEKLEEETDALEELMEDIPP---LYEELKTELPDQLEELKEGYREMEEE-------GYALEHL-----NVDKE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 200 LSTLNEKQESEIHSLKK-ELKKAASEL--IKSKV-TCQHKMEEESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQ 275
Cdd:pfam06160 239 IQQLEEQLEENLALLENlELDEAEEALeeIEERIdQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQ 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 276 E---------------EKQ--DIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLErdnelqrEKVKENEEKFLSLE 338
Cdd:pfam06160 319 QsytlnenelervrglEKQleELEKRYDEIVERLEEKEVAYSELQEELEEILEQLEEIE-------EEQEEFKESLQSLR 391
|
330 340 350
....*....|....*....|....*....|..
gi 148695785 339 KEHERAlgtwKKHVEELSGEMNGIKNELSSLR 370
Cdd:pfam06160 392 KDELEA----REKLDEFKLELREIKRLVEKSN 419
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
50-378 |
1.51e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 52.15 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 50 TQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAM----------GVLKNQLQMKMYALEEEKGKYKLATEikEKE 119
Cdd:PRK04778 115 DLIEEDIEQILEELQELLESEEKNREEVEQLKDLYRELRksllanrfsfGPALDELEKQLENLEEEFSQFVELTE--SGD 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 120 IEGLKETLKTLQVSQYSLQKKVSEMEQkahLYHLAKEDYHKQLNEIEKYYAAitnqfgLVRENHVKLEQNVqeaiqlnkr 199
Cdd:PRK04778 193 YVEAREILDQLEEELAALEQIMEEIPE---LLKELQTELPDQLQELKAGYRE------LVEEGYHLDHLDI--------- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 200 lstlnekqESEIHSLKKELKKAASELikskvtcqhkmeeESIDLIIKEQKYEELQERLN-----MELEV---------NK 265
Cdd:PRK04778 255 --------EKEIQDLKEQIDENLALL-------------EELDLDEAEEKNEEIQERIDqlydiLEREVkarkyveknSD 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 266 KINEEITHIQEEKQDIIISFQHMQQ---LLQQETQANTEIDAELKvlrennqTLERDNELQREKVKENEEKFLSLEKEHE 342
Cdd:PRK04778 314 TLPDFLEHAKEQNKELKEEIDRVKQsytLNESELESVRQLEKQLE-------SLEKQYDEITERIAEQEIAYSELQEELE 386
|
330 340 350
....*....|....*....|....*....|....*.
gi 148695785 343 RalgtWKKHVEELSGEMNGIKNELSSLRETHAKLQE 378
Cdd:PRK04778 387 E----ILKQLEEIEKEQEKLSEMLQGLRKDELEARE 418
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
17-281 |
1.87e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 17 QSSSETMVSIQLLDFRTSLLEALEELRMRRKA-----------ETQYEEQIAKIILETQELKWQKEALQNQkealIKQHK 85
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDElneelkelaekRDELNAQVKELREEAQELREKRDELNEK----VKELK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 86 EAMGVLK---NQLQMKMYALEEEKGKYKLAT---EIKEKEIEGLketLKTLQVSQYSLQK------KVSEMEQKAHlyhl 153
Cdd:COG1340 78 EERDELNeklNELREELDELRKELAELNKAGgsiDKLRKEIERL---EWRQQTEVLSPEEekelveKIKELEKELE---- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 154 AKEDYHKQLNEIEKYYAAITNQFGLVRENHVKLEQNVQEAIQLNKRLSTLNEKQEseihslkkELKKAASELIKSKVTCQ 233
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEAD--------ELRKEADELHKEIVEAQ 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 148695785 234 HKMEEESIDLIIKEQKYEELQERLNMELEVNKKINEEITH--IQEEKQDI 281
Cdd:COG1340 223 EKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKeeLEEKAEEI 272
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
50-424 |
3.56e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.17 E-value: 3.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 50 TQYEEQIAKIILETQELKWQKEALQNQKEAL---IKQHKEamgvLKNQLQMKMYALEEEKgkyklatEIKEKEIEGLKET 126
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEK----LNQQKDEQIKKLQQEK-------ELLEKEIERLKET 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 127 LKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYYaaitnqfglvRENHVKLEQNVQEAIQLNKRLSTLNEK 206
Cdd:TIGR04523 435 IIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSI----------NKIKQNLEQKQKELKSKEKELKKLNEE 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 207 qeseihslKKELKKAASELIKSKVTCQHKMEEESIDLIIKEQKYEELQERLNMELEVNKKIN--EEITHIQEEkqdiIIS 284
Cdd:TIGR04523 505 --------KKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKE----IEE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 285 FQHMQQLLqqeTQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEKEHERalgtwkkhveeLSGEMNGIKN 364
Cdd:TIGR04523 573 LKQTQKSL---KKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK-----------LSSIIKNIKS 638
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 365 ELSSLrethaklqehyNKLCEQKKTEEYKKFQNVPELNNENSDELTRKKSENIITQKYNS 424
Cdd:TIGR04523 639 KKNKL-----------KQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLK 687
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
43-378 |
5.35e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 50.89 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 43 RMRRKAETQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAMGVLKNQlqmkmyaleeekgkyklateiKEKEIEG 122
Cdd:pfam15921 224 KILRELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISE---------------------HEVEITG 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 123 LKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAkedYHKQLNEIEKYYAaitnqfglvrenhvkleqnvqeaiQLNKRLST 202
Cdd:pfam15921 283 LTEKASSARSQANSIQSQLEIIQEQARNQNSM---YMRQLSDLESTVS------------------------QLRSELRE 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 203 LNEKQESEIHSLKKELKKAASELIKSKvTCQHKMEEESIDLIIKEQK-YEELQER---LNMELEVNKKINEE-------I 271
Cdd:pfam15921 336 AKRMYEDKIEELEKQLVLANSELTEAR-TERDQFSQESGNLDDQLQKlLADLHKRekeLSLEKEQNKRLWDRdtgnsitI 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 272 THIQEEKQDIIISFQHMQQLLQQ-ETQANTEIDAELKVLRENNQTLER----------DNELQREKVKENEEKFLSLEKE 340
Cdd:pfam15921 415 DHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAAIQGKNESLEKvssltaqlesTKEMLRKVVEELTAKKMTLESS 494
|
330 340 350
....*....|....*....|....*....|....*....
gi 148695785 341 hERALGTWKKHVEELSGEMNGIKNELSSLR-ETHAKLQE 378
Cdd:pfam15921 495 -ERTVSDLTASLQEKERAIEATNAEITKLRsRVDLKLQE 532
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
24-239 |
5.43e-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: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 24 VSIQLLDFRTSLLEALEELRMRRKAETQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAMGVLkNQLQMKMYALE 103
Cdd:TIGR02169 299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL-EDLRAELEEVD 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 104 EEKGKYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEkyyAAITNQFGLVRENH 183
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELE---EEKEDKALEIKKQE 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 148695785 184 VKLEQNVQEAIQLNKRLSTLNEKQESeihsLKKELKKAASELIKSKVTCQHKMEEE 239
Cdd:TIGR02169 455 WKLEQLAADLSKYEQELYDLKEEYDR----VEKELSKLQRELAEAEAQARASEERV 506
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
26-391 |
1.07e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 26 IQLLDFRTSLLEALEELRMRRKAETQYEEQIAKIILETQELKWQKEA---LQNQKEALIKQHKEAMGVLKNQLQMKMYAL 102
Cdd:COG4717 111 LEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQLSLAT 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 103 EEEKGKYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAkedyhKQLNEIEKYYAAITNQFGLVREN 182
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE-----ERLKEARLLLLIAAALLALLGLG 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 183 HV--KLEQNVQEAIQLNKRLSTLnekqeSEIHSLKKELKKAASELIKSKVTCQHKMEEESIDLIIKEQKYEELQ--ERLN 258
Cdd:COG4717 266 GSllSLILTIAGVLFLVLGLLAL-----LFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLspEELL 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 259 MELEVNKKINEEITHIQEEKQDI-IISFQHMQQLLQQETQANTE--IDAELKVLRENNQTLERDNELQREkVKENEEKFL 335
Cdd:COG4717 341 ELLDRIEELQELLREAEELEEELqLEELEQEIAALLAEAGVEDEeeLRAALEQAEEYQELKEELEELEEQ-LEELLGELE 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 148695785 336 SLEKEHERAlgTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEE 391
Cdd:COG4717 420 ELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAE 473
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
10-317 |
1.21e-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: 49.73 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 10 SASTFTLQSSSETMVsiqllDFRTSLLEALEELRMRRKAETQYEEQIAKIILETQELKWQKEALQNQK---EALIKQHKE 86
Cdd:pfam15921 485 TAKKMTLESSERTVS-----DLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQtecEALKLQMAE 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 87 ---AMGVLKNQLQmKMYALEEEKGKYKLATEIK----EKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAK---- 155
Cdd:pfam15921 560 kdkVIEILRQQIE-NMTQLVGQHGRTAGAMQVEkaqlEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKvklv 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 156 ---EDYHKQLNEIEKYYAAITNQfglVRENHVKLEQNVQEAIQLNKRLSTLNEKQESEIHSLKKELKKAASELIKSKVTC 232
Cdd:pfam15921 639 nagSERLRAVKDIKQERDQLLNE---VKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTL 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 233 Q-------HKMEEE---SIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIiisfqhMQQLLQQETQANtEI 302
Cdd:pfam15921 716 KsmegsdgHAMKVAmgmQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKL------SQELSTVATEKN-KM 788
|
330
....*....|....*
gi 148695785 303 DAELKVLRENNQTLE 317
Cdd:pfam15921 789 AGELEVLRSQERRLK 803
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
34-325 |
2.15e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.80 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 34 SLLEALEELRMRRK-AETQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAMgvlknQLQMKMYALEEEKGkyklA 112
Cdd:COG3096 358 ELTERLEEQEEVVEeAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAI-----QYQQAVQALEKARA----L 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 113 TEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHK-------------------------------- 160
Cdd:COG3096 429 CGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiageversqawqtarellrryrsqq 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 161 -----------QLNEIEKYYAAITNQFGLVRENHVKLEQNVQEAIQLNKRLSTLNEKQEseihslkkELKKAASELIKSK 229
Cdd:COG3096 509 alaqrlqqlraQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLE--------ELEEQAAEAVEQR 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 230 VTCQHKMEE--ESID-LIIKEQKYEELQERLNmelevnkKINEEITHIQEEKQDIIisfQHMQQLLQQETQANTEIDael 306
Cdd:COG3096 581 SELRQQLEQlrARIKeLAARAPAWLAAQDALE-------RLREQSGEALADSQEVT---AAMQQLLEREREATVERD--- 647
|
330
....*....|....*....
gi 148695785 307 kvlrennQTLERDNELQRE 325
Cdd:COG3096 648 -------ELAARKQALESQ 659
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
37-225 |
2.75e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.84 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 37 EALEELRMRRKaetQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAMGVLkNQLQMKMYALEEEKGKYKLATEIK 116
Cdd:COG4942 20 DAAAEAEAELE---QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-RALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 117 EKEIEGLKETLKTLQVSQYSL-----------QKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYYAAITNQFGLVRENHVK 185
Cdd:COG4942 96 RAELEAQKEELAELLRALYRLgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 148695785 186 LEQNVQEAIQLNKRLSTLNEKQESEIHSLKKELKKAASEL 225
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAEL 215
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
29-404 |
3.14e-05 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 48.18 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 29 LDFRTSLLEALEELRMRRKAETqyeEQIAKIILETQELKWQKEALQNQKEALIKQHKEAMGVLKNQlQMKMYALEEEKGK 108
Cdd:pfam05483 386 LQKKSSELEEMTKFKNNKEVEL---EELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR-EKEIHDLEIQLTA 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 109 YKLATEIKEKEIEGLK-----ETLKTLQVSQYS--LQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYYAAITNQFGLVRE 181
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKtelekEKLKNIELTAHCdkLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEE 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 182 NHVKLEQNVQ----EAIQLNKRLSTLNEKQESEIHSLKKELKKAASELIKSKVTC-----QHKMEEESIDLIIKEQK--- 249
Cdd:pfam05483 542 KEMNLRDELEsvreEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCnnlkkQIENKNKNIEELHQENKalk 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 250 ------------YEELQERLNMELEVNKKINEEITH-IQEEKQDIIISfqhMQQLLQQETQANTEIDAELKVLRENNQTL 316
Cdd:pfam05483 622 kkgsaenkqlnaYEIKVNKLELELASAKQKFEEIIDnYQKEIEDKKIS---EEKLLEEVEKAKAIADEAVKLQKEIDKRC 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 317 ERDNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEEYKKFQ 396
Cdd:pfam05483 699 QHKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
....*...
gi 148695785 397 NVPELNNE 404
Cdd:pfam05483 779 NTAILKDK 786
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
82-390 |
3.19e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.04 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 82 KQHKEAMG---VLKNQLQMKMYALEEEKGKYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEdy 158
Cdd:TIGR00618 187 AKKKSLHGkaeLLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQ-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 159 hkQLNEIEKYyaaiTNQFGLVRENHVKLEQNVQEA--IQLNKRLSTLNEKQESEIHSLKKELKKAASELIKSKVTCQHKM 236
Cdd:TIGR00618 265 --LRARIEEL----RAQEAVLEETQERINRARKAAplAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 237 E-EESIDLIIKEQKYEELQERLNME----LEVNKKINEEITHIQEEKQDIIISFQHMQ---QLLQQETQANTEIDAEL-- 306
Cdd:TIGR00618 339 SiEEQRRLLQTLHSQEIHIRDAHEVatsiREISCQQHTLTQHIHTLQQQKTTLTQKLQslcKELDILQREQATIDTRTsa 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 307 -KVLRENNQTLERDNELQREKVKENE---EKFLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHA----KLQE 378
Cdd:TIGR00618 419 fRDLQGQLAHAKKQQELQQRYAELCAaaiTCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAvvlaRLLE 498
|
330
....*....|..
gi 148695785 379 HYNKLCEQKKTE 390
Cdd:TIGR00618 499 LQEEPCPLCGSC 510
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
33-413 |
3.47e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 3.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 33 TSLLEALEELRMRrKAETQYEEQIAKiiLETQELKWQKEALQNQKEALIKQ------HKEAMGVLKNQLQMKMYALEEEK 106
Cdd:PRK02224 254 ETLEAEIEDLRET-IAETEREREELA--EEVRDLRERLEELEEERDDLLAEaglddaDAEAVEARREELEDRDEELRDRL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 107 GKYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYYAAITNQFGLVRENHVKL 186
Cdd:PRK02224 331 EECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 187 EQNVQEaiqLNKRLSTLNEKQ---ESEIHSLKKELKKAASELIKSKV-TCQHKMEEESIDLII--KEQKYEELQERL-NM 259
Cdd:PRK02224 411 EDFLEE---LREERDELREREaelEATLRTARERVEEAEALLEAGKCpECGQPVEGSPHVETIeeDRERVEELEAELeDL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 260 ELE---VNKKINEEITHIQEEKQdiIISFQHMQQLLQQ--ETQANTEIDAELKV--LRENNQTLERDNELQREKVKENEE 332
Cdd:PRK02224 488 EEEveeVEERLERAEDLVEAEDR--IERLEERREDLEEliAERRETIEEKRERAeeLRERAAELEAEAEEKREAAAEAEE 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 333 kflslekEHERALGTwkkhVEELSGEMNGIKNELSSLRETHAKLQEHYNklCEQKKTEEYKKFQNVPELNNENSDELTRK 412
Cdd:PRK02224 566 -------EAEEAREE----VAELNSKLAELKERIESLERIRTLLAAIAD--AEDEIERLREKREALAELNDERRERLAEK 632
|
.
gi 148695785 413 K 413
Cdd:PRK02224 633 R 633
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
39-388 |
4.54e-05 |
|
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: 47.86 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 39 LEELRMRRKAE-TQYEEQIAKIILETQELKWQ----KEALQ----------NQKEALIKQHKEamgvLKNQLQMKMYALE 103
Cdd:pfam01576 206 LEKAKRKLEGEsTDLQEQIAELQAQIAELRAQlakkEEELQaalarleeetAQKNNALKKIRE----LEAQISELQEDLE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 104 EEKGKYKLATEIK---EKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAhlyhlakEDYHKQLNEIEKYYAAitnQFGLVR 180
Cdd:pfam01576 282 SERAARNKAEKQRrdlGEELEALKTELEDTLDTTAAQQELRSKREQEV-------TELKKALEEETRSHEA---QLQEMR 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 181 ENHVKLEQNVQEAIQLNKRLSTLNEKQESEIHSLKKELKKAASELIKSKVTCQH---KMEEESIDLIIK----EQKYEEL 253
Cdd:pfam01576 352 QKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHkrkKLEGQLQELQARlsesERQRAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 254 QERLN---MELE-VNKKINE---EITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLerdnelqREK 326
Cdd:pfam01576 432 AEKLSklqSELEsVSSLLNEaegKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSL-------QEQ 504
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148695785 327 VKENEEKFLSLEKE---HERALGTWKKHVEELSGEMNGI-------KNELSSLRETHAKLQEHYNKLCEQKK 388
Cdd:pfam01576 505 LEEEEEAKRNVERQlstLQAQLSDMKKKLEEDAGTLEALeegkkrlQRELEALTQQLEEKAAAYDKLEKTKN 576
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
40-406 |
4.91e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 4.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 40 EELRMRRKAETQYEEQIAKiileTQELKWQKEALQNQKEALIKQHKEAMGVLKNQLQMKMYALEEEKGKYKLATEIKEKE 119
Cdd:PTZ00121 1480 EEAKKADEAKKKAEEAKKK----ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAE 1555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 120 IEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYYAAITNQFGLVRENHVKLEQnVQEAIQLNKR 199
Cdd:PTZ00121 1556 ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEE-LKKAEEEKKK 1634
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 200 LSTLNEKQESEIHSlKKELKKAASELIKSKVTCQHKMEEEsidliikEQKYEELQErlnmELEVNKKINEEITHIQEEKQ 279
Cdd:PTZ00121 1635 VEQLKKKEAEEKKK-AEELKKAEEENKIKAAEEAKKAEED-------KKKAEEAKK----AEEDEKKAAEALKKEAEEAK 1702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 280 DIiisfQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKEneekfLSLEKEHERALGTWKKHVEELSGEM 359
Cdd:PTZ00121 1703 KA----EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE-----AKKDEEEKKKIAHLKKEEEKKAEEI 1773
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 148695785 360 NGIKNELssLRETHAKLQEHYNKLCEQKKTEEYKKFQNVPELNNENS 406
Cdd:PTZ00121 1774 RKEKEAV--IEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGN 1818
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
182-282 |
5.03e-05 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 44.10 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 182 NHVKLEQNVQEAIQLNKRLSTLNEKQESEIHSLKKELKKAASELIKSKVTCQHKMEEESIDLIIKEQKYEELQERLNMEL 261
Cdd:pfam03938 6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQEL 85
|
90 100
....*....|....*....|.
gi 148695785 262 evNKKINEEITHIQEEKQDII 282
Cdd:pfam03938 86 --QKKQQELLQPIQDKINKAI 104
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
41-413 |
5.34e-05 |
|
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: 47.35 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 41 ELRMRRKAETQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAMGVLKNQLQMKMYALEEEKGKYKLATEIKEKEI 120
Cdd:TIGR00606 738 IIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQG 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 121 EGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEkyyaAITNQFGLVRenhVKLEQNVQEAIQLNKRL 200
Cdd:TIGR00606 818 SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLK----SKTNELKSEK---LQIGTNLQRRQQFEEQL 890
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 201 STLNekqeSEIHSLKKELKKAAselikskvtcqhkmEEESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQD 280
Cdd:TIGR00606 891 VELS----TEVQSLIREIKDAK--------------EQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKN 952
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 281 IIISFQHMQQLLQ-----QETQANTEIDAELKVLRENNQTLERDNELQREKVKEneekfLSLEKEHERALGtwkkhvEEL 355
Cdd:TIGR00606 953 IHGYMKDIENKIQdgkddYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQD-----IDTQKIQERWLQ------DNL 1021
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 148695785 356 SgeMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEEYKKFQ-NVPELNNENSDELTRKK 413
Cdd:TIGR00606 1022 T--LRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEeNIDLIKRNHVLALGRQK 1078
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
45-415 |
6.54e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 6.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 45 RRKAETQYEEQIAKIiletQELKWQKEALQNQKEALIKQHKEAMGVLKNQLQMKMYALEEEKGKYKLATEIKEKEIEGLK 124
Cdd:PTZ00121 1212 RKAEEARKAEDAKKA----EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 125 ETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEdYHKQLNEIEKYYAAITNQfglVRENHVKLEQNVQEAIQLNKRLSTLN 204
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKADAAKKK---AEEAKKAAEAAKAEAEAAADEAEAAE 1363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 205 EKQESEihSLKKELKKAASELIKSKVTCQHKMEEESIDLIIKEQKYEELQERlnmelEVNKKINEEITHIQEEKQDIiis 284
Cdd:PTZ00121 1364 EKAEAA--EKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA-----AAAKKKADEAKKKAEEKKKA--- 1433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 285 fQHMQQLLQQETQANteidaELKVLRENNQTLERDNELQREKVKENEEKFLSLEK----EHERALGTWKKHVEELSGEMN 360
Cdd:PTZ00121 1434 -DEAKKKAEEAKKAD-----EAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAkkadEAKKKAEEAKKKADEAKKAAE 1507
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 148695785 361 GIKNELSSLRETHAKLQEHYNKLCEQKKTEEYKKFQNVPELNNENSDELTRKKSE 415
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
117-394 |
7.75e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 117 EKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYYAAITNQfglVRENHVKLEQNVQEAIQL 196
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEK---VKELKEERDELNEKLNEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 197 NKRLSTLNEKQESEIHS--LKKELKKAASELIKSKVTCQHKMEEEsIDLIIKEQKYEELQERLNMELEVNKKINEEITHI 274
Cdd:COG1340 91 REELDELRKELAELNKAggSIDKLRKEIERLEWRQQTEVLSPEEE-KELVEKIKELEKELEKAKKALEKNEKLKELRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 275 QEEKQDIIISFQHMQQLLQQETQANTEIDAELKvlrennqtlERDNelQREKVKENEEKFLSLEKEheralgtwkkhVEE 354
Cdd:COG1340 170 KELRKEAEEIHKKIKELAEEAQELHEEMIELYK---------EADE--LRKEADELHKEIVEAQEK-----------ADE 227
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 148695785 355 LSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEEYKK 394
Cdd:COG1340 228 LHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEE 267
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
211-394 |
8.68e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 8.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 211 IHS-LKKELKKAASELIKSK-------VTCQHKMEEESIDLIIKEQKYEELQERL---NMELEVNKKINEEITHIQEEKQ 279
Cdd:COG4717 43 IRAmLLERLEKEADELFKPQgrkpelnLKELKELEEELKEAEEKEEEYAELQEELeelEEELEELEAELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 280 DIIISFQHMQQL------LQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEKEHERALGTWKKHVE 353
Cdd:COG4717 123 KLLQLLPLYQELealeaeLAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148695785 354 ELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEEYKK 394
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
24-418 |
8.91e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.59 E-value: 8.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 24 VSIQLLDFRTSLLEALEELRMRRKAETQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAMG-------VLKNQLQ 96
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGfsegvkaLLKNQSG 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 97 MKMYA-----LEEEKGKYKLATEI----------------KEKEIEGLKETLKT----LQVSQYSLQK-KVSEMEQKAhl 150
Cdd:TIGR02168 518 LSGILgvlseLISVDEGYEAAIEAalggrlqavvvenlnaAKKAIAFLKQNELGrvtfLPLDSIKGTEiQGNDREILK-- 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 151 yhlAKEDYHKQLNEIEKYYAAITNQFGLvRENHVKLEQNVQEAIQLNKRLS------TLN--------------EKQESE 210
Cdd:TIGR02168 596 ---NIEGFLGVAKDLVKFDPKLRKALSY-LLGGVLVVDDLDNALELAKKLRpgyrivTLDgdlvrpggvitggsAKTNSS 671
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 211 IHSLKKELKKAASELikskvtcqHKMEEESIDLIIKEQKYEELQERLNMELE-VNKKINEEITHIQEEKQDIIISFQHMQ 289
Cdd:TIGR02168 672 ILERRREIEELEEKI--------EELEEKIAELEKALAELRKELEELEEELEqLRKELEELSRQISALRKDLARLEAEVE 743
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 290 QLLQQETQanteIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEKEheralgtwkkhVEELSGEMNGIKNELSSL 369
Cdd:TIGR02168 744 QLEERIAQ----LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ-----------IEQLKEELKALREALDEL 808
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 148695785 370 RETHAKLQEHYNKLceQKKTEEYKKFQNVPELNNENSDELTRKKSENII 418
Cdd:TIGR02168 809 RAELTLLNEEAANL--RERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
22-393 |
9.15e-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: 46.65 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 22 TMVSIQLLDFRTSLLEALEELRmrrKAETQYEEQIAKiiLETQELKWQKEALQNQKEAliKQHKEAMGVLKNQLQMKMYA 101
Cdd:pfam15921 313 SMYMRQLSDLESTVSQLRSELR---EAKRMYEDKIEE--LEKQLVLANSELTEARTER--DQFSQESGNLDDQLQKLLAD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 102 LEEekgkyklateiKEKEIEGLKETLKTLQVSqyslqkkvsEMEQKAHLYHLAKE--DYHKQLNEIEKYYAAITNQFGLV 179
Cdd:pfam15921 386 LHK-----------REKELSLEKEQNKRLWDR---------DTGNSITIDHLRREldDRNMEVQRLEALLKAMKSECQGQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 180 RENHVKLEQNVQEAIQlnkRLSTLNekqeSEIHSLKKELKKAASELIKSKVTCQHKmEEESIDLIIKEQKYE-------- 251
Cdd:pfam15921 446 MERQMAAIQGKNESLE---KVSSLT----AQLESTKEMLRKVVEELTAKKMTLESS-ERTVSDLTASLQEKEraieatna 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 252 ---ELQERLNMELEVNKKINEEITHIQE-------------EKQDII----ISFQHMQQLLQQ-----------ETQANT 300
Cdd:pfam15921 518 eitKLRSRVDLKLQELQHLKNEGDHLRNvqtecealklqmaEKDKVIeilrQQIENMTQLVGQhgrtagamqveKAQLEK 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 301 EID------AELKVLRENNQTLERDNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHA 374
Cdd:pfam15921 598 EINdrrlelQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYE 677
|
410
....*....|....*....
gi 148695785 375 KLQEHYNKLCEQKKTEEYK 393
Cdd:pfam15921 678 VLKRNFRNKSEEMETTTNK 696
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
15-413 |
1.13e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 46.50 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 15 TLQSSSETMVSIQLLDFRTSLLEALE-ELRMRRKAETQYEEQIAKIileTQELKWQKEALQNQK------------EALI 81
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEkELKHLREALQQTQQSHAYL---TQKREAQEEQLKKQQllkqlrarieelRAQE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 82 KQHKEAMGVLKNQLQMKMYALEE------EKGKYKLATEIKEKEieglKETLKTLQVSQYSLQKKVSEMEQKAHLYHL-A 154
Cdd:TIGR00618 277 AVLEETQERINRARKAAPLAAHIkavtqiEQQAQRIHTELQSKM----RSRAKLLMKRAAHVKQQSSIEEQRRLLQTLhS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 155 KEDYHKQLNEIEKYYAAITNQFGLVRENHVKLEQNVQEAIQLNKRLSTLNEKQESEIHSLKKELKKAASE---LIKSKVT 231
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLqgqLAHAKKQ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 232 CQHKMEEESIDLIIKEQKYEELQERLNMELEVNKKINEEithIQEEKQdiiisfqhMQQLLQQETQANTEIDAELKVLRE 311
Cdd:TIGR00618 433 QELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKER---EQQLQT--------KEQIHLQETRKKAVVLARLLELQE 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 312 N-----NQTLERDNELQREKVKE-NEEKFLSLEKEHERAlgtwKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKL-- 383
Cdd:TIGR00618 502 EpcplcGSCIHPNPARQDIDNPGpLTRRMQRGEQTYAQL----ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILtq 577
|
410 420 430
....*....|....*....|....*....|
gi 148695785 384 CEQKKTEEYKKFQNVPELNNENSDELTRKK 413
Cdd:TIGR00618 578 CDNRSKEDIPNLQNITVRLQDLTEKLSEAE 607
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
134-344 |
1.27e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 134 QYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYYAAITNQFGLVRENhVKLEQNVQEAIQLNKRLSTLNEKQ---ESE 210
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLS-EEAKLLLQQLSELESQLAEARAELaeaEAR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 211 IHSLKKELKK---AASELIKSKVTCQHKMEEESIdliikEQKYEELQERLNME----LEVNKKINEEITHIQEEKQDIII 283
Cdd:COG3206 242 LAALRAQLGSgpdALPELLQSPVIQQLRAQLAEL-----EAELAELSARYTPNhpdvIALRAQIAALRAQLQQEAQRILA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 148695785 284 SFQH-MQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREkVKENEEKFLSLEKEHERA 344
Cdd:COG3206 317 SLEAeLEALQAREASLQAQLAQLEARLAELPELEAELRRLERE-VEVARELYESLLQRLEEA 377
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
118-378 |
1.27e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.53 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 118 KEIEGLKETLKTLQVSQYSLQKKVSEMEQKahlyhlaKEDYHKQLNEIEKYYAAITNQfglvrenhvkLEQNVQEAIQLN 197
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE-------EKALLKQLAALERRIAALARR----------IRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 198 KRLSTLnekqESEIHSLKKELKKAASELIKSKVTCQHKMEEESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEE 277
Cdd:COG4942 83 AELAEL----EKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 278 KQDIiisfqhmqqllqqetqanTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSG 357
Cdd:COG4942 159 LAEL------------------AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
250 260
....*....|....*....|.
gi 148695785 358 EMNGIKNELSSLRETHAKLQE 378
Cdd:COG4942 221 EAEELEALIARLEAEAAAAAE 241
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
118-434 |
1.79e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.81 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 118 KEIEGLKETLKTLQVSQYSLQKKV-SEMEQKahlyhLAKEDYHKQLNEIEKYYAAITNQFGLVRENHVKLEQNVQEAIQL 196
Cdd:TIGR01612 503 KDFKDIIDFMELYKPDEVPSKNIIgFDIDQN-----IKAKLYKEIEAGLKESYELAKNWKKLIHEIKKELEEENEDSIHL 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 197 NKRLSTLNEK------QESEIHSLKKELKKA------ASELIKSKVTCQHKMEEES--IDLIIKEQKYeELQERLNMELE 262
Cdd:TIGR01612 578 EKEIKDLFDKyleiddEIIYINKLKLELKEKiknisdKNEYIKKAIDLKKIIENNNayIDELAKISPY-QVPEHLKNKDK 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 263 VNKKINEEITHIQEEKQDIIisFQHMQQLLQQETQANTEIDAELKVLrennqtlerdnelqREKVKENEEKFLSLEKEhe 342
Cdd:TIGR01612 657 IYSTIKSELSKIYEDDIDAL--YNELSSIVKENAIDNTEDKAKLDDL--------------KSKIDKEYDKIQNMETA-- 718
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 343 ralgTWKKHVEELSGEmngiKNELSSL-----RETHAKLQEHYNKLCEQKKTEEYKKFQNVPELNNENsDELTRKKSE-N 416
Cdd:TIGR01612 719 ----TVELHLSNIENK----KNELLDIiveikKHIHGEINKDLNKILEDFKNKEKELSNKINDYAKEK-DELNKYKSKiS 789
|
330
....*....|....*...
gi 148695785 417 IITQKYNSGPEIwgKNTK 434
Cdd:TIGR01612 790 EIKNHYNDQINI--DNIK 805
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
70-320 |
1.87e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 45.67 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 70 KEALQNQKEAL--IKQHKEAMGVLKNQLQMKMYALEEEKgKYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMeqk 147
Cdd:PRK11281 38 EADVQAQLDALnkQKLLEAEDKLVQQDLEQTLALLDKID-RQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE--- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 148 ahlyhlAKEDYHKQ-LNEIEKYYAAITNQFglvrenhvkleQNVQEAI-QLNKRLSTLN---EKQESEIHSLKKELKKAA 222
Cdd:PRK11281 114 ------TRETLSTLsLRQLESRLAQTLDQL-----------QNAQNDLaEYNSQLVSLQtqpERAQAALYANSQRLQQIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 223 SELIKSKVTcQHKMEEESIDLIIKEQKYEELQERLN-MELEVNKKI-----------NEEITHIQEEKQDI--------- 281
Cdd:PRK11281 177 NLLKGGKVG-GKALRPSQRVLLQAEQALLNAQNDLQrKSLEGNTQLqdllqkqrdylTARIQRLEHQLQLLqeainskrl 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 148695785 282 IISFQHMQQ--------------LLQQETQANTEIDAELKVLRENNQTLERDN 320
Cdd:PRK11281 256 TLSEKTVQEaqsqdeaariqanpLVAQELEINLQLSQRLLKATEKLNTLTQQN 308
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
120-326 |
2.48e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 45.01 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 120 IEGLKETLKTLQVSQYSLQKKVsemeqkahlyhlakEDYHKQLNEIEKYYAAITNQFGLVRENHVKLEQNVQEAI-QLNK 198
Cdd:PHA02562 176 IRELNQQIQTLDMKIDHIQQQI--------------KTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIeELTD 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 199 RLSTLNEKQESEIHSLKKELKKAAseLIKSKV-----------------TCQHKMEEE----------------SIDLIi 245
Cdd:PHA02562 242 ELLNLVMDIEDPSAALNKLNTAAA--KIKSKIeqfqkvikmyekggvcpTCTQQISEGpdritkikdklkelqhSLEKL- 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 246 kEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIII---SFQHMQQLLQQETQANTEIDAELKVLRENNQTLERD-NE 321
Cdd:PHA02562 319 -DTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITlvdKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTkSE 397
|
....*
gi 148695785 322 LQREK 326
Cdd:PHA02562 398 LVKEK 402
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
35-343 |
5.37e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 35 LLEALEELRMRRK-AETQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAMgvlknQLQMKMYALEEEKGKYKLAt 113
Cdd:PRK04863 360 LEERLEEQNEVVEeADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAI-----QYQQAVQALERAKQLCGLP- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 114 eikEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYYAAIT-----NQFGLVRENHVKLEQ 188
Cdd:PRK04863 434 ---DLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSrseawDVARELLRRLREQRH 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 189 NVQEAIQLNKRLSTLNEK--QESEIHSLKKELKKAASelikskvtcqhKMEEESIDLIIKEQKYEELQERLNMELEVNKK 266
Cdd:PRK04863 511 LAEQLQQLRMRLSELEQRlrQQQRAERLLAEFCKRLG-----------KNLDDEDELEQLQEELEARLESLSESVSEARE 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 267 INEEITHIQEE-KQDIiisfqhmQQLLQQETQANTEIDAeLKVLREN---------------NQTLERDNELQREKVKEN 330
Cdd:PRK04863 580 RRMALRQQLEQlQARI-------QRLAARAPAWLAAQDA-LARLREQsgeefedsqdvteymQQLLERERELTVERDELA 651
|
330
....*....|...
gi 148695785 331 EEKFlSLEKEHER 343
Cdd:PRK04863 652 ARKQ-ALDEEIER 663
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
180-391 |
6.56e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 6.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 180 RENHVKLEQNVQEAIQLNKRLstlnEKQESEIHSLKKELKKAASELIKSkvtcqhkmeEESIDLIikEQKYEELQERLNm 259
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKEL----AALKKEEKALLKQLAALERRIAAL---------ARRIRAL--EQELAALEAELA- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 260 elEVNKKINEEITHIQEEKQDI------------------IIS------FQHMQQLLQQETQAN----TEIDAELKVLRE 311
Cdd:COG4942 87 --ELEKEIAELRAELEAQKEELaellralyrlgrqpplalLLSpedfldAVRRLQYLKYLAPARreqaEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 312 NNQTLERDNELQREKVKENEEKFLSLEKEHERAlgtwKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEE 391
Cdd:COG4942 165 LRAELEAERAELEALLAELEEERAALEALKAER----QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
28-383 |
6.60e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 43.88 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 28 LLDFRTSLLEALEELRMRRKAETQYEEQIAKIILETQELKwqkEALQNQKEALIKQhKEAMGVLKNQLQMKMYALE---E 104
Cdd:PRK02224 330 LEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELE---SELEEAREAVEDR-REEIEELEEEIEELRERFGdapV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 105 EKGKYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQkahLYHLAK-----------------EDYHKQLNEIEK 167
Cdd:PRK02224 406 DLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEA---LLEAGKcpecgqpvegsphvetiEEDRERVEELEA 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 168 YYAAITNQFGLVRENHVKLEqnvqEAIQLNKRLSTLNEKQE--SEIHSLKKELKKAASELIKSKVTCQHKMEEESIDlii 245
Cdd:PRK02224 483 ELEDLEEEVEEVEERLERAE----DLVEAEDRIERLEERREdlEELIAERRETIEEKRERAEELRERAAELEAEAEE--- 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 246 KEQKYEELQERLNMELEVNKKINEEITHIQEEKQdiiiSFQHMQQLLQqetqANTEIDAELKVLRENNQTLERDNELQRE 325
Cdd:PRK02224 556 KREAAAEAEEEAEEAREEVAELNSKLAELKERIE----SLERIRTLLA----AIADAEDEIERLREKREALAELNDERRE 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 326 KVKENEEKFLSLEKEHERA-----------LGTWKKHVEE-----------LSGEMNGIKNE---LSSLRETHAKLQEHY 380
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEArieearedkerAEEYLEQVEEkldelreerddLQAEIGAVENEleeLEELRERREALENRV 707
|
...
gi 148695785 381 NKL 383
Cdd:PRK02224 708 EAL 710
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
45-469 |
8.73e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.59 E-value: 8.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 45 RRKAETQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAMGVLKNQLQMKMYALEEEKGKYKLATEIKEKEIEGLK 124
Cdd:PTZ00121 1277 ARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAA 1356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 125 ETLKTLQVSQYSLQKKVSEMEQKAhlyhlakEDYHKQLNEIEKyyaaiTNQFGLVRENHVKLEQNVQEAIQLNKRLSTLN 204
Cdd:PTZ00121 1357 DEAEAAEEKAEAAEKKKEEAKKKA-------DAAKKKAEEKKK-----ADEAKKKAEEDKKKADELKKAAAAKKKADEAK 1424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 205 EKQES--EIHSLKK---------ELKKAASELIKSKVTCQHKMEEESIDLIIKEQKYEELQERLNMELEVNKKINEEITH 273
Cdd:PTZ00121 1425 KKAEEkkKADEAKKkaeeakkadEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKK 1504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 274 IQEEKQDiIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEK---EHERALGTWK- 349
Cdd:PTZ00121 1505 AAEAKKK-ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAkkaEEDKNMALRKa 1583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 350 ---KHVEELSGE--MNGIKNELSSLRETHAKLQEHYNKLCEQKKTEEYKKFQNVPELNNENSD---ELTRKKSENIITQK 421
Cdd:PTZ00121 1584 eeaKKAEEARIEevMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkaEELKKAEEENKIKA 1663
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 148695785 422 YNSGPEIWGKNTKSFCLDTEYREEEKKDLPVGKTAEDLQPFEISAKSE 469
Cdd:PTZ00121 1664 AEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKE 1711
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
15-225 |
1.05e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 15 TLQSSSETMVSIQLLDFRTSLLEALEELRMRRKAETQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAMGVLKNQ 94
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 95 LQMKMYALEEEKGKyklateiKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAhlyHLAKEDYHKQLNEIEKYYAAITN 174
Cdd:COG4913 343 LEREIERLERELEE-------RERRRARLEALLAALGLPLPASAEEFAALRAEA---AALLEALEEELEALEEALAEAEA 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 148695785 175 QFGLVRENHVKLEQNVQEaiqLNKRLSTLNEKQESEIHSLKKELKKAASEL 225
Cdd:COG4913 413 ALRDLRRELRELEAEIAS---LERRKSNIPARLLALRDALAEALGLDEAEL 460
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
154-328 |
1.08e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 154 AKEDYHKQLNEIEKYYAAITNQFGLVRENHVKLEQNVQEAIQLNKRLSTLNEKQESEIHSLKKELKKAASELIKS----- 228
Cdd:PRK00409 507 AKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEakkea 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 229 -KVTCQHKMEEESIDLIIKEQKYEELQERLN---MELEVNKKINEEITHIQEEKQDI-IISFQHMQQLLQQETQANTEID 303
Cdd:PRK00409 587 dEIIKELRQLQKGGYASVKAHELIEARKRLNkanEKKEKKKKKQKEKQEELKVGDEVkYLSLGQKGEVLSIPDDKEAIVQ 666
|
170 180
....*....|....*....|....*
gi 148695785 304 AELKVLRENNQTLERDNELQREKVK 328
Cdd:PRK00409 667 AGIMKMKVPLSDLEKIQKPKKKKKK 691
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
17-281 |
1.16e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.04 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 17 QSSSETMVSIQLLDFRTSLLEALEELRMRRKAETQYEEQIAKiiletqelkwQKEALQNQKEALIKQHKEAMGVLKNQLQ 96
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEEL----------KEEAELLEEEQLLIEQEEKIKEEELEEL 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 97 MKMyALEEEKGKYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEkyyaaitnQF 176
Cdd:pfam02463 839 ALE-LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQ--------KL 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 177 GLVRENHVKLEQNVQEAIQLNKRLSTLNEKQESEIHSLKKELKKAASELIKSKVTCQHKMEEESIDLIIKEQKYEELQER 256
Cdd:pfam02463 910 NLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989
|
250 260
....*....|....*....|....*
gi 148695785 257 LNMELEVNKKINEEITHIQEEKQDI 281
Cdd:pfam02463 990 YNKDELEKERLEEEKKKLIRAIIEE 1014
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
216-420 |
1.19e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 216 KELKKAASELIKskvtcQHKMEEESI-DLIIKEQKYEELQERLNMELEVNKKINEeithiqeekqdiiisFQHMQQLLQQ 294
Cdd:PRK12704 34 KEAEEEAKRILE-----EAKKEAEAIkKEALLEAKEEIHKLRNEFEKELRERRNE---------------LQKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 295 ETQAnteidaelkvLRENNQTLE-RDNELQrEKVKENEEKFLSLEKEHERALGTWKKHVEELSgemngiknELSSLRETH 373
Cdd:PRK12704 94 KEEN----------LDRKLELLEkREEELE-KKEKELEQKQQELEKKEEELEELIEEQLQELE--------RISGLTAEE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 148695785 374 AKlQEHYNKLCEQKKTEEYKKFQNVPELNNENSDeltrKKSENIITQ 420
Cdd:PRK12704 155 AK-EILLEKVEEEARHEAAVLIKEIEEEAKEEAD----KKAKEILAQ 196
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
93-413 |
1.23e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 93 NQLQMKMYALEEEKGKYKLATE--IKEKE---------IEGLKETLKTLQVSQYSLQKKVSEMEQK-----------AHL 150
Cdd:pfam05483 77 SRLYSKLYKEAEKIKKWKVSIEaeLKQKEnklqenrkiIEAQRKAIQELQFENEKVSLKLEEEIQEnkdlikennatRHL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 151 YHLAKEDYHKQLNEIEKYYAAITNqfglVRENHVKLEQNVQEAIQLNKRLSTLNEKQESEIH---------------SLK 215
Cdd:pfam05483 157 CNLLKETCARSAEKTKKYEYEREE----TRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfklkedhekiqhleeEYK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 216 KEL---KKAASELIKSKVTCQHKMEEESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIISFQH---MQ 289
Cdd:pfam05483 233 KEIndkEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRsmsTQ 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 290 QLLQQETQANTEIDAEL---------------------------------KVLRENNQTLERDN--------ELQREKVK 328
Cdd:pfam05483 313 KALEEDLQIATKTICQLteekeaqmeelnkakaahsfvvtefeattcsleELLRTEQQRLEKNEdqlkiitmELQKKSSE 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 329 ENEEKFLSLEKEHE-----------RALGTWKKHVEELSGEMNGIKNELSSLRETHAK--------------LQEHYNKL 383
Cdd:pfam05483 393 LEEMTKFKNNKEVEleelkkilaedEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKeihdleiqltaiktSEEHYLKE 472
|
410 420 430
....*....|....*....|....*....|.
gi 148695785 384 CEQKKTE-EYKKFQNVPELNNENSDELTRKK 413
Cdd:pfam05483 473 VEDLKTElEKEKLKNIELTAHCDKLLLENKE 503
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
36-379 |
1.25e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 36 LEALEElrMRRKAETQYEEQIAKIILE-TQELKWQKEALQNQKEALIKQHKEAMGVLKNQLQmkmyALEEEKGKYKLATE 114
Cdd:pfam12128 363 LKALTG--KHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALES----ELREQLEAGKLEFN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 115 IKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYYAAITNQFGLVRENHVKLEQNVQEAI 194
Cdd:pfam12128 437 EEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLE 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 195 QLNKRLSTLNEKQESEIHSLKKELKKAA-------SELIKSKVTCQHKMEEESIDLIIKEQ----------KYEELQERL 257
Cdd:pfam12128 517 ERQSALDELELQLFPQAGTLLHFLRKEApdweqsiGKVISPELLHRTDLDPEVWDGSVGGElnlygvkldlKRIDVPEWA 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 258 NMELEVNKKINEEITHIQEEKQDIiisfqhmQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSL 337
Cdd:pfam12128 597 ASEEELRERLDKAEEALQSAREKQ-------AAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK 669
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 148695785 338 EKEHERALGTWKKHVEELSGEMNGIKNELSS-LRETHAKLQEH 379
Cdd:pfam12128 670 NKALAERKDSANERLNSLEAQLKQLDKKHQAwLEEQKEQKREA 712
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
109-277 |
1.27e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 109 YKLATEIKEKEIEGLKETLKTLqvsqysLQKKVSEMEQKAHLYHL-AKEDYHKQLNEIEKYYAAitnqfglvRENHV-KL 186
Cdd:PRK12704 22 YFVRKKIAEAKIKEAEEEAKRI------LEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRE--------RRNELqKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 187 EQNV-QEAIQLNKRLSTLnEKQESEIHSLKKELKKAASELIKSKVTCQHKMEE-----ESIDLIIKEQKYEELQERLNME 260
Cdd:PRK12704 88 EKRLlQKEENLDRKLELL-EKREEELEKKEKELEQKQQELEKKEEELEELIEEqlqelERISGLTAEEAKEILLEKVEEE 166
|
170
....*....|....*....
gi 148695785 261 L--EVNKKINEEITHIQEE 277
Cdd:PRK12704 167 ArhEAAVLIKEIEEEAKEE 185
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
39-345 |
1.75e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.83 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 39 LEELRMRRKAETQYEEQIAKIILEtqELKWQKEALQNQKEALIKQHKEAMGVLKNQLqmkmyalEEEKGKYKLATEIKEK 118
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEE--ERERALEEEEEKEEERKEERKRYRQELEEQI-------EEREQKRQEEYEEKLQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 119 EIEGLKETLKTLQVsqyslqkkvsEMEQKAHLYHLAKEDYHKQLNEIEKyyaaitnqfglvRENHVKLEQNVQEAIQLNK 198
Cdd:pfam13868 99 EREQMDEIVERIQE----------EDQAEAEEKLEKQRQLREEIDEFNE------------EQAEWKELEKEEEREEDER 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 199 RLSTLNEKQESEI-HSLKKELKKAASELIKSKVTCQHKMEEESidliiKEQKYEELQERLNMELEVNKKINEEITHIQEE 277
Cdd:pfam13868 157 ILEYLKEKAEREEeREAEREEIEEEKEREIARLRAQQEKAQDE-----KAERDELRAKLYQEEQERKERQKEREEAEKKA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 148695785 278 KQDIIISFQHMQQLLQQETQANTEIDAElkvlRENNQTLERDNELQREKVKENEEKFLSLEKEHERAL 345
Cdd:pfam13868 232 RQRQELQQAREEQIELKERRLAEEAERE----EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRREL 295
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
187-337 |
1.78e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 187 EQNVQEAIQlnkRLSTLNEKQESEIHSLKKELKKAasELIKSKVtcqhkmeeesidliikEQKYEELQERL-NMELEVNK 265
Cdd:PRK00409 515 KEKLNELIA---SLEELERELEQKAEEAEALLKEA--EKLKEEL----------------EEKKEKLQEEEdKLLEEAEK 573
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148695785 266 KINEEITHIQEEKQDIIISFQHMQQlLQQETQANTEIDAELKVLRENNQTLE---RDNELQREKVKENEE-KFLSL 337
Cdd:PRK00409 574 EAQQAIKEAKKEADEIIKELRQLQK-GGYASVKAHELIEARKRLNKANEKKEkkkKKQKEKQEELKVGDEvKYLSL 648
|
|
| PTZ00341 |
PTZ00341 |
Ring-infected erythrocyte surface antigen; Provisional |
120-392 |
1.82e-03 |
|
Ring-infected erythrocyte surface antigen; Provisional
Pssm-ID: 173534 [Multi-domain] Cd Length: 1136 Bit Score: 42.47 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 120 IEGLKEtlKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYyaaITNQFGLVRENHVKLEQNVQEAIQLNKR 199
Cdd:PTZ00341 870 DEGLDE--KKLKKRAESLKKLANAIEKYAGGGKKDKKAKKKDAKDLSGN---IAHEINLINKELKNQNENVPEHLKEHAE 944
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 200 LSTLNEKQESEIHSLKKELKKAASELIKSKVtcQHKMEE---ESIDLIIKEQKYEELQERL--NMELEVNKKINEEITHI 274
Cdd:PTZ00341 945 ANIEEDAEENVEEDAEENVEENVEENVEENV--EENVEEnveENVEENVEENVEENVEENIeeNVEENVEENIEENVEEY 1022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 275 QEE-----KQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKflSLEKEHERALGTWK 349
Cdd:PTZ00341 1023 DEEnveevEENVEEYDEENVEEIEENAEENVEENIEENIEEYDEENVEEIEENIEENIEENVEE--NVEENVEEIEENVE 1100
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 148695785 350 KHVEElsgemngikNELSSLRETHAKLQEHYNKLCEQKKTEEY 392
Cdd:PTZ00341 1101 ENVEE---------NAEENAEENAEENAEEYDDENPEEHNEEY 1134
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
35-217 |
2.26e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.12 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 35 LLEALEELRmrRKAETQYEEqIAKIILETQELKwqkEALQNQKEALIKQHKEamgvlknqlqmkmyALEEEKGKYKLATE 114
Cdd:PRK00409 521 LIASLEELE--RELEQKAEE-AEALLKEAEKLK---EELEEKKEKLQEEEDK--------------LLEEAEKEAQQAIK 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 115 IKEKEIEGLKETLKTLQVSQYSLQKkvsemEQKAhlyhlakEDYHKQLNEIEKyyaaitnqfglVRENHVKLEQNVQEAI 194
Cdd:PRK00409 581 EAKKEADEIIKELRQLQKGGYASVK-----AHEL-------IEARKRLNKANE-----------KKEKKKKKQKEKQEEL 637
|
170 180
....*....|....*....|...
gi 148695785 195 QLNKRLSTLNEKQESEIHSLKKE 217
Cdd:PRK00409 638 KVGDEVKYLSLGQKGEVLSIPDD 660
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
71-329 |
2.30e-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: 41.80 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 71 EALQNQKEALIKQHKEAMGVLKNQLQMKmyalEEEKGKYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAhl 150
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQR----EKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKY-- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 151 yhlakedyhkqlNEIEKYYAAITNQFGLVRENHVKLEQNVQEAIQLNKRLSTLNEKQESEIHSLKKELKKAASELikskv 230
Cdd:pfam07888 104 ------------KELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQR----- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 231 tcqHKMEEESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLR 310
Cdd:pfam07888 167 ---KEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQ 243
|
250
....*....|....*....
gi 148695785 311 ENNQTLERDNELQREKVKE 329
Cdd:pfam07888 244 ERLNASERKVEGLGEELSS 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
69-336 |
2.33e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.67 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 69 QKEALQNQKEALIKQhkeamgvlKNQLQMKMYALEEEKGKYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKa 148
Cdd:COG4942 21 AAAEAEAELEQLQQE--------IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 149 hlyhlaKEDYHKQLNEIEKYYAA-ITNQFGLVRENHVKL---EQNVQEAIQLNKRLSTLNEKQESEIHSLKKELKkaase 224
Cdd:COG4942 92 ------IAELRAELEAQKEELAElLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 225 likskvtcqhkmeeesiDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQdiiisfqhmqQLLQQETQANTEIDA 304
Cdd:COG4942 161 -----------------ELAALRAELEAERAELEALLAELEEERAALEALKAERQ----------KLLARLEKELAELAA 213
|
250 260 270
....*....|....*....|....*....|..
gi 148695785 305 ELKVLRENNQTLERDNELQREKVKENEEKFLS 336
Cdd:COG4942 214 ELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
26-148 |
2.47e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 26 IQLLDFRTSLLEALEELRMRRKAETQYEEQIAKIILETQELKWQKEALQNQKEALIKqhkeamgvLKNQLQMKMYALEEE 105
Cdd:COG4942 122 LALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA--------LLAELEEERAALEAL 193
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 148695785 106 KGKYKLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKA 148
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
53-307 |
2.72e-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: 41.93 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 53 EEQIAKIILETQELKWQKEALqNQKEALIKQHKEAMGVLKNQLQMKMYALEEE--KGKYKLATEIKEKEIEGLKETLKTL 130
Cdd:TIGR04523 495 EKELKKLNEEKKELEEKVKDL-TKKISSLKEKIEKLESEKKEKESKISDLEDElnKDDFELKKENLEKEIDEKNKEIEEL 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 131 QVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYYAAITNQFGLVRENHVKLEQNVqeaiqlnKRLSTLNEKQESE 210
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII-------KNIKSKKNKLKQE 646
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 211 IHSLKKELKKaaselIKSKVTcqhKMEEESIDLIIKEQKYEELQERLNMELEV--NKKINEEITHIQEEKqdIIISFQHM 288
Cdd:TIGR04523 647 VKQIKETIKE-----IRNKWP---EIIKKIKESKTKIDDIIELMKDWLKELSLhyKKYITRMIRIKDLPK--LEEKYKEI 716
|
250
....*....|....*....
gi 148695785 289 QQLLQQETQANTEIDAELK 307
Cdd:TIGR04523 717 EKELKKLDEFSKELENIIK 735
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
238-383 |
2.75e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.77 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 238 EESIDLIIKEQKYEELQERLnmelevnkkINEEIThiqEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLE 317
Cdd:COG2433 366 DEVKARVIRGLSIEEALEEL---------IEKELP---EEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELE 433
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148695785 318 RDNELQREKVKENEEKfLSLEKEHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKL 383
Cdd:COG2433 434 AELEEKDERIERLERE-LSEARSEERREIRKDREISRLDREIERLERELEEERERIEELKRKLERL 498
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
192-386 |
2.87e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 41.96 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 192 EAIQ-LNKRLSTLNEKQESEIHSlkKELKKAASELIKSKVTCQHKMEEES--IDLIIKEQKYEELQERLnmeLEVNKKIN 268
Cdd:PRK10929 45 EIVEaLQSALNWLEERKGSLERA--KQYQQVIDNFPKLSAELRQQLNNERdePRSVPPNMSTDALEQEI---LQVSSQLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 269 EEITHIQEEKQDIIISFQHMQQLLQQETQAN---TEIDAELKVLRENNQTLER--------DNELQREKVKENEEKFLSL 337
Cdd:PRK10929 120 EKSRQAQQEQDRAREISDSLSQLPQQQTEARrqlNEIERRLQTLGTPNTPLAQaqltalqaESAALKALVDELELAQLSA 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 148695785 338 EKEHERA---LGTWKKHVEELSGEMNGIKNELSSLRETHAKLQ-EHYNKLCEQ 386
Cdd:PRK10929 200 NNRQELArlrSELAKKRSQQLDAYLQALRNQLNSQRQREAERAlESTELLAEQ 252
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
37-329 |
3.60e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 40.79 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 37 EALEELRMRRKAETQYEEQIAKIILETQ----ELKW--QKEALQNQ-KEALIKQHKEAMGVLKNQLQMKMyalEEEKGKY 109
Cdd:pfam15558 61 EQWQAEKEQRKARLGREERRRADRREKQviekESRWreQAEDQENQrQEKLERARQEAEQRKQCQEQRLK---EKEEELQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 110 KLATEIKEKEIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAK----------EDYHKQLNEIEKYYAAITNQFGLV 179
Cdd:pfam15558 138 ALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARkvlvdcqakaEELLRRLSLEQSLQRSQENYEQLV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 180 RENHVKLEQNVQEAIQLNKRLSTLNEKQESEIHSLKKELKKAASELIKSKVTCQHKmeeesidliIKEQKYEELQErLNM 259
Cdd:pfam15558 218 EERHRELREKAQKEEEQFQRAKWRAEEKEEERQEHKEALAELADRKIQQARQVAHK---------TVQDKAQRARE-LNL 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 148695785 260 ELEVNKKIN------EEITHIQEEKQDIIISFQHMQQLLQQETQAnteidaelkvlRENNQTLERDNELQREKVKE 329
Cdd:pfam15558 288 EREKNHHILklkvekEEKCHREGIKEAIKKKEQRSEQISREKEAT-----------LEEARKTARASFHMREKVRE 352
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
33-410 |
4.02e-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: 41.19 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 33 TSLLEALEELRMRR----------KAETQYEEQIAKIILETQELKWQKEALQNQKEALIKQHKEAMGVLKNQLQmkmyAL 102
Cdd:TIGR00606 182 TRYIKALETLRQVRqtqgqkvqehQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLK----EI 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 103 EEEKGKyklateikekeIEGLKETLKTLQVSQYSLQKKVSEMEQKAHLYHLAKEDyhkQLNEIEKYYAAITNQFGLVREN 182
Cdd:TIGR00606 258 EHNLSK-----------IMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE---QLNDLYHNHQRTVREKERELVD 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 183 -HVKLEQNVQEAIQLNKRLSTLNEKQES--------EIHSLKKELKKAASELIKSKVTCQHKMEEESIDLIIKEQKYEEL 253
Cdd:TIGR00606 324 cQRELEKLNKERRLLNQEKTELLVEQGRlqlqadrhQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQ 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 254 QERLNMELEVNKKINEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEK 333
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKA 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 334 FLSLEKEHERAL-GTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEEYK--KFQNVPELNNENSDELT 410
Cdd:TIGR00606 484 ERELSKAEKNSLtETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKmdKDEQIRKIKSRHSDELT 563
|
|
| COG4026 |
COG4026 |
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ... |
252-383 |
4.47e-03 |
|
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];
Pssm-ID: 443204 [Multi-domain] Cd Length: 287 Bit Score: 40.48 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 252 ELQERLNMELEvnkkinEEITHIQEEKQDIIISFQHMQQLLQQETQANTEIDAELKVLrennQTLERDNELqREKVKENE 331
Cdd:COG4026 73 ELAEKFFEELK------GMVGHVERMKLPLGHDVEYVDVELVRKEIKNAIIRAGLKSL----QNIPEYNEL-REELLELK 141
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 148695785 332 EKFLSLEKEHERALgtwkKHVEELSGEMNGIKNELSSLRETHAKLQEHYNKL 383
Cdd:COG4026 142 EKIDEIAKEKEKLT----KENEELESELEELREEYKKLREENSILEEEFDNI 189
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
53-327 |
5.83e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 40.71 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 53 EEQIAKIILETQELkwqkEALQNQKEALIKQHKEAMGVLKNQLQMkmyaLEEEKGKYK-LATEIKEKEIEGLKETLKTLQ 131
Cdd:PRK04863 836 EAELRQLNRRRVEL----ERALADHESQEQQQRSQLEQAKEGLSA----LNRLLPRLNlLADETLADRVEEIREQLDEAE 907
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 132 VSQYSLQKKVSEMEQKAHLYHLAKED--YHKQLNeiEKYYAAITNQ-------FGLV----RENHVKLEQNVQ---EAIQ 195
Cdd:PRK04863 908 EAKRFVQQHGNALAQLEPIVSVLQSDpeQFEQLK--QDYQQAQQTQrdakqqaFALTevvqRRAHFSYEDAAEmlaKNSD 985
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 196 LNKRLSTLNEKQESEIHSLKKELKKAASELIK-SKVTCQHKmeeESIDliIKEQKYEELQERLNmELEVNKKINEEI-TH 273
Cdd:PRK04863 986 LNEKLRQRLEQAEQERTRAREQLRQAQAQLAQyNQVLASLK---SSYD--AKRQMLQELKQELQ-DLGVPADSGAEErAR 1059
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 148695785 274 IQEEK--QDIIISFQHMQQLLQQETQANTEIDAELKVLREnnqtLERDNELQREKV 327
Cdd:PRK04863 1060 ARRDElhARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRK----LERDYHEMREQV 1111
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
192-380 |
6.09e-03 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 40.55 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 192 EAIQLNKRLSTLNEKQESEIHSLKKELKKAAS--ELIKSKVTCQHKMEEESIDLIIKEQKYEELQERLNMELEVNKKIN- 268
Cdd:COG5391 284 ERKELNESTSKAIHNILSIFSLFEKILIQLESeeESLTRLLESLNNLLLLVLNFSGVFAKRLEQNQNSILNEGVVQAETl 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 269 -EEITHIQEEKQDIIISFQH----MQQLLQQETQANTEIDAELKVL----RENNQTLERDNELQREKVKENEEKFLSLEK 339
Cdd:COG5391 364 rSSLKELLTQLQDEIKSRESliltDSNLEKLTDQNLEDVEELSRSLrknsSQRAVVSQQPEGLTSFSKLSYKLRDFVQEK 443
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 148695785 340 EHERALGTWKKHVEELSGEMNGIKNELSSLRETHAKLQEHY 380
Cdd:COG5391 444 SRSKSIESLQQDKEKLEEQLAIAEKDAQEINEELKNELKFF 484
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
202-344 |
7.73e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 40.43 E-value: 7.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 202 TLNEKQESEIHSLKKELKKAASELikskVTCQHKMEEESIDLIIKEQKYEELQERLNMELEVNKKINEEITHIQEEKQDI 281
Cdd:pfam05911 681 EENKRLKEEFEQLKSEKENLEVEL----ASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKCMAESYEDL 756
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 148695785 282 iisfqhmqqllqqETQAnTEIDAELKVLRENNQTLErdNELQREK--VKENEEKFLSLEKEHERA 344
Cdd:pfam05911 757 -------------ETRL-TELEAELNELRQKFEALE--VELEEEKncHEELEAKCLELQEQLERN 805
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
53-281 |
7.76e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 40.01 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 53 EEQIAKIILETQELKWQKE----ALQNQKEALIKQHKEAMGVLKnQLQMKMYALEEEKGKYKLATEIKEKEIEGLKETLK 128
Cdd:pfam05667 316 TSSPPTKVETEEELQQQREeeleELQEQLEDLESSIQELEKEIK-KLESSIKQVEEELEELKEQNEELEKQYKVKKKTLD 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 129 TLQVSQYS---LQKKVSEMEQKahLYHLAKEDYHKQLNEIEKYyaaitnqfglvrenhvkleqnvqeaiqlnKRLSTLNE 205
Cdd:pfam05667 395 LLPDAEENiakLQALVDASAQR--LVELAGQWEKHRVPLIEEY-----------------------------RALKEAKS 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 206 KQESEIHSLKKELKKaaselIKSkvtcqhKMEEESIDLIIKEQKYEELQERL-NMELEVN-----KKINEEITHIQEEKQ 279
Cdd:pfam05667 444 NKEDESQRKLEEIKE-----LRE------KIKEVAEEAKQKEELYKQLVAEYeRLPKDVSrsaytRRILEIVKNIKKQKE 512
|
..
gi 148695785 280 DI 281
Cdd:pfam05667 513 EI 514
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
291-386 |
8.86e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 37.98 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 291 LLQQETQANTEIDAELKVLRENNQTLERDNELQREKVKENEEKFLSLEKEHERALGTWKKHVEELSGEMNGIKNE-LSSL 369
Cdd:pfam09744 37 LLESLASRNQEHNVELEELREDNEQLETQYEREKALRKRAEEELEEIEDQWEQETKDLLSQVESLEEENRRLEADhVSRL 116
|
90
....*....|....*..
gi 148695785 370 RETHAKLQEHYNKLCEQ 386
Cdd:pfam09744 117 EEKEAELKKEYSKLHER 133
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
38-394 |
9.51e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.12 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 38 ALEELRMRRKAETQYEEQIAKiiLETQELKWQKEALQNQKEALIK--QHKEAMGVLKNQLQMKMYALEEEKGKYKLATEI 115
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMK--LYEEEKKMKAEEAKKAEEAKIKaeELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 116 KEKEIEGLKETLKT---------LQVSQYSLQKKVSEMEQKAHLYHLAKEDYHKQLNEIEKYYAAITNQfglvRENHVKL 186
Cdd:PTZ00121 1657 EENKIKAAEEAKKAeedkkkaeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE----EENKIKA 1732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 187 EQNVQEAIQLNKRLSTL--NEKQESEIHSLKKELKKAASELIKSKvtcqhkmeeesiDLIIKEQKYEELQERLNMELEVN 264
Cdd:PTZ00121 1733 EEAKKEAEEDKKKAEEAkkDEEEKKKIAHLKKEEEKKAEEIRKEK------------EAVIEEELDEEDEKRRMEVDKKI 1800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 148695785 265 KKINEEITHIQEEKQDIIISFQHMQQLLQQETQanteidaelKVLRENNQTLERDNELQREKVKENEEKFLSLEKEHERA 344
Cdd:PTZ00121 1801 KDIFDNFANIIEGGKEGNLVINDSKEMEDSAIK---------EVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFN 1871
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 148695785 345 LGTWKK-----HVEELSGEMNGIKNELSSLRETHAKLQEHYNKLCEQKKTEEYKK 394
Cdd:PTZ00121 1872 KEKDLKeddeeEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIK 1926
|
|
| |
